#################################################### # Disordered Binding Sites (DIBS) database # # Version: 13-05-2019 # # Source: http://dibs.enzim.ttk.mta.hu/ # #################################################### [Entry] [Accession]=DI1000001 [Disorder status]=Confirmed [Kd]=9.33E-05 [Name]=c-Myc bound to the SH3 domain of BIN1 [Source organism]=Homo sapiens [PDB ID]=1mv0 [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH3 [Type chain A]=Disordered [Evidence chain A]=The 1-167 region described in DisProt entry DP00260 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains three known functional linear motifs (DEG_SCF_FBW7_1, DOC_WW_Pin1_4, LIG_SH3_2) and two known modification sites (MOD_GSK3_1, MOD_ProDKin_1). [Type chain B]=Ordered [Evidence chain B]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF14604). A solved monomeric structure of the domain is represented by PDB ID 1muz. [Chain A name]=Myc proto-oncogene protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P01106 [Chain A UniProt boundaries]=55-68 [Chain A UniProt coverage]=3.2% [Chain A UniRef90 accession]=UniRef90_P01106 [Chain A UniRef90 boundaries]=55-68 [Chain B name]=Myc box-dependent-interacting protein 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O00499 [Chain B UniProt boundaries]=513-593 [Chain B UniProt coverage]=13.7% [Chain B UniRef90 accession]=UniRef90_O00499 [Chain B UniRef90 boundaries]=513-593 [Entry] [Accession]=DI1000002 [Disorder status]=Confirmed [Kd]=5.00E-05 [Name]=p53 peptide interacting with CBP Bromodomain [Source organism]=Homo sapiens [PDB ID]=1jsp [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Bromodomain [Type chain A]=Disordered [Evidence chain A]=The 320-393 region described in DisProt entry DP00086 and the 364-389 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. [Type chain B]=Ordered [Evidence chain B]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 2d82. [Modified residues chain A]=N(6)-acetyllysine#K#382 [Chain A name]=Cellular tumor antigen p53 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P04637 [Chain A UniProt boundaries]=367-386 [Chain A UniProt coverage]=5.1% [Chain A UniRef90 accession]=UniRef90_P04637 [Chain A UniRef90 boundaries]=367-386 [Chain B name]=CREB-binding protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q92793 [Chain B UniProt boundaries]=1077-1197 [Chain B UniProt coverage]=5% [Chain B UniRef90 accession]=UniRef90_Q92793 [Chain B UniRef90 boundaries]=1078-1197 [Entry] [Accession]=DI1000003 [Disorder status]=Confirmed [Kd]=9.60E-07 [Name]=p53 transactivation domain 2 bound to the PH domain of human TFIIH [Source organism]=Homo sapiens [PDB ID]=2ruk [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PH [Type chain A]=Disordered [Evidence chain A]=The 1-73 region described in DisProt entry DP00086 and the 1-96 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains the known functional linear motif TADII (http://www.uniprot.org/uniprot/P04637#family_and_domains). [Type chain B]=Ordered [Evidence chain B]=The PH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF08567). A solved monomeric structure of the domain is represented by PDB ID 1pfj. [Modified residues chain A]=phosphoserine#S#46|phosphothreonine#T#55 [Chain A name]=Cellular tumor antigen p53 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P04637 [Chain A UniProt boundaries]=41-62 [Chain A UniProt coverage]=5.6% [Chain A UniRef90 accession]=UniRef90_P04637 [Chain A UniRef90 boundaries]=41-62 [Chain B name]=General transcription factor IIH subunit 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P32780 [Chain B UniProt boundaries]=1-108 [Chain B UniProt coverage]=19.7% [Chain B UniRef90 accession]=UniRef90_P32780 [Chain B UniRef90 boundaries]=1-108 [Entry] [Accession]=DI1020001 [Disorder status]=Confirmed [Kd]=2.30E-07 [Name]=E6 protein bound to the PDZ domain of MAGI1 [Source organism]=Human papillomavirus type 16 / Homo sapiens [PDB ID]=2kpl [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PDZ [Type chain B]=Disordered [Evidence chain B]=The 151-158 region described in IDEAL entry IID90005 covers 73% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_1). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 2kpk. [Modified residues chain A]=phosphoserine#S#46|phosphothreonine#T#55 [Chain B name]=Protein E6 [Chain B source organism]=Human papillomavirus type 16 [Chain B UniProt accession]=P03126 [Chain B UniProt boundaries]=148-158 [Chain B UniProt coverage]=7% [Chain B UniRef90 accession]=UniRef90_P03126 [Chain B UniRef90 boundaries]=148-158 [Chain A name]=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96QZ7 [Chain A UniProt boundaries]=452-580 [Chain A UniProt coverage]=8.7% [Chain A UniRef90 accession]=UniRef90_Q96QZ7 [Chain A UniRef90 boundaries]=454-580 [Entry] [Accession]=DI1020002 [Disorder status]=Confirmed [Kd]=2.30E-07 [Name]=Adenoviral early E1A oncoprotein bound to CBP TAZ2 domain. [Source organism]=Human adenovirus C serotype 5 / Homo sapiens [PDB ID]=2kje [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=TAZ type 2 zinc finger [Type chain B]=Disordered [Evidence chain B]=The 1-139 region described in IDEAL entry IID90003 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif, the FxDxxxL motif (PMID:21146412). [Type chain A]=Ordered [Evidence chain A]=The TAZ zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02135). A solved monomeric structure of a close homologue is represented by PDB ID 1f81. [Modified residues chain A]=phosphoserine#S#46|phosphothreonine#T#55 [Chain B name]=Early E1A 32 kDa protein [Chain B source organism]=Human adenovirus C serotype 5 [Chain B UniProt accession]=P03255 [Chain B UniProt boundaries]=50-91 [Chain B UniProt coverage]=14.5% [Chain B UniRef90 accession]=UniRef90_P03255 [Chain B UniRef90 boundaries]=53-86 [Chain A name]=CREB-binding protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q92793 [Chain A UniProt boundaries]=1763-1854 [Chain A UniProt coverage]=3.8% [Chain A UniRef90 accession]=UniRef90_Q92793 [Chain A UniRef90 boundaries]=1763-1851 [Entry] [Accession]=DI1000004 [Disorder status]=Confirmed [Kd]=8.77E-07 [Name]=p53 TAD2:p300 Taz2 complex [Source organism]=Homo sapiens [PDB ID]=2mzd [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=TAZ type 2 zinc finger [Type chain B]=Disordered [Evidence chain B]=The 1-73 region described in DisProt entry DP00086 and the 1-96 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains the known functional linear motif TADII (http://www.uniprot.org/uniprot/P04637#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The TAZ zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02135). A solved monomeric structure of the domain is represented by PDB ID 3io2. [Modified residues chain A]=phosphoserine#S#46|phosphothreonine#T#55 [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=35-59 [Chain B UniProt coverage]=6.4% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=35-59 [Chain A name]=Histone acetyltransferase p300 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q09472 [Chain A UniProt boundaries]=1723-1812 [Chain A UniProt coverage]=3.7% [Chain A UniRef90 accession]=UniRef90_Q09472 [Chain A UniRef90 boundaries]=1723-1809 [Entry] [Accession]=DI1000005 [Disorder status]=Confirmed [Kd]=8.77E-07 [Name]=NF-kB-K310ac peptide bound to BRD4 [Source organism]=Homo sapiens [PDB ID]=2lsp [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Bromodomain [Type chain A]=Disordered [Evidence chain A]=The 302-320 region described in IDEAL entry IID00207 covers 100% of the sequence present in the structure. [Type chain B]=Ordered [Evidence chain B]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 2i8n. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain A name]=Transcription factor p65 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q04206 [Chain A UniProt boundaries]=304-316 [Chain A UniProt coverage]=2.4% [Chain A UniRef90 accession]=UniRef90_Q04206 [Chain A UniRef90 boundaries]=304-316 [Chain B name]=Bromodomain-containing protein 4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O60885 [Chain B UniProt boundaries]=333-460 [Chain B UniProt coverage]=9.4% [Chain B UniRef90 accession]=UniRef90_O60885 [Chain B UniRef90 boundaries]=333-460 [Related structures]=4kv4 [Entry] [Accession]=DI1010001 [Disorder status]=Confirmed [Kd]=8.77E-07 [Name]=Autoimmune Regulator (AIRE) in complex with histone H3(1-20Cys) peptide [Source organism]=Zygosaccharomyces bailii / Homo sapiens [PDB ID]=2kft [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=The 1-39 region described in IDEAL entry IID50143 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 1xwh. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Histone H3 [Chain B source organism]=Zygosaccharomyces bailii [Chain B UniProt accession]=P61836 [Chain B UniProt boundaries]=2-22 [Chain B UniProt coverage]=15.4% [Chain B UniRef90 accession]=UniRef90_Q757N1 [Chain B UniRef90 boundaries]=2-22 [Chain A name]=Autoimmune regulator [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O43918 [Chain A UniProt boundaries]=292-347 [Chain A UniProt coverage]=10.3% [Chain A UniRef90 accession]=UniRef90_O43918 [Chain A UniRef90 boundaries]=294-347 [Entry] [Accession]=DI1000006 [Disorder status]=Confirmed [Kd]=2.22E-05 [Name]=Hox-C9 homeodomain recognition by the cell-cycle regulator Geminin [Source organism]=Homo sapiens [PDB ID]=2lp0 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Homeobox [Type chain B]=Disordered [Evidence chain B]=The 160-209 region described in IDEAL entry IID00409 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Homeobox domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1bw5. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Geminin [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O75496 [Chain B UniProt boundaries]=171-190 [Chain B UniProt coverage]=9.6% [Chain B UniRef90 accession]=UniRef90_O75496 [Chain B UniRef90 boundaries]=171-190 [Chain A name]=Homeobox protein Hox-C9 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P31274 [Chain A UniProt boundaries]=192-251 [Chain A UniProt coverage]=23.1% [Chain A UniRef90 accession]=UniRef90_P31274 [Chain A UniRef90 boundaries]=192-251 [Entry] [Accession]=DI1000007 [Disorder status]=Confirmed [Kd]=6.50E-06 [Name]=SUMO-1 in complex with a SUMO-binding motif of PIAS2 [Source organism]=Homo sapiens [PDB ID]=2asq [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SUMO [Type chain B]=Disordered [Evidence chain B]=The 427-488 region described in IDEAL entry IID00136 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_SUMO_SIM_par_1). [Type chain A]=Ordered [Evidence chain A]=The SUMO domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF11976). A solved monomeric structure of the domain is represented by PDB ID 1a5r. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=E3 SUMO-protein ligase PIAS2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O75928 [Chain B UniProt boundaries]=466-490 [Chain B UniProt coverage]=4% [Chain B UniRef90 accession]=UniRef90_O75928 [Chain B UniRef90 boundaries]=466-489 [Chain A name]=Small ubiquitin-related modifier 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63165 [Chain A UniProt boundaries]=1-97 [Chain A UniProt coverage]=96% [Chain A UniRef90 accession]=UniRef90_P63165 [Chain A UniRef90 boundaries]=1-97 [Entry] [Accession]=DI1010002 [Disorder status]=Confirmed [Kd]=2.20E-07 [Name]=Rxxk motif-containing Slp-76 peptide bound to the Gads SH3 Domain [Source organism]=Homo sapiens / Mus musculus [PDB ID]=1h3h [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH3 [Type chain B]=Disordered [Evidence chain B]=The 232-241 region described in IDEAL entry IID00318 covers 91% of the sequence present in the structure. The protein region involved in the interaction contains a RXXK motif (PMID:12620234). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00018). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2a36. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Lymphocyte cytosolic protein 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q13094 [Chain B UniProt boundaries]=232-242 [Chain B UniProt coverage]=2.1% [Chain B UniRef90 accession]=UniRef90_Q13094 [Chain B UniRef90 boundaries]=232-241 [Chain A name]=GRB2-related adaptor protein 2 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=O89100 [Chain A UniProt boundaries]=263-322 [Chain A UniProt coverage]=18.6% [Chain A UniRef90 accession]=UniRef90_O89100 [Chain A UniRef90 boundaries]=263-322 [Entry] [Accession]=DI1010003 [Disorder status]=Confirmed [Kd]=3.91E-07 [Name]=p53 transactivation domain 2 bound to the PH domain of S. cerevisiae TFIIH [Source organism]=Homo sapiens / Saccharomyces cerevisiae [PDB ID]=2gs0 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PH [Type chain B]=Disordered [Evidence chain B]=The 1-73 region described in DisProt entry DP00086 and the 1-96 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The PH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF08567). A solved monomeric structure of the domain is represented by PDB ID 1y5o. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=20-73 [Chain B UniProt coverage]=13.7% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=20-66 [Chain A name]=RNA polymerase II transcription factor B subunit 1 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P32776 [Chain A UniProt boundaries]=1-115 [Chain A UniProt coverage]=17.9% [Chain A UniRef90 accession]=UniRef90_P32776 [Chain A UniRef90 boundaries]=2-115 [Entry] [Accession]=DI1000008 [Disorder status]=Confirmed [Kd]=2.70E-06 [Name]=p53 TAD1:p300 Taz2 complex [Source organism]=Homo sapiens [PDB ID]=2k8f [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=TAZ type 2 zinc finger [Type chain B]=Disordered [Evidence chain B]=The 1-73 region described in DisProt entry DP00086 and the 1-96 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The TAZ zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02135). A solved monomeric structure of the domain is represented by PDB ID 3io2. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=1-39 [Chain B UniProt coverage]=9.9% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=1-39 [Chain A name]=Histone acetyltransferase p300 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q09472 [Chain A UniProt boundaries]=1723-1812 [Chain A UniProt coverage]=3.7% [Chain A UniRef90 accession]=UniRef90_Q09472 [Chain A UniRef90 boundaries]=1723-1809 [Entry] [Accession]=DI1000009 [Disorder status]=Confirmed [Kd]=3.46E-07 [Name]=p53 transactivation domain bound to the HMG-box of HMGB1 [Source organism]=Homo sapiens [PDB ID]=2ly4 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=HMG-box [Type chain B]=Disordered [Evidence chain B]=The 1-73 region described in DisProt entry DP00086 and the 1-96 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The HMG-box domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF09011). A solved monomeric structure of the domain is represented by PDB ID 2rtu. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=1-93 [Chain B UniProt coverage]=23.7% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=1-93 [Chain A name]=High mobility group protein B1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P09429 [Chain A UniProt boundaries]=2-84 [Chain A UniProt coverage]=38.6% [Chain A UniRef90 accession]=UniRef90_P09429 [Chain A UniRef90 boundaries]=2-84 [Entry] [Accession]=DI1010004 [Disorder status]=Confirmed [Kd]=3.46E-07 [Name]=APP peptide bound Mint2 PARM [Source organism]=Homo sapiens / Rattus norvegicus [PDB ID]=3sv1 [PDB chain IDs]=D:A [PDB note]=Chains B, C, E and F were removed as chains A and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.30 [Domain]=PID [Type chain D]=Disordered [Evidence chain D]=The 729-770 region described in IDEAL entry IID00294 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_PTB_Apo_2). [Type chain A]=Ordered [Evidence chain A]=The PID domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00640). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4dbb. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain D name]=Amyloid beta A4 protein [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P05067 [Chain D UniProt boundaries]=754-767 [Chain D UniProt coverage]=1.8% [Chain D UniRef90 accession]=UniRef90_P05067 [Chain D UniRef90 boundaries]=754-767 [Chain A name]=Amyloid beta A4 precursor protein-binding family A member 2 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=O35431 [Chain A UniProt boundaries]=365-552 [Chain A UniProt coverage]=25.1% [Chain A UniRef90 accession]=UniRef90_Q99767 [Chain A UniRef90 boundaries]=364-551 [Entry] [Accession]=DI1120001 [Disorder status]=Confirmed [Kd]=3.60E-07 [Name]=Complex between Tfb1 subunit of TFIIH and the activation domain of VP16 [Source organism]=Human herpesvirus 1 / Saccharomyces cerevisiae [PDB ID]=2k2u [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PH [Type chain B]=Disordered [Evidence chain B]=The 412-490 region described in IDEAL entry IID90006 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The PH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF08567). A solved monomeric structure of the domain is represented by PDB ID 1y5o. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Tegument protein VP16 [Chain B source organism]=Human herpesvirus 1 [Chain B UniProt accession]=P04486 [Chain B UniProt boundaries]=456-490 [Chain B UniProt coverage]=7.1% [Chain B UniRef90 accession]=UniRef90_P06492 [Chain B UniRef90 boundaries]=456-490 [Chain A name]=RNA polymerase II transcription factor B subunit 1 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P32776 [Chain A UniProt boundaries]=1-115 [Chain A UniProt coverage]=17.9% [Chain A UniRef90 accession]=UniRef90_P32776 [Chain A UniRef90 boundaries]=2-115 [Entry] [Accession]=DI1000010 [Disorder status]=Confirmed [Kd]=2.40E-05 [Name]=PxxDY motif of CD3 epsilon chain bound by EPS8L1 [Source organism]=Homo sapiens [PDB ID]=2rol [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH3 [Type chain B]=Disordered [Evidence chain B]=The 153-207 region described in DisProt entry DP00506 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_SH3_5). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00018). A solved monomeric structure of the domain is represented by PDB ID 2k2m. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=T-cell surface glycoprotein CD3 epsilon chain [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P07766 [Chain B UniProt boundaries]=181-192 [Chain B UniProt coverage]=5.8% [Chain B UniRef90 accession]=UniRef90_P07766 [Chain B UniRef90 boundaries]=181-192 [Chain A name]=Epidermal growth factor receptor kinase substrate 8-like protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q8TE68 [Chain A UniProt boundaries]=474-537 [Chain A UniProt coverage]=8.9% [Chain A UniRef90 accession]=UniRef90_Q8TE68 [Chain A UniRef90 boundaries]=478-537 [Entry] [Accession]=DI1000011 [Disorder status]=Confirmed [Kd]=7.80E-07 [Name]=ERCC1-XPA heterodimer [Source organism]=Homo sapiens [PDB ID]=2jnw [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=ERCC4 [Type chain B]=Disordered [Evidence chain B]=The 67-80 region described in IDEAL entry IID00196 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains the highly conserved TGGGFI-binding motif. (PMID:17948053) [Type chain A]=Ordered [Evidence chain A]=The ERCC4 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03834). A solved monomeric structure of the domain is represented by PDB ID 2jpd. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=DNA repair protein complementing XP-A cells [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P23025 [Chain B UniProt boundaries]=67-80 [Chain B UniProt coverage]=5.1% [Chain B UniRef90 accession]=UniRef90_P23025 [Chain B UniRef90 boundaries]=67-80 [Chain A name]=DNA excision repair protein ERCC-1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P07992 [Chain A UniProt boundaries]=96-214 [Chain A UniProt coverage]=40.1% [Chain A UniRef90 accession]=UniRef90_P07992 [Chain A UniRef90 boundaries]=96-214 [Entry] [Accession]=DI1020003 [Disorder status]=Inferred from motif [Kd]=7.80E-07 [Name]=SH2 domain from the tyrosine kinase Fyn in complex with middle T antigen peptide [Source organism]=Hamster polyomavirus / Homo sapiens [PDB ID]=1aou [PDB chain IDs]=P:F [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH2 [Type chain P]=Disordered [Evidence chain P]=The protein region involved in the interaction contains a known functional linear motif (LIG_SH2_SRC). [Type chain F]=Ordered [Evidence chain F]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ab2. [Modified residues chain P]=phosphotyrosine#Y#204 [Chain P name]=Middle T antigen [Chain P source organism]=Hamster polyomavirus [Chain P UniProt accession]=P03079 [Chain P UniProt boundaries]=321-331 [Chain P UniProt coverage]=2.7% [Chain P UniRef90 accession]=UniRef90_P03079 [Chain P UniRef90 boundaries]=321-331 [Chain F name]=Tyrosine-protein kinase Fyn [Chain F source organism]=Homo sapiens [Chain F UniProt accession]=P06241 [Chain F UniProt boundaries]=143-248 [Chain F UniProt coverage]=19.7% [Chain F UniRef90 accession]=UniRef90_P06241 [Chain F UniRef90 boundaries]=143-248 [Related structures]=1aot,4u1p [Entry] [Accession]=DI1000012 [Disorder status]=Confirmed [Kd]=7.80E-07 [Name]=Shc SH2 domain complexed with peptide from the T-cell receptor CD247 [Source organism]=Homo sapiens [PDB ID]=1tce [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The 52-164 region described in DisProt entry DP00200 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (ITAM - PF02189). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain is represented by PDB ID 1mil. [Modified residues chain B]=phosphotyrosine#Y#206 [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=T-cell surface glycoprotein CD3 zeta chain [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P20963 [Chain B UniProt boundaries]=137-150 [Chain B UniProt coverage]=8.5% [Chain B UniRef90 accession]=UniRef90_P20963 [Chain B UniRef90 boundaries]=137-150 [Chain A name]=SHC-transforming protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P29353 [Chain A UniProt boundaries]=480-583 [Chain A UniProt coverage]=17.8% [Chain A UniRef90 accession]=UniRef90_P29353 [Chain A UniRef90 boundaries]=480-583 [Entry] [Accession]=DI1000013 [Disorder status]=Confirmed [Kd]=7.70E-04 [Name]=C-terminal domain of RNAP II bound to TDRD3 [Source organism]=Homo sapiens [PDB ID]=2lto [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Tudor [Type chain B]=Disordered [Evidence chain B]=The 1593-1960 region described in IDEAL entry IID00126 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Tudor domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00567). A solved monomeric structure of the domain is represented by PDB ID 3pmt. [Modified residues chain B]=NG,NG-dimethyl-L-arginine#R#617 [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=DNA-directed RNA polymerase II subunit RPB1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P24928 [Chain B UniProt boundaries]=1804-1816 [Chain B UniProt coverage]=0.7% [Chain B UniRef90 accession]=UniRef90_P24928 [Chain B UniRef90 boundaries]=1895-1907 [Chain A name]=Tudor domain-containing protein 3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9H7E2 [Chain A UniProt boundaries]=553-610 [Chain A UniProt coverage]=8.9% [Chain A UniRef90 accession]=UniRef90_Q9H7E2 [Chain A UniRef90 boundaries]=554-608 [Entry] [Accession]=DI1000014 [Disorder status]=Confirmed [Kd]=2.36E-05 [Name]=Complex between the DDEF1 SH3 domain and the APC SAMP1 motif [Source organism]=Homo sapiens [PDB ID]=2rqu [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH3 [Type chain B]=Disordered [Evidence chain B]=The 1362-1745 region described in DisProt entry DP00519 and in IDEAL entry IID00035 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00018). A solved monomeric structure of the domain is represented by PDB ID 2rqt. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Adenomatous polyposis coli protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P25054 [Chain B UniProt boundaries]=1578-1596 [Chain B UniProt coverage]=0.7% [Chain B UniRef90 accession]=UniRef90_P25054 [Chain B UniRef90 boundaries]=1578-1596 [Chain A name]=Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9ULH1 [Chain A UniProt boundaries]=1069-1129 [Chain A UniProt coverage]=5.4% [Chain A UniRef90 accession]=UniRef90_Q9QWY8 [Chain A UniRef90 boundaries]=1087-1147 [Entry] [Accession]=DI1000015 [Disorder status]=Confirmed [Kd]=7.50E-08 [Name]=Interaction between human splicing factors U2AF65 and SF1/mBBP [Source organism]=Homo sapiens [PDB ID]=1opi [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=RRM [Type chain B]=Disordered [Evidence chain B]=The 1-35 region described in IDEAL entry IID00247 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_ULM_U2AF65_1) and a nuclear localization signal (http://www.uniprot.org/uniprot/Q15637#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The RRM domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00076). A solved monomeric structure of a close homologue is represented by PDB ID 2m52. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Splicing factor 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q15637 [Chain B UniProt boundaries]=13-25 [Chain B UniProt coverage]=2% [Chain B UniRef90 accession]=UniRef90_Q15637 [Chain B UniRef90 boundaries]=13-25 [Chain A name]=Splicing factor U2AF 65 kDa subunit [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P26368 [Chain A UniProt boundaries]=372-475 [Chain A UniProt coverage]=21.9% [Chain A UniRef90 accession]=UniRef90_P26368 [Chain A UniRef90 boundaries]=372-475 [Related structures]=1o0p,2m0g,4fxw [Entry] [Accession]=DI1000016 [Disorder status]=Confirmed [Kd]=5.00E-07 (PMID:19215094) [Name]=RAP74 C-terminal domain complexed with FCP1 C-terminal peptide [Source organism]=Homo sapiens [PDB ID]=1onv [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Winged helix [Type chain B]=Disordered [Evidence chain B]=The 879-961 region described in DisProt entry DP00177 and in IDEAL entry IID00117 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The winged helix domain involved in the interaction is known to adopt a stable structure in isolation (see PMID:10679470). A solved monomeric structure of the domain is represented by PDB ID 1i27. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=RNA polymerase II subunit A C-terminal domain phosphatase [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9Y5B0 [Chain B UniProt boundaries]=879-961 [Chain B UniProt coverage]=8.6% [Chain B UniRef90 accession]=UniRef90_Q9Y5B0 [Chain B UniRef90 boundaries]=890-961 [Chain A name]=General transcription factor IIF subunit 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P35269 [Chain A UniProt boundaries]=436-517 [Chain A UniProt coverage]=15.9% [Chain A UniRef90 accession]=UniRef90_P35269 [Chain A UniRef90 boundaries]=436-517 [Related structures]=1j2x [Entry] [Accession]=DI1400001 [Disorder status]=Confirmed [Kd]=1.32E-05 [Name]=Measles virus P protein in complex with N protein [Source organism]=Measles virus [PDB ID]=1t6o [PDB chain IDs]=B:A [PDB note]=Chain L was removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Paramyxovirus P/V phosphoprotein C-terminal [Type chain B]=Disordered [Evidence chain B]=The 400-523 region described in DisProt entry DP00640 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=Paramyxovirus P/V phosphoprotein C-terminal domain, which is involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03210). A solved monomeric structure of a close homologue is represented by PDB ID 1oks. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Nucleoprotein [Chain B source organism]=Measles virus [Chain B UniProt accession]=B1AAA7 [Chain B UniProt boundaries]=486-505 [Chain B UniProt coverage]=3.8% [Chain B UniRef90 accession]=UniRef90_Q89933 [Chain B UniRef90 boundaries]=486-505 [Chain A name]=Phosphoprotein [Chain A source organism]=Measles virus [Chain A UniProt accession]=Q9WMB4 [Chain A UniProt boundaries]=457-507 [Chain A UniProt coverage]=10.1% [Chain A UniRef90 accession]=UniRef90_P35974 [Chain A UniRef90 boundaries]=457-507 [Entry] [Accession]=DI1000017 [Disorder status]=Confirmed [Kd]=4.50E-09 [Name]=C-terminal domain of centrin 2 in complex with group C-complementing protein [Source organism]=Homo sapiens [PDB ID]=2a4j [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=EF-hand [Type chain B]=Disordered [Evidence chain B]=The 847-863 region described in IDEAL entry IID00164 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The EF-hand domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13499). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2ami. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=DNA repair protein complementing XP-C cells [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q01831 [Chain B UniProt boundaries]=847-863 [Chain B UniProt coverage]=1.8% [Chain B UniRef90 accession]=UniRef90_Q01831 [Chain B UniRef90 boundaries]=847-863 [Chain A name]=Centrin-2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P41208 [Chain A UniProt boundaries]=94-172 [Chain A UniProt coverage]=45.9% [Chain A UniRef90 accession]=UniRef90_P41208 [Chain A UniRef90 boundaries]=94-172 [Related structures]=2ggm,2obh [Entry] [Accession]=DI1010005 [Disorder status]=Confirmed [Kd]=5.20E-08 [Name]=CBP-TAZ2/STAT1-TAD complex [Source organism]=Homo sapiens / Mus musculus [PDB ID]=2ka6 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=TAZ type 2 zinc finger [Type chain B]=Disordered [Evidence chain B]=The 710-750 region described in DisProt entry DP00962 and IDEAL entry IID00046 covers 91% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The TAZ zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02135). A solved monomeric structure of a close homologue is represented by PDB ID 1f81. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Signal transducer and activator of transcription 1-alpha/beta [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P42224 [Chain B UniProt boundaries]=706-750 [Chain B UniProt coverage]=6% [Chain B UniRef90 accession]=UniRef90_P42224 [Chain B UniRef90 boundaries]=709-750 [Chain A name]=CREB-binding protein [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P45481 [Chain A UniProt boundaries]=1764-1855 [Chain A UniProt coverage]=3.8% [Chain A UniRef90 accession]=UniRef90_Q92793 [Chain A UniRef90 boundaries]=1763-1851 [Entry] [Accession]=DI1010006 [Disorder status]=Confirmed [Kd]=5.20E-08 [Name]=Crk SH2 domain in interaction with a Crk-derived phophopeptide [Source organism]=Mus musculus / Homo sapiens [PDB ID]=1ju5 [PDB chain IDs]=B:A [PDB note]=Chain C was removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=NMR [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The 192-293 region described in DisProt entry DP00748 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ab2. [Modified residues chain B]=phosphotyrosine#Y#221 [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Adapter molecule crk [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q64010 [Chain B UniProt boundaries]=217-229 [Chain B UniProt coverage]=4.3% [Chain B UniRef90 accession]=UniRef90_P46108 [Chain B UniRef90 boundaries]=217-228 [Chain A name]=Adapter molecule crk [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P46108 [Chain A UniProt boundaries]=12-120 [Chain A UniProt coverage]=35.9% [Chain A UniRef90 accession]=UniRef90_P46108 [Chain A UniRef90 boundaries]=12-120 [Entry] [Accession]=DI1010007 [Disorder status]=Confirmed [Kd]=5.80E-08 [Name]=CBP-TAZ1/STAT2-TAD complex [Source organism]=Homo sapiens / Mus musculus [PDB ID]=2ka4 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=TAZ type 1 zinc finger [Type chain B]=Disordered [Evidence chain B]=The 786-838 region described in DisProt entry DP00961 and IDEAL entry IID00053 covers 93% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The TAZ zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02135). A solved monomeric structure of the domain is represented by PDB ID 3io2. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Signal transducer and activator of transcription 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P52630 [Chain B UniProt boundaries]=782-838 [Chain B UniProt coverage]=6.7% [Chain B UniRef90 accession]=UniRef90_P52630 [Chain B UniRef90 boundaries]=783-838 [Chain A name]=Crebbp protein (Fragment) [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q6GQV9 [Chain A UniProt boundaries]=340-439 [Chain A UniProt coverage]=6.3% [Chain A UniRef90 accession]=UniRef90_Q6GQV9 [Chain A UniRef90 boundaries]=340-439 [Entry] [Accession]=DI1000018 [Disorder status]=Confirmed [Kd]=2.70E-03 [Name]=PWWP domain of Peregrin in complex with trimethylated H3K36 peptide [Source organism]=Homo sapiens [PDB ID]=2x4w [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.50 [Domain]=PWWP [Type chain B]=Disordered [Evidence chain B]=The 1-43 region described in IDEAL entry IID00088 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The PWWP domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00855). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2daq. [Modified residues chain B]=N-trimethyllysine#K#36 [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Histone H3.2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q71DI3 [Chain B UniProt boundaries]=23-43 [Chain B UniProt coverage]=15.4% [Chain B UniRef90 accession]=UniRef90_Q71DI3 [Chain B UniRef90 boundaries]=23-43 [Chain A name]=Peregrin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P55201 [Chain A UniProt boundaries]=1074-1205 [Chain A UniProt coverage]=10.9% [Chain A UniRef90 accession]=UniRef90_P55201 [Chain A UniRef90 boundaries]=1076-1205 [Related structures]=3mo8,2x4x,2x4y [Entry] [Accession]=DI1000019 [Disorder status]=Confirmed [Kd]=1.30E-06 [Name]=SUMO-interacting motif of ATF7-interacting protein bound to SUMO-2 [Source organism]=Homo sapiens [PDB ID]=2rpq [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SUMO [Type chain B]=Disordered [Evidence chain B]=The 976-981 region described in IDEAL entry IID00216 covers 75% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_SUMO_SIM_par_1). [Type chain A]=Ordered [Evidence chain A]=The SUMO domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF11976). A solved monomeric structure of the domain is represented by PDB ID 2awt. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Activating transcription factor 7-interacting protein 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q6VMQ6 [Chain B UniProt boundaries]=938-981 [Chain B UniProt coverage]=3.5% [Chain B UniRef90 accession]=UniRef90_Q6VMQ6 [Chain B UniRef90 boundaries]=938-981 [Chain A name]=Small ubiquitin-related modifier 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P61956 [Chain A UniProt boundaries]=1-93 [Chain A UniProt coverage]=97.9% [Chain A UniRef90 accession]=UniRef90_P61956 [Chain A UniRef90 boundaries]=1-93 [Entry] [Accession]=DI1000020 [Disorder status]=Confirmed [Kd]=2.18E-04 [Name]=CBP Bromodomain interacting with a H4 peptide (14-28) [Source organism]=Homo sapiens [PDB ID]=2rny [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Bromodomain [Type chain B]=Disordered [Evidence chain B]=The 1-28 region described in IDEAL entry IID00058 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 2d82. [Modified residues chain B]=N(6)-acetyllysine#K#20 [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Histone H4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P62805 [Chain B UniProt boundaries]=14-28 [Chain B UniProt coverage]=14.6% [Chain B UniRef90 accession]=UniRef90_P62805 [Chain B UniRef90 boundaries]=14-28 [Chain A name]=CREB-binding protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q92793 [Chain A UniProt boundaries]=1077-1197 [Chain A UniProt coverage]=5% [Chain A UniRef90 accession]=UniRef90_Q92793 [Chain A UniRef90 boundaries]=1078-1197 [Related structures]=4n3w [Entry] [Accession]=DI1000021 [Disorder status]=Confirmed [Kd]=5.53E-05 [Name]=Daxx bound to SUMO [Source organism]=Homo sapiens [PDB ID]=2kqs [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SUMO [Type chain B]=Disordered [Evidence chain B]=The 721-740 region described in IDEAL entry IID00398 covers 91% of the sequence present in the structure. The protein region involved in the interaction contains two known functional linear motifs (LIG_SUMO_SIM_anti_2 and LIG_SUMO_SIM_par_1). [Type chain A]=Ordered [Evidence chain A]=The SUMO domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF11976). A solved monomeric structure of the domain is represented by PDB ID 1a5r. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Death domain-associated protein 6 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9UER7 [Chain B UniProt boundaries]=719-740 [Chain B UniProt coverage]=3% [Chain B UniRef90 accession]=UniRef90_Q9UER7 [Chain B UniRef90 boundaries]=721-740 [Chain A name]=Small ubiquitin-related modifier 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63165 [Chain A UniProt boundaries]=1-97 [Chain A UniProt coverage]=96% [Chain A UniRef90 accession]=UniRef90_P63165 [Chain A UniRef90 boundaries]=1-97 [Entry] [Accession]=DI1000022 [Disorder status]=Confirmed [Kd]=9.00E-07 (PMID:19624289) [Name]=CHD4-PHD2 in complex with histone H3.1 peptide [Source organism]=Homo sapiens [PDB ID]=2l75 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=The 1-60 region described in IDEAL entry IID00062 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 1mm2. [Modified residues chain B]=N-trimethyllysine#K#152 [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Histone H3.1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68431 [Chain B UniProt boundaries]=2-15 [Chain B UniProt coverage]=10.3% [Chain B UniRef90 accession]=UniRef90_P68431 [Chain B UniRef90 boundaries]=2-14 [Chain A name]=Chromodomain-helicase-DNA-binding protein 4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q14839 [Chain A UniProt boundaries]=441-501 [Chain A UniProt coverage]=3.2% [Chain A UniRef90 accession]=UniRef90_Q14839 [Chain A UniRef90 boundaries]=446-501 [Entry] [Accession]=DI1100001 [Disorder status]=Confirmed [Kd]=2.44E-07 [Name]=RelA-TAD/CBP-TAZ1 complex [Source organism]=Mus musculus [PDB ID]=2lww [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=TAZ type 1 zinc finger [Type chain B]=Disordered [Evidence chain B]=The 428-551 region described in DisProt entry DP00085 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains two ZXXZZ motif and a ZZXXZXXZ sequence (Z is a bulky hydrophobic residue: Leu, Val or Phe), which extensively interact with the hydrophobic pockets of TAZ1. (PMID:24019758) [Type chain A]=Ordered [Evidence chain A]=The TAZ zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02135). A solved monomeric structure of the domain is represented by PDB ID 1u2n. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Nuclear transcription factor RelA [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q548Y4 [Chain B UniProt boundaries]=421-490 [Chain B UniProt coverage]=12.8% [Chain B UniRef90 accession]=UniRef90_Q04206 [Chain B UniRef90 boundaries]=429-491 [Chain A name]=CREB-binding protein [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P45481 [Chain A UniProt boundaries]=340-439 [Chain A UniProt coverage]=4.1% [Chain A UniRef90 accession]=UniRef90_Q92793 [Chain A UniRef90 boundaries]=341-440 [Entry] [Accession]=DI1010008 [Disorder status]=Confirmed [Kd]=1.40E-06 (PMID:14705930) [Name]=MAD1-Sin3B Interaction [Source organism]=Homo sapiens / Mus musculus [PDB ID]=1e91 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PAH [Type chain B]=Disordered [Evidence chain B]=The 8-20 region described in IDEAL entry IID00165 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_Sin3_1). [Type chain A]=Ordered [Evidence chain A]=The PAH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02671). A solved monomeric structure of the domain is represented by PDB ID 2f05. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Max dimerization protein 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q05195 [Chain B UniProt boundaries]=8-20 [Chain B UniProt coverage]=5.9% [Chain B UniRef90 accession]=UniRef90_Q05195 [Chain B UniRef90 boundaries]=8-20 [Chain A name]=Paired amphipathic helix protein Sin3b [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q62141 [Chain A UniProt boundaries]=148-232 [Chain A UniProt coverage]=7.7% [Chain A UniRef90 accession]=UniRef90_Q62141 [Chain A UniRef90 boundaries]=148-232 [Related structures]=1pd7 [Entry] [Accession]=DI1100002 [Disorder status]=Confirmed [Kd]=1.40E-06 (PMID:14705930) [Name]=BCL-XL in complex with BAD [Source organism]=Mus musculus [PDB ID]=2bzw [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.3 [Domain]=Bcl-2 homology [Type chain B]=Disordered [Evidence chain B]=The 1-204 region described in DisProt entry DP00563 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=Bcl-2 homology (BH) domains, such as the one involved in the interaction, are known to adopt a stable structure in isolation (see Pfam domain PF00452). A solved monomeric structure of the domain is represented by PDB ID 1pq0. [Modified residues chain A]=N(6)-acetyllysine#K#7 [Chain B name]=Bcl2 antagonist of cell death [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q61337 [Chain B UniProt boundaries]=137-163 [Chain B UniProt coverage]=13.2% [Chain B UniRef90 accession]=UniRef90_Q61337 [Chain B UniRef90 boundaries]=137-163 [Chain A name]=Bcl-2-like protein 1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q64373 [Chain A UniProt boundaries]=1-211 [Chain A UniProt coverage]=90.6% [Chain A UniRef90 accession]=UniRef90_Q07817 [Chain A UniRef90 boundaries]=1-211 [Entry] [Accession]=DI1000023 [Disorder status]=Confirmed [Kd]=1.40E-06 (PMID:14705930) [Name]=HIF-1alpha CTAD/p300 CH1 Complex [Source organism]=Homo sapiens [PDB ID]=1l3e [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=TAZ type 1 zinc finger [Type chain A]=Disordered [Evidence chain A]=The 776-826 region described in DisProt entry DP00262 and the 775-826 region described in IDEAL entry IID00085 cover 100% of the sequence present in the structure. [Type chain B]=Ordered [Evidence chain B]=The TAZ zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02135). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1f81. [Chain A name]=Hypoxia-inducible factor 1-alpha [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q16665 [Chain A UniProt boundaries]=785-826 [Chain A UniProt coverage]=5.1% [Chain A UniRef90 accession]=UniRef90_Q16665 [Chain A UniRef90 boundaries]=786-826 [Chain B name]=Histone acetyltransferase p300 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q09472 [Chain B UniProt boundaries]=323-423 [Chain B UniProt coverage]=4.2% [Chain B UniRef90 accession]=UniRef90_Q09472 [Chain B UniRef90 boundaries]=323-423 [Entry] [Accession]=DI1010009 [Disorder status]=Confirmed [Kd]=2.70E-06 [Name]=PHD domain from the human BPTF in complex with H3(1-15)K4me3 peptide [Source organism]=Zygosaccharomyces bailii / Homo sapiens [PDB ID]=2fuu [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=The 1-39 region described in IDEAL entry IID50143 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2e6s. [Modified residues chain B]=N-trimethyllysine#K#4 [Chain B name]=Histone H3 [Chain B source organism]=Zygosaccharomyces bailii [Chain B UniProt accession]=P61836 [Chain B UniProt boundaries]=2-16 [Chain B UniProt coverage]=11% [Chain B UniRef90 accession]=UniRef90_Q757N1 [Chain B UniRef90 boundaries]=2-16 [Chain A name]=Nucleosome-remodeling factor subunit BPTF [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q12830 [Chain A UniProt boundaries]=2865-2921 [Chain A UniProt coverage]=1.9% [Chain A UniRef90 accession]=UniRef90_Q12830 [Chain A UniRef90 boundaries]=2865-2921 [Related structures]=2f6j [Entry] [Accession]=DI1010010 [Disorder status]=Confirmed [Kd]=1.00E-08 (PMID:14594809) [Name]=HIF-1alpha/CBP complex [Source organism]=Homo sapiens / Mus musculus [PDB ID]=1l8c [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=TAZ type 1 zinc finger [Type chain B]=Disordered [Evidence chain B]=The 776-826 region described in DisProt entry DP00262 and the 775-826 region described in IDEAL entry IID00085 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a four residue motif LPQL, which binds TAZ1 (PMID:14594809). [Type chain A]=Ordered [Evidence chain A]=The TAZ zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02135). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1u2n. [Chain B name]=Hypoxia-inducible factor 1-alpha [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q16665 [Chain B UniProt boundaries]=776-826 [Chain B UniProt coverage]=6.2% [Chain B UniRef90 accession]=UniRef90_Q16665 [Chain B UniRef90 boundaries]=776-826 [Chain A name]=CREB-binding protein [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P45481 [Chain A UniProt boundaries]=345-439 [Chain A UniProt coverage]=3.9% [Chain A UniRef90 accession]=UniRef90_Q92793 [Chain A UniRef90 boundaries]=346-440 [Entry] [Accession]=DI1000024 [Disorder status]=Confirmed [Kd]=2.20E-06 [Name]=UHRF1 in complex with unmodified H3.1t N-terminal tail [Source organism]=Homo sapiens [PDB ID]=3t6r [PDB chain IDs]=D:B [PDB note]=Chain A was removed as chains B and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.95 [Domain]=PHD zinc finger [Type chain D]=Disordered [Evidence chain D]=The 1-38 region described in IDEAL entry IID00086 covers 100% of the sequence present in the structure. [Type chain B]=Ordered [Evidence chain B]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 2lgl. [Chain D name]=Histone H3.1t [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=Q16695 [Chain D UniProt boundaries]=2-8 [Chain D UniProt coverage]=5.1% [Chain D UniRef90 accession]=UniRef90_Q16695 [Chain D UniRef90 boundaries]=2-8 [Chain B name]=E3 ubiquitin-protein ligase UHRF1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q96T88 [Chain B UniProt boundaries]=293-364 [Chain B UniProt coverage]=9.1% [Chain B UniRef90 accession]=UniRef90_Q96T88 [Chain B UniRef90 boundaries]=299-364 [Entry] [Accession]=DI1010011 [Disorder status]=Confirmed [Kd]=1.05E-03 [Name]=Histone H3 tail bound to histone acetyltransferase PCAF [Source organism]=Saccharomyces cerevisiae / Homo sapiens [PDB ID]=2rnw [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Bromodomain [Type chain B]=Disordered [Evidence chain B]=The 1-39 region described in IDEAL entry IID50143 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 1n72. [Modified residues chain B]=N(6)-acetyllysine#K#9 [Chain B name]=Histone H3 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P61830 [Chain B UniProt boundaries]=2-16 [Chain B UniProt coverage]=11% [Chain B UniRef90 accession]=UniRef90_Q757N1 [Chain B UniRef90 boundaries]=2-16 [Chain A name]=Histone acetyltransferase KAT2B [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q92831 [Chain A UniProt boundaries]=715-832 [Chain A UniProt coverage]=14.2% [Chain A UniRef90 accession]=UniRef90_Q92831 [Chain A UniRef90 boundaries]=715-832 [Entry] [Accession]=DI1010012 [Disorder status]=Confirmed [Kd]=3.30E-05 [Name]=Histone H3 tail bound to PHD finger protein 21A [Source organism]=Zygosaccharomyces bailii / Homo sapiens [PDB ID]=2puy [PDB chain IDs]=E:B [PDB note]=Chain A was removed as chains B and E represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.43 [Domain]=PHD zinc finger [Type chain E]=Disordered [Evidence chain E]=The 1-39 region described in IDEAL entry IID50143 covers 100% of the sequence present in the structure. [Type chain B]=Ordered [Evidence chain B]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 2yql. [Modified residues chain B]=N(6)-acetyllysine#K#9 [Chain E name]=Histone H3 [Chain E source organism]=Zygosaccharomyces bailii [Chain E UniProt accession]=P61836 [Chain E UniProt boundaries]=2-11 [Chain E UniProt coverage]=7.4% [Chain E UniRef90 accession]=UniRef90_Q757N1 [Chain E UniRef90 boundaries]=2-11 [Chain B name]=PHD finger protein 21A [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q96BD5 [Chain B UniProt boundaries]=484-543 [Chain B UniProt coverage]=8.8% [Chain B UniRef90 accession]=UniRef90_Q96BD5 [Chain B UniRef90 boundaries]=486-543 [Entry] [Accession]=DI1010013 [Disorder status]=Confirmed [Kd]=1.30E-08 [Name]=CBP TAZ1/CITED2 complex [Source organism]=Homo sapiens / Rattus norvegicus [PDB ID]=1r8u [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=TAZ type 1 zinc finger [Type chain A]=Disordered [Evidence chain A]=The 220-269 region described in DisProt entry DP00356 and IDEAL entry IID00179 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a four residue motif LP(E/Q)L, which binds TAZ1 (PMID:14594809). [Type chain B]=Ordered [Evidence chain B]=The TAZ zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02135). A solved monomeric structure of a close homologue is represented by PDB ID 1u2n. [Modified residues chain B]=N(6)-acetyllysine#K#9 [Chain A name]=Cbp/p300-interacting transactivator 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q99967 [Chain A UniProt boundaries]=220-269 [Chain A UniProt coverage]=18.5% [Chain A UniRef90 accession]=UniRef90_O35740 [Chain A UniRef90 boundaries]=219-268 [Chain B name]=CREB-binding protein [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=Q6JHU9 [Chain B UniProt boundaries]=340-439 [Chain B UniProt coverage]=4.1% [Chain B UniRef90 accession]=UniRef90_Q92793 [Chain B UniRef90 boundaries]=341-440 [Entry] [Accession]=DI1000025 [Disorder status]=Confirmed [Kd]=1.30E-08 [Name]=PHF2 PHD domain complexed with H3K4Me3 peptide [Source organism]=Homo sapiens [PDB ID]=3kqi [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.78 [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=The 1-60 region described in IDEAL entry IID00062 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2e6s. [Modified residues chain B]=N-trimethyllysine#K#4 [Chain B name]=Histone H3.1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68431 [Chain B UniProt boundaries]=2-13 [Chain B UniProt coverage]=8.8% [Chain B UniRef90 accession]=UniRef90_P68431 [Chain B UniRef90 boundaries]=2-13 [Chain A name]=Lysine-specific demethylase PHF2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O75151 [Chain A UniProt boundaries]=1-70 [Chain A UniProt coverage]=6.4% [Chain A UniRef90 accession]=UniRef90_O75151 [Chain A UniRef90 boundaries]=1-70 [Entry] [Accession]=DI1010014 [Disorder status]=Confirmed [Kd]=6.00E-07 [Name]=Xenopus laevis MDM2 bound to the p53 transactivation domain [Source organism]=Homo sapiens / Xenopus laevis [PDB ID]=1ycq [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=SWIB [Type chain B]=Disordered [Evidence chain B]=The 1-73 region described in DisProt entry DP00086 and the 1-96 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (DEG_MDM2_SWIB_1) and a known modification site (MOD_CK1_1). [Type chain A]=Ordered [Evidence chain A]=The SWIB domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02201). A solved monomeric structure of the domain is represented by PDB ID 1ttv. [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=13-29 [Chain B UniProt coverage]=4.3% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=13-29 [Chain A name]=E3 ubiquitin-protein ligase Mdm2 [Chain A source organism]=Xenopus laevis [Chain A UniProt accession]=P56273 [Chain A UniProt boundaries]=13-119 [Chain A UniProt coverage]=22.6% [Chain A UniRef90 accession]=UniRef90_P56273 [Chain A UniRef90 boundaries]=13-119 [Entry] [Accession]=DI1100003 [Disorder status]=Confirmed [Kd]=2.19E-05 [Name]=Brdt bromodomain bound to a diacetylated histone H4 peptide [Source organism]=Mus musculus [PDB ID]=2wp2 [PDB chain IDs]=P:A [PDB note]=Chains B and Q were removed as chains A and P represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.37 [Domain]=Bromodomain [Type chain P]=Disordered [Evidence chain P]=The 1-28 region described in IDEAL entry IID00058 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1n72. [Modified residues chain P]=N(6)-acetyllysine#K#5|N(6)-acetyllysine#K#8 [Chain P name]=Histone H4 [Chain P source organism]=Mus musculus [Chain P UniProt accession]=P62806 [Chain P UniProt boundaries]=2-21 [Chain P UniProt coverage]=19.4% [Chain P UniRef90 accession]=UniRef90_P62805 [Chain P UniRef90 boundaries]=2-21 [Chain A name]=Bromodomain testis-specific protein [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q91Y44 [Chain A UniProt boundaries]=17-136 [Chain A UniProt coverage]=12.6% [Chain A UniRef90 accession]=UniRef90_Q91Y44 [Chain A UniRef90 boundaries]=17-136 [Entry] [Accession]=DI1020004 [Disorder status]=Inferred from motif [Kd]=3.70E-07 [Name]=Nck2 SH2-domain in complex with a dodecaphosphopeptide from Tir [Source organism]=Escherichia coli O127:H6 / Homo sapiens [PDB ID]=2cia [PDB chain IDs]=L:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.45 [Domain]=SH2 [Type chain L]=Disordered [Evidence chain L]=The protein region involved in the interaction contains a known functional SH2-domain binding linear motif (PMID:16636066). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2ci8. [Modified residues chain L]=phosphotyrosine#Y#474 [Chain L name]=Translocated intimin receptor Tir [Chain L source organism]=Escherichia coli O127:H6 [Chain L UniProt accession]=B7UM99 [Chain L UniProt boundaries]=471-481 [Chain L UniProt coverage]=2% [Chain L UniRef90 accession]=UniRef90_B7UM99 [Chain L UniRef90 boundaries]=472-481 [Chain A name]=Cytoplasmic protein NCK2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O43639 [Chain A UniProt boundaries]=279-380 [Chain A UniProt coverage]=26.8% [Chain A UniRef90 accession]=UniRef90_O43639 [Chain A UniRef90 boundaries]=282-380 [Entry] [Accession]=DI1000026 [Disorder status]=Confirmed [Kd]=1.80E-06 [Name]=MORC3 in complex with the amino terminus of histone H3.3 [Source organism]=Homo sapiens [PDB ID]=4qq4 [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.75 [Domain]=CW-type zinc finger [Type chain C]=Disordered [Evidence chain C]=The 1-45 region described in IDEAL entry IID00239 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The CW-type zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF07496). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2e61. [Modified residues chain C]=N-trimethyllysine#K#4 [Chain C name]=Histone H3.3 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P84243 [Chain C UniProt boundaries]=2-17 [Chain C UniProt coverage]=11.8% [Chain C UniRef90 accession]=UniRef90_P84243 [Chain C UniRef90 boundaries]=2-16 [Chain A name]=MORC family CW-type zinc finger protein 3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q14149 [Chain A UniProt boundaries]=399-460 [Chain A UniProt coverage]=6.6% [Chain A UniRef90 accession]=UniRef90_Q14149 [Chain A UniRef90 boundaries]=400-460 [Entry] [Accession]=DI1010015 [Disorder status]=Confirmed [Kd]=1.90E-07 [Name]=C-terminal beta-catenin bound to TIP-1 [Source organism]=Homo sapiens / Mus musculus [PDB ID]=3diw [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=PDZ [Type chain C]=Disordered [Evidence chain C]=The 692-781 region described in IDEAL entry IID00039 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_1). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 2vz5. [Chain C name]=Catenin beta-1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P35222 [Chain C UniProt boundaries]=772-781 [Chain C UniProt coverage]=1.3% [Chain C UniRef90 accession]=UniRef90_Q02248 [Chain C UniRef90 boundaries]=772-781 [Chain A name]=Tax1-binding protein 3 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q9DBG9 [Chain A UniProt boundaries]=1-124 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q9DBG9 [Chain A UniRef90 boundaries]=1-124 [Entry] [Accession]=DI1100004 [Disorder status]=Confirmed [Kd]=3.00E-06 (PMID:21621319) [Name]=Intermediate chain peptide bound to dynein light chain 1 [Source organism]=Drosophila melanogaster [PDB ID]=2p2t [PDB chain IDs]=C:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=3.00 [Domain]=Dynein light chain [Type chain C]=Disordered [Evidence chain C]=The 109-135 region described in DisProt entry DP00605 and the 84-143 region described in IDEAL entry IID50052 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_Dynein_DLC8_1). [Type chain A]=Ordered [Evidence chain A]=The dynein light chain domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01221). A solved monomeric structure of the domain is represented by PDB ID 1rhw. [Chain C name]=Cytoplasmic dynein 1 intermediate chain [Chain C source organism]=Drosophila melanogaster [Chain C UniProt accession]=Q24246 [Chain C UniProt boundaries]=123-138 [Chain C UniProt coverage]=2.4% [Chain C UniRef90 accession]=UniRef90_Q24246 [Chain C UniRef90 boundaries]=123-138 [Chain A name]=Dynein light chain 1, cytoplasmic [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=Q24117 [Chain A UniProt boundaries]=1-89 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q24117 [Chain A UniRef90 boundaries]=1-89 [Entry] [Accession]=DI1000027 [Disorder status]=Confirmed [Kd]=2.20E-07 [Name]=Intracellular domain of human APP in complex with Fe65-PTB2 [Source organism]=Homo sapiens [PDB ID]=3dxc [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=PID [Type chain B]=Disordered [Evidence chain B]=The 729-770 region described in IDEAL entry IID00294 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a NPXY PTB-binding motif (PMID:18833287). [Type chain A]=Ordered [Evidence chain A]=The PID domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00640). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4dbb. [Chain B name]=Amyloid beta A4 protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P05067 [Chain B UniProt boundaries]=736-770 [Chain B UniProt coverage]=4.5% [Chain B UniRef90 accession]=UniRef90_P05067 [Chain B UniRef90 boundaries]=738-770 [Chain A name]=Amyloid beta A4 precursor protein-binding family B member 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O00213 [Chain A UniProt boundaries]=534-673 [Chain A UniProt coverage]=19.7% [Chain A UniRef90 accession]=UniRef90_O00213 [Chain A UniRef90 boundaries]=534-667 [Related structures]=3dxd,3dxe [Entry] [Accession]=DI1000028 [Disorder status]=Confirmed [Kd]=2.20E-07 [Name]=CD4 endocytosis motif bound to the FAT domain of the focal adhesion kinase [Source organism]=Homo sapiens [PDB ID]=3b71 [PDB chain IDs]=D:A [PDB note]=Chains B, C, E and F were removed as chains A and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.82 [Domain]=Focal adhesion targeting region [Type chain D]=Disordered [Evidence chain D]=The 398-458 region described in DisProt entry DP00123 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (TRG_LysEnd_APsAcLL_1). [Type chain A]=Ordered [Evidence chain A]=The Focal adhesion targeting region domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03623). A solved monomeric structure of the domain from a closely homologous protein is represented by PDB ID 1qvx. [Chain D name]=T-cell surface glycoprotein CD4 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P01730 [Chain D UniProt boundaries]=428-450 [Chain D UniProt coverage]=5% [Chain D UniRef90 accession]=UniRef90_P01730 [Chain D UniRef90 boundaries]=428-450 [Chain A name]=Focal adhesion kinase 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q05397 [Chain A UniProt boundaries]=891-1052 [Chain A UniProt coverage]=15.4% [Chain A UniRef90 accession]=UniRef90_Q05397 [Chain A UniRef90 boundaries]=891-1052 [Entry] [Accession]=DI1020005 [Disorder status]=Confirmed [Kd]=2.20E-07 [Name]=CFTR Associated Ligand bound to HPV16 E6 oncoprotein C-terminal peptide [Source organism]=Human papillomavirus type 16 / Homo sapiens [PDB ID]=4jop [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=PDZ [Type chain C]=Disordered [Evidence chain C]=The 151-158 region described in IDEAL entry IID90005 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_1). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 2dc2. [Chain C name]=Protein E6 [Chain C source organism]=Human papillomavirus type 16 [Chain C UniProt accession]=P03126 [Chain C UniProt boundaries]=152-158 [Chain C UniProt coverage]=4.4% [Chain C UniRef90 accession]=UniRef90_P03126 [Chain C UniRef90 boundaries]=152-158 [Chain A name]=Golgi-associated PDZ and coiled-coil motif-containing protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9HD26 [Chain A UniProt boundaries]=284-370 [Chain A UniProt coverage]=18.8% [Chain A UniRef90 accession]=UniRef90_Q9HD26 [Chain A UniRef90 boundaries]=284-370 [Entry] [Accession]=DI1000029 [Disorder status]=Confirmed [Kd]=4.00E-07 [Name]=Human MDM2 bound to the p53 transactivation domain [Source organism]=Homo sapiens [PDB ID]=4hfz [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.69 [Domain]=SWIB [Type chain B]=Disordered [Evidence chain B]=The 1-73 region described in DisProt entry DP00086 and the 1-96 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (DEG_MDM2_SWIB_1) and a known modification site (MOD_CK1_1). [Type chain A]=Ordered [Evidence chain A]=The SWIB domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02201). A solved monomeric structure of the domain is represented by PDB ID 2lzg. [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=15-29 [Chain B UniProt coverage]=3.8% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=15-29 [Chain A name]=E3 ubiquitin-protein ligase Mdm2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q00987 [Chain A UniProt boundaries]=17-125 [Chain A UniProt coverage]=22.2% [Chain A UniRef90 accession]=UniRef90_Q00987 [Chain A UniRef90 boundaries]=17-125 [Related structures]=1ycr [Entry] [Accession]=DI1010016 [Disorder status]=Confirmed [Kd]=4.00E-07 [Name]=Danio rerio MDM4 bound to the p53 transactivation domain [Source organism]=Homo sapiens / Danio rerio [PDB ID]=3dac [PDB chain IDs]=B:A [PDB note]=Chains M and P were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=SWIB [Type chain B]=Disordered [Evidence chain B]=The 1-73 region described in DisProt entry DP00086 and the 1-96 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (DEG_MDM2_SWIB_1) and a known modification site (MOD_GSK3_1). [Type chain A]=Ordered [Evidence chain A]=The SWIB domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02201). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4hg7. [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=17-37 [Chain B UniProt coverage]=5.3% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=17-37 [Chain A name]=Protein Mdm4 [Chain A source organism]=Danio rerio [Chain A UniProt accession]=Q7ZUW7 [Chain A UniProt boundaries]=14-129 [Chain A UniProt coverage]=23.4% [Chain A UniRef90 accession]=UniRef90_Q7ZUW7 [Chain A UniRef90 boundaries]=14-129 [Related structures]=2z5s,2z5t [Entry] [Accession]=DI1000030 [Disorder status]=Confirmed [Kd]=9.90E-05 [Name]=Nucleosome-remodeling factor subunit BPTF bound to a H4 histone tail peptide (H4K16ac) [Source organism]=Homo sapiens [PDB ID]=3qzs [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=Bromodomain [Type chain C]=Disordered [Evidence chain C]=The 1-28 region described in IDEAL entry IID00058 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 3uv2. [Modified residues chain C]=N(6)-acetyllysine#K#16 [Chain C name]=Histone H4 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P62805 [Chain C UniProt boundaries]=13-22 [Chain C UniProt coverage]=9.7% [Chain C UniRef90 accession]=UniRef90_P62805 [Chain C UniRef90 boundaries]=13-22 [Chain A name]=Nucleosome-remodeling factor subunit BPTF [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q12830 [Chain A UniProt boundaries]=2919-3033 [Chain A UniProt coverage]=3.8% [Chain A UniRef90 accession]=UniRef90_Q12830 [Chain A UniRef90 boundaries]=2923-3033 [Related structures]=3qzt [Entry] [Accession]=DI1000031 [Disorder status]=Confirmed [Kd]=9.90E-05 [Name]=Human MDM4 bound to the p53 transactivation domain [Source organism]=Homo sapiens [PDB ID]=3dab [PDB chain IDs]=B:A [PDB note]=Chains C, D, E, F, G and H were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=SWIB [Type chain B]=Disordered [Evidence chain B]=The 1-73 region described in DisProt entry DP00086 and the 1-96 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (DEG_MDM2_SWIB_1) and a known modification site (MOD_CK1_1). [Type chain A]=Ordered [Evidence chain A]=The SWIB domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02201). A solved monomeric structure of the domain represented by PDB ID 3lbj. [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=15-29 [Chain B UniProt coverage]=3.8% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=15-29 [Chain A name]=Protein Mdm4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O15151 [Chain A UniProt boundaries]=22-111 [Chain A UniProt coverage]=18.4% [Chain A UniRef90 accession]=UniRef90_O15151 [Chain A UniRef90 boundaries]=23-111 [Related structures]=2mwy [Entry] [Accession]=DI1020006 [Disorder status]=Confirmed [Kd]=9.90E-05 [Name]=SIVmac239 Nef in complex with TCR zeta ITAM 1 polypeptide [Source organism]=Homo sapiens / Simian immunodeficiency virus [PDB ID]=3ik5 [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.05 [Domain]=Nef [Type chain B]=Disordered [Evidence chain B]=The 28-164 region described in DisProt entry DP00200 and the 78-93 region described in the IDEAL entry IID00544 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_TYR_ITAM). [Type chain A]=Ordered [Evidence chain A]=The Nef domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00469). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2nef. [Chain B name]=T-cell surface glycoprotein CD3 zeta chain [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P20963 [Chain B UniProt boundaries]=63-80 [Chain B UniProt coverage]=11% [Chain B UniRef90 accession]=UniRef90_P20963 [Chain B UniRef90 boundaries]=63-80 [Chain A name]=Protein Nef [Chain A source organism]=Simian immunodeficiency virus [Chain A UniProt accession]=Q5QGG3 [Chain A UniProt boundaries]=93-235 [Chain A UniProt coverage]=54.4% [Chain A UniRef90 accession]=UniRef90_P11262 [Chain A UniRef90 boundaries]=97-235 [Related structures]=3ioz [Entry] [Accession]=DI2000001 [Disorder status]=Confirmed [Kd]=9.90E-05 [Name]=Bromodomain of human BRPF1 in complex with histone H4K5acK8ac peptide [Source organism]=Homo sapiens [PDB ID]=5ffw [PDB chain IDs]=C:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.50 [Domain]=Bromodomain [Type chain C]=Disordered [Evidence chain C]=The 1-28 region described in IDEAL entry IID00058 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 4lc2. [Type chain B]=Ordered [Evidence chain B]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 4lc2. [Modified residues chain C]=N(6)-acetyllysine#K#5|N(6)-acetyllysine#K#8 [Chain C name]=Histone H4 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q0VAS5 [Chain C UniProt boundaries]=2-11 [Chain C UniProt coverage]=9.7% [Chain C UniRef90 accession]=UniRef90_P02309 [Chain C UniRef90 boundaries]=2-11 [Chain A name]=Peregrin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P55201 [Chain A UniProt boundaries]=625-740 [Chain A UniProt coverage]=9.6% [Chain A UniRef90 accession]=UniRef90_P55201 [Chain A UniRef90 boundaries]=625-740 [Chain B name]=Peregrin [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P55201 [Chain B UniProt boundaries]=625-740 [Chain B UniProt coverage]=9.6% [Chain B UniRef90 accession]=UniRef90_P55201 [Chain B UniRef90 boundaries]=625-740 [Entry] [Accession]=DI2010001 [Disorder status]=Confirmed [Kd]=1.68E-05 [Name]=Domain-swapped ZO-1 PDZ2 in complex with the Cx43 peptide [Source organism]=Rattus norvegicus / Homo sapiens [PDB ID]=3cyy [PDB chain IDs]=C:AB [PDB note]=Chain D was removed as chains A, B and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=PDZ [Type chain C]=Disordered [Evidence chain C]=The 346-382 region described in DisProt entry DP00278 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The ordered partner is a domain-swapped PDZ dimer. PDZ domains are known to adopt a stable structure in isolation, even in their monomeric form (see Pfam domain PF00595). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2kpk. [Type chain B]=Ordered [Evidence chain B]=The ordered partner is a domain-swapped PDZ dimer. PDZ domains are known to adopt a stable structure in isolation, even in their monomeric form (see Pfam domain PF00595). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2kpk. [Chain C name]=Gap junction alpha-1 protein [Chain C source organism]=Rattus norvegicus [Chain C UniProt accession]=P08050 [Chain C UniProt boundaries]=374-382 [Chain C UniProt coverage]=2.4% [Chain C UniRef90 accession]=UniRef90_P17302 [Chain C UniRef90 boundaries]=374-382 [Chain A name]=Tight junction protein ZO-1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q07157 [Chain A UniProt boundaries]=182-273 [Chain A UniProt coverage]=5.3% [Chain A UniRef90 accession]=UniRef90_Q07157 [Chain A UniRef90 boundaries]=182-273 [Chain B name]=Tight junction protein ZO-1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q07157 [Chain B UniProt boundaries]=182-273 [Chain B UniProt coverage]=5.3% [Chain B UniRef90 accession]=UniRef90_Q07157 [Chain B UniRef90 boundaries]=182-273 [Entry] [Accession]=DI1010017 [Disorder status]=Confirmed [Kd]=4.93E-05 [Name]=Rhino chromodomain in complex with H3.1 histone tail peptide [Source organism]=Homo sapiens / Drosophila melanogaster [PDB ID]=4u68 [PDB chain IDs]=D:A [PDB note]=Chains B, C, E and F were removed as chains A and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=Chromodomain [Type chain D]=Disordered [Evidence chain D]=The 1-60 region described in IDEAL entry IID00062 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The chromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00385). A solved monomeric structure of the domain represented by PDB ID 4quc. [Modified residues chain D]=N-trimethyllysine#K#9 [Chain D name]=Histone H3.1 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P68431 [Chain D UniProt boundaries]=5-15 [Chain D UniProt coverage]=8.1% [Chain D UniRef90 accession]=UniRef90_P68431 [Chain D UniRef90 boundaries]=5-15 [Chain A name]=RE36324p [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=Q7JXA8 [Chain A UniProt boundaries]=16-90 [Chain A UniProt coverage]=17.9% [Chain A UniRef90 accession]=UniRef90_Q7JXA8 [Chain A UniRef90 boundaries]=17-84 [Entry] [Accession]=DI1000032 [Disorder status]=Confirmed [Kd]=3.48E-05 [Name]=Bub1 TPR domain in complex with the KI motif of Knl1 [Source organism]=Homo sapiens [PDB ID]=4a1g [PDB chain IDs]=E:A [PDB note]=Chains B, C, D, F, G and H were removed as chains A and E represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=Tetratricopeptide [Type chain E]=Disordered [Evidence chain E]=The 176-201 region described in IDEAL entry IID00417 covers 74% of the sequence present in the structure. The protein region involved in the interaction contains two distinct but related KI motifs (consensus sequence: KI(D/N)XXXF(L/I)XXLK, X is nonconserved residue) (PMID:22331848). [Type chain A]=Ordered [Evidence chain A]=The BUB1 N-terminal tetratricopeptide domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF08311). A solved monomeric structure of the domain represented by PDB ID 2lah. [Chain E name]=Protein CASC5 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=Q8NG31 [Chain E UniProt boundaries]=174-226 [Chain E UniProt coverage]=2.3% [Chain E UniRef90 accession]=UniRef90_Q8NG31 [Chain E UniRef90 boundaries]=176-226 [Chain A name]=Mitotic checkpoint serine/threonine-protein kinase BUB1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O43683 [Chain A UniProt boundaries]=1-150 [Chain A UniProt coverage]=13.8% [Chain A UniRef90 accession]=UniRef90_O43683 [Chain A UniRef90 boundaries]=1-150 [Entry] [Accession]=DI1000033 [Disorder status]=Confirmed [Kd]=6.06E-06 [Name]=p53 N terminal fragment bound to RPA70N [Source organism]=Homo sapiens [PDB ID]=2b3g [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.60 [Domain]=Replication factor-A protein 1, N-terminal domain [Type chain B]=Disordered [Evidence chain B]=The 1-73 region described in DisProt entry DP00086 and the 1-96 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The replication factor-A protein 1, N-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04057). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ewi. [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=33-60 [Chain B UniProt coverage]=7.1% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=33-60 [Chain A name]=Replication protein A 70 kDa DNA-binding subunit [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P27694 [Chain A UniProt boundaries]=1-120 [Chain A UniProt coverage]=19.5% [Chain A UniRef90 accession]=UniRef90_P27694 [Chain A UniRef90 boundaries]=1-120 [Entry] [Accession]=DI1000034 [Disorder status]=Confirmed [Kd]=3.20E-07 [Name]=Amyloid beta A4 peptide bound to X11 PID domain [Source organism]=Homo sapiens [PDB ID]=1x11 [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=PID [Type chain C]=Disordered [Evidence chain C]=The 729-770 region described in IDEAL entry IID00294 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains two known functional linear motifs (LIG_PTB_Apo_2 and LIG_SH2_GRB2). [Type chain A]=Ordered [Evidence chain A]=The PID domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00640). A solved monomeric structure of the domain from a closely homologous protein is represented by PDB ID 4dbb. [Chain C name]=Amyloid beta A4 protein [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P05067 [Chain C UniProt boundaries]=754-766 [Chain C UniProt coverage]=1.7% [Chain C UniRef90 accession]=UniRef90_P05067 [Chain C UniRef90 boundaries]=754-766 [Chain A name]=Amyloid beta A4 precursor protein-binding family A member 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q02410 [Chain A UniProt boundaries]=452-623 [Chain A UniProt coverage]=20.5% [Chain A UniRef90 accession]=UniRef90_Q02410 [Chain A UniRef90 boundaries]=453-623 [Entry] [Accession]=DI1000035 [Disorder status]=Confirmed [Kd]=9.00E-08 [Name]=RNF2 E3 ligase bound to RYBP C-terminal peptide [Source organism]=Homo sapiens [PDB ID]=3ixs [PDB chain IDs]=B:A [PDB note]=Chains C, D, E, F, G, H, I, J, K and L were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=RAWUL [Type chain B]=Disordered [Evidence chain B]=The 1-228 region described in DisProt entry DP00694 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The RAWUL domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00640). A solved monomeric structure of the domain represented by PDB ID 3h8h. [Chain B name]=RING1 and YY1-binding protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q8N488 [Chain B UniProt boundaries]=143-179 [Chain B UniProt coverage]=16.2% [Chain B UniRef90 accession]=UniRef90_Q8CCI5 [Chain B UniRef90 boundaries]=144-176 [Chain A name]=E3 ubiquitin-protein ligase RING2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q99496 [Chain A UniProt boundaries]=223-333 [Chain A UniProt coverage]=33% [Chain A UniRef90 accession]=UniRef90_Q99496 [Chain A UniRef90 boundaries]=223-333 [Entry] [Accession]=DI1020007 [Disorder status]=Confirmed [Kd]=5.00E-07 [Name]=EspFu-R47 domain bound to IRTKS-SH3 domain [Source organism]=Escherichia coli O157:H7 / Homo sapiens [PDB ID]=2kxc [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH3 [Type chain B]=Disordered [Evidence chain B]=The 221-314 region described in IDEAL entry IID90008 covers 98% of the sequence present in the structure. The protein region involved in the interaction contains tandem PxxP SH3-binding motifs (PMID:21098279). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF14604). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ark. [Chain B name]=Secreted effector protein EspF(U) [Chain B source organism]=Escherichia coli O157:H7 [Chain B UniProt accession]=P0DJ89 [Chain B UniProt boundaries]=220-267 [Chain B UniProt coverage]=14.2% [Chain B UniRef90 accession]=UniRef90_P0DJ88 [Chain B UniRef90 boundaries]=221-267 [Chain A name]=Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UHR4 [Chain A UniProt boundaries]=336-402 [Chain A UniProt coverage]=13.1% [Chain A UniRef90 accession]=UniRef90_Q9UHR4 [Chain A UniRef90 boundaries]=339-402 [Related structures]=2lnh [Entry] [Accession]=DI1000036 [Disorder status]=Confirmed [Kd]=1.97E-05 [Name]=PQBP1 fragment bound to thioredoxin-like protein 4A [Source organism]=Homo sapiens [PDB ID]=4bwq [PDB chain IDs]=B:A [PDB note]=Chains C, D, E, F, G and H were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=DIM1 [Type chain B]=Disordered [Evidence chain B]=The 193-265 region described in IDEAL entry IID00187 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a YxxPxxVL linear motif (PMID:24781215). [Type chain A]=Ordered [Evidence chain A]=The DIM1 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02966). A solved monomeric structure of the domain is represented by PDB ID 1pqn. [Chain B name]=Polyglutamine-binding protein 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O60828 [Chain B UniProt boundaries]=223-265 [Chain B UniProt coverage]=16.2% [Chain B UniRef90 accession]=UniRef90_O60828 [Chain B UniRef90 boundaries]=223-265 [Chain A name]=Thioredoxin-like protein 4A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P83876 [Chain A UniProt boundaries]=1-137 [Chain A UniProt coverage]=96.5% [Chain A UniRef90 accession]=UniRef90_P83876 [Chain A UniRef90 boundaries]=3-137 [Related structures]=4bws,4cdo [Entry] [Accession]=DI1000037 [Disorder status]=Inferred from homology [Kd]=4.65E-05 [Name]=Complex of human Tuba C-terminal SH3 domain with human N-WASP proline-rich peptide [Source organism]=Homo sapiens [PDB ID]=4cc2 [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.55 [Domain]=SH3 [Type chain B]=Disordered [Evidence chain B]=The 452-484 region described in IDEAL entry IID00256 covers 100% of the sequence present in the structure in a closely homologous protein. [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00018). A solved monomeric structure of the domain is represented by PDB ID 1uhc. [Chain B name]=Neural Wiskott-Aldrich syndrome protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O00401 [Chain B UniProt boundaries]=346-357 [Chain B UniProt coverage]=2.4% [Chain B UniRef90 accession]=UniRef90_O00401 [Chain B UniRef90 boundaries]=458-469 [Chain A name]=Dynamin-binding protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q6XZF7 [Chain A UniProt boundaries]=1511-1577 [Chain A UniProt coverage]=4.2% [Chain A UniRef90 accession]=UniRef90_Q6XZF7 [Chain A UniRef90 boundaries]=1513-1577 [Related structures]=4cc7 [Entry] [Accession]=DI1000038 [Disorder status]=Confirmed [Kd]=4.65E-05 [Name]=MOZ double PHD finger interacting with unmodified histone H3.1 tail [Source organism]=Homo sapiens [PDB ID]=4lk9 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.60 [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=The 1-60 region described in IDEAL entry IID0062 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_14-3-3_CanoR_1). [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 4ljn. [Chain B name]=Histone H3.1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68431 [Chain B UniProt boundaries]=2-22 [Chain B UniProt coverage]=15.4% [Chain B UniRef90 accession]=UniRef90_P68431 [Chain B UniRef90 boundaries]=2-22 [Chain A name]=Histone acetyltransferase KAT6A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q92794 [Chain A UniProt boundaries]=188-323 [Chain A UniProt coverage]=6.8% [Chain A UniRef90 accession]=UniRef90_Q92794 [Chain A UniRef90 boundaries]=194-323 [Related structures]=3v43 [Entry] [Accession]=DI1000039 [Disorder status]=Confirmed [Kd]=1.04E-07 [Name]=Nuclear NIPP1:PP1 Holoenzyme [Source organism]=Homo sapiens [PDB ID]=3v4y [PDB chain IDs]=B:A [PDB note]=Chains C, D, E, F, G and H were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=Calcineurin-like phosphoesterase [Type chain B]=Disordered [Evidence chain B]=The interacting region of NIPP1 has been shown to be intrinsically disordered (PMID:22940584). The 144-225 region described in DisProt entry DP00937 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional nuclear localization signal (http://www.uniprot.org/uniprot/Q12972#family_and_domains). The protein region involved in the interaction contains a RVXF PP1-binding motif (PMID:22940584). [Type chain A]=Ordered [Evidence chain A]=The calcineurin-like phosphoesterase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00149). A solved monomeric structure of the domain is represented by PDB ID 4mov. [Chain B name]=Nuclear inhibitor of protein phosphatase 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q12972 [Chain B UniProt boundaries]=160-214 [Chain B UniProt coverage]=15.7% [Chain B UniRef90 accession]=UniRef90_Q12972 [Chain B UniRef90 boundaries]=160-214 [Chain A name]=Serine/threonine-protein phosphatase PP1-alpha catalytic subunit [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P62136 [Chain A UniProt boundaries]=7-299 [Chain A UniProt coverage]=88.8% [Chain A UniRef90 accession]=UniRef90_P62136 [Chain A UniRef90 boundaries]=7-299 [Entry] [Accession]=DI1000040 [Disorder status]=Confirmed [Kd]=3.10E-06 (PMID:15327768) [Name]=Beta-catenin in complex with an unphosphorylated APC fragment [Source organism]=Homo sapiens [PDB ID]=1t08 [PDB chain IDs]=C:A [PDB note]=Chain B was removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=Armadillo repeat [Type chain C]=Disordered [Evidence chain C]=The interacting region of APC has been shown to be intrinsically disordered (PMID:24130866). [Type chain A]=Ordered [Evidence chain A]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain is represented by PDB ID 2z6h. [Chain C name]=Adenomatous polyposis coli protein [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P25054 [Chain C UniProt boundaries]=1484-1498 [Chain C UniProt coverage]=0.5% [Chain C UniRef90 accession]=UniRef90_P25054 [Chain C UniRef90 boundaries]=1484-1498 [Chain A name]=Catenin beta-1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P35222 [Chain A UniProt boundaries]=146-664 [Chain A UniProt coverage]=66.5% [Chain A UniRef90 accession]=UniRef90_Q02248 [Chain A UniRef90 boundaries]=164-664 [Entry] [Accession]=DI1000041 [Disorder status]=Confirmed [Kd]=8.63E-05 (PMID:25082813) [Name]=LEDGF/p75 IBD in complex with MLL1 peptide [Source organism]=Homo sapiens [PDB ID]=2msr [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=LEDGF [Type chain A]=Disordered [Evidence chain A]=The 135-160 region described in IDEAL entry IID00379 covers 95% of the sequence present in the structure. [Type chain B]=Ordered [Evidence chain B]=The Lens epithelium-derived growth factor (LEDGF) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF11467). A solved monomeric structure of the domain is represented by PDB ID 1z9e. [Chain A name]=Histone-lysine N-methyltransferase 2A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q03164 [Chain A UniProt boundaries]=140-160 [Chain A UniProt coverage]=0.5% [Chain A UniRef90 accession]=UniRef90_Q03164 [Chain A UniRef90 boundaries]=140-160 [Chain B name]=PC4 and SFRS1-interacting protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O75475 [Chain B UniProt boundaries]=339-426 [Chain B UniProt coverage]=16.6% [Chain B UniRef90 accession]=UniRef90_O75475 [Chain B UniRef90 boundaries]=344-426 [Related structures]=2mtn,3u88 [Entry] [Accession]=DI1000042 [Disorder status]=Confirmed [Kd]=2.40E-06 (PMID:24795046) [Name]=CAPERalpha UHM bound to SF3b155 ULM5 [Source organism]=Homo sapiens [PDB ID]=4oz1 [PDB chain IDs]=C:B [PDB note]=Chain A was removed as chains B and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.74 [Domain]=RRM [Type chain C]=Disordered [Evidence chain C]=The 190-344 region described in IDEAL entry IID00190 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_ULM_U2AF65_1). [Type chain B]=Ordered [Evidence chain B]=The RRM domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of a close homologue is represented by PDB ID 2lq5. [Chain C name]=Splicing factor 3B subunit 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=O75533 [Chain C UniProt boundaries]=333-342 [Chain C UniProt coverage]=0.8% [Chain C UniRef90 accession]=UniRef90_O75533 [Chain C UniRef90 boundaries]=333-342 [Chain B name]=RNA-binding protein 39 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q14498 [Chain B UniProt boundaries]=416-530 [Chain B UniProt coverage]=21.7% [Chain B UniRef90 accession]=UniRef90_Q14498 [Chain B UniRef90 boundaries]=418-530 [Entry] [Accession]=DI1000043 [Disorder status]=Confirmed [Kd]=1.15E-05 [Name]=GABA type A receptor associated protein in complex with its binding epitope on calreticulin [Source organism]=Homo sapiens [PDB ID]=3dow [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=Atg8 [Type chain B]=Disordered [Evidence chain B]=The 1-417 region described in DisProt entry DP00333 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_LIR_Gen_1). [Type chain A]=Ordered [Evidence chain A]=The Atg8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02991). A solved monomeric structure of the domain is represented by PDB ID 1gnu. [Chain B name]=Calreticulin [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P27797 [Chain B UniProt boundaries]=195-206 [Chain B UniProt coverage]=2.9% [Chain B UniRef90 accession]=UniRef90_P27797 [Chain B UniRef90 boundaries]=195-205 [Chain A name]=Gamma-aminobutyric acid receptor-associated protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O95166 [Chain A UniProt boundaries]=1-117 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_O95166 [Chain A UniRef90 boundaries]=1-117 [Entry] [Accession]=DI1010018 [Disorder status]=Confirmed [Kd]=1.15E-05 [Name]=Human chromobox homolog 6 (Cbx6) with H3K9 peptide [Source organism]=Xenopus laevis / Homo sapiens [PDB ID]=3gv6 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.76 [Domain]=Chromodomain [Type chain B]=Disordered [Evidence chain B]=The 1-38 region described in IDEAL entry IID00086 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The chromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00385). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4quc. [Modified residues chain B]=N-trimethyllysine#K#9 [Chain B name]=Histone H3 [Chain B source organism]=Xenopus laevis [Chain B UniProt accession]=Q92133 [Chain B UniProt boundaries]=2-16 [Chain B UniProt coverage]=11% [Chain B UniRef90 accession]=UniRef90_Q16695 [Chain B UniRef90 boundaries]=2-16 [Chain A name]=Chromobox protein homolog 6 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O95503 [Chain A UniProt boundaries]=8-65 [Chain A UniProt coverage]=14.1% [Chain A UniRef90 accession]=UniRef90_O95503 [Chain A UniRef90 boundaries]=8-65 [Entry] [Accession]=DI1010019 [Disorder status]=Inferred from homology [Kd]=1.10E-04 (PMID:21047797) [Name]=Human chromobox protein Cbx7 with H3K27me3 [Source organism]=Xenopus laevis / Homo sapiens [PDB ID]=2l1b [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Chromodomain [Type chain B]=Disordered [Evidence chain B]=The corresponding region of a closely homologous protein has been shown to be disordered in the 1-38 region described in IDEAL entry IID00086 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The chromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00385). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4quc. [Modified residues chain B]=N-trimethyllysine#K#27 [Chain B name]=Histone H3 [Chain B source organism]=Xenopus laevis [Chain B UniProt accession]=Q92133 [Chain B UniProt boundaries]=20-34 [Chain B UniProt coverage]=11% [Chain B UniRef90 accession]=UniRef90_Q16695 [Chain B UniRef90 boundaries]=20-34 [Chain A name]=Chromobox protein homolog 7 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O95931 [Chain A UniProt boundaries]=7-62 [Chain A UniProt coverage]=22.3% [Chain A UniRef90 accession]=UniRef90_O95931 [Chain A UniRef90 boundaries]=7-62 [Entry] [Accession]=DI1010020 [Disorder status]=Confirmed [Kd]=1.10E-04 (PMID:21047797) [Name]=Phospholipase A2 complexed with beta-amyloid fragment (VGGVVIA) [Source organism]=Homo sapiens / Naja sagittifera [PDB ID]=3jti [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=Phospholipase A2 [Type chain B]=Disordered [Evidence chain B]=The 671-713 region described in IDEAL entry IID00294 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Phospholipase A2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00068). A solved monomeric structure of the domain is represented by PDB ID 1ln8. [Chain B name]=Amyloid beta A4 protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P05067 [Chain B UniProt boundaries]=699-706 [Chain B UniProt coverage]=1% [Chain B UniRef90 accession]=UniRef90_P05067 [Chain B UniRef90 boundaries]=699-706 [Chain A name]=Acidic phospholipase A2 3 (Fragment) [Chain A source organism]=Naja sagittifera [Chain A UniProt accession]=P60045 [Chain A UniProt boundaries]=8-126 [Chain A UniProt coverage]=94.4% [Chain A UniRef90 accession]=UniRef90_P00598 [Chain A UniRef90 boundaries]=28-145 [Entry] [Accession]=DI1010021 [Disorder status]=Confirmed [Kd]=1.10E-04 (PMID:21047797) [Name]=Phospholipase A2 complexed with beta-amyloid fragment (KGAIIGLM) [Source organism]=Homo sapiens / Naja sagittifera [PDB ID]=3gci [PDB chain IDs]=P:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.04 [Domain]=Phospholipase A2 [Type chain P]=Disordered [Evidence chain P]=The 671-713 region described in IDEAL entry IID00294 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Phospholipase A2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00068). A solved monomeric structure of the domain is represented by PDB ID 1ln8. [Chain P name]=Amyloid beta A4 protein [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=P05067 [Chain P UniProt boundaries]=707-713 [Chain P UniProt coverage]=0.9% [Chain P UniRef90 accession]=UniRef90_P05067 [Chain P UniRef90 boundaries]=707-713 [Chain A name]=Acidic phospholipase A2 3 (Fragment) [Chain A source organism]=Naja sagittifera [Chain A UniProt accession]=P60045 [Chain A UniProt boundaries]=8-126 [Chain A UniProt coverage]=94.4% [Chain A UniRef90 accession]=UniRef90_P00598 [Chain A UniRef90 boundaries]=28-145 [Entry] [Accession]=DI1120002 [Disorder status]=Inferred from homology [Kd]=1.10E-04 (PMID:21047797) [Name]=0.5b anti-HIV antibody complex with the gp120 V3 peptide [Source organism]=Human immunodeficiency virus 1 / Mus musculus [PDB ID]=1qnz [PDB chain IDs]=P:H [PDB note]=Chain L was removed as chains H and P represent the biologically relevant interaction. [PDB experimental technique]=NMR [Domain]=V-set [Type chain P]=Disordered [Evidence chain P]=The corresponding region of a closely homologous protein has been shown to be disordered in the 297-331 region described in DisProt entry DP00976 (covers 100% of the sequence present in the structure). [Type chain H]=Ordered [Evidence chain H]=The V-set domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF07686). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ah1. [Chain P name]=Envelope protein (Fragment) [Chain P source organism]=Human immunodeficiency virus 1 [Chain P UniProt accession]=Q79416 [Chain P UniProt boundaries]=9-26 [Chain P UniProt coverage]=50% [Chain P UniRef90 accession]=UniRef90_P04578 [Chain P UniRef90 boundaries]=304-321 [Chain H name]=Ig heavy chain V region 102 [Chain H source organism]=Mus musculus [Chain H UniProt accession]=P01750 [Chain H UniProt boundaries]=21-117 [Chain H UniProt coverage]=82.9% [Chain H UniRef90 accession]=UniRef90_A0A075B5V8 [Chain H UniRef90 boundaries]=1-97 [Entry] [Accession]=DI1020008 [Disorder status]=Inferred from homology [Kd]=5.00E-05 (PMID:21070952) [Name]=Tsg101 UEV domain in complex with a HIV-1 PTAP peptide [Source organism]=Human immunodeficiency virus 1 / Homo sapiens [PDB ID]=3obu [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.60 [Domain]=UEV [Type chain B]=Disordered [Evidence chain B]=The corresponding region of a closely homologous protein has been shown to be disordered in the 449-462 region described in DisProt entry DP00101 (covers 100% of the sequence present in the structure). The protein region involved in the interaction contains a known functional linear motif (LIG_PTAP_UEV_1). [Type chain A]=Ordered [Evidence chain A]=The UEV domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF05743). A solved monomeric structure of the domain is represented by PDB ID 1kpp. [Chain B name]=Gag polyprotein [Chain B source organism]=Human immunodeficiency virus 1 [Chain B UniProt accession]=Q72497 [Chain B UniProt boundaries]=453-461 [Chain B UniProt coverage]=1.8% [Chain B UniRef90 accession]=UniRef90_P04591 [Chain B UniRef90 boundaries]=453-461 [Chain A name]=Tumor susceptibility gene 101 protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q99816 [Chain A UniProt boundaries]=2-145 [Chain A UniProt coverage]=36.9% [Chain A UniRef90 accession]=UniRef90_Q99816 [Chain A UniRef90 boundaries]=2-145 [Related structures]=3obx,1m4p [Entry] [Accession]=DI1110001 [Disorder status]=Confirmed [Kd]=5.00E-05 (PMID:21070952) [Name]=N-domain Troponin C in complex with skeletal Troponin I [Source organism]=Oryctolagus cuniculus / Gallus gallus [PDB ID]=1npq [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=EF-hand [Type chain B]=Disordered [Evidence chain B]=The C-terminal region of troponin I was shown to be intrinsically disordered (PMID:21322033). [Type chain A]=Ordered [Evidence chain A]=The EF-hand domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13833). A solved monomeric structure of the domain is represented by PDB ID 1blq. [Chain B name]=Troponin I, fast skeletal muscle [Chain B source organism]=Oryctolagus cuniculus [Chain B UniProt accession]=P02643 [Chain B UniProt boundaries]=116-132 [Chain B UniProt coverage]=9.3% [Chain B UniRef90 accession]=UniRef90_P48788-2 [Chain B UniRef90 boundaries]=116-132 [Chain A name]=Troponin C, skeletal muscle [Chain A source organism]=Gallus gallus [Chain A UniProt accession]=P02588 [Chain A UniProt boundaries]=2-91 [Chain A UniProt coverage]=55.2% [Chain A UniRef90 accession]=UniRef90_P02588 [Chain A UniRef90 boundaries]=2-91 [Entry] [Accession]=DI1010022 [Disorder status]=Inferred from homology [Kd]=5.00E-05 (PMID:21070952) [Name]=G1 to S phase transition 1 in complex with Polyadenylate-binding protein 1 [Source organism]=Mus musculus / Homo sapiens [PDB ID]=2rqg [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PABP [Type chain A]=Disordered [Evidence chain A]=The corresponding region of a homologous protein has been shown to be disordered in the 106-127 region described in IDEAL entry IID00582 (covers 100% of the sequence present in the structure). [Type chain B]=Ordered [Evidence chain B]=The PABP domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00658). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1i2t. [Chain A name]=Eukaryotic peptide chain release factor GTP-binding subunit ERF3A [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q8R050 [Chain A UniProt boundaries]=64-82 [Chain A UniProt coverage]=3% [Chain A UniRef90 accession]=UniRef90_G5C143 [Chain A UniRef90 boundaries]=58-76 [Chain B name]=Polyadenylate-binding protein 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P11940 [Chain B UniProt boundaries]=541-623 [Chain B UniProt coverage]=13.1% [Chain B UniRef90 accession]=UniRef90_P11940 [Chain B UniRef90 boundaries]=541-623 [Related structures]=2rqh [Entry] [Accession]=DI1000044 [Disorder status]=Inferred from homology [Kd]=5.00E-05 (PMID:21070952) [Name]=Axin RGS-homologous domain in complex with a SAMP repeat from APC [Source organism]=Homo sapiens [PDB ID]=1emu [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=RGS [Type chain B]=Disordered [Evidence chain B]=The interacting region contains the SAMP motif (Pfam motif PF05924) that has been shown to be disordered in the 1362-1745 region of DisProt entry DP00519 and IDEAL entry IID00035. [Type chain A]=Ordered [Evidence chain A]=The Regulator of G protein signalling (RGS) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00615). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1zv4. [Chain B name]=Adenomatous polyposis coli protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P25054 [Chain B UniProt boundaries]=2034-2049 [Chain B UniProt coverage]=0.6% [Chain B UniRef90 accession]=UniRef90_P25054 [Chain B UniRef90 boundaries]=2034-2049 [Chain A name]=Axin-1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O15169 [Chain A UniProt boundaries]=80-211 [Chain A UniProt coverage]=15.3% [Chain A UniRef90 accession]=UniRef90_O15169 [Chain A UniRef90 boundaries]=80-211 [Entry] [Accession]=DI1010023 [Disorder status]=Inferred from homology [Kd]=5.00E-05 (PMID:21070952) [Name]=CITED2 transactivation domain in complex with the p300 CH1 domain [Source organism]=Mus musculus / Homo sapiens [PDB ID]=1p4q [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=TAZ type 2 zinc finger [Type chain A]=Disordered [Evidence chain A]=The corresponding region of a closely homologous protein has been shown to be disordered in the 220-269 region described in DisProt entry DP00356 and IDEAL entry IID00179 (covers 91% of the sequence present in the structure). The protein region involved in the interaction contains a LPXL motif (PMID:12736686). [Type chain B]=Ordered [Evidence chain B]=The TAZ zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02135). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1f81. [Chain A name]=Cbp/p300-interacting transactivator 2 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=O35740 [Chain A UniProt boundaries]=215-258 [Chain A UniProt coverage]=16.4% [Chain A UniRef90 accession]=UniRef90_O35740 [Chain A UniRef90 boundaries]=215-258 [Chain B name]=Histone acetyltransferase p300 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q09472 [Chain B UniProt boundaries]=323-423 [Chain B UniProt coverage]=4.2% [Chain B UniRef90 accession]=UniRef90_Q09472 [Chain B UniRef90 boundaries]=323-423 [Entry] [Accession]=DI1110002 [Disorder status]=Inferred from homology [Kd]=5.00E-05 (PMID:21070952) [Name]=Alzheimer's disease amyloid A4 protein homolog bound to the phosphotyrosine binding domain (PTB) of mouse Disabled 1 (Dab1) [Source organism]=Rattus norvegicus / Mus musculus [PDB ID]=1oqn [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=PID [Type chain C]=Disordered [Evidence chain C]=The corresponding region of a closely homologous protein has been shown to be disordered in the 729-770 region described in IDEAL entry IID00294 (covers 100% of the sequence present in the structure). The protein region involved in the interaction contains a known functional linear motif (LIG_PTB_Apo_2). [Type chain A]=Ordered [Evidence chain A]=The PID domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00640). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4dbb. [Chain C name]=Amyloid beta A4 protein [Chain C source organism]=Rattus norvegicus [Chain C UniProt accession]=P08592 [Chain C UniProt boundaries]=755-763 [Chain C UniProt coverage]=1.2% [Chain C UniRef90 accession]=UniRef90_P05067 [Chain C UniRef90 boundaries]=755-763 [Chain A name]=Disabled homolog 1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P97318 [Chain A UniProt boundaries]=25-183 [Chain A UniProt coverage]=27% [Chain A UniRef90 accession]=UniRef90_P97318 [Chain A UniRef90 boundaries]=25-183 [Entry] [Accession]=DI1100005 [Disorder status]=Inferred from homology [Kd]=5.00E-05 (PMID:21070952) [Name]=C-terminal PID Domain of Fe65L1 Complexed with the Cytoplasmic Tail of APP [Source organism]=Mus musculus [PDB ID]=2roz [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PID [Type chain A]=Disordered [Evidence chain A]=The corresponding region of a closely homologous protein has been shown to be disordered in the 729-770 region described in IDEAL entry IID00294 (covers 100% of the sequence present in the structure). The protein region involved in the interaction contains a NPXY PTB-binding motif (PMID:18650440). [Type chain B]=Ordered [Evidence chain B]=The PID domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00640). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4dbb. [Chain A name]=Amyloid beta A4 protein [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P12023 [Chain A UniProt boundaries]=739-770 [Chain A UniProt coverage]=4.2% [Chain A UniRef90 accession]=UniRef90_P05067 [Chain A UniRef90 boundaries]=739-770 [Chain B name]=Amyloid beta A4 precursor protein-binding family B member 2 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q9DBR4 [Chain B UniProt boundaries]=575-710 [Chain B UniProt coverage]=17.9% [Chain B UniRef90 accession]=UniRef90_Q92870 [Chain B UniRef90 boundaries]=580-702 [Entry] [Accession]=DI1100006 [Disorder status]=Confirmed [Kd]=4.00E-06 [Name]=Chromo domain of HP1 complexed with histone H3 tail [Source organism]=Drosophila melanogaster [PDB ID]=1kne [PDB chain IDs]=P:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=Chromodomain [Type chain P]=Disordered [Evidence chain P]=The 1-43 region described in IDEAL entry IID00088 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The chromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00385). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4quc. [Modified residues chain P]=N-trimethyllysine#K#9 [Chain P name]=Histone H3 [Chain P source organism]=Drosophila melanogaster [Chain P UniProt accession]=P02299 [Chain P UniProt boundaries]=2-17 [Chain P UniProt coverage]=11.8% [Chain P UniRef90 accession]=UniRef90_Q71DI3 [Chain P UniRef90 boundaries]=2-16 [Chain A name]=Heterochromatin protein 1 [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=P05205 [Chain A UniProt boundaries]=17-76 [Chain A UniProt coverage]=29.1% [Chain A UniRef90 accession]=UniRef90_P05205 [Chain A UniRef90 boundaries]=24-76 [Related structures]=1kna [Entry] [Accession]=DI1100007 [Disorder status]=Confirmed [Kd]=1.90E-07 [Name]=PH domain of the Tfb1 subunit from TFIIH in complex with Rad2 [Source organism]=Saccharomyces cerevisiae [PDB ID]=2lox [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PH [Type chain B]=Disordered [Evidence chain B]=The 642-690 region described in IDEAL entry IID50166 covers 94% of the sequence present in the structure. The protein region involved in the interaction contains a Tfb1PH-binding motif that consists of an aromatic residue (W or F) followed by two acidic residues and a valine residue located within a highly acidic segment (PMID:22373916). [Type chain A]=Ordered [Evidence chain A]=The PH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF08567). A solved monomeric structure of the domain is represented by PDB ID 1y5o. [Chain B name]=DNA repair protein RAD2 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P07276 [Chain B UniProt boundaries]=640-691 [Chain B UniProt coverage]=5% [Chain B UniRef90 accession]=UniRef90_P07276 [Chain B UniRef90 boundaries]=640-690 [Chain A name]=RNA polymerase II transcription factor B subunit 1 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P32776 [Chain A UniProt boundaries]=1-119 [Chain A UniProt coverage]=18.5% [Chain A UniRef90 accession]=UniRef90_P32776 [Chain A UniRef90 boundaries]=2-115 [Entry] [Accession]=DI1100008 [Disorder status]=Inferred from homology [Kd]=2.77E-04 [Name]=Vps27 amino-terminal UIM-ubiquitin complex [Source organism]=Saccharomyces cerevisiae [PDB ID]=1q0w [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Ubiquitin [Type chain A]=Disordered [Evidence chain A]=The interacting region contains the Ubiquitin interacting motif (UIM) (Pfam motif PF02809) that has been shown to be disordered in the 174-364 region of DisProt entry DP00576 and the 144-575 region of DisProt entry DP00251. [Type chain B]=Ordered [Evidence chain B]=The ubiquitin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00240). A solved monomeric structure of a close homologue is represented by PDB ID 1bt0. [Chain A name]=Vacuolar protein sorting-associated protein 27 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P40343 [Chain A UniProt boundaries]=255-278 [Chain A UniProt coverage]=3.9% [Chain A UniRef90 accession]=UniRef90_P40343 [Chain A UniRef90 boundaries]=256-278 [Chain B name]=Polyubiquitin [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P0CG63 [Chain B UniProt boundaries]=1-76 [Chain B UniProt coverage]=19.9% [Chain B UniRef90 accession]=UniRef90_P0CG63 [Chain B UniRef90 boundaries]=1-76 [Entry] [Accession]=DI1120003 [Disorder status]=Confirmed [Kd]=5.40E-07 (PMID:24675874) [Name]=Complex between the acidic transactivation domain of EBNA2 and the Tfb1/p62 subunit of TFIIH [Source organism]=Epstein-Barr virus / Saccharomyces cerevisiae [PDB ID]=2mkr [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PH [Type chain B]=Disordered [Evidence chain B]=The 431-487 region described in IDEAL entry IID90021 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains the ZXXZZ motif crucial for binding Tfb1PH and transactivation (Z is hydrophobic/aromatic) (PMID:24675874). [Type chain A]=Ordered [Evidence chain A]=The PH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF08567). A solved monomeric structure of the domain is represented by PDB ID 1y5o. [Chain B name]=Epstein-Barr nuclear antigen 2 [Chain B source organism]=Epstein-Barr virus [Chain B UniProt accession]=P12978 [Chain B UniProt boundaries]=453-465 [Chain B UniProt coverage]=2.7% [Chain B UniRef90 accession]=UniRef90_P12978 [Chain B UniRef90 boundaries]=453-465 [Chain A name]=RNA polymerase II transcription factor B subunit 1 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P32776 [Chain A UniProt boundaries]=1-115 [Chain A UniProt coverage]=17.9% [Chain A UniRef90 accession]=UniRef90_P32776 [Chain A UniRef90 boundaries]=2-115 [Entry] [Accession]=DI1100009 [Disorder status]=Confirmed [Kd]=5.00E-08 (PMID:23295669) [Name]=Complex between the PH domain of the Tfb1 subunit from TFIIH and Rad4 [Source organism]=Saccharomyces cerevisiae [PDB ID]=2m14 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PH [Type chain B]=Disordered [Evidence chain B]=The 1-125 region described in IDEAL entry IID50167 covers 100% of the sequence present in the structure. The protein region of Rad4 involved in the interaction contains an N-terminal Tfb1PH-binding motif similar to the Tfb1PH-binding motifs of Rad2 (PMID:23295669). [Type chain A]=Ordered [Evidence chain A]=The PH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF08567). A solved monomeric structure of the domain is represented by PDB ID 1y5o. [Chain B name]=DNA repair protein RAD4 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P14736 [Chain B UniProt boundaries]=74-115 [Chain B UniProt coverage]=5.6% [Chain B UniRef90 accession]=UniRef90_P14736 [Chain B UniRef90 boundaries]=75-115 [Chain A name]=RNA polymerase II transcription factor B subunit 1 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P32776 [Chain A UniProt boundaries]=1-119 [Chain A UniProt coverage]=18.5% [Chain A UniRef90 accession]=UniRef90_P32776 [Chain A UniRef90 boundaries]=2-115 [Entry] [Accession]=DI2200001 [Disorder status]=Confirmed [Kd]=5.00E-08 (PMID:23295669) [Name]=CcdB dimer in complex with the C-terminal domain of F-plasmid CcdA (E. coli) [Source organism]=Escherichia coli [PDB ID]=3hpw [PDB chain IDs]=C:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.45 [Domain]=CcdB [Type chain C]=Disordered [Evidence chain C]=The 37-72 region described in DisProt entry DP00928 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The monomers of the controller of cell division or death B protein (CcdB) form well folded monomers (PMID:14763902). [Type chain B]=Ordered [Evidence chain B]=The monomers of the controller of cell division or death B protein (CcdB) form well folded monomers (PMID:14763902). [Chain C name]=Antitoxin CcdA [Chain C source organism]=Escherichia coli [Chain C UniProt accession]=P62552 [Chain C UniProt boundaries]=37-72 [Chain C UniProt coverage]=50% [Chain C UniRef90 accession]=UniRef90_P62553 [Chain C UniRef90 boundaries]=37-72 [Chain A name]=Toxin CcdB [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=P62554 [Chain A UniProt boundaries]=1-101 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q52042 [Chain A UniRef90 boundaries]=1-101 [Chain B name]=Toxin CcdB [Chain B source organism]=Escherichia coli [Chain B UniProt accession]=P62554 [Chain B UniProt boundaries]=1-101 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_Q52042 [Chain B UniRef90 boundaries]=1-101 [Related structures]=3g7z [Entry] [Accession]=DI1110003 [Disorder status]=Confirmed [Kd]=5.00E-06 (PMID:12897054) [Name]=Polycomb chromodomain complexed with the histone H3 tail [Source organism]=Mus musculus / Drosophila melanogaster [PDB ID]=1pdq [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.76 [Domain]=Chromodomain [Type chain B]=Disordered [Evidence chain B]=The 1-45 region described in IDEAL entry IID00239 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The chromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00385). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4quc. [Modified residues chain B]=N-trimethyllysine#K#27 [Chain B name]=Histone H3.3 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=P84244 [Chain B UniProt boundaries]=16-33 [Chain B UniProt coverage]=13.2% [Chain B UniRef90 accession]=UniRef90_P84243 [Chain B UniRef90 boundaries]=16-33 [Chain A name]=Polycomb group protein Pc [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=P26017 [Chain A UniProt boundaries]=15-77 [Chain A UniProt coverage]=16.2% [Chain A UniRef90 accession]=UniRef90_P26017 [Chain A UniRef90 boundaries]=15-77 [Entry] [Accession]=DI1010024 [Disorder status]=Confirmed [Kd]=1.50E-05 (PMID:28334776) [Name]=Complex between the PH domain of the Tfb1 subunit from TFIIH and the transactivation domain 1 of p65 [Source organism]=Homo sapiens / Saccharomyces cerevisiae [PDB ID]=5urn [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PH [Type chain B]=Disordered [Evidence chain B]=The 428-551 region described in DisProt entry DP00085 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a ZXXZZ motif, Z representing hydrophobic residues (PMID:28334776). [Type chain A]=Ordered [Evidence chain A]=The PH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF08567). A solved monomeric structure of the domain is represented by PDB ID 1y5o. [Chain B name]=Transcription factor p65 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q04206 [Chain B UniProt boundaries]=519-551 [Chain B UniProt coverage]=6% [Chain B UniRef90 accession]=UniRef90_Q04206 [Chain B UniRef90 boundaries]=519-551 [Chain A name]=RNA polymerase II transcription factor B subunit 1 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P32776 [Chain A UniProt boundaries]=1-115 [Chain A UniProt coverage]=17.9% [Chain A UniRef90 accession]=UniRef90_P32776 [Chain A UniRef90 boundaries]=2-115 [Entry] [Accession]=DI1000045 [Disorder status]=Confirmed [Kd]=1.43E-07 (PMID:26278177) [Name]=Complex between XPC acidic domain and TFIIH p62 PH domain [Source organism]=Homo sapiens [PDB ID]=2rvb [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PH [Type chain A]=Disordered [Evidence chain A]=The 109-156 region described in IDEAL entry IID00164 covers 92% of the sequence present in the structure. The protein region involved in the interaction contains a highly conserved (D/E)(F/W)E(D/E)V binding motif (PMID:26278177). [Type chain B]=Ordered [Evidence chain B]=The PH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF08567). A solved monomeric structure of the domain is represented by PDB ID 1pfj. [Chain A name]=DNA repair protein complementing XP-C cells [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q01831 [Chain A UniProt boundaries]=105-156 [Chain A UniProt coverage]=5.5% [Chain A UniRef90 accession]=UniRef90_Q01831 [Chain A UniRef90 boundaries]=109-156 [Chain B name]=General transcription factor IIH subunit 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P32780 [Chain B UniProt boundaries]=1-108 [Chain B UniProt coverage]=19.7% [Chain B UniRef90 accession]=UniRef90_P32780 [Chain B UniRef90 boundaries]=1-108 [Entry] [Accession]=DI1000046 [Disorder status]=Confirmed [Kd]=2.80E-07 (PMID:28276594) [Name]=N domain of cardiac troponin C bound to the switch fragment of fast skeletal troponin I [Source organism]=Homo sapiens [PDB ID]=2mkp [PDB chain IDs]=I:C [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=EF-hand [Type chain I]=Disordered [Evidence chain I]=The C-terminal region of troponin I was shown to be intrinsically disordered (PMID:21322033). [Type chain C]=Ordered [Evidence chain C]=The EF-hand domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13833). A solved monomeric structure of the domain is represented by PDB ID 1ap4. [Chain I name]=Troponin I, fast skeletal muscle [Chain I source organism]=Homo sapiens [Chain I UniProt accession]=P48788 [Chain I UniProt boundaries]=116-132 [Chain I UniProt coverage]=9.3% [Chain I UniRef90 accession]=UniRef90_P48788 [Chain I UniRef90 boundaries]=116-132 [Chain C name]=Troponin C, slow skeletal and cardiac muscles [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P63316 [Chain C UniProt boundaries]=1-89 [Chain C UniProt coverage]=55.3% [Chain C UniRef90 accession]=UniRef90_P63316 [Chain C UniRef90 boundaries]=1-89 [Entry] [Accession]=DI1000047 [Disorder status]=Confirmed [Kd]=2.80E-07 (PMID:28276594) [Name]=Bromodomain of human BRPF1 in complex with histone H4K5ac peptide [Source organism]=Homo sapiens [PDB ID]=2rs9 [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Bromodomain [Type chain A]=Disordered [Evidence chain A]=The 1-28 region described in IDEAL entry IID00058 covers 100% of the sequence present in the structure. [Type chain B]=Ordered [Evidence chain B]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 4lc2. [Modified residues chain A]=N(6)-acetyllysine#K#5 [Chain A name]=Histone H4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P62805 [Chain A UniProt boundaries]=2-11 [Chain A UniProt coverage]=9.7% [Chain A UniRef90 accession]=UniRef90_P62805 [Chain A UniRef90 boundaries]=2-11 [Chain B name]=Peregrin [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P55201 [Chain B UniProt boundaries]=626-746 [Chain B UniProt coverage]=10% [Chain B UniRef90 accession]=UniRef90_P55201 [Chain B UniRef90 boundaries]=633-740 [Entry] [Accession]=DI1000048 [Disorder status]=Confirmed [Kd]=8.95E-05 (PMID:25281266) [Name]=Bromodomain of human BRPF1 in complex with histone H4K12ac peptide [Source organism]=Homo sapiens [PDB ID]=4qyd [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.94 [Domain]=Bromodomain [Type chain B]=Disordered [Evidence chain B]=The 1-28 region described in IDEAL entry IID00058 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 4lc2. [Modified residues chain B]=N(6)-acetyllysine#K#12 [Modified residues chain A]=N(6)-acetyllysine#K#5 [Chain B name]=Histone H4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P62805 [Chain B UniProt boundaries]=5-18 [Chain B UniProt coverage]=13.6% [Chain B UniRef90 accession]=UniRef90_P62805 [Chain B UniRef90 boundaries]=5-18 [Chain A name]=Peregrin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P55201 [Chain A UniProt boundaries]=626-742 [Chain A UniProt coverage]=9.6% [Chain A UniRef90 accession]=UniRef90_P55201 [Chain A UniRef90 boundaries]=628-742 [Entry] [Accession]=DI1000049 [Disorder status]=Confirmed [Kd]=1.00E-08 (PMID:15327768) [Name]=Beta-catenin in complex with a 5x phosphorylated APC fragment [Source organism]=Homo sapiens [PDB ID]=1th1 [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=Armadillo repeat [Type chain C]=Disordered [Evidence chain C]=The interacting region of APC has been shown to be intrinsically disordered (PMID:24130866). [Type chain A]=Ordered [Evidence chain A]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain is represented by PDB ID 2z6h. [Modified residues chain C]=phosphothreonine#T#1487|phosphoserine#S#1504|phosphoserine#S#1505|phosphoserine#S#1507|phosphoserine#S#1510 [Modified residues chain A]=N(6)-acetyllysine#K#5 [Chain C name]=Adenomatous polyposis coli protein [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P25054 [Chain C UniProt boundaries]=1469-1529 [Chain C UniProt coverage]=2.1% [Chain C UniRef90 accession]=UniRef90_P25054 [Chain C UniRef90 boundaries]=1469-1529 [Chain A name]=Catenin beta-1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P35222 [Chain A UniProt boundaries]=146-664 [Chain A UniProt coverage]=66.5% [Chain A UniRef90 accession]=UniRef90_Q02248 [Chain A UniRef90 boundaries]=146-664 [Entry] [Accession]=DI1010025 [Disorder status]=Confirmed [Kd]=1.00E-08 (PMID:15327768) [Name]=Beta-catenin binding domain of Axin in complex with beta-catenin [Source organism]=Xenopus laevis / Homo sapiens [PDB ID]=1qz7 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=Armadillo repeat [Type chain B]=Disordered [Evidence chain B]=The interacting region of Axin1 has been shown to be intrinsically disordered (PMID:21087614). [Type chain A]=Ordered [Evidence chain A]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain is represented by PDB ID 2z6h. [Modified residues chain A]=N(6)-acetyllysine#K#5 [Chain B name]=Axin-1 [Chain B source organism]=Xenopus laevis [Chain B UniProt accession]=Q9YGY0 [Chain B UniProt boundaries]=466-482 [Chain B UniProt coverage]=2% [Chain B UniRef90 accession]=UniRef90_Q9YGY0 [Chain B UniRef90 boundaries]=466-482 [Chain A name]=Catenin beta-1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P35222 [Chain A UniProt boundaries]=142-665 [Chain A UniProt coverage]=67.1% [Chain A UniRef90 accession]=UniRef90_Q02248 [Chain A UniRef90 boundaries]=142-665 [Entry] [Accession]=DI1000050 [Disorder status]=Confirmed [Kd]=1.00E-08 (PMID:15327768) [Name]=GSK-3/Axin complex [Source organism]=Homo sapiens [PDB ID]=1o9u [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=Protein kinase [Type chain B]=Disordered [Evidence chain B]=The interacting region of Axin1 has been shown to be intrinsically disordered (PMID:21087614). The protein region involved in the interaction contains a known functional linear motif (DOC_GSK3_Axin_1). [Type chain A]=Ordered [Evidence chain A]=The protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 1i09. [Modified residues chain A]=N(6)-acetyllysine#K#5 [Chain B name]=Axin-1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O15169 [Chain B UniProt boundaries]=383-400 [Chain B UniProt coverage]=2.1% [Chain B UniRef90 accession]=UniRef90_O15169 [Chain B UniRef90 boundaries]=383-400 [Chain A name]=Glycogen synthase kinase-3 beta [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P49841 [Chain A UniProt boundaries]=35-384 [Chain A UniProt coverage]=83.3% [Chain A UniRef90 accession]=UniRef90_P49841 [Chain A UniRef90 boundaries]=35-384 [Related structures]=3zdi,4b7t,4nm0,4nm3,4nm5,4nm7,4nu1 [Entry] [Accession]=DI1010026 [Disorder status]=Confirmed [Kd]=5.50E-05 (PMID:21047797) [Name]=Chromobox protein 7 in interaction with H3K9me3 peptide [Source organism]=Xenopus laevis / Homo sapiens [PDB ID]=2l12 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Chromodomain [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The corresponding region of a closely homologous protein has been shown to be disordered in the 1-38 region described in IDEAL entry IID00086 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The chromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00385). A solved monomeric structure of the domain is represented by PDB ID 2k1b. [Modified residues chain B]=N-trimethyllysine#K#9 [Modified residues chain A]=N(6)-acetyllysine#K#5 [Chain B name]=Histone H3 [Chain B source organism]=Xenopus laevis [Chain B UniProt accession]=Q92133 [Chain B UniProt boundaries]=2-16 [Chain B UniProt coverage]=11% [Chain B UniRef90 accession]=UniRef90_Q16695 [Chain B UniRef90 boundaries]=2-16 [Chain A name]=Chromobox protein homolog 7 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=B0QYP2 [Chain A UniProt boundaries]=7-62 [Chain A UniProt coverage]=35.4% [Chain A UniRef90 accession]=UniRef90_Q8VDS3 [Chain A UniRef90 boundaries]=7-62 [Entry] [Accession]=DI1010027 [Disorder status]=Confirmed [Kd]=1.50E-05 (PMID:21047797) [Name]=Chromobox protein homolog 3 in interaction with H3K9me3 peptide [Source organism]=Xenopus laevis / Homo sapiens [PDB ID]=2l11 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Chromodomain [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The corresponding region of a closely homologous protein has been shown to be disordered in the 1-38 region described in IDEAL entry IID00086 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The chromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00385). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4quc. [Modified residues chain B]=N-trimethyllysine#K#9 [Modified residues chain A]=N(6)-acetyllysine#K#5 [Chain B name]=Histone H3 [Chain B source organism]=Xenopus laevis [Chain B UniProt accession]=Q92133 [Chain B UniProt boundaries]=2-16 [Chain B UniProt coverage]=11% [Chain B UniRef90 accession]=UniRef90_Q16695 [Chain B UniRef90 boundaries]=2-16 [Chain A name]=Chromobox protein homolog 3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q13185 [Chain A UniProt boundaries]=28-81 [Chain A UniProt coverage]=29.5% [Chain A UniRef90 accession]=UniRef90_Q13185 [Chain A UniRef90 boundaries]=29-81 [Entry] [Accession]=DI1000051 [Disorder status]=Confirmed [Kd]=9.90E-06 [Name]=CW-type zinc finger of ZCWPW2 in complex with the amino terminus of histone H3 [Source organism]=Homo sapiens [PDB ID]=4o62 [PDB chain IDs]=D:B [PDB note]=Chains A and C were removed as chains B and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.78 [Domain]=CW-type zinc finger [Type chain D]=Disordered [Evidence chain D]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain B]=Ordered [Evidence chain B]=The CW-type zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF07496). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2e61. [Modified residues chain D]=N-trimethyllysine#K#4 [Modified residues chain B]=N-trimethyllysine#K#9 [Chain D name]=Histone H3.3 (Fragment) [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=K7ES00 [Chain D UniProt boundaries]=2-12 [Chain D UniProt coverage]=7.3% [Chain D UniRef90 accession]=UniRef90_K7ES00 [Chain D UniRef90 boundaries]=2-12 [Chain B name]=Zinc finger CW-type PWWP domain protein 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q504Y3 [Chain B UniProt boundaries]=20-78 [Chain B UniProt coverage]=16.6% [Chain B UniRef90 accession]=UniRef90_Q504Y3 [Chain B UniRef90 boundaries]=21-78 [Entry] [Accession]=DI1010028 [Disorder status]=Confirmed [Kd]=3.00E-05 (PMID:21047797) [Name]=Human chromobox homolog 5 (CBX5) with H3K9me3 peptide [Source organism]=Siphlonella sp. EP083 / Homo sapiens [PDB ID]=3fdt [PDB chain IDs]=T:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Chromodomain [Type chain T]=Disordered [Evidence chain T]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The chromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00385). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4quc. [Modified residues chain T]=N-trimethyllysine#K#18 [Modified residues chain A]=N(6)-acetyllysine#K#5 [Chain T name]=Histone H3 (Fragment) [Chain T source organism]=Siphlonella sp. EP083 [Chain T UniProt accession]=Q3BDD9 [Chain T UniProt boundaries]=2-16 [Chain T UniProt coverage]=12% [Chain T UniRef90 accession]=UniRef90_Q3BDD9 [Chain T UniRef90 boundaries]=2-16 [Chain A name]=Chromobox protein homolog 5 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P45973 [Chain A UniProt boundaries]=17-75 [Chain A UniProt coverage]=30.9% [Chain A UniRef90 accession]=UniRef90_P45973 [Chain A UniRef90 boundaries]=20-75 [Entry] [Accession]=DI1000052 [Disorder status]=Confirmed [Kd]=6.20E-05 (PMID:21422291) [Name]=RAD18 (RAD6 binding domain) in complex with RAD6B [Source organism]=Homo sapiens [PDB ID]=2ybf [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Ubiquitin-conjugating enzyme [Type chain B]=Disordered [Evidence chain B]=The 340-366 region described in IDEAL entry IID00588 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Ubiquitin-conjugating enzyme domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00179). A solved monomeric structure of the domain is represented by PDB ID 1jas. [Modified residues chain A]=N(6)-acetyllysine#K#5 [Chain B name]=E3 ubiquitin-protein ligase RAD18 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9NS91 [Chain B UniProt boundaries]=340-366 [Chain B UniProt coverage]=5.5% [Chain B UniRef90 accession]=UniRef90_Q9NS91 [Chain B UniRef90 boundaries]=340-366 [Chain A name]=Ubiquitin-conjugating enzyme E2 B [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63146 [Chain A UniProt boundaries]=1-152 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P63146 [Chain A UniRef90 boundaries]=1-152 [Entry] [Accession]=DI1000053 [Disorder status]=Confirmed [Kd]=6.71E-05 (PMID:22464331) [Name]=BRD3 second bromodomain in complex with histone H3 acetylation at K18 [Source organism]=Homo sapiens [PDB ID]=5hjc [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=Bromodomain [Type chain B]=Disordered [Evidence chain B]=The 1-60 region described in IDEAL entry IID00062 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 2e7n. [Modified residues chain B]=N(6)-acetyllysine#K#18 [Modified residues chain A]=N(6)-acetyllysine#K#5 [Chain B name]=Histone H3.1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68431 [Chain B UniProt boundaries]=16-24 [Chain B UniProt coverage]=6.6% [Chain B UniRef90 accession]=UniRef90_P68431 [Chain B UniRef90 boundaries]=16-24 [Chain A name]=Bromodomain-containing protein 3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q15059 [Chain A UniProt boundaries]=307-416 [Chain A UniProt coverage]=15.2% [Chain A UniRef90 accession]=UniRef90_Q15059 [Chain A UniRef90 boundaries]=307-416 [Entry] [Accession]=DI1000054 [Disorder status]=Confirmed [Kd]=1.73E-06 (PMID:22837395) [Name]=UHRF1 in complex with unmodified H3.3 histone tail [Source organism]=Homo sapiens [PDB ID]=3asl [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.41 [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=The 1-45 region described in IDEAL entry IID00239 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 2lgl. [Modified residues chain A]=N(6)-acetyllysine#K#5 [Chain B name]=Histone H3.3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P84243 [Chain B UniProt boundaries]=2-12 [Chain B UniProt coverage]=8.1% [Chain B UniRef90 accession]=UniRef90_P84243 [Chain B UniRef90 boundaries]=2-12 [Chain A name]=E3 ubiquitin-protein ligase UHRF1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96T88 [Chain A UniProt boundaries]=298-367 [Chain A UniProt coverage]=8.8% [Chain A UniRef90 accession]=UniRef90_Q96T88 [Chain A UniRef90 boundaries]=298-367 [Entry] [Accession]=DI1100010 [Disorder status]=Confirmed [Kd]=9.10E-06 [Name]=PHD domain from the yeast YNG1 protein in complex with H3(1-9)K4me3 peptide [Source organism]=Saccharomyces cerevisiae [PDB ID]=2jmj [PDB chain IDs]=P:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PHD zinc finger [Type chain P]=Disordered [Evidence chain P]=The 1-39 region described in IDEAL entry IID50143 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 2jmi. [Modified residues chain P]=N-trimethyllysine#K#4 [Modified residues chain A]=N(6)-acetyllysine#K#5 [Chain P name]=Histone H3 [Chain P source organism]=Saccharomyces cerevisiae [Chain P UniProt accession]=P61830 [Chain P UniProt boundaries]=2-10 [Chain P UniProt coverage]=6.6% [Chain P UniRef90 accession]=UniRef90_Q757N1 [Chain P UniRef90 boundaries]=2-10 [Chain A name]=Protein YNG1 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=Q08465 [Chain A UniProt boundaries]=141-219 [Chain A UniProt coverage]=36.1% [Chain A UniRef90 accession]=UniRef90_Q08465 [Chain A UniRef90 boundaries]=141-219 [Entry] [Accession]=DI1100011 [Disorder status]=Confirmed [Kd]=1.90E-07 (PMID:19362535) [Name]=Chromodomain of Chp1 in complex with Histone H3K9me3 peptide [Source organism]=Schizosaccharomyces pombe [PDB ID]=3g7l [PDB chain IDs]=P:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=Chromodomain [Type chain P]=Disordered [Evidence chain P]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The corresponding region of a closely homologous protein has been shown to be disordered in the 1-38 region described in IDEAL entry IID00086 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The chromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00385). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4quc. [Modified residues chain P]=N-trimethyllysine#K#9 [Modified residues chain A]=N(6)-acetyllysine#K#5 [Chain P name]=Histone H3.1/H3.2 [Chain P source organism]=Schizosaccharomyces pombe [Chain P UniProt accession]=P09988 [Chain P UniProt boundaries]=2-17 [Chain P UniProt coverage]=11.8% [Chain P UniRef90 accession]=UniRef90_Q16695 [Chain P UniRef90 boundaries]=2-16 [Chain A name]=Chromo domain-containing protein 1 [Chain A source organism]=Schizosaccharomyces pombe [Chain A UniProt accession]=Q10103 [Chain A UniProt boundaries]=15-75 [Chain A UniProt coverage]=6.4% [Chain A UniRef90 accession]=UniRef90_Q10103 [Chain A UniRef90 boundaries]=15-64 [Entry] [Accession]=DI1010029 [Disorder status]=Confirmed [Kd]=8.85E-05 (PMID:27223324) [Name]=PHF13 in complex with H3K4me3 [Source organism]=Xenopus laevis / Homo sapiens [PDB ID]=3o7a [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.67 [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The corresponding region of a closely homologous protein has been shown to be disordered in the 1-38 region described in IDEAL entry IID00086 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2lgl. [Modified residues chain B]=N-trimethyllysine#K#4 [Modified residues chain A]=N(6)-acetyllysine#K#5 [Chain B name]=Histone H3 [Chain B source organism]=Xenopus laevis [Chain B UniProt accession]=Q92133 [Chain B UniProt boundaries]=2-12 [Chain B UniProt coverage]=8.1% [Chain B UniRef90 accession]=UniRef90_Q16695 [Chain B UniRef90 boundaries]=2-12 [Chain A name]=PHD finger protein 13 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q86YI8 [Chain A UniProt boundaries]=229-280 [Chain A UniProt coverage]=17.3% [Chain A UniRef90 accession]=UniRef90_Q86YI8 [Chain A UniRef90 boundaries]=229-280 [Entry] [Accession]=DI1000055 [Disorder status]=Confirmed [Kd]=1.67E-05 [Name]=Zinc finger CW-type PWWP domain protein 1 in complex with a H3K4me3 peptide [Source organism]=Homo sapiens [PDB ID]=2rr4 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=CW-type zinc finger [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The corresponding region of a closely homologous protein has been shown to be disordered in the 1-38 region described in IDEAL entry IID00086 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The CW-type zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF07496). A solved monomeric structure of the domain is represented by PDB ID 2e61. [Modified residues chain B]=N-trimethyllysine#K#4 [Modified residues chain A]=N(6)-acetyllysine#K#5 [Chain B name]=Histone H3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=A8K4Y7 [Chain B UniProt boundaries]=2-11 [Chain B UniProt coverage]=7.4% [Chain B UniRef90 accession]=UniRef90_Q16695 [Chain B UniRef90 boundaries]=2-11 [Chain A name]=Zinc finger CW-type PWWP domain protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9H0M4 [Chain A UniProt boundaries]=239-307 [Chain A UniProt coverage]=10.6% [Chain A UniRef90 accession]=UniRef90_Q9H0M4 [Chain A UniRef90 boundaries]=244-307 [Entry] [Accession]=DI1100012 [Disorder status]=Confirmed [Kd]=1.67E-05 [Name]=C-terminal domain of Akazara scallop troponin C in complex with a troponin I fragment [Source organism]=Chlamys nipponensis akazara [PDB ID]=3tz1 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=EF-hand [Type chain B]=Disordered [Evidence chain B]=The C-terminal region of troponin I was shown to be intrinsically disordered (PMID:21322033). [Type chain A]=Ordered [Evidence chain A]=The EF-hand domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13499). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1blq. [Modified residues chain A]=N(6)-acetyllysine#K#5 [Chain B name]=Troponin I [Chain B source organism]=Chlamys nipponensis akazara [Chain B UniProt accession]=Q7M3Y3 [Chain B UniProt boundaries]=143-166 [Chain B UniProt coverage]=8.2% [Chain B UniRef90 accession]=UniRef90_Q7M3Y3 [Chain B UniRef90 boundaries]=143-166 [Chain A name]=Troponin C [Chain A source organism]=Chlamys nipponensis akazara [Chain A UniProt accession]=Q27428 [Chain A UniProt boundaries]=80-153 [Chain A UniProt coverage]=48.4% [Chain A UniRef90 accession]=UniRef90_Q27428 [Chain A UniRef90 boundaries]=81-153 [Entry] [Accession]=DI1010030 [Disorder status]=Confirmed [Kd]=6.90E-06 (PMID:24628338) [Name]=Cytoplasmic tail of proHB-EGF-CT complexed with mBAG-1-UBH [Source organism]=Homo sapiens / Mus musculus [PDB ID]=2m8s [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Ubiquitin-like [Type chain B]=Disordered [Evidence chain B]=The 186-208 region described in IDEAL entry IID00579 covers 96% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The ubiquitin-like domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00240). A solved monomeric structure of the domain is represented by PDB ID 2lwp. [Modified residues chain A]=N(6)-acetyllysine#K#5 [Chain B name]=Proheparin-binding EGF-like growth factor [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q99075 [Chain B UniProt boundaries]=185-208 [Chain B UniProt coverage]=11.5% [Chain B UniRef90 accession]=UniRef90_Q99075 [Chain B UniRef90 boundaries]=185-208 [Chain A name]=BAG family molecular chaperone regulator 1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q60739 [Chain A UniProt boundaries]=137-233 [Chain A UniProt coverage]=27.3% [Chain A UniRef90 accession]=UniRef90_Q60739 [Chain A UniRef90 boundaries]=137-233 [Entry] [Accession]=DI1010031 [Disorder status]=Confirmed [Kd]=5.00E-04 (PMID:20368734) [Name]=Bromodomain of Human Polybromo in complex with an acetylated peptide from Histone 3 [Source organism]=Neurospora crassa / Homo sapiens [PDB ID]=2ktb [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Bromodomain [Type chain A]=Disordered [Evidence chain A]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain B]=Ordered [Evidence chain B]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1n72. [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain A name]=Histone H3 [Chain A source organism]=Neurospora crassa [Chain A UniProt accession]=P07041 [Chain A UniProt boundaries]=2-21 [Chain A UniProt coverage]=14.7% [Chain A UniRef90 accession]=UniRef90_Q6DL03 [Chain A UniRef90 boundaries]=2-21 [Chain B name]=Protein polybromo-1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q86U86 [Chain B UniProt boundaries]=173-293 [Chain B UniProt coverage]=7.2% [Chain B UniRef90 accession]=UniRef90_Q86U86 [Chain B UniRef90 boundaries]=174-293 [Entry] [Accession]=DI1010032 [Disorder status]=Confirmed [Kd]=4.02E-04 [Name]=Histone acetyltransferase PCAF in complex with histone H3 tail [Source organism]=Saccharomyces cerevisiae / Homo sapiens [PDB ID]=2rnx [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Bromodomain [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 1n72. [Modified residues chain B]=N(6)-acetyllysine#K#36 [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain B name]=Histone H3 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P61830 [Chain B UniProt boundaries]=32-44 [Chain B UniProt coverage]=9.6% [Chain B UniRef90 accession]=UniRef90_Q757N1 [Chain B UniRef90 boundaries]=32-43 [Chain A name]=Histone acetyltransferase KAT2B [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q92831 [Chain A UniProt boundaries]=715-832 [Chain A UniProt coverage]=14.2% [Chain A UniRef90 accession]=UniRef90_Q92831 [Chain A UniRef90 boundaries]=715-832 [Entry] [Accession]=DI1000056 [Disorder status]=Confirmed [Kd]=4.02E-04 [Name]=Bromodomain of human BRPF1 in complex with H3K14ac histone peptide [Source organism]=Homo sapiens [PDB ID]=5ffv [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.30 [Domain]=Bromodomain [Type chain C]=Disordered [Evidence chain C]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 4lc2. [Modified residues chain C]=N(6)-acetyllysine#K#14 [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain C name]=Histone H3 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=K7EMV3 [Chain C UniProt boundaries]=10-20 [Chain C UniProt coverage]=12% [Chain C UniRef90 accession]=UniRef90_K7EMV3 [Chain C UniRef90 boundaries]=10-20 [Chain A name]=Peregrin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P55201 [Chain A UniProt boundaries]=625-740 [Chain A UniProt coverage]=9.6% [Chain A UniRef90 accession]=UniRef90_P55201 [Chain A UniRef90 boundaries]=625-740 [Entry] [Accession]=DI1000057 [Disorder status]=Confirmed [Kd]=3.60E-05 (PMID:23142980) [Name]=PHF1 Tudor in complex with H3K36me3 [Source organism]=Homo sapiens [PDB ID]=4hcz [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.85 [Domain]=Tudor [Type chain C]=Disordered [Evidence chain C]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The Tudor domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 2e5p. [Modified residues chain C]=N-trimethyllysine#K#36 [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain C name]=H3L-like histone (Fragment) [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q6TXQ4 [Chain C UniProt boundaries]=17-26 [Chain C UniProt coverage]=9.3% [Chain C UniRef90 accession]=UniRef90_V9HWS8 [Chain C UniRef90 boundaries]=21-30 [Chain A name]=PHD finger protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O43189 [Chain A UniProt boundaries]=28-85 [Chain A UniProt coverage]=10.2% [Chain A UniRef90 accession]=UniRef90_O43189 [Chain A UniRef90 boundaries]=28-85 [Entry] [Accession]=DI1000058 [Disorder status]=Confirmed [Kd]=3.60E-05 (PMID:23142980) [Name]=GABARAP-L1 in complex with an unmodified ATG4B peptide [Source organism]=Homo sapiens [PDB ID]=5lxh [PDB chain IDs]=E:A [PDB note]=Chains B, C, F and G were removed as chains A and E represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.58 [Domain]=Atg8 [Type chain E]=Disordered [Evidence chain E]=The 374-393 region described in IDEAL entry IID00347 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a LIR motif (PMID:28330855). [Type chain A]=Ordered [Evidence chain A]=The Atg8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02991). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1gnu. [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain E name]=Cysteine protease ATG4B [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=Q9Y4P1 [Chain E UniProt boundaries]=384-393 [Chain E UniProt coverage]=2.5% [Chain E UniRef90 accession]=UniRef90_Q9Y4P1 [Chain E UniRef90 boundaries]=384-393 [Chain A name]=Gamma-aminobutyric acid receptor-associated protein-like 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9H0R8 [Chain A UniProt boundaries]=1-117 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q9H0R8 [Chain A UniRef90 boundaries]=1-117 [Entry] [Accession]=DI1110005 [Disorder status]=Confirmed [Kd]=3.60E-05 (PMID:23142980) [Name]=Polycomb chromodomain bound to histone H3 methylated at K27 [Source organism]=Strongylocentrotus purpuratus / Drosophila melanogaster [PDB ID]=1pfb [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.40 [Domain]=Chromodomain [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The corresponding region of a closely homologous protein has been shown to be disordered in the 1-38 region described in IDEAL entry IID00086 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The chromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00385). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4quc. [Modified residues chain B]=N-trimethyllysine#K#27 [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain B name]=Histone H3, embryonic [Chain B source organism]=Strongylocentrotus purpuratus [Chain B UniProt accession]=P06352 [Chain B UniProt boundaries]=21-31 [Chain B UniProt coverage]=8.1% [Chain B UniRef90 accession]=UniRef90_Q16695 [Chain B UniRef90 boundaries]=21-31 [Chain A name]=Polycomb group protein Pc [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=P26017 [Chain A UniProt boundaries]=23-77 [Chain A UniProt coverage]=14.1% [Chain A UniRef90 accession]=UniRef90_P26017 [Chain A UniRef90 boundaries]=23-77 [Entry] [Accession]=DI2210001 [Disorder status]=Inferred from homology [Kd]=3.60E-05 (PMID:23142980) [Name]=CcdB dimer (V. fisheri) in complex with the C-terminal domain of F-plasmid CcdA [Source organism]=Escherichia coli O157:H7 / Aliivibrio fischeri [PDB ID]=3tcj [PDB chain IDs]=T:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.93 [Domain]=CcdB [Type chain T]=Disordered [Evidence chain T]=The corresponding region of a closely homologous protein has been shown to be disordered in the 37-72 region described in DisProt entry DP00928 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The monomers of the controller of cell division or death B protein (CcdB) form well folded monomers (PMID:14763902). [Type chain B]=Ordered [Evidence chain B]=The monomers of the controller of cell division or death B protein (CcdB) form well folded monomers (PMID:14763902). [Modified residues chain A]=N(6)-acetyllysine#K#14 [Modified residues chain B]=N-trimethyllysine#K#27 [Chain T name]=Antitoxin CcdA [Chain T source organism]=Escherichia coli O157:H7 [Chain T UniProt accession]=P62553 [Chain T UniProt boundaries]=37-72 [Chain T UniProt coverage]=50% [Chain T UniRef90 accession]=UniRef90_P62553 [Chain T UniRef90 boundaries]=37-72 [Chain A name]=CcdB [Chain A source organism]=Aliivibrio fischeri [Chain A UniProt accession]=Q84B82 [Chain A UniProt boundaries]=1-105 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q84B82 [Chain A UniRef90 boundaries]=1-105 [Chain B name]=CcdB [Chain B source organism]=Aliivibrio fischeri [Chain B UniProt accession]=Q84B82 [Chain B UniProt boundaries]=1-105 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_Q84B82 [Chain B UniRef90 boundaries]=1-105 [Entry] [Accession]=DI1000059 [Disorder status]=Confirmed [Kd]=3.00E-06 (PMID:18381289) [Name]=Histone H3K4me3 bound by ING4 [Source organism]=Homo sapiens [PDB ID]=2vnf [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.76 [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The corresponding region of a closely homologous protein has been shown to be disordered in the 1-38 region described in IDEAL entry IID00086 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 1xwh. [Modified residues chain B]=N-trimethyllysine#K#4 [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain B name]=Histone H3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q5TEC6 [Chain B UniProt boundaries]=2-11 [Chain B UniProt coverage]=7.4% [Chain B UniRef90 accession]=UniRef90_Q16695 [Chain B UniRef90 boundaries]=2-11 [Chain A name]=Inhibitor of growth protein 4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UNL4 [Chain A UniProt boundaries]=187-246 [Chain A UniProt coverage]=24.1% [Chain A UniRef90 accession]=UniRef90_Q9UNL4 [Chain A UniRef90 boundaries]=187-246 [Entry] [Accession]=DI1100013 [Disorder status]=Confirmed [Kd]=2.51E-04 [Name]=Brdt bromodomain 2 bound to an acetylated histone H3 peptide [Source organism]=Mus musculus [PDB ID]=2wp1 [PDB chain IDs]=P:A [PDB note]=Chains B and Q were removed as chains A and P represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=Bromodomain [Type chain P]=Disordered [Evidence chain P]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The corresponding region of a closely homologous protein has been shown to be disordered in the 1-43 region described in IDEAL entry IID00088 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1n72. [Modified residues chain P]=N(6)-acetyllysine#K#18 [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain P name]=Histone H3 [Chain P source organism]=Mus musculus [Chain P UniProt accession]=B9EI85 [Chain P UniProt boundaries]=15-24 [Chain P UniProt coverage]=7.4% [Chain P UniRef90 accession]=UniRef90_Q71DI3 [Chain P UniRef90 boundaries]=15-24 [Chain A name]=Bromodomain testis-specific protein [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q91Y44 [Chain A UniProt boundaries]=257-382 [Chain A UniProt coverage]=13.2% [Chain A UniRef90 accession]=UniRef90_Q91Y44 [Chain A UniRef90 boundaries]=257-382 [Entry] [Accession]=DI1000060 [Disorder status]=Confirmed [Kd]=3.50E-07 (PMID:14685257) [Name]=C-terminal PABC domain of human poly(A)-binding protein in complex with the peptide from Paip2 [Source organism]=Homo sapiens [PDB ID]=1jgn [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PABP [Type chain B]=Disordered [Evidence chain B]=The 106-127 region described in IDEAL entry IID00582 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_PAM2_1). [Type chain A]=Ordered [Evidence chain A]=The PABP domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00658). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1i2t. [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain B name]=Polyadenylate-binding protein-interacting protein 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9BPZ3 [Chain B UniProt boundaries]=106-127 [Chain B UniProt coverage]=17.3% [Chain B UniRef90 accession]=UniRef90_Q9BPZ3 [Chain B UniRef90 boundaries]=106-127 [Chain A name]=Polyadenylate-binding protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P11940 [Chain A UniProt boundaries]=539-636 [Chain A UniProt coverage]=15.4% [Chain A UniRef90 accession]=UniRef90_P11940 [Chain A UniRef90 boundaries]=544-636 [Related structures]=3kut,3kus [Entry] [Accession]=DI1000061 [Disorder status]=Confirmed [Kd]=1.08E-05 [Name]=MOZ double PHD finger in complex with histone H3 propionylation at K14 [Source organism]=Homo sapiens [PDB ID]=5b77 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.55 [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 2ln0. [Modified residues chain B]=N(6)-propionyllysine#K#14 [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain B name]=Histone H3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=K7EMV3 [Chain B UniProt boundaries]=2-26 [Chain B UniProt coverage]=27.2% [Chain B UniRef90 accession]=UniRef90_K7EMV3 [Chain B UniRef90 boundaries]=2-26 [Chain A name]=Histone acetyltransferase KAT6A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q92794 [Chain A UniProt boundaries]=193-323 [Chain A UniProt coverage]=6.5% [Chain A UniRef90 accession]=UniRef90_Q92794 [Chain A UniRef90 boundaries]=194-323 [Related structures]=5b75,5b76,5b78 [Entry] [Accession]=DI1020009 [Disorder status]=Inferred from motif [Kd]=1.57E-04 (PMID:22000519) [Name]=MAST205-PDZ complexed with the C-terminus of a rabies virus G protein [Source organism]=Rabies virus / Homo sapiens [PDB ID]=3nfk [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.43 [Domain]=PDZ [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a functional PDZ-binding linear motif (PMID:22000519). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2ev8. [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain C name]=Glycoprotein [Chain C source organism]=Rabies virus [Chain C UniProt accession]=P03524 [Chain C UniProt boundaries]=512-524 [Chain C UniProt coverage]=2.5% [Chain C UniRef90 accession]=UniRef90_P03524 [Chain C UniRef90 boundaries]=512-524 [Chain A name]=Tyrosine-protein phosphatase non-receptor type 4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P29074 [Chain A UniProt boundaries]=498-604 [Chain A UniProt coverage]=11.6% [Chain A UniRef90 accession]=UniRef90_P29074 [Chain A UniRef90 boundaries]=499-604 [Entry] [Accession]=DI1000062 [Disorder status]=Confirmed [Kd]=4.85E-05 (PMID:25281266) [Name]=BRPF1 bromodomain in complex with a histone H2AK5ac peptide [Source organism]=Homo sapiens [PDB ID]=4qyl [PDB chain IDs]=E:A [PDB note]=Chains B, C, D, F, G and H were removed as chains A and E represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=Bromodomain [Type chain E]=Disordered [Evidence chain E]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 4lc2. [Modified residues chain E]=N(6)-acetyllysine#K#5 [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain E name]=Histone H2A type 1 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P0C0S8 [Chain E UniProt boundaries]=2-13 [Chain E UniProt coverage]=9.2% [Chain E UniRef90 accession]=UniRef90_P0C0S8 [Chain E UniRef90 boundaries]=2-13 [Chain A name]=Peregrin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P55201 [Chain A UniProt boundaries]=626-742 [Chain A UniProt coverage]=9.6% [Chain A UniRef90 accession]=UniRef90_P55201 [Chain A UniRef90 boundaries]=628-742 [Entry] [Accession]=DI1000063 [Disorder status]=Confirmed [Kd]=5.50E-06 (PMID:20181956) [Name]=PABC-TNRC6C complex [Source organism]=Homo sapiens [PDB ID]=2x04 [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.49 [Domain]=PABP [Type chain C]=Disordered [Evidence chain C]=The 1380-1401 region described in IDEAL entry IID00587 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_PAM2_2). [Type chain A]=Ordered [Evidence chain A]=The PABP domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00658). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1i2t. [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain C name]=Trinucleotide repeat-containing gene 6C protein [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q9HCJ0 [Chain C UniProt boundaries]=1382-1399 [Chain C UniProt coverage]=1.1% [Chain C UniRef90 accession]=UniRef90_Q9HCJ0 [Chain C UniRef90 boundaries]=1382-1399 [Chain A name]=Polyadenylate-binding protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P11940 [Chain A UniProt boundaries]=540-619 [Chain A UniProt coverage]=12.6% [Chain A UniRef90 accession]=UniRef90_P11940 [Chain A UniRef90 boundaries]=545-619 [Related structures]=3ktp [Entry] [Accession]=DI1010033 [Disorder status]=Inferred from homology [Kd]=8.50E-07 (PMID:19140243) [Name]=Dileucine peptide RM(pS)QIKRLLSE from CD4 bound to clathrin adaptor AP-2 complex subunit sigma-1 [Source organism]=Homo sapiens / Mus musculus [PDB ID]=2jkr [PDB chain IDs]=P:S [PDB note]=Chains A, B, E, I, L, M, Q and U were removed to highlight the presumably independent interaction between chains P and S. [PDB experimental technique]=X-ray [PDB resolution]=2.98 [Domain]=Clathrin adaptor complex small chain [Type chain P]=Disordered [Evidence chain P]=The corresponding region of a homologous protein has been shown to be disordered in the 398-458 region described in DisProt entry DP00123 (covers 100% of the sequence present in the structure). The protein region involved in the interaction contains an endocytic dileucine motif (consensus sequence: [ED]xxxL[LI]) (PMID:19140243). [Type chain S]=Ordered [Evidence chain S]=The Clathrin adaptor complex small chain domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01217). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2hf6. [Modified residues chain P]=phosphoserine#S#3 [Chain P name]=cDNA, FLJ79547, highly similar to T-cell surface glycoprotein CD4 [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=B0AZV7 [Chain P UniProt boundaries]=252-262 [Chain P UniProt coverage]=3.9% [Chain P UniRef90 accession]=UniRef90_B0AZV7 [Chain P UniRef90 boundaries]=252-262 [Chain S name]=AP-2 complex subunit sigma [Chain S source organism]=Mus musculus [Chain S UniProt accession]=P62743 [Chain S UniProt boundaries]=1-142 [Chain S UniProt coverage]=100% [Chain S UniRef90 accession]=UniRef90_P53680 [Chain S UniRef90 boundaries]=1-142 [Related structures]=2jkt [Entry] [Accession]=DI1000064 [Disorder status]=Confirmed [Kd]=1.54E-04 (PMID:10387074) [Name]=Regulatory domain of cardiac F77W-Troponin C in complex with the cardiac Troponin I switch peptide [Source organism]=Homo sapiens [PDB ID]=2kgb [PDB chain IDs]=I:C [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=EF-hand [Type chain I]=Disordered [Evidence chain I]=The C-terminal region of troponin I was shown to be intrinsically disordered (PMID:21322033). [Type chain C]=Ordered [Evidence chain C]=The EF-hand domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13833). A solved monomeric structure of the domain is represented by PDB ID 1ap4. [Chain I name]=Troponin I, cardiac muscle [Chain I source organism]=Homo sapiens [Chain I UniProt accession]=P19429 [Chain I UniProt boundaries]=145-164 [Chain I UniProt coverage]=9.5% [Chain I UniRef90 accession]=UniRef90_P19429 [Chain I UniRef90 boundaries]=145-164 [Chain C name]=Troponin C, slow skeletal and cardiac muscles [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P63316 [Chain C UniProt boundaries]=1-89 [Chain C UniProt coverage]=55.3% [Chain C UniRef90 accession]=UniRef90_P63316 [Chain C UniRef90 boundaries]=1-89 [Related structures]=1lxf,1mxl,2krd,2l1r,2mzp,1j1d,1j1e,2n7l,4y99 [Entry] [Accession]=DI1100014 [Disorder status]=Confirmed [Kd]=1.80E-07 [Name]=Mouse A1 bound to the BMF BH3-domain [Source organism]=Mus musculus [PDB ID]=2vog [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.9 [Domain]=Bcl-2 homology [Type chain B]=Disordered [Evidence chain B]=The 1-185 region described in DisProt entry DP00645 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_BH_BH3_1). [Type chain A]=Ordered [Evidence chain A]=Bcl-2 homology (BH) domains, such as the one involved in the interaction, are known to adopt a stable structure in isolation (see Pfam domain PF00452). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1pq0. [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain B name]=Bcl-2-modifying factor [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q91ZE9 [Chain B UniProt boundaries]=126-152 [Chain B UniProt coverage]=14.6% [Chain B UniRef90 accession]=UniRef90_Q91ZE9 [Chain B UniRef90 boundaries]=126-152 [Chain A name]=Bcl-2-related protein A1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q07440 [Chain A UniProt boundaries]=1-152 [Chain A UniProt coverage]=88.4% [Chain A UniRef90 accession]=UniRef90_Q07440 [Chain A UniRef90 boundaries]=1-152 [Entry] [Accession]=DI1000065 [Disorder status]=Confirmed [Kd]=1.80E-07 [Name]=Human BRD4 in complex with a diacetylated histone 4 peptide (H4K16acK20ac) [Source organism]=Homo sapiens [PDB ID]=3uvy [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.02 [Domain]=Bromodomain [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The 1-28 region described in IDEAL entry IID00058 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 2oss. [Modified residues chain B]=N(6)-acetyllysine#K#16|N(6)-acetyllysine#K#20 [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain B name]=Histone H4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P62805 [Chain B UniProt boundaries]=16-26 [Chain B UniProt coverage]=10.7% [Chain B UniRef90 accession]=UniRef90_P62805 [Chain B UniRef90 boundaries]=16-26 [Chain A name]=Bromodomain-containing protein 4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O60885 [Chain A UniProt boundaries]=42-168 [Chain A UniProt coverage]=9.3% [Chain A UniRef90 accession]=UniRef90_O60885 [Chain A UniRef90 boundaries]=42-168 [Entry] [Accession]=DI1000066 [Disorder status]=Confirmed [Kd]=4.61E-05 (PMID:22464331) [Name]=Human BRD4 in complex with a diacetylated histone 4 peptide (H4K12acK16ac) [Source organism]=Homo sapiens [PDB ID]=3uvx [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.91 [Domain]=Bromodomain [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The 1-28 region described in IDEAL entry IID00058 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 2oss. [Modified residues chain B]=N(6)-acetyllysine#K#12|N(6)-acetyllysine#K#16 [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain B name]=Histone H4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P62805 [Chain B UniProt boundaries]=11-17 [Chain B UniProt coverage]=6.8% [Chain B UniRef90 accession]=UniRef90_P62805 [Chain B UniRef90 boundaries]=11-17 [Chain A name]=Bromodomain-containing protein 4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O60885 [Chain A UniProt boundaries]=42-168 [Chain A UniProt coverage]=9.3% [Chain A UniRef90 accession]=UniRef90_O60885 [Chain A UniRef90 boundaries]=42-168 [Entry] [Accession]=DI2000002 [Disorder status]=Confirmed [Kd]=2.74E-05 (PMID:22464331) [Name]=Human BRD4 in complex with a diacetylated histone 4 peptide (H4K8acK12ac) [Source organism]=Homo sapiens [PDB ID]=3uw9 [PDB chain IDs]=E:AC [PDB note]=Chains B, D and F were removed as chains A, C and E represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=Bromodomain [Type chain E]=Disordered [Evidence chain E]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The 1-28 region described in IDEAL entry IID00058 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 2oss. [Type chain C]=Ordered [Evidence chain C]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 2oss. [Modified residues chain E]=N(6)-acetyllysine#K#1 [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain E name]=Histone H4 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P62805 [Chain E UniProt boundaries]=8-18 [Chain E UniProt coverage]=10.7% [Chain E UniRef90 accession]=UniRef90_P62805 [Chain E UniRef90 boundaries]=8-18 [Chain A name]=Bromodomain-containing protein 4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O60885 [Chain A UniProt boundaries]=42-168 [Chain A UniProt coverage]=9.3% [Chain A UniRef90 accession]=UniRef90_O60885 [Chain A UniRef90 boundaries]=42-168 [Chain C name]=Bromodomain-containing protein 4 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=O60885 [Chain C UniProt boundaries]=42-168 [Chain C UniProt coverage]=9.3% [Chain C UniRef90 accession]=UniRef90_O60885 [Chain C UniRef90 boundaries]=42-168 [Entry] [Accession]=DI1000067 [Disorder status]=Confirmed [Kd]=6.80E-06 (PMID:22464331) [Name]=Human BRD4 in complex with a diacetylated histone 4 peptide (H4K5acK8ac) [Source organism]=Homo sapiens [PDB ID]=3uvw [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.37 [Domain]=Bromodomain [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The 1-28 region described in IDEAL entry IID00058 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 2oss. [Modified residues chain B]=N(6)-acetyllysine#K#5|N(6)-acetyllysine#K#8 [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain B name]=Histone H4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P62805 [Chain B UniProt boundaries]=2-13 [Chain B UniProt coverage]=11.7% [Chain B UniRef90 accession]=UniRef90_P62805 [Chain B UniRef90 boundaries]=2-12 [Chain A name]=Bromodomain-containing protein 4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O60885 [Chain A UniProt boundaries]=42-168 [Chain A UniProt coverage]=9.3% [Chain A UniRef90 accession]=UniRef90_O60885 [Chain A UniRef90 boundaries]=42-168 [Entry] [Accession]=DI1000068 [Disorder status]=Confirmed [Kd]=6.80E-06 (PMID:22464331) [Name]=BRD4 bromodomain 1 in complex with acetylated Rel peptide from p65 [Source organism]=Homo sapiens [PDB ID]=4kv1 [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.50 [Domain]=Bromodomain [Type chain C]=Disordered [Evidence chain C]=The 302-320 region described in IDEAL entry IID00207 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 2oss. [Modified residues chain C]=N(6)-acetyllysine#K#202 [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain C name]=Transcription factor p65 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q04206 [Chain C UniProt boundaries]=308-314 [Chain C UniProt coverage]=1.3% [Chain C UniRef90 accession]=UniRef90_Q04206 [Chain C UniRef90 boundaries]=308-314 [Chain A name]=Bromodomain-containing protein 4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O60885 [Chain A UniProt boundaries]=41-168 [Chain A UniProt coverage]=9.4% [Chain A UniRef90 accession]=UniRef90_O60885 [Chain A UniRef90 boundaries]=41-168 [Entry] [Accession]=DI1000069 [Disorder status]=Confirmed [Kd]=4.60E-05 (PMID:23269674) [Name]=NSD3 tandem PHD5-C5HCH domains complexed with an unmodified H3.3 peptide [Source organism]=Homo sapiens [PDB ID]=4gnf [PDB chain IDs]=C:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.55 [Domain]=PHD zinc finger [Type chain C]=Disordered [Evidence chain C]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The 1-45 region described in IDEAL entry IID00239 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 4gnd. [Modified residues chain A]=N(6)-acetyllysine#K#14 [Chain C name]=Histone H3.3 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P84243 [Chain C UniProt boundaries]=2-16 [Chain C UniProt coverage]=11% [Chain C UniRef90 accession]=UniRef90_P84243 [Chain C UniRef90 boundaries]=2-16 [Chain A name]=Histone-lysine N-methyltransferase NSD3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9BZ95 [Chain A UniProt boundaries]=1307-1413 [Chain A UniProt coverage]=7.4% [Chain A UniRef90 accession]=UniRef90_Q9BZ95 [Chain A UniRef90 boundaries]=1310-1413 [Related structures]=4gne [Entry] [Accession]=DI1010034 [Disorder status]=Confirmed [Kd]=7.00E-09 (PMID:20972448) [Name]=Phi0 PKI NES peptide in complex with CRM1-RanGTP [Source organism]=Oryctolagus cuniculus / Homo sapiens [PDB ID]=2l1l [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=CRM1 [Type chain A]=Disordered [Evidence chain A]=The 1-76 region described in DisProt entry DP00015 and IDEAL entry IID00349 covers 100% of the sequence present in the structure. A close homologue (UniProt:P61925) is known to harbor afuncional linear motif (TRG_NES_CRM1_1) at this sequence region. [Type chain B]=Ordered [Evidence chain B]=The CRM1 domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 4bsm. [Modified residues chain B]=N(6)-acetyllysine#K#5|N(6)-acetyllysine#K#8 [Chain A name]=cAMP-dependent protein kinase inhibitor alpha [Chain A source organism]=Oryctolagus cuniculus [Chain A UniProt accession]=P61926 [Chain A UniProt boundaries]=30-54 [Chain A UniProt coverage]=32.9% [Chain A UniRef90 accession]=UniRef90_P61925 [Chain A UniRef90 boundaries]=30-54 [Chain B name]=Exportin-1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O14980 [Chain B UniProt boundaries]=504-630 [Chain B UniProt coverage]=11.9% [Chain B UniRef90 accession]=UniRef90_O14980 [Chain B UniRef90 boundaries]=504-630 [Entry] [Accession]=DI1000070 [Disorder status]=Confirmed [Kd]=7.00E-08 (PMID:19197237) [Name]=Pex14 in complex with Pex5 [Source organism]=Homo sapiens [PDB ID]=2w84 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Pex14 (N-terminal) [Type chain B]=Disordered [Evidence chain B]=The 1-324 region described in DisProt entry DP00472 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_Pex14_1). [Type chain A]=Ordered [Evidence chain A]=The N-terminal domain of Pex14 (see Pfam domain PF04695) has been shown by NMR to be ordered in its monomeric form (PMID:19197237). [Chain B name]=Peroxisomal targeting signal 1 receptor [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P50542 [Chain B UniProt boundaries]=108-127 [Chain B UniProt coverage]=3.1% [Chain B UniRef90 accession]=UniRef90_P50542 [Chain B UniRef90 boundaries]=108-127 [Chain A name]=Peroxisomal membrane protein PEX14 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O75381 [Chain A UniProt boundaries]=12-81 [Chain A UniProt coverage]=18.6% [Chain A UniRef90 accession]=UniRef90_O75381 [Chain A UniRef90 boundaries]=15-80 [Entry] [Accession]=DI1000071 [Disorder status]=Confirmed [Kd]=1.00E-07 (PMID:24235149) [Name]=Pex14 in complex with Pex5 LVxEF motif [Source organism]=Homo sapiens [PDB ID]=4bxu [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Pex14 (N-terminal) [Type chain B]=Disordered [Evidence chain B]=The 1-324 region described in DisProt entry DP00472 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_Pex14_3). [Type chain A]=Ordered [Evidence chain A]=The N-terminal domain of Pex14 (see Pfam domain PF04695) has been shown by NMR to be ordered in its monomeric form (PMID:19197237). [Chain B name]=Peroxisomal targeting signal 1 receptor [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P50542 [Chain B UniProt boundaries]=57-71 [Chain B UniProt coverage]=2.3% [Chain B UniRef90 accession]=UniRef90_P50542 [Chain B UniRef90 boundaries]=57-71 [Chain A name]=Peroxisomal membrane protein PEX14 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O75381 [Chain A UniProt boundaries]=12-80 [Chain A UniProt coverage]=18.3% [Chain A UniRef90 accession]=UniRef90_O75381 [Chain A UniRef90 boundaries]=15-80 [Entry] [Accession]=DI1000072 [Disorder status]=Confirmed [Kd]=3.00E-06 (PMID:27725184) [Name]=STAM2 SH3 with AMSH derived peptide [Source organism]=Homo sapiens [PDB ID]=5ixf [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH3 [Type chain B]=Disordered [Evidence chain B]=The 219-251 region described in IDEAL entry IID00261 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a specialised SH3-binding motif PX[VI][DN]RXXKP motif that binds the SH3 domains of STAM1 and STAM2/EAST/Hbp, a family of proteins involved in cytokine signaling and receptor-mediated endocytosis and exocytosis (PMID:10982817). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00018). A solved monomeric structure of the domain is represented by PDB ID 1x2q. [Chain B name]=STAM-binding protein (Fragment) [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=C9JK83 [Chain B UniProt boundaries]=228-241 [Chain B UniProt coverage]=4.4% [Chain B UniRef90 accession]=UniRef90_O95630 [Chain B UniRef90 boundaries]=228-241 [Chain A name]=Signal transducing adapter molecule 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O75886 [Chain A UniProt boundaries]=157-265 [Chain A UniProt coverage]=20.8% [Chain A UniRef90 accession]=UniRef90_O75886 [Chain A UniRef90 boundaries]=162-265 [Entry] [Accession]=DI1000073 [Disorder status]=Confirmed [Kd]=2.00E-05 [Name]=53BP1 tandem Tudor domains in complex with a p53K370me2 peptide [Source organism]=Homo sapiens [PDB ID]=2mwo [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Tudor-like [Type chain B]=Disordered [Evidence chain B]=The 320-393 region described in DisProt entry DP00086 and the 364-389 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (DOC_USP7_MATH_1). [Type chain A]=Ordered [Evidence chain A]=The Tudor-like domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF09038). A solved monomeric structure of the domain is represented by PDB ID 2g3r. [Modified residues chain B]=N-dimethyl-lysine#K#370 [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=363-377 [Chain B UniProt coverage]=3.8% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=363-377 [Chain A name]=Tumor suppressor p53-binding protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q12888 [Chain A UniProt boundaries]=1481-1603 [Chain A UniProt coverage]=6.2% [Chain A UniRef90 accession]=UniRef90_Q12888 [Chain A UniRef90 boundaries]=1484-1603 [Entry] [Accession]=DI1000074 [Disorder status]=Confirmed [Kd]=9.00E-07 [Name]=53BP1 tandem Tudor domains in complex with a p53K382me2 peptide [Source organism]=Homo sapiens [PDB ID]=2mwp [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Tudor-like [Type chain B]=Disordered [Evidence chain B]=The 320-393 region described in DisProt entry DP00086 and the 364-389 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (DOC_CYCLIN_1). [Type chain A]=Ordered [Evidence chain A]=The Tudor-like domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF09038). A solved monomeric structure of the domain is represented by PDB ID 2g3r. [Modified residues chain B]=N-dimethyl-lysine#K#382 [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=376-387 [Chain B UniProt coverage]=3.1% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=376-387 [Chain A name]=Tumor suppressor p53-binding protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q12888 [Chain A UniProt boundaries]=1481-1603 [Chain A UniProt coverage]=6.2% [Chain A UniRef90 accession]=UniRef90_Q12888 [Chain A UniRef90 boundaries]=1484-1603 [Entry] [Accession]=DI1100015 [Disorder status]=Confirmed [Kd]=1.01E-05 (PMID:22195967) [Name]=Central activation domain of Gcn4 bound to the mediator co-activator domain 1 of Gal11/med15 [Source organism]=Saccharomyces cerevisiae [PDB ID]=2lpb [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Mediator co-activator domain 1 [Type chain B]=Disordered [Evidence chain B]=The 101-134 region described in DisProt entry DP00083 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a hydrophobic motif WTSLF motif (consensus sequence: ZxxZZ; Z is hydrophobic residue) able to adopt a helical fold when bound to its targets (PMID:22195967). [Type chain A]=Ordered [Evidence chain A]=The mediator co-activator domain 1 of Gal11 has been shown to be ordered using NMR (PMID:22195967). [Chain B name]=General control protein GCN4 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P03069 [Chain B UniProt boundaries]=101-134 [Chain B UniProt coverage]=12.1% [Chain B UniRef90 accession]=UniRef90_P03069 [Chain B UniRef90 boundaries]=101-134 [Chain A name]=Mediator of RNA polymerase II transcription subunit 15 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P19659 [Chain A UniProt boundaries]=158-238 [Chain A UniProt coverage]=7.5% [Chain A UniRef90 accession]=UniRef90_P19659 [Chain A UniRef90 boundaries]=170-232 [Entry] [Accession]=DI1120004 [Disorder status]=Confirmed [Kd]=5.21E-05 (PMID:17437719) [Name]=Mouse Itch 3rd WW domain complex with the Epstein-Barr virus latent membrane protein 2A derived peptide [Source organism]=Epstein-Barr virus / Mus musculus [PDB ID]=2jo9 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=WW [Type chain B]=Disordered [Evidence chain B]=The 1-118 region described in DisProt entry DP01060 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_WW_1). [Type chain A]=Ordered [Evidence chain A]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain is represented by PDB ID 1yiu. [Chain B name]=Latent membrane protein 2 [Chain B source organism]=Epstein-Barr virus [Chain B UniProt accession]=P13285 [Chain B UniProt boundaries]=54-62 [Chain B UniProt coverage]=1.8% [Chain B UniRef90 accession]=UniRef90_P13285 [Chain B UniRef90 boundaries]=97-101 [Chain A name]=E3 ubiquitin-protein ligase Itchy [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q8C863 [Chain A UniProt boundaries]=396-432 [Chain A UniProt coverage]=4.3% [Chain A UniRef90 accession]=UniRef90_Q96J02-3 [Chain A UniRef90 boundaries]=286-320 [Entry] [Accession]=DI1100016 [Disorder status]=Confirmed [Kd]=4.30E-04 [Name]=Nedd4 WW2 Domain-Cx43CT Peptide Complex [Source organism]=Rattus norvegicus [PDB ID]=2n8t [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=WW [Type chain B]=Disordered [Evidence chain B]=The 255-316 region described in DisProt entry DP00278 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a PPXY motif (PMID:26841867). [Type chain A]=Ordered [Evidence chain A]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain is represented by PDB ID 2n8u. [Modified residues chain B]=phosphoserine#S#43|phosphoserine#S#46 [Chain B name]=Gap junction alpha-1 protein [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=P08050 [Chain B UniProt boundaries]=276-289 [Chain B UniProt coverage]=3.7% [Chain B UniRef90 accession]=UniRef90_P17302 [Chain B UniRef90 boundaries]=276-289 [Chain A name]=E3 ubiquitin-protein ligase NEDD4 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=Q62940 [Chain A UniProt boundaries]=399-437 [Chain A UniProt coverage]=4.4% [Chain A UniRef90 accession]=UniRef90_P46935 [Chain A UniRef90 boundaries]=403-440 [Entry] [Accession]=DI1000075 [Disorder status]=Confirmed [Kd]=4.98E-05 (PMID:24997600) [Name]=CID of human RPRD1A in complex with a phosphorylated peptide from RPB1-CTD [Source organism]=Homo sapiens [PDB ID]=4jxt [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=CID [Type chain B]=Disordered [Evidence chain B]=The 1593-1960 region described in IDEAL entry IID00126 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The CID domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04818). A solved monomeric structure of the domain is represented by PDB ID 4nac. [Modified residues chain B]=phosphoserine#S#1621|phosphoserine#S#1628 [Chain B name]=DNA-directed RNA polymerase II subunit RPB1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P24928 [Chain B UniProt boundaries]=1611-1631 [Chain B UniProt coverage]=1.1% [Chain B UniRef90 accession]=UniRef90_P24928 [Chain B UniRef90 boundaries]=1913-1931 [Chain A name]=Regulation of nuclear pre-mRNA domain-containing protein 1A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96P16 [Chain A UniProt boundaries]=1-137 [Chain A UniProt coverage]=43.9% [Chain A UniRef90 accession]=UniRef90_Q96P16 [Chain A UniRef90 boundaries]=1-137 [Entry] [Accession]=DI1000076 [Disorder status]=Confirmed [Kd]=4.98E-05 (PMID:24997600) [Name]=Second WW domain from human YAP in complex with a human Smad1 derived peptide [Source organism]=Homo sapiens [PDB ID]=2law [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=WW [Type chain B]=Disordered [Evidence chain B]=The 217-269 region described in IDEAL entry IID00174 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_WW_1). [Type chain A]=Ordered [Evidence chain A]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2n8u. [Chain B name]=Mothers against decapentaplegic homolog 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q15797 [Chain B UniProt boundaries]=222-233 [Chain B UniProt coverage]=2.6% [Chain B UniRef90 accession]=UniRef90_Q15797 [Chain B UniRef90 boundaries]=222-233 [Chain A name]=Transcriptional coactivator YAP1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P46937 [Chain A UniProt boundaries]=227-263 [Chain A UniProt coverage]=7.3% [Chain A UniRef90 accession]=UniRef90_P46937 [Chain A UniRef90 boundaries]=227-263 [Entry] [Accession]=DI1110006 [Disorder status]=Confirmed [Kd]=2.40E-05 (PMID:18638481) [Name]=Talin F3 in complex with layilin cytodomain [Source organism]=Mus musculus / Gallus gallus [PDB ID]=2k00 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PH-like [Type chain B]=Disordered [Evidence chain B]=The 367-381 region described in IDEAL entry IID50232 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_PTB_Apo_2). [Type chain A]=Ordered [Evidence chain A]=The PH-like domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1mix. [Chain B name]=Layilin [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q8C351 [Chain B UniProt boundaries]=367-381 [Chain B UniProt coverage]=3.9% [Chain B UniRef90 accession]=UniRef90_Q8C351 [Chain B UniRef90 boundaries]=367-381 [Chain A name]=Talin-1 [Chain A source organism]=Gallus gallus [Chain A UniProt accession]=P54939 [Chain A UniProt boundaries]=309-400 [Chain A UniProt coverage]=3.6% [Chain A UniRef90 accession]=UniRef90_P54939 [Chain A UniRef90 boundaries]=309-400 [Entry] [Accession]=DI1000077 [Disorder status]=Confirmed [Kd]=2.90E-05 (PMID:23104054) [Name]=Tudor domain of PHD finger protein 19 in complex with histone H3 tail [Source organism]=Homo sapiens [PDB ID]=4bd3 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Tudor [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The 1-60 region described in IDEAL entry IID00062 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Tudor domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 2e5q. [Modified residues chain B]=N-trimethyllysine#K#36 [Chain B name]=Histone H3.1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68431 [Chain B UniProt boundaries]=32-42 [Chain B UniProt coverage]=8.1% [Chain B UniRef90 accession]=UniRef90_P68431 [Chain B UniRef90 boundaries]=32-42 [Chain A name]=PHD finger protein 19 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q5T6S3 [Chain A UniProt boundaries]=38-95 [Chain A UniProt coverage]=10% [Chain A UniRef90 accession]=UniRef90_Q5T6S3 [Chain A UniRef90 boundaries]=38-95 [Entry] [Accession]=DI1000078 [Disorder status]=Confirmed [Kd]=1.97E-05 (PMID:17190600) [Name]=Human 53BP1 tandem Tudor domains in complex with a histone H4K20me2 peptide [Source organism]=Homo sapiens [PDB ID]=2lvm [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Tudor-like [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The 1-28 region described in IDEAL entry IID00058 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Tudor-like domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF09038). A solved monomeric structure of the domain is represented by PDB ID 2g3r. [Modified residues chain B]=N-dimethyl-lysine#K#20 [Chain B name]=Histone H4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P62805 [Chain B UniProt boundaries]=15-28 [Chain B UniProt coverage]=13.6% [Chain B UniRef90 accession]=UniRef90_P62805 [Chain B UniRef90 boundaries]=18-28 [Chain A name]=Tumor suppressor p53-binding protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q12888 [Chain A UniProt boundaries]=1481-1603 [Chain A UniProt coverage]=6.2% [Chain A UniRef90 accession]=UniRef90_Q12888 [Chain A UniRef90 boundaries]=1484-1603 [Related structures]=2ig0 [Entry] [Accession]=DI1010035 [Disorder status]=Confirmed [Kd]=1.97E-05 (PMID:17190600) [Name]=Third WW domain of human Nedd4L in complex with doubly phosphorylated human Smad3 derived peptide [Source organism]=Homo sapiens / Mus musculus [PDB ID]=2laj [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=WW [Type chain B]=Disordered [Evidence chain B]=The 146-229 region described in IDEAL entry IID00113 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (DOC_WW_Pin1_4). [Type chain A]=Ordered [Evidence chain A]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain from a closely homologous protein is represented by PDB ID 1wr7. [Modified residues chain B]=phosphoserine#S#204|phosphoserine#S#208 [Chain B name]=Mothers against decapentaplegic homolog 3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P84022 [Chain B UniProt boundaries]=202-211 [Chain B UniProt coverage]=2.4% [Chain B UniRef90 accession]=UniRef90_P84022 [Chain B UniRef90 boundaries]=202-211 [Chain A name]=E3 ubiquitin-protein ligase NEDD4-like [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q8CFI0 [Chain A UniProt boundaries]=525-564 [Chain A UniProt coverage]=4% [Chain A UniRef90 accession]=UniRef90_Q96PU5 [Chain A UniRef90 boundaries]=496-535 [Entry] [Accession]=DI1000079 [Disorder status]=Confirmed [Kd]=1.97E-05 (PMID:17190600) [Name]=Second WW domain of human Nedd4L in complex with a phosphorylated human Smad3 derived peptide [Source organism]=Homo sapiens [PDB ID]=2lb2 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=WW [Type chain B]=Disordered [Evidence chain B]=The 146-229 region described in IDEAL entry IID00113 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (DOC_WW_Pin1_4). [Type chain A]=Ordered [Evidence chain A]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain from a closely homologous protein is represented by PDB ID 1wr4. [Modified residues chain B]=phosphothreonine#T#179 [Chain B name]=Mothers against decapentaplegic homolog 3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P84022 [Chain B UniProt boundaries]=178-189 [Chain B UniProt coverage]=2.8% [Chain B UniRef90 accession]=UniRef90_P84022 [Chain B UniRef90 boundaries]=178-189 [Chain A name]=E3 ubiquitin-protein ligase NEDD4-like [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96PU5 [Chain A UniProt boundaries]=386-420 [Chain A UniProt coverage]=3.6% [Chain A UniRef90 accession]=UniRef90_Q96PU5 [Chain A UniRef90 boundaries]=386-420 [Entry] [Accession]=DI1000080 [Disorder status]=Confirmed [Kd]=3.05E-05 (PMID:28241141) [Name]=ENL YEATS in complex with histone H3 acetylation at K27 [Source organism]=Homo sapiens [PDB ID]=5j9s [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.70 [Domain]=YEATS [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The 1-60 region described in IDEAL entry IID00062 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The YEATS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03366). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3rls. [Modified residues chain B]=N(6)-acetyllysine#K#27 [Chain B name]=Histone H3.1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68431 [Chain B UniProt boundaries]=16-40 [Chain B UniProt coverage]=18.4% [Chain B UniRef90 accession]=UniRef90_P68431 [Chain B UniRef90 boundaries]=16-40 [Chain A name]=Protein ENL [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q03111 [Chain A UniProt boundaries]=1-154 [Chain A UniProt coverage]=27.5% [Chain A UniRef90 accession]=UniRef90_Q03111 [Chain A UniRef90 boundaries]=1-148 [Entry] [Accession]=DI1000081 [Disorder status]=Confirmed [Kd]=5.95E-05 (PMID:27545619) [Name]=AF9 YEATS domain in complex with histone H3.1 acetylation at K18 [Source organism]=Homo sapiens [PDB ID]=2ndf [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=YEATS [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The YEATS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03366). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3rls. [Modified residues chain B]=N(6)-acetyllysine#K#218 [Chain B name]=Histone H3.1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68431 [Chain B UniProt boundaries]=13-25 [Chain B UniProt coverage]=9.6% [Chain B UniRef90 accession]=UniRef90_P68431 [Chain B UniRef90 boundaries]=13-25 [Chain A name]=Protein AF-9 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P42568 [Chain A UniProt boundaries]=1-138 [Chain A UniProt coverage]=24.3% [Chain A UniRef90 accession]=UniRef90_P42568 [Chain A UniRef90 boundaries]=1-138 [Entry] [Accession]=DI1000082 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:25417107) [Name]=AF9 YEATS domain in complex with histone H3.3 acetylation at K9 [Source organism]=Homo sapiens [PDB ID]=4tmp [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=YEATS [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The 1-45 region described in IDEAL entry IID00239 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The YEATS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03366). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3rls. [Modified residues chain B]=N(6)-acetyllysine#K#9 [Chain B name]=Histone H3.3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P84243 [Chain B UniProt boundaries]=2-12 [Chain B UniProt coverage]=8.1% [Chain B UniRef90 accession]=UniRef90_P84243 [Chain B UniRef90 boundaries]=2-12 [Chain A name]=Protein AF-9 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P42568 [Chain A UniProt boundaries]=1-138 [Chain A UniProt coverage]=24.3% [Chain A UniRef90 accession]=UniRef90_P42568 [Chain A UniRef90 boundaries]=1-138 [Entry] [Accession]=DI1100017 [Disorder status]=Confirmed [Kd]=9.50E-06 (PMID:27089029) [Name]=Taf14 YEATS domain in complex with H3K9ac [Source organism]=Saccharomyces cerevisiae [PDB ID]=5d7e [PDB chain IDs]=C:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=YEATS [Type chain C]=Disordered [Evidence chain C]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The YEATS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03366). A solved monomeric structure of the domain is represented by PDB ID 2l7e. [Modified residues chain C]=N(6)-acetyllysine#K#8 [Chain C name]=Histone H3 [Chain C source organism]=Saccharomyces cerevisiae [Chain C UniProt accession]=P61830 [Chain C UniProt boundaries]=6-12 [Chain C UniProt coverage]=5.1% [Chain C UniRef90 accession]=UniRef90_Q757N1 [Chain C UniRef90 boundaries]=6-12 [Chain A name]=Transcription initiation factor TFIID subunit 14 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P35189 [Chain A UniProt boundaries]=1-137 [Chain A UniProt coverage]=56.1% [Chain A UniRef90 accession]=UniRef90_P35189 [Chain A UniRef90 boundaries]=1-137 [Related structures]=5iok [Entry] [Accession]=DI1000083 [Disorder status]=Confirmed [Kd]=2.10E-06 (PMID:27105114) [Name]=AF9 YEATS in complex with histone H3.1 Crotonylation at K9 [Source organism]=Homo sapiens [PDB ID]=5hjb [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.70 [Domain]=YEATS [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The YEATS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03366). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3rls. [Modified residues chain B]=N-6-crotonyl-L-lysine#K#9 [Chain B name]=Histone H3.1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68431 [Chain B UniProt boundaries]=4-9 [Chain B UniProt coverage]=4.4% [Chain B UniRef90 accession]=UniRef90_P68431 [Chain B UniRef90 boundaries]=4-9 [Chain A name]=Protein AF-9 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P42568 [Chain A UniProt boundaries]=1-138 [Chain A UniProt coverage]=24.3% [Chain A UniRef90 accession]=UniRef90_P42568 [Chain A UniRef90 boundaries]=1-138 [Entry] [Accession]=DI1000084 [Disorder status]=Confirmed [Kd]=3.17E-05 (PMID:27103431) [Name]=YEATS2 YEATS domain bound to H3K27cr peptide [Source organism]=Homo sapiens [PDB ID]=5iql [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=YEATS [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The YEATS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03366). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3rls. [Modified residues chain B]=N-6-crotonyl-L-lysine#K#27 [Chain B name]=Histone H3.1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68431 [Chain B UniProt boundaries]=25-32 [Chain B UniProt coverage]=5.9% [Chain B UniRef90 accession]=UniRef90_P68431 [Chain B UniRef90 boundaries]=25-32 [Chain A name]=YEATS domain-containing protein 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9ULM3 [Chain A UniProt boundaries]=200-332 [Chain A UniProt coverage]=9.4% [Chain A UniRef90 accession]=UniRef90_Q9ULM3 [Chain A UniRef90 boundaries]=201-332 [Entry] [Accession]=DI1010036 [Disorder status]=Confirmed [Kd]=3.17E-05 (PMID:27103431) [Name]=NRSF/REST-mSin3B PAH1 complex [Source organism]=Homo sapiens / Mus musculus [PDB ID]=2czy [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PAH [Type chain B]=Disordered [Evidence chain B]=The 1-83 region described in IDEAL entry IID00169 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a PAH1-interaction motif LIMLAXVAL (consensus sequence: LXXLZX(V/A)A; X is any non-proline residue, Z is hydrophobic) (PMID:16288918). [Type chain A]=Ordered [Evidence chain A]=The PAH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02671). A solved monomeric structure of the domain is represented by PDB ID 2cr7. [Chain B name]=RE1-silencing transcription factor [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q13127 [Chain B UniProt boundaries]=43-57 [Chain B UniProt coverage]=1.4% [Chain B UniRef90 accession]=UniRef90_Q13127 [Chain B UniRef90 boundaries]=43-57 [Chain A name]=Paired amphipathic helix protein Sin3b [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q62141 [Chain A UniProt boundaries]=31-107 [Chain A UniProt coverage]=7% [Chain A UniRef90 accession]=UniRef90_Q62141 [Chain A UniRef90 boundaries]=31-107 [Entry] [Accession]=DI1000085 [Disorder status]=Confirmed [Kd]=3.17E-05 (PMID:27103431) [Name]=Second WW domain of Smurf1 in complex with a Smad1 derived peptide [Source organism]=Homo sapiens [PDB ID]=2lb1 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=WW [Type chain B]=Disordered [Evidence chain B]=The 217-269 region described in IDEAL entry IID00174 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2n8u. [Chain B name]=Mothers against decapentaplegic homolog 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q15797 [Chain B UniProt boundaries]=220-234 [Chain B UniProt coverage]=3.2% [Chain B UniRef90 accession]=UniRef90_Q15797 [Chain B UniRef90 boundaries]=220-233 [Chain A name]=E3 ubiquitin-protein ligase SMURF1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9HCE7 [Chain A UniProt boundaries]=305-340 [Chain A UniProt coverage]=4.8% [Chain A UniRef90 accession]=UniRef90_Q9HCE7 [Chain A UniRef90 boundaries]=305-340 [Entry] [Accession]=DI1100018 [Disorder status]=Confirmed [Kd]=3.17E-05 (PMID:27103431) [Name]=mSin3A PAH1-SAP25 SID complex [Source organism]=Mus musculus [PDB ID]=2rms [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PAH [Type chain B]=Disordered [Evidence chain B]=The 126-186 region described in IDEAL entry IID50088 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a PAH1-interaction motif LXXLL (consensus sequence: sZxsZZxZs; S is residue with short side chain, Z is bulky hydrophobic, x is any non-proline) (PMID:18089292). [Type chain A]=Ordered [Evidence chain A]=The PAH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02671). A solved monomeric structure of the domain is represented by PDB ID 2rmr. [Chain B name]=Histone deacetylase complex subunit SAP25 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q1EHW4 [Chain B UniProt boundaries]=126-186 [Chain B UniProt coverage]=32.8% [Chain B UniRef90 accession]=UniRef90_Q1EHW4 [Chain B UniRef90 boundaries]=126-186 [Chain A name]=Paired amphipathic helix protein Sin3a [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q60520 [Chain A UniProt boundaries]=119-189 [Chain A UniProt coverage]=5.6% [Chain A UniRef90 accession]=UniRef90_Q60520 [Chain A UniRef90 boundaries]=119-189 [Entry] [Accession]=DI1010037 [Disorder status]=Confirmed [Kd]=2.90E-08 (PMID:11106735) [Name]=Mad1 SID bound to mSin3A PAH2 [Source organism]=Homo sapiens / Mus musculus [PDB ID]=1s5q [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PAH [Type chain A]=Disordered [Evidence chain A]=The 8-20 region described in IDEAL entry IID00165 covers 81% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_Sin3_1). [Type chain B]=Ordered [Evidence chain B]=The PAH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02671). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2rmr. [Chain A name]=Max dimerization protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q05195 [Chain A UniProt boundaries]=6-21 [Chain A UniProt coverage]=7.2% [Chain A UniRef90 accession]=UniRef90_Q05195 [Chain A UniRef90 boundaries]=6-21 [Chain B name]=Paired amphipathic helix protein Sin3a [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q60520 [Chain B UniProt boundaries]=295-383 [Chain B UniProt coverage]=7% [Chain B UniRef90 accession]=UniRef90_Q60520 [Chain B UniRef90 boundaries]=295-383 [Related structures]=1g1e [Entry] [Accession]=DI1100019 [Disorder status]=Confirmed [Kd]=5.20E-06 (PMID:11106735) [Name]=HBP1 SID bound to mSin3A PAH2 [Source organism]=Mus musculus [PDB ID]=1s5r [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PAH [Type chain A]=Disordered [Evidence chain A]=The 358-380 region described in IDEAL entry IID50097 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a PAH2-interaction motif (consensus sequenve: A(A/V)xZZxxZ; Z is hydrophobic) (PMID:15235594). [Type chain B]=Ordered [Evidence chain B]=The PAH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02671). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2rmr. [Chain A name]=HMG box-containing protein 1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q8R316 [Chain A UniProt boundaries]=358-380 [Chain A UniProt coverage]=4.5% [Chain A UniRef90 accession]=UniRef90_Q8R316 [Chain A UniRef90 boundaries]=358-380 [Chain B name]=Paired amphipathic helix protein Sin3a [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q60520 [Chain B UniProt boundaries]=295-383 [Chain B UniProt coverage]=7% [Chain B UniRef90 accession]=UniRef90_Q60520 [Chain B UniRef90 boundaries]=295-383 [Entry] [Accession]=DI1010038 [Disorder status]=Confirmed [Kd]=2.20E-06 (PMID:21440557) [Name]=Pf1 SID1 bound to mSin3A PAH2 [Source organism]=Homo sapiens / Mus musculus [PDB ID]=2l9s [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PAH [Type chain A]=Disordered [Evidence chain A]=The 200-241 region described in IDEAL entry IID00326 covers 93% of the sequence present in the structure. The protein region involved in the interaction contains a SID1 (or Type I PAH2 interaction) motif (consensus sequence: ZxxZZxAAxxZ-; Z is F, I, L, M, or V; -: E or D) (PMID:21440557). [Type chain B]=Ordered [Evidence chain B]=The PAH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02671). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2rmr. [Chain A name]=PHD finger protein 12 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96QT6 [Chain A UniProt boundaries]=197-241 [Chain A UniProt coverage]=4.5% [Chain A UniRef90 accession]=UniRef90_Q96QT6 [Chain A UniRef90 boundaries]=200-241 [Chain B name]=Paired amphipathic helix protein Sin3a [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q60520 [Chain B UniProt boundaries]=292-385 [Chain B UniProt coverage]=7.4% [Chain B UniRef90 accession]=UniRef90_Q60520 [Chain B UniRef90 boundaries]=295-385 [Entry] [Accession]=DI1120005 [Disorder status]=Inferred from homology [Kd]=2.20E-06 (PMID:21440557) [Name]=vSET in complex with meK27 H3 peptide [Source organism]=Strongylocentrotus purpuratus / Paramecium bursaria Chlorella virus 1 [PDB ID]=2g46 [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=NMR [Domain]=SET [Type chain C]=Disordered [Evidence chain C]=The corresponding region of a closely homologous protein has been shown to be disordered in the 1-38 region described in IDEAL entry IID00086 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The SET domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00856). A solved structure of the domain without bound ligands is represented by PDB ID 1n3j. [Modified residues chain C]=N-methyl-lysine#K#215 [Chain C name]=Histone H3, embryonic [Chain C source organism]=Strongylocentrotus purpuratus [Chain C UniProt accession]=P06352 [Chain C UniProt boundaries]=14-34 [Chain C UniProt coverage]=15.4% [Chain C UniRef90 accession]=UniRef90_Q16695 [Chain C UniRef90 boundaries]=14-34 [Chain A name]=Histone H3K27 methylase [Chain A source organism]=Paramecium bursaria Chlorella virus 1 [Chain A UniProt accession]=O41094 [Chain A UniProt boundaries]=1-119 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_O41094 [Chain A UniRef90 boundaries]=1-119 [Entry] [Accession]=DI1000086 [Disorder status]=Confirmed [Kd]=1.10E-06 (PMID:17589525) [Name]=UHM domain of human SPF45 in complex with SF3b155-ULM5 [Source organism]=Homo sapiens [PDB ID]=2peh [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.11 [Domain]=RRM [Type chain C]=Disordered [Evidence chain C]=The 190-344 region described in IDEAL entry IID00190 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_ULM_U2AF65_1). [Type chain A]=Ordered [Evidence chain A]=The RRM domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00076). A solved monomeric structure of the domain is represented by PDB ID 2pe8. [Chain C name]=Splicing factor 3B subunit 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=O75533 [Chain C UniProt boundaries]=333-342 [Chain C UniProt coverage]=0.8% [Chain C UniRef90 accession]=UniRef90_O75533 [Chain C UniRef90 boundaries]=333-342 [Chain A name]=Splicing factor 45 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96I25 [Chain A UniProt boundaries]=297-401 [Chain A UniProt coverage]=26.2% [Chain A UniRef90 accession]=UniRef90_Q96I25 [Chain A UniRef90 boundaries]=301-401 [Entry] [Accession]=DI2020001 [Disorder status]=Confirmed [Kd]=1.50E-05 [Name]=VP16 binding to PC4 [Source organism]=Human herpesvirus 1 / Homo sapiens [PDB ID]=2phe [PDB chain IDs]=C:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PC4 [Type chain C]=Disordered [Evidence chain C]=The 403-490 region described in IDEAL entry IID90007 covers 100% of the sequence present in the structure. [Type chain A]=Ordered component [Evidence chain A]=The PC4 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF02229). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1pcf. [Type chain B]=Ordered component [Evidence chain B]=The PC4 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF02229). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1pcf. [Chain C name]=Tegument protein VP16 [Chain C source organism]=Human herpesvirus 1 [Chain C UniProt accession]=P06492 [Chain C UniProt boundaries]=465-490 [Chain C UniProt coverage]=5.3% [Chain C UniRef90 accession]=UniRef90_P06492 [Chain C UniRef90 boundaries]=465-490 [Chain A name]=Activated RNA polymerase II transcriptional coactivator p15 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P53999 [Chain A UniProt boundaries]=62-127 [Chain A UniProt coverage]=52% [Chain A UniRef90 accession]=UniRef90_P53999 [Chain A UniRef90 boundaries]=63-127 [Chain B name]=Activated RNA polymerase II transcriptional coactivator p15 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P53999 [Chain B UniProt boundaries]=62-127 [Chain B UniProt coverage]=52% [Chain B UniRef90 accession]=UniRef90_P53999 [Chain B UniRef90 boundaries]=63-127 [Entry] [Accession]=DI2100001 [Disorder status]=Confirmed [Kd]=1.80E-06 (PMID:21217703) [Name]=Sir3 peptide bound to RAP1 [Source organism]=Saccharomyces cerevisiae [PDB ID]=3owt [PDB chain IDs]=C:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Rap1 C terminal [Type chain C]=Disordered [Evidence chain C]=The 216-549 region described in DisProt entry DP00533 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a spRap1-binding motif (RBM) (PMID:21217703). [Type chain A]=Ordered [Evidence chain A]=The Rap1 C terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF11626). A solved structure of the domain without bound ligands is represented by PDB ID 3cz6. [Type chain B]=Ordered [Evidence chain B]=The Rap1 C terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF11626). A solved structure of the domain without bound ligands is represented by PDB ID 3cz6. [Chain C name]=Regulatory protein SIR3 [Chain C source organism]=Saccharomyces cerevisiae [Chain C UniProt accession]=P06701 [Chain C UniProt boundaries]=455-481 [Chain C UniProt coverage]=2.8% [Chain C UniRef90 accession]=UniRef90_P06701 [Chain C UniRef90 boundaries]=456-481 [Chain A name]=DNA-binding protein RAP1 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P11938 [Chain A UniProt boundaries]=671-827 [Chain A UniProt coverage]=19% [Chain A UniRef90 accession]=UniRef90_P11938 [Chain A UniRef90 boundaries]=672-827 [Chain B name]=DNA-binding protein RAP1 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P11938 [Chain B UniProt boundaries]=671-827 [Chain B UniProt coverage]=19% [Chain B UniRef90 accession]=UniRef90_P11938 [Chain B UniRef90 boundaries]=672-827 [Entry] [Accession]=DI2010002 [Disorder status]=Confirmed [Kd]=2.56E-07 (PMID:20708017) [Name]=AML1-ETO Nervy domain - PKA(RIIa) complex [Source organism]=Mus musculus / Homo sapiens [PDB ID]=2kyg [PDB chain IDs]=C:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=RIIa [Type chain C]=Disordered [Evidence chain C]=The 437-467 region described in IDEAL entry IID00381 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains AKAP (A-Kinase Anchoring Protein) sequence motifs (with consensus amphipathic helical structure) (PMID:20708017). [Type chain A]=Ordered component [Evidence chain A]=The RIIa domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF02197). A solved structure of the domain dimer from a homologous protein without bound ligands is represented by PDB ID 1l6e. [Type chain B]=Ordered component [Evidence chain B]=The RIIa domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF02197). A solved structure of the domain dimer from a homologous protein without bound ligands is represented by PDB ID 1l6e. [Chain C name]=Protein CBFA2T1 [Chain C source organism]=Mus musculus [Chain C UniProt accession]=Q61909 [Chain C UniProt boundaries]=410-440 [Chain C UniProt coverage]=5.4% [Chain C UniRef90 accession]=UniRef90_Q06455 [Chain C UniRef90 boundaries]=437-467 [Chain A name]=cAMP-dependent protein kinase type II-alpha regulatory subunit [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P13861 [Chain A UniProt boundaries]=1-45 [Chain A UniProt coverage]=11.1% [Chain A UniRef90 accession]=UniRef90_P13861 [Chain A UniRef90 boundaries]=1-45 [Chain B name]=cAMP-dependent protein kinase type II-alpha regulatory subunit [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P13861 [Chain B UniProt boundaries]=1-45 [Chain B UniProt coverage]=11.1% [Chain B UniRef90 accession]=UniRef90_P13861 [Chain B UniRef90 boundaries]=1-45 [Entry] [Accession]=DI1010039 [Disorder status]=Confirmed [Kd]=3.40E-05 (PMID:18025461) [Name]=RAG2-PHD finger in complex with H3.1 histone peptide (H3K4me3) [Source organism]=Homo sapiens / Mus musculus [PDB ID]=2v83 [PDB chain IDs]=D:A [PDB note]=Chains B, C and E were removed as chains A and D highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.4 [Domain]=RAG2 PHD [Type chain D]=Disordered [Evidence chain D]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The corresponding region of a closely homologous protein has been shown to be disordered in the 1-38 region described in IDEAL entry IID00086 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The RAG2 PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13341). A solved monomeric structure of the domain is represented by PDB ID 2jwo. [Modified residues chain D]=N-trimethyllysine#K#4 [Chain D name]=Histone H3 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=Q5TEC6 [Chain D UniProt boundaries]=2-10 [Chain D UniProt coverage]=6.6% [Chain D UniRef90 accession]=UniRef90_Q16695 [Chain D UniRef90 boundaries]=2-10 [Chain A name]=V(D)J recombination-activating protein 2 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P21784 [Chain A UniProt boundaries]=406-487 [Chain A UniProt coverage]=15.6% [Chain A UniRef90 accession]=UniRef90_P21784 [Chain A UniRef90 boundaries]=414-487 [Related structures]=2v89 [Entry] [Accession]=DI1100020 [Disorder status]=Confirmed [Kd]=3.46E-05 (PMID:18025461) [Name]=RAG2-PHD finger in complex with H3.1 histone peptide (H3K4me3) [Source organism]=Mus musculus [PDB ID]=2v86 [PDB chain IDs]=E:A [PDB note]=Chains B and D were removed as chains A and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.05 [Domain]=RAG2 PHD [Type chain E]=Disordered [Evidence chain E]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The RAG2 PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13341). A solved monomeric structure of the domain is represented by PDB ID 2jwo. [Modified residues chain E]=NG,NG-dimethyl-L-arginine#R#2|N-trimethyllysine#K#4 [Chain E name]=Histone H3.2 [Chain E source organism]=Mus musculus [Chain E UniProt accession]=P84228 [Chain E UniProt boundaries]=2-9 [Chain E UniProt coverage]=5.9% [Chain E UniRef90 accession]=UniRef90_Q71DI3 [Chain E UniRef90 boundaries]=2-9 [Chain A name]=V(D)J recombination-activating protein 2 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P21784 [Chain A UniProt boundaries]=406-487 [Chain A UniProt coverage]=15.6% [Chain A UniRef90 accession]=UniRef90_P21784 [Chain A UniRef90 boundaries]=414-487 [Related structures]=2v87 [Entry] [Accession]=DI1100021 [Disorder status]=Confirmed [Kd]=1.90E-06 (PMID:23636332) [Name]=SHH1 SAWADEE domain in complex with H3.2 peptide (H3K9me1) [Source organism]=Arabidopsis thaliana [PDB ID]=4iut [PDB chain IDs]=C:B [PDB note]=Chain A was removed as chains B and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.70 [Domain]=SAWADEE [Type chain C]=Disordered [Evidence chain C]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain B]=Ordered [Evidence chain B]=The SAWADEE domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF16719). A solved monomeric structure of the domain is represented by PDB ID 4iuq. [Modified residues chain C]=N-dimethyl-lysine#K#9 [Chain C name]=Histone H3.2 [Chain C source organism]=Arabidopsis thaliana [Chain C UniProt accession]=P59226 [Chain C UniProt boundaries]=2-16 [Chain C UniProt coverage]=11% [Chain C UniRef90 accession]=UniRef90_P59226 [Chain C UniRef90 boundaries]=2-16 [Chain B name]=Protein SAWADEE HOMEODOMAIN HOMOLOG 1 [Chain B source organism]=Arabidopsis thaliana [Chain B UniProt accession]=Q9XI47 [Chain B UniProt boundaries]=124-258 [Chain B UniProt coverage]=52.3% [Chain B UniRef90 accession]=UniRef90_Q9XI47 [Chain B UniRef90 boundaries]=125-258 [Related structures]=4iuu,4iur [Entry] [Accession]=DI1010040 [Disorder status]=Confirmed [Kd]=5.00E-07 [Name]=Double PHD finger of human transcriptional protein DPF3 bound to a H3.1 histone peptide (H3K14ac) [Source organism]=Neurospora crassa / Homo sapiens [PDB ID]=2kwj [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1xwh. [Modified residues chain B]=N(6)-acetyllysine#K#14 [Chain B name]=Histone H3 [Chain B source organism]=Neurospora crassa [Chain B UniProt accession]=P07041 [Chain B UniProt boundaries]=2-21 [Chain B UniProt coverage]=14.7% [Chain B UniRef90 accession]=UniRef90_Q6DL03 [Chain B UniRef90 boundaries]=2-21 [Chain A name]=Zinc finger protein DPF3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q92784 [Chain A UniProt boundaries]=259-372 [Chain A UniProt coverage]=30.2% [Chain A UniRef90 accession]=UniRef90_Q92784 [Chain A UniRef90 boundaries]=260-372 [Related structures]=5i3l [Entry] [Accession]=DI1000087 [Disorder status]=Confirmed [Kd]=4.69E-05 [Name]=Double PHD finger of human transcriptional protein DPF3 bound to a H4 histone peptide (H4K16ac) [Source organism]=Homo sapiens [PDB ID]=2kwn [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1xwh. [Modified residues chain B]=N(6)-acetyllysine#K#16 [Chain B name]=Histone H4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P62805 [Chain B UniProt boundaries]=9-23 [Chain B UniProt coverage]=14.6% [Chain B UniRef90 accession]=UniRef90_P62805 [Chain B UniRef90 boundaries]=9-23 [Chain A name]=Zinc finger protein DPF3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q92784 [Chain A UniProt boundaries]=259-372 [Chain A UniProt coverage]=30.2% [Chain A UniRef90 accession]=UniRef90_Q92784 [Chain A UniRef90 boundaries]=260-372 [Entry] [Accession]=DI2200002 [Disorder status]=Inferred from homology [Kd]=4.70E-06 [Name]=E. coli MazF in complex with MazE [Source organism]=Escherichia coli [PDB ID]=5cqx [PDB chain IDs]=C:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.63 [Domain]=PemK toxin [Type chain C]=Disordered [Evidence chain C]=The corresponding region of a closely homologous protein has been shown to be disordered in the 45-82 region described in DisProt entry DP00296 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered component [Evidence chain A]=The PemK toxin domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF02452). A solved structure of the domain dimer without bound ligands is represented by PDB ID 5ck9. [Type chain B]=Ordered component [Evidence chain B]=The PemK toxin domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF02452). A solved structure of the domain dimer without bound ligands is represented by PDB ID 5ck9. [Modified residues chain B]=N(6)-acetyllysine#K#16 [Chain C name]=Antitoxin MazE [Chain C source organism]=Escherichia coli [Chain C UniProt accession]=P0AE72 [Chain C UniProt boundaries]=68-82 [Chain C UniProt coverage]=18.3% [Chain C UniRef90 accession]=UniRef90_P0AE73 [Chain C UniRef90 boundaries]=68-82 [Chain A name]=Endoribonuclease MazF [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=P0AE70 [Chain A UniProt boundaries]=1-111 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P0AE71 [Chain A UniRef90 boundaries]=1-111 [Chain B name]=Endoribonuclease MazF [Chain B source organism]=Escherichia coli [Chain B UniProt accession]=P0AE70 [Chain B UniProt boundaries]=1-111 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P0AE71 [Chain B UniRef90 boundaries]=1-111 [Related structures]=1ub4,5cqy [Entry] [Accession]=DI3100001 [Disorder status]=Confirmed [Kd]=4.70E-06 [Name]=Sac3:Sus1:Cdc31:Nup1 complex (1) [Source organism]=Saccharomyces cerevisiae [PDB ID]=4mbe [PDB chain IDs]=G:ABC [PDB note]=Chains D, E, F, H, X and Y were removed as chains A, B, C and G highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.61 [Domain]=Sac3:Sus1:Cdc31 interaction platform [Type chain G]=Disordered [Evidence chain G]=The 300-1076 region described in DisProt entry DP01075 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains FDFI motif that binds to TREX2. (PMID:24705649). [Type chain A]=Ordered component [Evidence chain A]=Cdc31 forms an ordered complex together with Sac3 and Sus1 serving as a platform for binding various substrate proteins (PMID:19328066). The structure of the Sac3:Sus1:Cdc31 interaction platform is represented by PDB ID 3fwc. [Type chain B]=Ordered component [Evidence chain B]=Sac3 forms an ordered complex together with Cdc31 and Sus1 serving as a platform for binding various substrate proteins (PMID:19328066). The structure of the Sac3:Sus1:Cdc31 interaction platform is represented by PDB ID 3fwc. [Type chain C]=Ordered component [Evidence chain C]=Sus1 forms an ordered complex together with Sac3 and Cdc31 serving as a platform for binding various substrate proteins (PMID:19328066). The structure of the Sac3:Sus1:Cdc31 interaction platform is represented by PDB ID 3fwc. [Modified residues chain B]=N(6)-acetyllysine#K#16 [Chain G name]=Nucleoporin NUP1 [Chain G source organism]=Saccharomyces cerevisiae [Chain G UniProt accession]=P20676 [Chain G UniProt boundaries]=316-340 [Chain G UniProt coverage]=2.3% [Chain G UniRef90 accession]=UniRef90_P20676 [Chain G UniRef90 boundaries]=316-340 [Chain A name]=Cell division control protein 31 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P06704 [Chain A UniProt boundaries]=1-161 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P06704 [Chain A UniRef90 boundaries]=1-161 [Chain B name]=Nuclear mRNA export protein SAC3 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P46674 [Chain B UniProt boundaries]=753-805 [Chain B UniProt coverage]=4.1% [Chain B UniRef90 accession]=UniRef90_P46674 [Chain B UniRef90 boundaries]=753-805 [Chain C name]=Transcription and mRNA export factor SUS1 [Chain C source organism]=Saccharomyces cerevisiae [Chain C UniProt accession]=Q6WNK7 [Chain C UniProt boundaries]=1-96 [Chain C UniProt coverage]=100% [Chain C UniRef90 accession]=UniRef90_Q6WNK7 [Chain C UniRef90 boundaries]=1-96 [Entry] [Accession]=DI3100002 [Disorder status]=Confirmed [Kd]=4.70E-06 [Name]=Sac3:Sus1:Cdc31:Nup1 complex (2) [Source organism]=Saccharomyces cerevisiae [PDB ID]=4mbe [PDB chain IDs]=X:ABC [PDB note]=Chains D, E, F, H, G and Y were removed as chains A, B, C and X highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.61 [Domain]=Sac3:Sus1:Cdc31 interaction platform [Type chain X]=Disordered [Evidence chain X]=The 300-1076 region described in DisProt entry DP01075 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains FDFI motif that binds to TREX2. (PMID:24705649). [Type chain A]=Ordered component [Evidence chain A]=Cdc31 forms an ordered complex together with Sac3 and Sus1 serving as a platform for binding various substrate proteins (PMID:19328066). The structure of the Sac3:Sus1:Cdc31 interaction platform is represented by PDB ID 3fwc. [Type chain B]=Ordered component [Evidence chain B]=Sac3 forms an ordered complex together with Cdc31 and Sus1 serving as a platform for binding various substrate proteins (PMID:19328066). The structure of the Sac3:Sus1:Cdc31 interaction platform is represented by PDB ID 3fwc. [Type chain C]=Ordered component [Evidence chain C]=Sus1 forms an ordered complex together with Sac3 and Cdc31 serving as a platform for binding various substrate proteins (PMID:19328066). The structure of the Sac3:Sus1:Cdc31 interaction platform is represented by PDB ID 3fwc. [Modified residues chain B]=N(6)-acetyllysine#K#16 [Chain X name]=Nucleoporin NUP1 [Chain X source organism]=Saccharomyces cerevisiae [Chain X UniProt accession]=P20676 [Chain X UniProt boundaries]=316-340 [Chain X UniProt coverage]=2.3% [Chain X UniRef90 accession]=UniRef90_P20676 [Chain X UniRef90 boundaries]=316-340 [Chain A name]=Cell division control protein 31 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P06704 [Chain A UniProt boundaries]=1-161 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P06704 [Chain A UniRef90 boundaries]=1-161 [Chain B name]=Nuclear mRNA export protein SAC3 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P46674 [Chain B UniProt boundaries]=753-805 [Chain B UniProt coverage]=4.1% [Chain B UniRef90 accession]=UniRef90_P46674 [Chain B UniRef90 boundaries]=753-805 [Chain C name]=Transcription and mRNA export factor SUS1 [Chain C source organism]=Saccharomyces cerevisiae [Chain C UniProt accession]=Q6WNK7 [Chain C UniProt boundaries]=1-96 [Chain C UniProt coverage]=100% [Chain C UniRef90 accession]=UniRef90_Q6WNK7 [Chain C UniRef90 boundaries]=1-96 [Entry] [Accession]=DI3000001 [Disorder status]=Confirmed [Kd]=3.10E-08 (PMID:12050673) [Name]=Hydroxylated HIF-1 alpha peptide bound to the pVHL/elongin-C/elongin-B complex [Source organism]=Homo sapiens [PDB ID]=1lqb [PDB chain IDs]=D:ABC [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=VCB complex [Type chain D]=Disordered [Evidence chain D]=The 403-698 region described in DisProt entry DP00262 and in IDEAL entry IID00085 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (DEG_ODPH_VHL_1). [Type chain A]=Ordered component [Evidence chain A]=Elongin B forms an ordered complex together with elongin C and pVHL (VCB complex) serving as part of an E3 ubiquitin ligase. The structure of the VCB complex without ligands is represented by PDB ID 1vcb. [Type chain B]=Ordered component [Evidence chain B]=Elongin C forms an ordered complex together with elongin B and pVHL (VCB complex) serving as part of an E3 ubiquitin ligase. The structure of the VCB complex without ligands is represented by PDB ID 1vcb. [Type chain C]=Ordered component [Evidence chain C]=pVHL forms an ordered complex together with elongin B and elongin C (VCB complex) serving as part of an E3 ubiquitin ligase. The structure of the VCB complex without ligands is represented by PDB ID 1vcb. [Modified residues chain D]=4-hydroxyproline#P#564 [Modified residues chain B]=N(6)-acetyllysine#K#16 [Chain D name]=Hypoxia-inducible factor 1-alpha [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=Q16665 [Chain D UniProt boundaries]=549-582 [Chain D UniProt coverage]=4.1% [Chain D UniRef90 accession]=UniRef90_Q16665 [Chain D UniRef90 boundaries]=549-582 [Chain A name]=Elongin-B [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q15370 [Chain A UniProt boundaries]=1-118 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q15370 [Chain A UniRef90 boundaries]=1-118 [Chain B name]=Elongin-C [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q15369 [Chain B UniProt boundaries]=17-112 [Chain B UniProt coverage]=85.7% [Chain B UniRef90 accession]=UniRef90_Q15369 [Chain B UniRef90 boundaries]=17-112 [Chain C name]=Von Hippel-Lindau disease tumor suppressor [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P40337 [Chain C UniProt boundaries]=52-213 [Chain C UniProt coverage]=76.1% [Chain C UniRef90 accession]=UniRef90_P40337 [Chain C UniRef90 boundaries]=53-213 [Related structures]=1lm8,4ajy [Entry] [Accession]=DI3000002 [Disorder status]=Confirmed [Kd]=9.00E-06 (PMID:16209941) [Name]=Skp1-Skp2-Cks1 in complex with a p27 peptide [Source organism]=Homo sapiens [PDB ID]=2ast [PDB chain IDs]=D:ABC [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=Skp1:Skp2:Cks1 complex [Type chain D]=Disordered [Evidence chain D]=The 1-198 region described in DisProt entry DP00018 and in IDEAL entry IID00049 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains two known functional linear motifs (DEG_SCF_SKP2-CKS1_1, DOC_WW_Pin1_4) and a known modification site (MOD_CDK_SPxK_1). [Type chain A]=Ordered component [Evidence chain A]=Skp1 forms an ordered complex together with Skp2 and Cks1 serving as part of an E3 ubiquitin ligase. The structure of the VCB complex without ligands is represented by PDB ID 2ass. [Type chain B]=Ordered component [Evidence chain B]=Skp2 forms an ordered complex together with Skp1 and Cks1 serving as part of an E3 ubiquitin ligase. The structure of the VCB complex without ligands is represented by PDB ID 2ass. [Type chain C]=Ordered component [Evidence chain C]=Cks1 forms an ordered complex together with Skp1 and Skp2 serving as part of an E3 ubiquitin ligase. The structure of the VCB complex without ligands is represented by PDB ID 2ass. [Modified residues chain D]=phosphothreonine#T#4187 [Modified residues chain B]=N(6)-acetyllysine#K#16 [Chain D name]=Cyclin-dependent kinase inhibitor 1B [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P46527 [Chain D UniProt boundaries]=181-190 [Chain D UniProt coverage]=5.1% [Chain D UniRef90 accession]=UniRef90_P46527 [Chain D UniRef90 boundaries]=181-190 [Chain A name]=S-phase kinase-associated protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63208 [Chain A UniProt boundaries]=2-160 [Chain A UniProt coverage]=97.5% [Chain A UniRef90 accession]=UniRef90_P63208 [Chain A UniRef90 boundaries]=2-160 [Chain B name]=S-phase kinase-associated protein 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q13309 [Chain B UniProt boundaries]=95-419 [Chain B UniProt coverage]=76.7% [Chain B UniRef90 accession]=UniRef90_Q13309 [Chain B UniRef90 boundaries]=95-419 [Chain C name]=Cyclin-dependent kinases regulatory subunit 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P61024 [Chain C UniProt boundaries]=5-73 [Chain C UniProt coverage]=87.3% [Chain C UniRef90 accession]=UniRef90_P61024 [Chain C UniRef90 boundaries]=5-73 [Entry] [Accession]=DI1000088 [Disorder status]=Confirmed [Kd]=5.00E-07 (PMID:21666679) [Name]=ATRX ADD bound to histone H3.3 (H3K9me3) peptide [Source organism]=Homo sapiens [PDB ID]=3ql9 [PDB chain IDs]=C:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=0.93 [Domain]=ADD [Type chain C]=Disordered [Evidence chain C]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The 1-45 region described in IDEAL entry IID00239 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The ADD domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 2jm1. [Modified residues chain C]=N-trimethyllysine#K#9 [Chain C name]=Histone H3.3 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P84243 [Chain C UniProt boundaries]=2-16 [Chain C UniProt coverage]=11% [Chain C UniRef90 accession]=UniRef90_P84243 [Chain C UniRef90 boundaries]=2-16 [Chain A name]=Transcriptional regulator ATRX [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P46100 [Chain A UniProt boundaries]=161-289 [Chain A UniProt coverage]=5.2% [Chain A UniRef90 accession]=UniRef90_P46100 [Chain A UniRef90 boundaries]=161-289 [Related structures]=3qla [Entry] [Accession]=DI1000089 [Disorder status]=Confirmed [Kd]=2.70E-07 (PMID:21666677) [Name]=ATRX ADD bound to histone H3.1 (H3K9me3) peptide [Source organism]=Homo sapiens [PDB ID]=2lbm [PDB chain IDs]=C:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=ADD [Type chain C]=Disordered [Evidence chain C]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The ADD domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 2jm1. [Modified residues chain C]=N-trimethyllysine#K#9 [Chain C name]=Histone H3.1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P68431 [Chain C UniProt boundaries]=2-16 [Chain C UniProt coverage]=11% [Chain C UniRef90 accession]=UniRef90_P68431 [Chain C UniRef90 boundaries]=2-16 [Chain A name]=Transcriptional regulator ATRX [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P46100 [Chain A UniProt boundaries]=155-296 [Chain A UniProt coverage]=5.7% [Chain A UniRef90 accession]=UniRef90_P46100 [Chain A UniRef90 boundaries]=159-296 [Entry] [Accession]=DI3000003 [Disorder status]=Confirmed [Kd]=2.70E-07 (PMID:21666677) [Name]=Casc3 bound in the exon junction complex (EJC) [Source organism]=Homo sapiens [PDB ID]=2j0s [PDB chain IDs]=T:ACD [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.21 [Domain]=EJC [Type chain T]=Disordered [Evidence chain T]=The 137-286 region described in IDEAL entry IID00185 covers 94% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=eIF4AIII forms an ordered structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 2hxy. [Type chain C]=Ordered component [Evidence chain C]=Mago nashi homolog together with Y14 forms an ordered dimer, represented by PDB ID 1p27. [Type chain D]=Ordered component [Evidence chain D]=Y14 together with mago nashi homolog forms an ordered dimer, represented by PDB ID 1p27. [Modified residues chain C]=N-trimethyllysine#K#9 [Modified residues chain D]=phosphothreonine#T#4187 [Chain T name]=Protein CASC3 [Chain T source organism]=Homo sapiens [Chain T UniProt accession]=O15234 [Chain T UniProt boundaries]=137-286 [Chain T UniProt coverage]=21.3% [Chain T UniRef90 accession]=UniRef90_O15234 [Chain T UniRef90 boundaries]=137-286 [Chain A name]=Eukaryotic initiation factor 4A-III [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P38919 [Chain A UniProt boundaries]=21-411 [Chain A UniProt coverage]=95.1% [Chain A UniRef90 accession]=UniRef90_P38919 [Chain A UniRef90 boundaries]=21-411 [Chain C name]=Protein mago nashi homolog [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P61326 [Chain C UniProt boundaries]=1-146 [Chain C UniProt coverage]=100% [Chain C UniRef90 accession]=UniRef90_P61326 [Chain C UniRef90 boundaries]=1-146 [Chain D name]=RNA-binding protein 8A [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=Q9Y5S9 [Chain D UniProt boundaries]=66-154 [Chain D UniProt coverage]=51.1% [Chain D UniRef90 accession]=UniRef90_Q9Y5S9 [Chain D UniRef90 boundaries]=66-154 [Related structures]=2j0q,3ex7,2hyi,2xb2,2j0u [Entry] [Accession]=DI1000090 [Disorder status]=Inferred from motif [Kd]=2.40E-08 (PMID:12169629) [Name]=C-terminal SH3 domain of p67phox complexed with the C-terminal tail region of p47phox [Source organism]=Homo sapiens [PDB ID]=1k4u [PDB chain IDs]=P:S [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH3 [Type chain P]=Disordered [Evidence chain P]=The C-terminal region of p47phox was shown to interact with the p67(phox) SH3 domain via two distinct regions, a canonical PxxP motif and a non-PxxP peptide segment (PMID:12169629) forming an extended interface compared to that of classical SH3 binding partners. [Type chain S]=Ordered [Evidence chain S]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00018). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2a36. [Chain P name]=Neutrophil cytosol factor 1 [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=P14598 [Chain P UniProt boundaries]=359-390 [Chain P UniProt coverage]=8.2% [Chain P UniRef90 accession]=UniRef90_P14598 [Chain P UniRef90 boundaries]=359-390 [Chain S name]=Neutrophil cytosol factor 2 [Chain S source organism]=Homo sapiens [Chain S UniProt accession]=P19878 [Chain S UniProt boundaries]=455-516 [Chain S UniProt coverage]=11.8% [Chain S UniRef90 accession]=UniRef90_P19878 [Chain S UniRef90 boundaries]=455-516 [Entry] [Accession]=DI2000003 [Disorder status]=Inferred from motif [Kd]=2.40E-08 (PMID:12169629) [Name]=IR1 domain from RanBP2 bound to SUMO2 and UBC9 [Source organism]=Homo sapiens [PDB ID]=3uin [PDB chain IDs]=D:AB [PDB note]=Chain C was removed as chains A, B and D highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=SUMO:Ubiquitin-conjugating enzyme [Type chain D]=Disordered [Evidence chain D]=The IR1 region of RanBP2 was shown to contain five tandem motifs that are involved in binding to RanGAP1-SUMO1/UBC9 forming an extended structure of the surface of the ordered partner proteins (PMID:15931224). [Type chain A]=Ordered [Evidence chain A]=The Ubiquitin-conjugating enzyme domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00179). A solved monomeric structure of the domain is represented by PDB ID 1a3s. [Type chain B]=Ordered [Evidence chain B]=The SUMO domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF11976). A solved monomeric structure of the domain is represented by PDB ID 1wm2. [Modified residues chain B]=N(6)-acetyllysine#K#16 [Chain D name]=E3 SUMO-protein ligase RanBP2 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P49792 [Chain D UniProt boundaries]=2627-2695 [Chain D UniProt coverage]=2.1% [Chain D UniRef90 accession]=UniRef90_P49792 [Chain D UniRef90 boundaries]=2629-2695 [Chain A name]=SUMO-conjugating enzyme UBC9 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63279 [Chain A UniProt boundaries]=2-158 [Chain A UniProt coverage]=99.4% [Chain A UniRef90 accession]=UniRef90_P63279 [Chain A UniRef90 boundaries]=2-158 [Chain B name]=Small ubiquitin-related modifier 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P61956 [Chain B UniProt boundaries]=14-93 [Chain B UniProt coverage]=84.2% [Chain B UniRef90 accession]=UniRef90_P61956 [Chain B UniRef90 boundaries]=14-93 [Related structures]=3uio [Entry] [Accession]=DI2000004 [Disorder status]=Inferred from motif [Kd]=2.40E-08 (PMID:12169629) [Name]=IR1 domain from RanBP2 bound to SUMO1 and UBC9 [Source organism]=Homo sapiens [PDB ID]=3uip [PDB chain IDs]=D:AB [PDB note]=Chain C was removed as chains A, B and D highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.29 [Domain]=SUMO:Ubiquitin-conjugating enzyme [Type chain D]=Disordered [Evidence chain D]=The IR1 region of RanBP2 was shown to contain five tandem motifs that are involved in binding to RanGAP1-SUMO1/UBC9 forming an extended structure of the surface of the ordered partner proteins (PMID:15931224). [Type chain A]=Ordered [Evidence chain A]=The Ubiquitin-conjugating enzyme domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00179). A solved monomeric structure of the domain is represented by PDB ID 1a3s. [Type chain B]=Ordered [Evidence chain B]=The SUMO domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF11976). A solved monomeric structure of the domain is represented by PDB ID 1a5r. [Modified residues chain D]=S,S-(2-hydroxyethyl)thiocysteine#C#2659 [Modified residues chain B]=N(6)-acetyllysine#K#16 [Chain D name]=E3 SUMO-protein ligase RanBP2 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P49792 [Chain D UniProt boundaries]=2631-2695 [Chain D UniProt coverage]=2% [Chain D UniRef90 accession]=UniRef90_P49792 [Chain D UniRef90 boundaries]=2631-2695 [Chain A name]=SUMO-conjugating enzyme UBC9 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63279 [Chain A UniProt boundaries]=2-158 [Chain A UniProt coverage]=99.4% [Chain A UniRef90 accession]=UniRef90_P63279 [Chain A UniRef90 boundaries]=2-158 [Chain B name]=Small ubiquitin-related modifier 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P63165 [Chain B UniProt boundaries]=18-97 [Chain B UniProt coverage]=79.2% [Chain B UniRef90 accession]=UniRef90_P63165 [Chain B UniRef90 boundaries]=18-97 [Related structures]=1z5s [Entry] [Accession]=DI1000091 [Disorder status]=Inferred from motif [Kd]=2.90E-04 (PMID:21070952) [Name]=Tsg101 UEV domain in complex with a human HRS PSAP peptide [Source organism]=Homo sapiens [PDB ID]=3obq [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.40 [Domain]=UEV [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_PTAP_UEV_1). [Type chain A]=Ordered [Evidence chain A]=The UEV domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF05743). A solved monomeric structure of the domain is represented by PDB ID 1kpp. [Chain B name]=Hepatocyte growth factor-regulated tyrosine kinase substrate [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O14964 [Chain B UniProt boundaries]=346-354 [Chain B UniProt coverage]=1.2% [Chain B UniRef90 accession]=UniRef90_O14964 [Chain B UniRef90 boundaries]=346-354 [Chain A name]=Tumor susceptibility gene 101 protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q99816 [Chain A UniProt boundaries]=2-145 [Chain A UniProt coverage]=36.9% [Chain A UniRef90 accession]=UniRef90_Q99816 [Chain A UniRef90 boundaries]=2-145 [Entry] [Accession]=DI1020010 [Disorder status]=Inferred from motif [Kd]=2.90E-04 (PMID:21070952) [Name]=Tsg101 UEV domain in complex with an ebola PTAP late domain peptide [Source organism]=Zaire ebolavirus / Homo sapiens [PDB ID]=4eje [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=UEV [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains two known functional linear motifs (LIG_PTAP_UEV_1 and LIG_WW_1). [Type chain A]=Ordered [Evidence chain A]=The UEV domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF05743). A solved monomeric structure of the domain is represented by PDB ID 1kpp. [Chain C name]=Matrix protein VP40 [Chain C source organism]=Zaire ebolavirus [Chain C UniProt accession]=Q05128 [Chain C UniProt boundaries]=5-13 [Chain C UniProt coverage]=2.8% [Chain C UniRef90 accession]=UniRef90_Q2PDK5 [Chain C UniRef90 boundaries]=5-13 [Chain A name]=Tumor susceptibility gene 101 protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q99816 [Chain A UniProt boundaries]=1-145 [Chain A UniProt coverage]=37.2% [Chain A UniRef90 accession]=UniRef90_Q99816 [Chain A UniRef90 boundaries]=1-145 [Entry] [Accession]=DI1000092 [Disorder status]=Inferred from motif [Kd]=3.90E-06 [Name]=p73 TAD bound to MDM2 [Source organism]=Homo sapiens [PDB ID]=2mps [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SWIB [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (DEG_MDM2_SWIB_1). [Type chain A]=Ordered [Evidence chain A]=The SWIB domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02201). A solved monomeric structure of the domain is represented by PDB ID 2lzg. [Chain B name]=Tumor protein p73 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O15350 [Chain B UniProt boundaries]=10-25 [Chain B UniProt coverage]=2.5% [Chain B UniRef90 accession]=UniRef90_O15350 [Chain B UniRef90 boundaries]=10-25 [Chain A name]=E3 ubiquitin-protein ligase Mdm2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q00987 [Chain A UniProt boundaries]=3-109 [Chain A UniProt coverage]=21.8% [Chain A UniRef90 accession]=UniRef90_Q00987 [Chain A UniRef90 boundaries]=3-109 [Entry] [Accession]=DI1000093 [Disorder status]=Confirmed [Kd]=6.36E-05 (PMID:19818708) [Name]=SPOP MATH domain in complex with a MacroH2A peptide [Source organism]=Homo sapiens [PDB ID]=3ivb [PDB chain IDs]=M:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.75 [Domain]=MATH [Type chain M]=Disordered [Evidence chain M]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 1zr5, 3iid, 3iif, 1zr3, 2fxk). The protein region involved in the interaction contains a known functional linear motif (DEG_SPOP_SBC_1). [Type chain A]=Ordered [Evidence chain A]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00917). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2f1w. [Chain M name]=Core histone macro-H2A.1 [Chain M source organism]=Homo sapiens [Chain M UniProt accession]=O75367 [Chain M UniProt boundaries]=167-181 [Chain M UniProt coverage]=4% [Chain M UniRef90 accession]=UniRef90_O75367 [Chain M UniRef90 boundaries]=167-181 [Chain A name]=Speckle-type POZ protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O43791 [Chain A UniProt boundaries]=22-166 [Chain A UniProt coverage]=38.8% [Chain A UniRef90 accession]=UniRef90_O43791 [Chain A UniRef90 boundaries]=28-166 [Related structures]=3hqh [Entry] [Accession]=DI1000094 [Disorder status]=Inferred from motif [Kd]=1.90E-04 (PMID:12426371) [Name]=CD2BP2-GYF domain in complex with proline-rich CD2 tail segment peptide [Source organism]=Homo sapiens [PDB ID]=1l2z [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=GYF [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains two known functional linear motifs (LIG_GYF and LIG_SH3_3). [Type chain A]=Ordered [Evidence chain A]=The GYF domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02213). A solved monomeric structure of the domain is represented by PDB ID 1gyf. [Chain B name]=T-cell surface antigen CD2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P06729 [Chain B UniProt boundaries]=294-304 [Chain B UniProt coverage]=3.1% [Chain B UniRef90 accession]=UniRef90_P06729 [Chain B UniRef90 boundaries]=294-304 [Chain A name]=CD2 antigen cytoplasmic tail-binding protein 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O95400 [Chain A UniProt boundaries]=280-341 [Chain A UniProt coverage]=18.2% [Chain A UniRef90 accession]=UniRef90_O95400 [Chain A UniRef90 boundaries]=280-341 [Entry] [Accession]=DI1010041 [Disorder status]=Inferred from motif [Kd]=4.00E-06 (PMID:22509010) [Name]=LDL receptor tail in complex with autosomal recessive hypercholesterolemia PTB domain [Source organism]=Homo sapiens / Mus musculus [PDB ID]=3so6 [PDB chain IDs]=Q:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.37 [Domain]=PID [Type chain Q]=Disordered [Evidence chain Q]=The protein region involved in the interaction contains a known functional linear motif (LIG_PTB_Apo_2). [Type chain A]=Ordered [Evidence chain A]=The PID domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00640). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4dbb. [Chain Q name]=Low-density lipoprotein receptor [Chain Q source organism]=Homo sapiens [Chain Q UniProt accession]=P01130 [Chain Q UniProt boundaries]=819-832 [Chain Q UniProt coverage]=1.6% [Chain Q UniRef90 accession]=UniRef90_P01130 [Chain Q UniRef90 boundaries]=819-832 [Chain A name]=Low density lipoprotein receptor adapter protein 1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q8C142 [Chain A UniProt boundaries]=42-174 [Chain A UniProt coverage]=43.2% [Chain A UniRef90 accession]=UniRef90_Q8C142 [Chain A UniRef90 boundaries]=42-174 [Entry] [Accession]=DI1020011 [Disorder status]=Inferred from motif [Kd]=1.00E-09 (PMID:7680435) [Name]=SH2 domain of p56lck in complex with a phosphotyrosyl peptide derived from polyomavirus antigen. [Source organism]=Hamster polyomavirus / Homo sapiens [PDB ID]=1lcj [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_SH2_SRC). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain is represented by PDB ID 1ijr. [Modified residues chain B]=phosphotyrosine#Y#204 [Chain B name]=Middle T antigen [Chain B source organism]=Hamster polyomavirus [Chain B UniProt accession]=P03079 [Chain B UniProt boundaries]=321-331 [Chain B UniProt coverage]=2.7% [Chain B UniRef90 accession]=UniRef90_P03079 [Chain B UniRef90 boundaries]=321-331 [Chain A name]=Tyrosine-protein kinase Lck [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P06239 [Chain A UniProt boundaries]=118-226 [Chain A UniProt coverage]=21.4% [Chain A UniRef90 accession]=UniRef90_P06239 [Chain A UniRef90 boundaries]=119-226 [Entry] [Accession]=DI1000095 [Disorder status]=Inferred from motif [Kd]=1.00E-09 (PMID:7680435) [Name]=p55 PDZ T85C domain complexed with the glycophorin C F127C peptide [Source organism]=Homo sapiens [PDB ID]=2ejy [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PDZ [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_2). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 2ev8. [Chain B name]=Glycophorin-C [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04921 [Chain B UniProt boundaries]=117-128 [Chain B UniProt coverage]=9.4% [Chain B UniRef90 accession]=UniRef90_P04921 [Chain B UniRef90 boundaries]=117-128 [Chain A name]=55 kDa erythrocyte membrane protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q00013 [Chain A UniProt boundaries]=69-153 [Chain A UniProt coverage]=18.2% [Chain A UniRef90 accession]=UniRef90_Q00013 [Chain A UniRef90 boundaries]=69-153 [Entry] [Accession]=DI1000096 [Disorder status]=Inferred from motif [Kd]=1.00E-09 (PMID:7680435) [Name]=Fyn SH2 domain in complex with the natural inhibitory phosphotyrosine peptide [Source organism]=Homo sapiens [PDB ID]=2mrk [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_SH2_SRC). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ab2. [Modified residues chain B]=phosphotyrosine#Y#4 [Chain B name]=Tyrosine-protein kinase Fyn [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P06241 [Chain B UniProt boundaries]=528-537 [Chain B UniProt coverage]=1.9% [Chain B UniRef90 accession]=UniRef90_P06241 [Chain B UniRef90 boundaries]=528-537 [Chain A name]=Tyrosine-protein kinase Fyn [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P06241 [Chain A UniProt boundaries]=149-248 [Chain A UniProt coverage]=18.6% [Chain A UniRef90 accession]=UniRef90_P06241 [Chain A UniRef90 boundaries]=149-248 [Entry] [Accession]=DI1000097 [Disorder status]=Inferred from motif [Kd]=1.00E-09 (PMID:7680435) [Name]=AF-6 PDZ domain complexed with the C-terminal peptide from the Bcr protein [Source organism]=Homo sapiens [PDB ID]=2ain [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PDZ [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_1). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 2kpk. [Chain B name]=Breakpoint cluster region protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P11274 [Chain B UniProt boundaries]=1266-1271 [Chain B UniProt coverage]=0.5% [Chain B UniRef90 accession]=UniRef90_P11274 [Chain B UniRef90 boundaries]=1266-1271 [Chain A name]=Afadin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P55196 [Chain A UniProt boundaries]=1002-1094 [Chain A UniProt coverage]=5.1% [Chain A UniRef90 accession]=UniRef90_Q9QZQ1 [Chain A UniRef90 boundaries]=1003-1094 [Entry] [Accession]=DI1000098 [Disorder status]=Inferred from motif [Kd]=3.50E-06 (PMID:12032548) [Name]=Complex of GGA3-VHS domain and CI-MPR C-terminal phosphopeptide [Source organism]=Homo sapiens [PDB ID]=1lf8 [PDB chain IDs]=E:A [PDB note]=Chains B, C, D, F, G and H were removed as chains A and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=VHS [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (TRG_LysEnd_GGAAcLL_1). [Type chain A]=Ordered [Evidence chain A]=The VHS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00790). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1jwf. [Modified residues chain E]=phosphoserine#S#305 [Chain E name]=Cation-independent mannose-6-phosphate receptor [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P11717 [Chain E UniProt boundaries]=2480-2491 [Chain E UniProt coverage]=0.5% [Chain E UniRef90 accession]=UniRef90_P11717 [Chain E UniRef90 boundaries]=2480-2491 [Chain A name]=ADP-ribosylation factor-binding protein GGA3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9NZ52 [Chain A UniProt boundaries]=1-166 [Chain A UniProt coverage]=23% [Chain A UniRef90 accession]=UniRef90_Q9NZ52 [Chain A UniRef90 boundaries]=1-157 [Entry] [Accession]=DI1000099 [Disorder status]=Inferred from homology [Kd]=1.50E-06 (PMID:14685257) [Name]=C-terminal PABC domain of human poly(A)-binding protein in complex with the peptide from Paip1 [Source organism]=Homo sapiens [PDB ID]=1jh4 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PABP [Type chain B]=Disordered [Evidence chain B]=The corresponding region of a homologous protein has been shown to be disordered in the 106-127 region described in IDEAL entry IID00582 (covers 100% of the sequence present in the structure). The protein region involved in the interaction contains a known functional linear motif (LIG_PAM2_1). [Type chain A]=Ordered [Evidence chain A]=The PABP domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00658). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1i2t. [Chain B name]=Polyadenylate-binding protein-interacting protein 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9H074 [Chain B UniProt boundaries]=123-144 [Chain B UniProt coverage]=4.6% [Chain B UniRef90 accession]=UniRef90_Q9H074 [Chain B UniRef90 boundaries]=123-144 [Chain A name]=Polyadenylate-binding protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P11940 [Chain A UniProt boundaries]=539-636 [Chain A UniProt coverage]=15.4% [Chain A UniRef90 accession]=UniRef90_P11940 [Chain A UniRef90 boundaries]=544-636 [Entry] [Accession]=DI1000100 [Disorder status]=Inferred from motif [Kd]=1.50E-06 (PMID:14685257) [Name]=C-terminal domain of human RPA32 complexed with UNG2 [Source organism]=Homo sapiens [PDB ID]=1dpu [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=RPA C-terminal [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_RPA_C_Vert). [Type chain A]=Ordered [Evidence chain A]=The RPA C-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF08784). A solved monomeric structure of the domain is represented by PDB ID 4ou0. [Chain B name]=Uracil-DNA glycosylase [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P13051 [Chain B UniProt boundaries]=73-88 [Chain B UniProt coverage]=5.1% [Chain B UniRef90 accession]=UniRef90_P13051 [Chain B UniRef90 boundaries]=73-88 [Chain A name]=Replication protein A 32 kDa subunit [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P15927 [Chain A UniProt boundaries]=172-270 [Chain A UniProt coverage]=36.7% [Chain A UniRef90 accession]=UniRef90_P15927 [Chain A UniRef90 boundaries]=172-270 [Entry] [Accession]=DI1000101 [Disorder status]=Inferred from motif [Kd]=2.90E-06 [Name]=C-terminal domain of human RPA32 complexed with Smarcal1 N-terminus [Source organism]=Homo sapiens [PDB ID]=4mqv [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.95 [Domain]=RPA C-terminal [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_RPA_C_Vert). [Type chain A]=Ordered [Evidence chain A]=The RPA C-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF08784). A solved monomeric structure of the domain is represented by PDB ID 4ou0. [Chain B name]=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9NZC9 [Chain B UniProt boundaries]=5-30 [Chain B UniProt coverage]=2.7% [Chain B UniRef90 accession]=UniRef90_Q9NZC9 [Chain B UniRef90 boundaries]=5-30 [Chain A name]=Replication protein A 32 kDa subunit [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P15927 [Chain A UniProt boundaries]=202-270 [Chain A UniProt coverage]=25.6% [Chain A UniRef90 accession]=UniRef90_P15927 [Chain A UniRef90 boundaries]=202-270 [Entry] [Accession]=DI1000102 [Disorder status]=Inferred from motif [Kd]=6.00E-06 (PMID:8599766) [Name]=IRS-1 PTB domain complexed with an IL-4 receptor phosphopeptide [Source organism]=Homo sapiens [PDB ID]=1irs [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=IRS-type PTB [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_PTB_Phospho_1). [Type chain A]=Ordered [Evidence chain A]=The IRS-type PTB domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02174). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2dlw. [Modified residues chain B]=phosphotyrosine#Y#497 [Chain B name]=Interleukin-4 receptor subunit alpha [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P24394 [Chain B UniProt boundaries]=489-499 [Chain B UniProt coverage]=1.3% [Chain B UniRef90 accession]=UniRef90_P24394 [Chain B UniRef90 boundaries]=489-499 [Chain A name]=Insulin receptor substrate 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P35568 [Chain A UniProt boundaries]=156-267 [Chain A UniProt coverage]=9% [Chain A UniRef90 accession]=UniRef90_P35568 [Chain A UniRef90 boundaries]=157-267 [Entry] [Accession]=DI1000103 [Disorder status]=Inferred from motif [Kd]=6.00E-06 (PMID:8599766) [Name]=SHP-1 C-terminal SH2 domain complexed with a tyrosine-phosphorylated peptide from NKG2A [Source organism]=Homo sapiens [PDB ID]=2yu7 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_TYR_ITIM). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain is represented by PDB ID 1x6c. [Modified residues chain B]=phosphotyrosine#Y#8 [Chain B name]=NKG2-A/NKG2-B type II integral membrane protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P26715 [Chain B UniProt boundaries]=33-47 [Chain B UniProt coverage]=6.4% [Chain B UniRef90 accession]=UniRef90_P26715 [Chain B UniRef90 boundaries]=33-47 [Chain A name]=Tyrosine-protein phosphatase non-receptor type 6 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P29350 [Chain A UniProt boundaries]=107-215 [Chain A UniProt coverage]=18.3% [Chain A UniRef90 accession]=UniRef90_P29350 [Chain A UniRef90 boundaries]=107-215 [Entry] [Accession]=DI1000104 [Disorder status]=Inferred from motif [Kd]=6.00E-06 (PMID:8599766) [Name]=SH2 domain of Grb2 complexed with the Shc-derived phosphotyrosine-containing peptide [Source organism]=Homo sapiens [PDB ID]=1qg1 [PDB chain IDs]=I:E [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH2 [Type chain I]=Disordered [Evidence chain I]=The protein region involved in the interaction contains a known functional linear motif (LIG_SH2_GRB2). [Type chain E]=Ordered [Evidence chain E]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain is represented by PDB ID 1fhs. [Modified residues chain I]=phosphotyrosine#Y#5 [Modified residues chain E]=phosphoserine#S#305 [Chain I name]=SHC-transforming protein 1 [Chain I source organism]=Homo sapiens [Chain I UniProt accession]=P29353 [Chain I UniProt boundaries]=423-435 [Chain I UniProt coverage]=2.2% [Chain I UniRef90 accession]=UniRef90_P29353 [Chain I UniRef90 boundaries]=423-435 [Chain E name]=Growth factor receptor-bound protein 2 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P62993 [Chain E UniProt boundaries]=56-159 [Chain E UniProt coverage]=47.9% [Chain E UniRef90 accession]=UniRef90_P62993 [Chain E UniRef90 boundaries]=58-159 [Entry] [Accession]=DI1100022 [Disorder status]=Inferred from motif [Kd]=6.00E-06 [Name]=Par3-PDZ3 in complex with VE-Cadherin C-terminus [Source organism]=Mus musculus [PDB ID]=2koh [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PDZ [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_2). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain from a closely homologous protein is represented by PDB ID 2k1z. [Chain B name]=Cadherin-5 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=P55284 [Chain B UniProt boundaries]=769-784 [Chain B UniProt coverage]=2% [Chain B UniRef90 accession]=UniRef90_P55284 [Chain B UniRef90 boundaries]=769-784 [Chain A name]=Partitioning defective 3 homolog [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q99NH2 [Chain A UniProt boundaries]=579-689 [Chain A UniProt coverage]=8.3% [Chain A UniRef90 accession]=UniRef90_Q99NH2 [Chain A UniRef90 boundaries]=580-689 [Entry] [Accession]=DI1000105 [Disorder status]=Inferred from motif [Kd]=8.70E-06 (PMID:19523899) [Name]=Second SH3-binding motif from Gab2 bound to the SH3C Domain of Grb2 [Source organism]=Homo sapiens [PDB ID]=2vwf [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.58 [Domain]=SH3 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (SH3-binding motif - http://www.uniprot.org/uniprot/Q9UQC2#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00018). A solved monomeric structure of the domain is represented by PDB ID 1gfc. [Chain B name]=GRB2-associated-binding protein 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9UQC2 [Chain B UniProt boundaries]=508-522 [Chain B UniProt coverage]=2.2% [Chain B UniRef90 accession]=UniRef90_Q9UQC2 [Chain B UniRef90 boundaries]=508-522 [Chain A name]=Growth factor receptor-bound protein 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P62993 [Chain A UniProt boundaries]=157-214 [Chain A UniProt coverage]=26.7% [Chain A UniRef90 accession]=UniRef90_P62993 [Chain A UniRef90 boundaries]=158-214 [Entry] [Accession]=DI1000106 [Disorder status]=Inferred from motif [Kd]=4.85E-05 (PMID:19523899) [Name]=First SH3-binding motif from Gab2 bound to the SH3C Domain of Grb2 [Source organism]=Homo sapiens [PDB ID]=2w0z [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=SH3 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (SH3-binding motif - http://www.uniprot.org/uniprot/Q9UQC2#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00018). A solved monomeric structure of the domain is represented by PDB ID 1gfc. [Chain B name]=GRB2-associated-binding protein 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9UQC2 [Chain B UniProt boundaries]=350-358 [Chain B UniProt coverage]=1.3% [Chain B UniRef90 accession]=UniRef90_Q9UQC2 [Chain B UniRef90 boundaries]=519-525 [Chain A name]=Growth factor receptor-bound protein 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P62993 [Chain A UniProt boundaries]=157-214 [Chain A UniProt coverage]=26.7% [Chain A UniRef90 accession]=UniRef90_P62993 [Chain A UniRef90 boundaries]=158-214 [Entry] [Accession]=DI1000107 [Disorder status]=Confirmed [Kd]=4.30E-07 (PMID:11140637) [Name]=Peptide from SMAC/DIABLO complexed to the BIR3 domain of XIAP [Source organism]=Homo sapiens [PDB ID]=1g3f [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=BIR [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (IAP-binding motif - http://www.uniprot.org/uniprot/Q9NR28#family_and_domains). The N terminal region of Smac has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 1few). [Type chain A]=Ordered [Evidence chain A]=The BIR domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00653). A solved monomeric structure of the domain is represented by PDB ID 1f9x. [Chain B name]=Diablo homolog, mitochondrial [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9NR28 [Chain B UniProt boundaries]=56-64 [Chain B UniProt coverage]=3.8% [Chain B UniRef90 accession]=UniRef90_Q9NR28 [Chain B UniRef90 boundaries]=56-64 [Chain A name]=E3 ubiquitin-protein ligase XIAP [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P98170 [Chain A UniProt boundaries]=240-356 [Chain A UniProt coverage]=23.5% [Chain A UniRef90 accession]=UniRef90_P98170 [Chain A UniRef90 boundaries]=241-356 [Related structures]=1g73 [Entry] [Accession]=DI1100023 [Disorder status]=Inferred from motif [Kd]=4.30E-07 (PMID:11140637) [Name]=LC3:p62 complex [Source organism]=Rattus norvegicus [PDB ID]=2k6q [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Atg8 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIR motif - http://www.uniprot.org/uniprot/O08623#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The Atg8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02991). A solved monomeric structure of the domain is represented by PDB ID 1ugm. [Chain B name]=Sequestosome-1 [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=O08623 [Chain B UniProt boundaries]=330-346 [Chain B UniProt coverage]=3.9% [Chain B UniRef90 accession]=UniRef90_Q13501 [Chain B UniRef90 boundaries]=332-347 [Chain A name]=Microtubule-associated proteins 1A/1B light chain 3B [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=Q62625 [Chain A UniProt boundaries]=1-120 [Chain A UniProt coverage]=84.5% [Chain A UniRef90 accession]=UniRef90_Q62625 [Chain A UniRef90 boundaries]=1-120 [Related structures]=2zjd [Entry] [Accession]=DI1000108 [Disorder status]=Inferred from motif [Kd]=1.06E-05 (PMID:25657007) [Name]=Complex of VPS4B MIT and IST1 MIM [Source organism]=Homo sapiens [PDB ID]=4u7y [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=MIT [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (MIT-interacting motif - http://www.uniprot.org/uniprot/P53990#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The MIT domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04212). A solved monomeric structure of the domain is represented by PDB ID 2jqh. [Chain B name]=IST1 homolog [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P53990 [Chain B UniProt boundaries]=341-364 [Chain B UniProt coverage]=6.6% [Chain B UniRef90 accession]=UniRef90_P53990 [Chain B UniRef90 boundaries]=341-364 [Chain A name]=Vacuolar protein sorting-associated protein 4B [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O75351 [Chain A UniProt boundaries]=1-89 [Chain A UniProt coverage]=20% [Chain A UniRef90 accession]=UniRef90_O75351 [Chain A UniRef90 boundaries]=1-89 [Entry] [Accession]=DI1000109 [Disorder status]=Inferred from motif [Kd]=4.02E-04 (PMID:17928862) [Name]=Complex of VPS4B MIT and CHMP2B [Source organism]=Homo sapiens [PDB ID]=2jqk [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=MIT [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (MIT-interacting motif - http://www.uniprot.org/uniprot/Q9UQN3#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The MIT domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04212). A solved monomeric structure of the domain is represented by PDB ID 2jqh. [Chain B name]=Charged multivesicular body protein 2b [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9UQN3 [Chain B UniProt boundaries]=195-213 [Chain B UniProt coverage]=8.9% [Chain B UniRef90 accession]=UniRef90_Q9UQN3 [Chain B UniRef90 boundaries]=195-213 [Chain A name]=Vacuolar protein sorting-associated protein 4B [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O75351 [Chain A UniProt boundaries]=1-86 [Chain A UniProt coverage]=19.4% [Chain A UniRef90 accession]=UniRef90_O75351 [Chain A UniRef90 boundaries]=1-86 [Entry] [Accession]=DI1000110 [Disorder status]=Inferred from motif [Kd]=5.00E-07 (PMID:24668264) [Name]=GABARAP-LIR peptide complex [Source organism]=Homo sapiens [PDB ID]=3wim [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=Atg8 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIR motif - http://www.uniprot.org/uniprot/Q8IZQ1#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The Atg8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02991). A solved monomeric structure of the domain is represented by PDB ID 1gnu. [Chain B name]=WD repeat and FYVE domain-containing protein 3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q8IZQ1 [Chain B UniProt boundaries]=3341-3354 [Chain B UniProt coverage]=0.4% [Chain B UniRef90 accession]=UniRef90_Q8IZQ1 [Chain B UniRef90 boundaries]=3341-3354 [Chain A name]=Gamma-aminobutyric acid receptor-associated protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O95166 [Chain A UniProt boundaries]=1-117 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_O95166 [Chain A UniRef90 boundaries]=1-117 [Entry] [Accession]=DI1100024 [Disorder status]=Inferred from motif [Kd]=5.40E-06 [Name]=Tah1 in complex with the Hsp90 C-terminal tail [Source organism]=Saccharomyces cerevisiae [PDB ID]=2lsv [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Tetratricopeptide [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (TPR repeat-binding motif - http://www.uniprot.org/uniprot/P02829#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=A solved monomeric structure of the domain involved in the interaction is represented by PDB ID 2lsu. [Chain B name]=ATP-dependent molecular chaperone HSP82 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P02829 [Chain B UniProt boundaries]=701-709 [Chain B UniProt coverage]=1.3% [Chain B UniRef90 accession]=UniRef90_P02829 [Chain B UniRef90 boundaries]=701-709 [Chain A name]=TPR repeat-containing protein associated with Hsp90 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P25638 [Chain A UniProt boundaries]=2-111 [Chain A UniProt coverage]=99.1% [Chain A UniRef90 accession]=UniRef90_P25638 [Chain A UniRef90 boundaries]=2-111 [Entry] [Accession]=DI1100025 [Disorder status]=Inferred from motif [Kd]=5.40E-06 [Name]=PSD-95 PDZ1 with 5HT2C receptor peptide [Source organism]=Rattus norvegicus [PDB ID]=2mho [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PDZ [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (PDZ-binding motif - http://www.uniprot.org/uniprot/P08909#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 1iu0. [Chain B name]=5-hydroxytryptamine receptor 2C [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=P08909 [Chain B UniProt boundaries]=452-460 [Chain B UniProt coverage]=2% [Chain B UniRef90 accession]=UniRef90_P08909 [Chain B UniRef90 boundaries]=452-460 [Chain A name]=Disks large homolog 4 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=P31016 [Chain A UniProt boundaries]=57-155 [Chain A UniProt coverage]=13.7% [Chain A UniRef90 accession]=UniRef90_P31016 [Chain A UniRef90 boundaries]=60-155 [Entry] [Accession]=DI1000111 [Disorder status]=Inferred from homology [Kd]=7.00E-07 (PMID:20181956) [Name]=Ataxin-2 peptide bound by poly(A)-binding protein [Source organism]=Homo sapiens [PDB ID]=3ktr [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=PABP [Type chain B]=Disordered [Evidence chain B]=The corresponding region of a homologous protein has been shown to be disordered in the 106-127 region described in IDEAL entry IID00582 (covers 100% of the sequence present in the structure). The protein region involved in the interaction contains a known functional linear motif (LIG_PAM2_1). [Type chain A]=Ordered [Evidence chain A]=The PABP domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00658). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1i2t. [Chain B name]=Ataxin-2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q99700 [Chain B UniProt boundaries]=912-928 [Chain B UniProt coverage]=1.3% [Chain B UniRef90 accession]=UniRef90_Q99700 [Chain B UniRef90 boundaries]=912-928 [Chain A name]=Polyadenylate-binding protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P11940 [Chain A UniProt boundaries]=539-626 [Chain A UniProt coverage]=13.8% [Chain A UniRef90 accession]=UniRef90_P11940 [Chain A UniRef90 boundaries]=544-626 [Entry] [Accession]=DI1110007 [Disorder status]=Inferred from motif [Kd]=7.00E-07 (PMID:20181956) [Name]=Complex between SAP97 PDZ2 and 5HT2A receptor peptide [Source organism]=Rattus norvegicus / Mus musculus [PDB ID]=4oaj [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=PDZ [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (PDZ-binding motif - http://www.uniprot.org/uniprot/P14842#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2k1z. [Chain B name]=5-hydroxytryptamine receptor 2A [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=P14842 [Chain B UniProt boundaries]=465-471 [Chain B UniProt coverage]=1.5% [Chain B UniRef90 accession]=UniRef90_P14842 [Chain B UniRef90 boundaries]=465-471 [Chain A name]=Disks large homolog 1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q811D0 [Chain A UniProt boundaries]=315-406 [Chain A UniProt coverage]=10.2% [Chain A UniRef90 accession]=UniRef90_Q12959 [Chain A UniRef90 boundaries]=317-406 [Entry] [Accession]=DI1000112 [Disorder status]=Inferred from motif [Kd]=2.04E-04 (PMID:18940607) [Name]=C-terminal calponin homology domain of alpha-parvin in complex with paxillin LD2 motif [Source organism]=Homo sapiens [PDB ID]=2vzg [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.8 [Domain]=CH [Type chain A]=Disordered [Evidence chain A]=The protein region involved in the interaction contains a known functional linear motif (LD motif 2 - http://www.uniprot.org/uniprot/P49023#family_and_domains). [Type chain B]=Ordered [Evidence chain B]=The CH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00307). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1bkr. [Chain A name]=Paxillin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P49023 [Chain A UniProt boundaries]=141-160 [Chain A UniProt coverage]=3.4% [Chain A UniRef90 accession]=UniRef90_P49023 [Chain A UniRef90 boundaries]=141-160 [Chain B name]=Alpha-parvin [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9NVD7 [Chain B UniProt boundaries]=242-372 [Chain B UniProt coverage]=35.2% [Chain B UniRef90 accession]=UniRef90_Q9NVD7 [Chain B UniRef90 boundaries]=242-372 [Entry] [Accession]=DI1000113 [Disorder status]=Inferred from motif [Kd]=7.70E-07 (PMID:26011858) [Name]=ULK3 kinase MIT domain bound to an IST1 homolog peptide [Source organism]=Homo sapiens [PDB ID]=4wzx [PDB chain IDs]=E:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.39 [Domain]=MIT [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (MIT-interacting motif - http://www.uniprot.org/uniprot/P53990#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The MIT domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04212). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2jqh. [Chain E name]=IST1 homolog [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P53990 [Chain E UniProt boundaries]=342-364 [Chain E UniProt coverage]=6.3% [Chain E UniRef90 accession]=UniRef90_P53990 [Chain E UniRef90 boundaries]=342-364 [Chain A name]=Serine/threonine-protein kinase ULK3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q6PHR2 [Chain A UniProt boundaries]=355-449 [Chain A UniProt coverage]=20.1% [Chain A UniRef90 accession]=UniRef90_Q6PHR2 [Chain A UniRef90 boundaries]=359-449 [Entry] [Accession]=DI1000114 [Disorder status]=Inferred from motif [Kd]=7.00E-06 (PMID:19204326) [Name]=eTAFH domain of AML1-ETO complexed with HEB peptide [Source organism]=Homo sapiens [PDB ID]=2knh [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=TAF homology [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (9aaTAD motif - http://www.uniprot.org/uniprot/Q99081#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The TAF homology domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF07531). A solved monomeric structure of the domain is represented by PDB ID 2pp4. [Chain B name]=Transcription factor 12 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q99081 [Chain B UniProt boundaries]=11-28 [Chain B UniProt coverage]=2.6% [Chain B UniRef90 accession]=UniRef90_Q99081 [Chain B UniRef90 boundaries]=11-28 [Chain A name]=Protein CBFA2T1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q06455 [Chain A UniProt boundaries]=114-216 [Chain A UniProt coverage]=17.1% [Chain A UniRef90 accession]=UniRef90_Q06455 [Chain A UniRef90 boundaries]=119-216 [Entry] [Accession]=DI1100026 [Disorder status]=Inferred from motif [Kd]=8.00E-06 [Name]=PDZ2 from PTP-BL in complex with the C-terminal ligand from the APC protein [Source organism]=Mus musculus [PDB ID]=1vj6 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PDZ [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_1). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 1gm1. [Chain B name]=Adenomatous polyposis coli protein [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q61315 [Chain B UniProt boundaries]=2834-2845 [Chain B UniProt coverage]=0.4% [Chain B UniRef90 accession]=UniRef90_Q61315 [Chain B UniRef90 boundaries]=2834-2845 [Chain A name]=Tyrosine-protein phosphatase non-receptor type 13 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q64512 [Chain A UniProt boundaries]=1343-1444 [Chain A UniProt coverage]=4.2% [Chain A UniRef90 accession]=UniRef90_Q64512 [Chain A UniRef90 boundaries]=1351-1444 [Entry] [Accession]=DI1010042 [Disorder status]=Inferred from motif [Kd]=1.40E-04 (PMID:18940607) [Name]=C-terminal calponin homology domain of alpha-parvin in complex with paxillin LD4 motif [Source organism]=Rattus norvegicus / Homo sapiens [PDB ID]=2vzi [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.2 [Domain]=CH [Type chain A]=Disordered [Evidence chain A]=The protein region involved in the interaction contains a known functional linear motif (LD motif 4 - http://www.uniprot.org/uniprot/P49023#family_and_domains). [Type chain B]=Ordered [Evidence chain B]=The CH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00307). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1bkr. [Chain A name]=Paxillin [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=Q66H76 [Chain A UniProt boundaries]=291-310 [Chain A UniProt coverage]=3.4% [Chain A UniRef90 accession]=UniRef90_Q66H76 [Chain A UniRef90 boundaries]=291-310 [Chain B name]=Alpha-parvin [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9NVD7 [Chain B UniProt boundaries]=242-372 [Chain B UniProt coverage]=35.2% [Chain B UniRef90 accession]=UniRef90_Q9NVD7 [Chain B UniRef90 boundaries]=242-372 [Entry] [Accession]=DI1000115 [Disorder status]=Inferred from motif [Kd]=9.60E-05 (PMID:18940607) [Name]=C-terminal calponin homology domain of alpha-parvin in complex with paxillin LD1 motif [Source organism]=Homo sapiens [PDB ID]=2k2r [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=CH [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LD motif 1 - http://www.uniprot.org/uniprot/P49023#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The CH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00307). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1bkr. [Chain B name]=Paxillin [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P49023 [Chain B UniProt boundaries]=3-12 [Chain B UniProt coverage]=1.7% [Chain B UniRef90 accession]=UniRef90_P49023 [Chain B UniRef90 boundaries]=3-12 [Chain A name]=Alpha-parvin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9NVD7 [Chain A UniProt boundaries]=244-372 [Chain A UniProt coverage]=34.7% [Chain A UniRef90 accession]=UniRef90_Q9NVD7 [Chain A UniRef90 boundaries]=244-372 [Related structures]=2vzd [Entry] [Accession]=DI1000116 [Disorder status]=Inferred from motif [Kd]=2.70E-05 [Name]=Beta-parvin CH2 domain in complex with paxillin LD1 motif [Source organism]=Homo sapiens [PDB ID]=4edn [PDB chain IDs]=K:A [PDB note]=Chains B, C, D, E, F, G, H, I, J, L, K, M, N, O, P and Q were removed as chains A and K highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.90 [Domain]=CH [Type chain K]=Disordered [Evidence chain K]=The protein region involved in the interaction contains a known functional linear motif (LD motif 1 - http://www.uniprot.org/uniprot/P49023#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The CH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00307). A solved monomeric structure of the domain is represented by PDB ID 4edl. [Chain K name]=Paxillin [Chain K source organism]=Homo sapiens [Chain K UniProt accession]=P49023 [Chain K UniProt boundaries]=2-13 [Chain K UniProt coverage]=2% [Chain K UniRef90 accession]=UniRef90_P49023 [Chain K UniRef90 boundaries]=2-13 [Chain A name]=Beta-parvin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9HBI1 [Chain A UniProt boundaries]=238-364 [Chain A UniProt coverage]=34.9% [Chain A UniRef90 accession]=UniRef90_Q9HBI1 [Chain A UniRef90 boundaries]=238-364 [Entry] [Accession]=DI2000005 [Disorder status]=Inferred from motif [Kd]=1.70E-05 (PMID:21632544) [Name]=CCM3 in complex with paxillin LD1 [Source organism]=Homo sapiens [PDB ID]=3rqe [PDB chain IDs]=E:CD [PDB note]=Chains A and B were removed as chains C, D and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=CCM3 [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (LD motif 1 - http://www.uniprot.org/uniprot/P49023#family_and_domains). [Type chain C]=Ordered component [Evidence chain C]=The CCM3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form; a solved structure of the domain dimer without bound ligands is represented by PDB ID 3l8i. [Type chain D]=Ordered component [Evidence chain D]=The CCM3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form; a solved structure of the domain dimer without bound ligands is represented by PDB ID 3l8i. [Modified residues chain D]=S,S-(2-hydroxyethyl)thiocysteine#C#2659 [Chain E name]=Paxillin [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P49023 [Chain E UniProt boundaries]=5-14 [Chain E UniProt coverage]=1.7% [Chain E UniRef90 accession]=UniRef90_P49023 [Chain E UniRef90 boundaries]=5-14 [Chain C name]=Programmed cell death protein 10 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q9BUL8 [Chain C UniProt boundaries]=1-210 [Chain C UniProt coverage]=99.1% [Chain C UniRef90 accession]=UniRef90_Q9BUL8 [Chain C UniRef90 boundaries]=1-210 [Chain D name]=Programmed cell death protein 10 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=Q9BUL8 [Chain D UniProt boundaries]=12-208 [Chain D UniProt coverage]=92.9% [Chain D UniRef90 accession]=UniRef90_Q9BUL8 [Chain D UniRef90 boundaries]=12-208 [Entry] [Accession]=DI2000006 [Disorder status]=Inferred from motif [Kd]=3.90E-05 (PMID:21632544) [Name]=CCM3 in complex with paxillin LD2 [Source organism]=Homo sapiens [PDB ID]=3rqf [PDB chain IDs]=E:AB [PDB note]=Chains C and D were removed as chains A, B and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.70 [Domain]=CCM3 [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (LD motif 2 - http://www.uniprot.org/uniprot/P49023#family_and_domains). [Type chain A]=Ordered component [Evidence chain A]=The CCM3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form; a solved structure of the domain dimer without bound ligands is represented by PDB ID 3l8i. [Type chain B]=Ordered component [Evidence chain B]=The CCM3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form; a solved structure of the domain dimer without bound ligands is represented by PDB ID 3l8i. [Chain E name]=Paxillin [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P49023 [Chain E UniProt boundaries]=143-153 [Chain E UniProt coverage]=1.9% [Chain E UniRef90 accession]=UniRef90_P49023 [Chain E UniRef90 boundaries]=143-153 [Chain A name]=Programmed cell death protein 10 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9BUL8 [Chain A UniProt boundaries]=16-212 [Chain A UniProt coverage]=92.9% [Chain A UniRef90 accession]=UniRef90_Q9BUL8 [Chain A UniRef90 boundaries]=16-212 [Chain B name]=Programmed cell death protein 10 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9BUL8 [Chain B UniProt boundaries]=10-210 [Chain B UniProt coverage]=94.8% [Chain B UniRef90 accession]=UniRef90_Q9BUL8 [Chain B UniRef90 boundaries]=10-210 [Entry] [Accession]=DI1000117 [Disorder status]=Inferred from motif [Kd]=4.00E-06 (PMID:14527389) [Name]=Paxillin LD2 motif bound to the Focal Adhesion Targeting (FAT) domain of the Focal Adhesion Kinase [Source organism]=Homo sapiens [PDB ID]=1ow8 [PDB chain IDs]=D:A [PDB note]=Chains B, C and F were removed as chains A and D highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.85 [Domain]=Focal adhesion targeting region [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a known functional linear motif (LD motif 2 - http://www.uniprot.org/uniprot/P49023#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The Focal adhesion targeting region domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03623). A solved monomeric structure of the domain from a closely homologous protein is represented by PDB ID 1qvx. [Chain D name]=Paxillin [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P49023 [Chain D UniProt boundaries]=142-153 [Chain D UniProt coverage]=2% [Chain D UniRef90 accession]=UniRef90_P49023 [Chain D UniRef90 boundaries]=142-153 [Chain A name]=Focal adhesion kinase 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q05397 [Chain A UniProt boundaries]=892-1052 [Chain A UniProt coverage]=15.3% [Chain A UniRef90 accession]=UniRef90_Q05397 [Chain A UniRef90 boundaries]=892-1052 [Entry] [Accession]=DI1010043 [Disorder status]=Inferred from motif [Kd]=6.90E-06 [Name]=Pyk2 interacting with Paxillin LD2 Motif (1) [Source organism]=Gallus gallus / Homo sapiens [PDB ID]=4r32 [PDB chain IDs]=B:A [PDB note]=Chain C was removed as chains A and B highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.50 [Domain]=Focal adhesion targeting region [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LD motif 2 - http://www.uniprot.org/uniprot/P49023#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The Focal adhesion targeting region domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03623). A solved monomeric structure of the domain is represented by PDB ID 2lk4. [Chain B name]=Paxillin [Chain B source organism]=Gallus gallus [Chain B UniProt accession]=P49024 [Chain B UniProt boundaries]=139-162 [Chain B UniProt coverage]=4.3% [Chain B UniRef90 accession]=UniRef90_P49024 [Chain B UniRef90 boundaries]=139-162 [Chain A name]=Protein-tyrosine kinase 2-beta [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q14289 [Chain A UniProt boundaries]=867-1005 [Chain A UniProt coverage]=13.8% [Chain A UniRef90 accession]=UniRef90_Q14289 [Chain A UniRef90 boundaries]=871-1005 [Entry] [Accession]=DI1010044 [Disorder status]=Inferred from motif [Kd]=3.52E-05 [Name]=Pyk2 interacting with Paxillin LD2 Motif (2) [Source organism]=Gallus gallus / Homo sapiens [PDB ID]=4r32 [PDB chain IDs]=C:A [PDB note]=Chain B was removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.50 [Domain]=Focal adhesion targeting region [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LD motif 2 - http://www.uniprot.org/uniprot/P49023#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The Focal adhesion targeting region domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03623). A solved monomeric structure of the domain is represented by PDB ID 2lk4. [Chain C name]=Paxillin [Chain C source organism]=Gallus gallus [Chain C UniProt accession]=P49024 [Chain C UniProt boundaries]=139-162 [Chain C UniProt coverage]=4.3% [Chain C UniRef90 accession]=UniRef90_P49024 [Chain C UniRef90 boundaries]=139-162 [Chain A name]=Protein-tyrosine kinase 2-beta [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q14289 [Chain A UniProt boundaries]=867-1005 [Chain A UniProt coverage]=13.8% [Chain A UniRef90 accession]=UniRef90_Q14289 [Chain A UniRef90 boundaries]=871-1005 [Entry] [Accession]=DI1000118 [Disorder status]=Inferred from motif [Kd]=4.00E-06 (PMID:14527389) [Name]=Paxillin LD4 motif bound to the Focal Adhesion Targeting (FAT) domain of the Focal Adhesion Kinase [Source organism]=Homo sapiens [PDB ID]=1ow6 [PDB chain IDs]=F:C [PDB note]=Chains A, B and D were removed as chains C and F highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.35 [Domain]=Focal adhesion targeting region [Type chain F]=Disordered [Evidence chain F]=The protein region involved in the interaction contains a known functional linear motif (LD motif 4 - http://www.uniprot.org/uniprot/P49023#family_and_domains). [Type chain C]=Ordered [Evidence chain C]=The Focal adhesion targeting region domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03623). A solved monomeric structure of the domain from a closely homologous protein is represented by PDB ID 1qvx. [Chain F name]=Paxillin [Chain F source organism]=Homo sapiens [Chain F UniProt accession]=P49023 [Chain F UniProt boundaries]=263-274 [Chain F UniProt coverage]=2% [Chain F UniRef90 accession]=UniRef90_P49023 [Chain F UniRef90 boundaries]=263-274 [Chain C name]=Focal adhesion kinase 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q05397 [Chain C UniProt boundaries]=892-1052 [Chain C UniProt coverage]=15.3% [Chain C UniRef90 accession]=UniRef90_Q05397 [Chain C UniRef90 boundaries]=892-1052 [Related structures]=1ow7 [Entry] [Accession]=DI1000119 [Disorder status]=Inferred from motif [Kd]=8.00E-06 (PMID:25174335) [Name]=Pyk2 interacting with Paxillin LD4 Motif (1) [Source organism]=Homo sapiens [PDB ID]=3gm1 [PDB chain IDs]=E:A [PDB note]=Chains B, C, D and F were removed as chains A and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.95 [Domain]=Focal adhesion targeting region [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (LIG_FAT_LD_1). [Type chain A]=Ordered [Evidence chain A]=The Focal adhesion targeting region domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03623). A solved monomeric structure of the domain is represented by PDB ID 2lk4. [Chain E name]=Paxillin [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P49023 [Chain E UniProt boundaries]=262-274 [Chain E UniProt coverage]=2.2% [Chain E UniRef90 accession]=UniRef90_P49023 [Chain E UniRef90 boundaries]=262-274 [Chain A name]=Protein-tyrosine kinase 2-beta [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q14289 [Chain A UniProt boundaries]=857-1009 [Chain A UniProt coverage]=15.2% [Chain A UniRef90 accession]=UniRef90_Q14289 [Chain A UniRef90 boundaries]=861-1009 [Related structures]=3u3f [Entry] [Accession]=DI1000120 [Disorder status]=Inferred from motif [Kd]=4.63E-05 (PMID:25174335) [Name]=Pyk2 interacting with Paxillin LD4 Motif (2) [Source organism]=Homo sapiens [PDB ID]=3gm1 [PDB chain IDs]=F:A [PDB note]=Chains B, C, D and E were removed as chains A and F highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.95 [Domain]=Focal adhesion targeting region [Type chain F]=Disordered [Evidence chain F]=The protein region involved in the interaction contains a known functional linear motif (LIG_FAT_LD_1). [Type chain A]=Ordered [Evidence chain A]=The Focal adhesion targeting region domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03623). A solved monomeric structure of the domain is represented by PDB ID 2lk4. [Chain F name]=Paxillin [Chain F source organism]=Homo sapiens [Chain F UniProt accession]=P49023 [Chain F UniProt boundaries]=262-274 [Chain F UniProt coverage]=2.2% [Chain F UniRef90 accession]=UniRef90_P49023 [Chain F UniRef90 boundaries]=262-274 [Chain A name]=Protein-tyrosine kinase 2-beta [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q14289 [Chain A UniProt boundaries]=857-1009 [Chain A UniProt coverage]=15.2% [Chain A UniRef90 accession]=UniRef90_Q14289 [Chain A UniRef90 boundaries]=861-1009 [Related structures]=3u3f [Entry] [Accession]=DI2000007 [Disorder status]=Inferred from motif [Kd]=2.30E-05 (PMID:21632544) [Name]=CCM3 in complex with paxillin LD4 [Source organism]=Homo sapiens [PDB ID]=3rqg [PDB chain IDs]=E:CD [PDB note]=Chains A and B were removed as chains C, D and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=CCM3 [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (LD motif 4 - http://www.uniprot.org/uniprot/P49023#family_and_domains). [Type chain C]=Ordered component [Evidence chain C]=The CCM3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form; a solved structure of the domain dimer without bound ligands is represented by PDB ID 3l8i. [Type chain D]=Ordered component [Evidence chain D]=The CCM3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form; a solved structure of the domain dimer without bound ligands is represented by PDB ID 3l8i. [Chain E name]=Paxillin [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P49023 [Chain E UniProt boundaries]=262-273 [Chain E UniProt coverage]=2% [Chain E UniRef90 accession]=UniRef90_P49023 [Chain E UniRef90 boundaries]=262-273 [Chain C name]=Programmed cell death protein 10 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q9BUL8 [Chain C UniProt boundaries]=1-210 [Chain C UniProt coverage]=99.1% [Chain C UniRef90 accession]=UniRef90_Q9BUL8 [Chain C UniRef90 boundaries]=1-210 [Chain D name]=Programmed cell death protein 10 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=Q9BUL8 [Chain D UniProt boundaries]=8-210 [Chain D UniProt coverage]=95.8% [Chain D UniRef90 accession]=UniRef90_Q9BUL8 [Chain D UniRef90 boundaries]=8-210 [Entry] [Accession]=DI1100027 [Disorder status]=Inferred from motif [Kd]=2.70E-07 (PMID:16095618) [Name]=RIM1alpha PDZ domain in complex with an ELKS1b C-terminal peptide [Source organism]=Rattus norvegicus [PDB ID]=1zub [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PDZ [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_2). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2k1z. [Chain B name]=ELKS/Rab6-interacting/CAST family member 1 [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=Q811U3 [Chain B UniProt boundaries]=938-948 [Chain B UniProt coverage]=1.2% [Chain B UniRef90 accession]=UniRef90_Q8IUD2-4 [Chain B UniRef90 boundaries]=939-948 [Chain A name]=Regulating synaptic membrane exocytosis protein 1 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=Q9JIR4 [Chain A UniProt boundaries]=592-705 [Chain A UniProt coverage]=7.1% [Chain A UniRef90 accession]=UniRef90_Q9JIR4 [Chain A UniRef90 boundaries]=595-705 [Entry] [Accession]=DI1400002 [Disorder status]=Confirmed [Kd]=2.70E-07 (PMID:16095618) [Name]=Doc in complex with the C-terminal peptide of Phd [Source organism]=Enterobacteria phage P1 [PDB ID]=3dd7 [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=Fido [Type chain B]=Disordered [Evidence chain B]=The 41-73 region described in DisProt entry DP00288 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Fido domain involved in the interaction is known to adopt a stable structure in isolation (PMID:20603017). [Modified residues chain B]=selenomethionine#M#70 [Chain B name]=Antitoxin phd [Chain B source organism]=Enterobacteria phage P1 [Chain B UniProt accession]=Q06253 [Chain B UniProt boundaries]=51-73 [Chain B UniProt coverage]=31.5% [Chain B UniRef90 accession]=UniRef90_Q06253 [Chain B UniRef90 boundaries]=51-73 [Chain A name]=Protein kinase doc [Chain A source organism]=Enterobacteria phage P1 [Chain A UniProt accession]=Q06259 [Chain A UniProt boundaries]=1-126 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q06259 [Chain A UniRef90 boundaries]=1-126 [Related structures]=3k33,3kh2 [Entry] [Accession]=DI1000121 [Disorder status]=Inferred from motif [Kd]=2.70E-07 (PMID:16095618) [Name]=LC3-LIR peptide complex [Source organism]=Homo sapiens [PDB ID]=5d94 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.53 [Domain]=Atg8 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_LIR_Gen_1). [Type chain A]=Ordered [Evidence chain A]=The Atg8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02991). A solved monomeric structure of the domain is represented by PDB ID 1v49. [Chain B name]=FYVE and coiled-coil domain-containing protein 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9BQS8 [Chain B UniProt boundaries]=1276-1288 [Chain B UniProt coverage]=0.9% [Chain B UniRef90 accession]=UniRef90_Q9BQS8 [Chain B UniRef90 boundaries]=1276-1288 [Chain A name]=Microtubule-associated proteins 1A/1B light chain 3B [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9GZQ8 [Chain A UniProt boundaries]=1-125 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q9GZQ8 [Chain A UniRef90 boundaries]=1-125 [Entry] [Accession]=DI1010045 [Disorder status]=Inferred from motif [Kd]=5.40E-07 (PMID:27246247) [Name]=FYCO1 LIR in complex with LC3A [Source organism]=Mus musculus / Homo sapiens [PDB ID]=5cx3 [PDB chain IDs]=E:A [PDB note]=Chains B, C, D, F, G and H were removed as chains A and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=Atg8 [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (LIG_LIR_Gen_1). [Type chain A]=Ordered [Evidence chain A]=The Atg8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02991). A solved monomeric structure of the domain is represented by PDB ID 3wal. [Chain E name]=FYVE and coiled-coil domain-containing protein 1 [Chain E source organism]=Mus musculus [Chain E UniProt accession]=Q8VDC1 [Chain E UniProt boundaries]=1232-1257 [Chain E UniProt coverage]=1.8% [Chain E UniRef90 accession]=UniRef90_Q8VDC1 [Chain E UniRef90 boundaries]=1232-1257 [Chain A name]=Microtubule-associated proteins 1A/1B light chain 3A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9H492 [Chain A UniProt boundaries]=1-121 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q9H492 [Chain A UniRef90 boundaries]=1-121 [Entry] [Accession]=DI1000122 [Disorder status]=Inferred from motif [Kd]=1.00E-05 (PMID:19297620) [Name]=Harmonin PDZ2 in complex with the carboxyl tail peptide of cadherin23 [Source organism]=Homo sapiens [PDB ID]=2kbs [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PDZ [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_1). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 1x5n. [Chain B name]=Cadherin-23 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9H251 [Chain B UniProt boundaries]=3347-3354 [Chain B UniProt coverage]=0.2% [Chain B UniRef90 accession]=UniRef90_Q9H251 [Chain B UniRef90 boundaries]=3347-3354 [Chain A name]=Harmonin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9Y6N9 [Chain A UniProt boundaries]=208-299 [Chain A UniProt coverage]=16.7% [Chain A UniRef90 accession]=UniRef90_Q9Y6N9 [Chain A UniRef90 boundaries]=208-299 [Entry] [Accession]=DI1000123 [Disorder status]=Inferred from motif [Kd]=3.34E-05 (PMID:17928862) [Name]=VPS4A MIT:CHMP1A complex [Source organism]=Homo sapiens [PDB ID]=2jq9 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=MIT [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (MIT-interacting motif - http://www.uniprot.org/uniprot/Q9HD42#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The MIT domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04212). A solved monomeric structure of the domain is represented by PDB ID 2jqh. [Chain B name]=Charged multivesicular body protein 1a [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9HD42 [Chain B UniProt boundaries]=180-196 [Chain B UniProt coverage]=8.7% [Chain B UniRef90 accession]=UniRef90_Q9HD42 [Chain B UniRef90 boundaries]=180-196 [Chain A name]=Vacuolar protein sorting-associated protein 4A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UN37 [Chain A UniProt boundaries]=1-84 [Chain A UniProt coverage]=19.2% [Chain A UniRef90 accession]=UniRef90_Q9UN37 [Chain A UniRef90 boundaries]=1-84 [Entry] [Accession]=DI1000124 [Disorder status]=Inferred from motif [Kd]=3.34E-05 (PMID:17928862) [Name]=MIT domain-containing protein 1:CHMP1A complex [Source organism]=Homo sapiens [PDB ID]=4a5x [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.91 [Domain]=MIT [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (MIT-interacting motif - http://www.uniprot.org/uniprot/Q9HD42#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The MIT domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04212). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2jqh. [Chain C name]=Charged multivesicular body protein 1a [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q9HD42 [Chain C UniProt boundaries]=184-196 [Chain C UniProt coverage]=6.6% [Chain C UniRef90 accession]=UniRef90_Q9HD42 [Chain C UniRef90 boundaries]=184-196 [Chain A name]=MIT domain-containing protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q8WV92 [Chain A UniProt boundaries]=9-85 [Chain A UniProt coverage]=30.9% [Chain A UniRef90 accession]=UniRef90_Q8WV92 [Chain A UniRef90 boundaries]=9-85 [Related structures]=2ymb [Entry] [Accession]=DI1100028 [Disorder status]=Inferred from motif [Kd]=3.34E-05 (PMID:17928862) [Name]=Saccharomyces cerevisiae Atg8 complexed with Atg32 AIM [Source organism]=Saccharomyces cerevisiae [PDB ID]=3vxw [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=3.00 [Domain]=Atg8 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_LIR_Gen_1). [Type chain A]=Ordered [Evidence chain A]=The Atg8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02991). A solved monomeric structure of the domain is represented by PDB ID 2kwc. [Chain B name]=Autophagy-related protein 32 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P40458 [Chain B UniProt boundaries]=85-90 [Chain B UniProt coverage]=1.1% [Chain B UniRef90 accession]=UniRef90_C7GUR3 [Chain B UniRef90 boundaries]=85-90 [Chain A name]=Autophagy-related protein 8 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P38182 [Chain A UniProt boundaries]=1-116 [Chain A UniProt coverage]=99.1% [Chain A UniRef90 accession]=UniRef90_Q6FXR8 [Chain A UniRef90 boundaries]=1-116 [Entry] [Accession]=DI1120006 [Disorder status]=Confirmed [Kd]=1.58E-06 [Name]=M11, the BCL-2 homolog of murine Gamma-herpesvirus 68, complexed with mouse Beclin-1 [Source organism]=Mus musculus / Murid herpesvirus 4 [PDB ID]=3bl2 [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=Bcl-2 homology [Type chain C]=Disordered [Evidence chain C]=The interacting region of Beclin-1 is embedded in an unstructured protein segment (PMID:18248095). The protein region involved in the interaction contains a known functional linear motif (LIG_BH_BH3_1). [Type chain A]=Ordered [Evidence chain A]=Bcl-2 homology (BH) domains, such as the one involved in the interaction, are known to adopt a stable structure in isolation (see Pfam domain PF15286). A solved monomeric structure of the domain is represented by PDB ID 2abo. [Chain C name]=Beclin-1 [Chain C source organism]=Mus musculus [Chain C UniProt accession]=O88597 [Chain C UniProt boundaries]=106-124 [Chain C UniProt coverage]=4.2% [Chain C UniRef90 accession]=UniRef90_Q14457 [Chain C UniRef90 boundaries]=108-126 [Chain A name]=Bcl-2 homolog (Gene 16?) [Chain A source organism]=Murid herpesvirus 4 [Chain A UniProt accession]=P89884 [Chain A UniProt boundaries]=5-135 [Chain A UniProt coverage]=76.6% [Chain A UniRef90 accession]=UniRef90_P89884 [Chain A UniRef90 boundaries]=5-135 [Related structures]=3dvu,4mi8 [Entry] [Accession]=DI1110008 [Disorder status]=Confirmed [Kd]=1.58E-06 [Name]=Karyopheryn (importin) alpha in complex with nucleoplasmin NLS peptide [Source organism]=Xenopus laevis / Saccharomyces cerevisiae [PDB ID]=1ee5 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=Armadillo repeat [Type chain B]=Disordered [Evidence chain B]=The 120-200 region described in DisProt entry DP00217 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (TRG_NLS_Bipartite_1). [Type chain A]=Ordered [Evidence chain A]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ial. [Chain B name]=Nucleoplasmin [Chain B source organism]=Xenopus laevis [Chain B UniProt accession]=P05221 [Chain B UniProt boundaries]=153-171 [Chain B UniProt coverage]=9.5% [Chain B UniRef90 accession]=UniRef90_P05221 [Chain B UniRef90 boundaries]=153-171 [Chain A name]=Importin subunit alpha [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=Q02821 [Chain A UniProt boundaries]=90-510 [Chain A UniProt coverage]=77.7% [Chain A UniRef90 accession]=UniRef90_Q02821 [Chain A UniRef90 boundaries]=90-510 [Entry] [Accession]=DI1110009 [Disorder status]=Confirmed [Kd]=2.70E-09 (PMID:22248489) [Name]=Importin alpha - nucleoplasmin NLS complex [Source organism]=Xenopus laevis / Mus musculus [PDB ID]=1ejy [PDB chain IDs]=N:I [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.90 [Domain]=Armadillo repeat [Type chain N]=Disordered [Evidence chain N]=The 120-200 region described in DisProt entry DP00217 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (TRG_NLS_Bipartite_1). [Type chain I]=Ordered [Evidence chain I]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain is represented by PDB ID 1ial. [Modified residues chain I]=phosphotyrosine#Y#5 [Chain N name]=Nucleoplasmin [Chain N source organism]=Xenopus laevis [Chain N UniProt accession]=P05221 [Chain N UniProt boundaries]=155-170 [Chain N UniProt coverage]=8% [Chain N UniRef90 accession]=UniRef90_P05221 [Chain N UniRef90 boundaries]=155-170 [Chain I name]=Importin subunit alpha-1 [Chain I source organism]=Mus musculus [Chain I UniProt accession]=P52293 [Chain I UniProt boundaries]=72-497 [Chain I UniProt coverage]=80.5% [Chain I UniRef90 accession]=UniRef90_P52293 [Chain I UniRef90 boundaries]=72-497 [Related structures]=3ul1 [Entry] [Accession]=DI1100029 [Disorder status]=Confirmed [Kd]=2.00E-09 (PMID:16222336) [Name]=Importin alpha with nucleoporin [Source organism]=Saccharomyces cerevisiae [PDB ID]=2c1t [PDB chain IDs]=D:B [PDB note]=Chains A and C were removed as chains B and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=Armadillo repeat [Type chain D]=Disordered [Evidence chain D]=The 1-720 region described in DisProt entry DP00222 and in IDEAL entry IID50007 cover 100% of the sequence present in the structure. [Type chain B]=Ordered [Evidence chain B]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ial. [Chain D name]=Nucleoporin NUP2 [Chain D source organism]=Saccharomyces cerevisiae [Chain D UniProt accession]=P32499 [Chain D UniProt boundaries]=2-46 [Chain D UniProt coverage]=6.3% [Chain D UniRef90 accession]=UniRef90_P32499 [Chain D UniRef90 boundaries]=2-46 [Chain B name]=Importin subunit alpha [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=Q02821 [Chain B UniProt boundaries]=88-510 [Chain B UniProt coverage]=78% [Chain B UniRef90 accession]=UniRef90_Q02821 [Chain B UniRef90 boundaries]=88-510 [Related structures]=1un0 [Entry] [Accession]=DI1010046 [Disorder status]=Confirmed [Kd]=5.00E-08 [Name]=4E-BP1 peptide bound to EIF4E [Source organism]=Homo sapiens / Mus musculus [PDB ID]=1ej4 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.25 [Domain]=IF4E [Type chain B]=Disordered [Evidence chain B]=The interacting region of 4E-BP1 has been shown to be intrinsically disordered (PMID:9684899 and PMID:10394359). The 1-118 region described in IDEAL entry IID00170 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_eIF4E_1). [Type chain A]=Ordered [Evidence chain A]=The IF4E domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01652). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3tf2. [Chain B name]=Eukaryotic translation initiation factor 4E-binding protein 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q13541 [Chain B UniProt boundaries]=51-64 [Chain B UniProt coverage]=11.9% [Chain B UniRef90 accession]=UniRef90_Q13541 [Chain B UniRef90 boundaries]=51-64 [Chain A name]=Eukaryotic translation initiation factor 4E [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P63073 [Chain A UniProt boundaries]=32-217 [Chain A UniProt coverage]=85.7% [Chain A UniRef90 accession]=UniRef90_P63073 [Chain A UniRef90 boundaries]=32-217 [Related structures]=1ejh,5bxv [Entry] [Accession]=DI1000125 [Disorder status]=Confirmed [Kd]=3.80E-06 [Name]=complex of eIF4E-m7GpppA-4EBP1 peptide [Source organism]=Homo sapiens [PDB ID]=1wkw [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=IF4E [Type chain B]=Disordered [Evidence chain B]=The interacting region of 4E-BP1 has been shown to be intrinsically disordered (PMID:9684899 and PMID:10394359). The 1-118 region described in IDEAL entry IID00170 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_eIF4E_1). [Type chain A]=Ordered [Evidence chain A]=The IF4E domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01652). A solved monomeric structure of the domain is represented by PDB ID 3tf2. [Chain B name]=Eukaryotic translation initiation factor 4E-binding protein 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q13541 [Chain B UniProt boundaries]=47-66 [Chain B UniProt coverage]=16.9% [Chain B UniRef90 accession]=UniRef90_Q13541 [Chain B UniRef90 boundaries]=47-66 [Chain A name]=Eukaryotic translation initiation factor 4E [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P06730 [Chain A UniProt boundaries]=27-217 [Chain A UniProt coverage]=88% [Chain A UniRef90 accession]=UniRef90_P06730 [Chain A UniRef90 boundaries]=27-217 [Related structures]=2v8w,2v8x,2v8y,3u7x,4ued,5ekv [Entry] [Accession]=DI1000126 [Disorder status]=Confirmed [Kd]=9.70E-09 (PMID:11237626) [Name]=Transcription factor 7-like 2 bound to beta-catenin [Source organism]=Homo sapiens [PDB ID]=2gl7 [PDB chain IDs]=E:D [PDB note]=Chains A, B, C and F were removed as chains E and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=Armadillo repeat [Type chain E]=Disordered [Evidence chain E]=The 1-56 region described in DisProt entry DP00175 and the 1-130 region described in IDEAL entry IID00100 cover 100% of the sequence present in the structure. [Type chain D]=Ordered [Evidence chain D]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain is represented by PDB ID 2z6h. [Chain E name]=Transcription factor 7-like 2 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=Q9NQB0 [Chain E UniProt boundaries]=12-50 [Chain E UniProt coverage]=6.3% [Chain E UniRef90 accession]=UniRef90_Q9NQB0 [Chain E UniRef90 boundaries]=12-50 [Chain D name]=Catenin beta-1 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P35222 [Chain D UniProt boundaries]=147-662 [Chain D UniProt coverage]=66.1% [Chain D UniRef90 accession]=UniRef90_Q02248 [Chain D UniRef90 boundaries]=147-662 [Related structures]=1jdh,1jpw [Entry] [Accession]=DI1100030 [Disorder status]=Confirmed [Kd]=9.70E-09 (PMID:11237626) [Name]=Proteinase A complexed with IA3 peptide inhibitor [Source organism]=Saccharomyces cerevisiae [PDB ID]=1dpj [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=Aspartyl protease [Type chain B]=Disordered [Evidence chain B]=The 1-68 region described in DisProt entry DP00179 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The aspartyl protease domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00026). A solved monomeric structure of the domain is represented by PDB ID 2jxr. [Chain B name]=Protease A inhibitor 3 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P01094 [Chain B UniProt boundaries]=3-31 [Chain B UniProt coverage]=42.6% [Chain B UniRef90 accession]=UniRef90_P01094 [Chain B UniRef90 boundaries]=3-31 [Chain A name]=Saccharopepsin [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P07267 [Chain A UniProt boundaries]=77-405 [Chain A UniProt coverage]=81.2% [Chain A UniRef90 accession]=UniRef90_P07267 [Chain A UniRef90 boundaries]=77-405 [Related structures]=1dp5,1g0v [Entry] [Accession]=DI1200001 [Disorder status]=Confirmed [Kd]=9.70E-09 (PMID:11237626) [Name]=Ribonucleotide reductase R1 protein mutant with ribonucleotide reductase R2 [Source organism]=Escherichia coli [PDB ID]=1r1r [PDB chain IDs]=D:A [PDB note]=Chains B, C, E, F and P were removed as chains A and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.90 [Domain]=Ribonucleotide reductase, barrel domain [Type chain D]=Disordered [Evidence chain D]=The 342-376 region described in DisProt entry DP00107 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The ribonucleotide reductase barrel domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02867). A solved monomeric structure of the domain is represented by PDB ID 1rlr. [Chain D name]=Ribonucleoside-diphosphate reductase 1 subunit beta [Chain D source organism]=Escherichia coli [Chain D UniProt accession]=P69924 [Chain D UniProt boundaries]=361-376 [Chain D UniProt coverage]=4.3% [Chain D UniRef90 accession]=UniRef90_P69925 [Chain D UniRef90 boundaries]=361-376 [Chain A name]=Ribonucleoside-diphosphate reductase 1 subunit alpha [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=P00452 [Chain A UniProt boundaries]=4-729 [Chain A UniProt coverage]=95.4% [Chain A UniRef90 accession]=UniRef90_P00452 [Chain A UniRef90 boundaries]=4-729 [Related structures]=2r1r,2x0x,2xak,2xap,2xav,2xaw,2xax,2xay,2xaz,2xo4,2xo5,3r1r,3uus,4erm,4erp,4r1r,5cns,5cnt,5cnu,5cnv,5r1r,6r1r,7r1r [Entry] [Accession]=DI1110010 [Disorder status]=Confirmed [Kd]=1.50E-06 [Name]=Ciboulot thymosin beta4-domain in complex with skeletal actin. [Source organism]=Drosophila melanogaster / Oryctolagus cuniculus [PDB ID]=1sqk [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=Actin [Type chain B]=Disordered [Evidence chain B]=The interacting region of ciboulot has been shown to be intrinsically disordered (PMID:15163409). The protein region involved in the interaction contains consensus actin binding beta-thymosin D1 motif (PMID:22193718, PMID:15163409). [Type chain A]=Ordered [Evidence chain A]=Actin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00022). A solved monomeric structure of the domain is represented by PDB ID 1j6z. [Chain B name]=Ciboulot, isoform A [Chain B source organism]=Drosophila melanogaster [Chain B UniProt accession]=O97428 [Chain B UniProt boundaries]=10-34 [Chain B UniProt coverage]=19.4% [Chain B UniRef90 accession]=UniRef90_O97428 [Chain B UniRef90 boundaries]=10-34 [Chain A name]=Actin, alpha skeletal muscle [Chain A source organism]=Oryctolagus cuniculus [Chain A UniProt accession]=P68135 [Chain A UniProt boundaries]=7-373 [Chain A UniProt coverage]=97.3% [Chain A UniRef90 accession]=UniRef90_P68133 [Chain A UniRef90 boundaries]=7-373 [Related structures]=3sjh,3u8x,3u9d,3u9z [Entry] [Accession]=DI1000127 [Disorder status]=Inferred from homology [Kd]=2.10E-06 (PMID:16903783) [Name]=Beta appendage from Ap2 in complex with beta-arrestin peptide [Source organism]=Homo sapiens [PDB ID]=2iv8 [PDB chain IDs]=P:A [PDB note]=Chain Q was removed as chains A and P represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=Adaptin C-terminal domain [Type chain P]=Disordered [Evidence chain P]=The corresponding region of a closely homologous protein has been shown to be disordered in the 383-393 region described in DisProt entry DP00390 (covers 78% of the sequence present in the structure). The protein region involved in the interaction contains a known functional linear motif (TRG_AP2beta_CARGO_1). [Type chain A]=Ordered [Evidence chain A]=Adaptin C-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domains PF02883/PF09066). A solved monomeric structure of the domain is represented by PDB ID 1e42. [Chain P name]=Beta-arrestin-1 [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=P49407 [Chain P UniProt boundaries]=383-396 [Chain P UniProt coverage]=3.3% [Chain P UniRef90 accession]=UniRef90_P49407 [Chain P UniRef90 boundaries]=383-396 [Chain A name]=AP-2 complex subunit beta [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63010 [Chain A UniProt boundaries]=705-937 [Chain A UniProt coverage]=24.9% [Chain A UniRef90 accession]=UniRef90_P63010 [Chain A UniRef90 boundaries]=705-937 [Entry] [Accession]=DI1000128 [Disorder status]=Confirmed [Kd]=1.60E-09 [Name]=Mcl-1:Bim BH3 complex [Source organism]=Homo sapiens [PDB ID]=2nl9 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.55 [Domain]=Bcl-2 homology [Type chain B]=Disordered [Evidence chain B]=The interacting region (Bcl-x interacting BH3 domain, see Pfam domain PF08946) of Bim has been shown to be intrinsically disordered in an aqueous environment, and undergo localized conformational change, involving helix formation of the contact residues in the BH3 domain, upon binding to its partner protein (PMID:16645638 and PMID:15694340). The protein region involved in the interaction contains a known functional linear motif (LIG_BH_BH3_1). [Type chain A]=Ordered [Evidence chain A]=Bcl-2 homology (BH) domains, such as the one involved in the interaction, are known to adopt a stable structure in isolation (see Pfam domain PF00452). A solved monomeric structure of the domain is represented by PDB ID 2mhs. [Chain B name]=Bcl-2-like protein 11 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O43521 [Chain B UniProt boundaries]=141-166 [Chain B UniProt coverage]=13.1% [Chain B UniRef90 accession]=UniRef90_O43521 [Chain B UniRef90 boundaries]=141-166 [Chain A name]=Induced myeloid leukemia cell differentiation protein Mcl-1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q07820 [Chain A UniProt boundaries]=171-327 [Chain A UniProt coverage]=44.9% [Chain A UniRef90 accession]=UniRef90_Q07820 [Chain A UniRef90 boundaries]=174-327 [Related structures]=3kj0,3kj1,3kj2 [Entry] [Accession]=DI1000129 [Disorder status]=Confirmed [Kd]=1.60E-09 [Name]=Tandem SH2 domain of the Syk tyrosine kinase bound to a dually phosphorylated ITAM peptide from T-cell surface glycoprotein CD3 epsilon chain [Source organism]=Homo sapiens [PDB ID]=1a81 [PDB chain IDs]=B:A [PDB note]=Chains C, D, E, F, G, H, I, J, K and L were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.00 [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The 153-207 region described in DisProt entry DP00506 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (ITAM - PF02189). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain is represented by PDB ID 4fl2. [Modified residues chain B]=phosphotyrosine#Y#170|phosphotyrosine#Y#181 [Chain B name]=T-cell surface glycoprotein CD3 epsilon chain [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P07766 [Chain B UniProt boundaries]=186-203 [Chain B UniProt coverage]=8.7% [Chain B UniRef90 accession]=UniRef90_P0776 [Chain B UniRef90 boundaries]=186-203 [Chain A name]=Tyrosine-protein kinase SYK [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P43405 [Chain A UniProt boundaries]=9-262 [Chain A UniProt coverage]=40% [Chain A UniRef90 accession]=UniRef90_P43405 [Chain A UniRef90 boundaries]=9-262 [Entry] [Accession]=DI1100031 [Disorder status]=Inferred from homology [Kd]=1.60E-09 [Name]=cAMP-dependent protein kinase complexed with an unmodified PKI-alpha peptide [Source organism]=Mus musculus [PDB ID]=1apm [PDB chain IDs]=I:E [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Protein kinase [Type chain I]=Disordered [Evidence chain I]=The corresponding region of a closely homologous protein has been shown to be disordered in the 1-76 region described in DisProt entry DP00015 (covers 100% of the sequence present in the structure). [Type chain E]=Ordered [Evidence chain E]=The protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 4nts. [Chain I name]=cAMP-dependent protein kinase inhibitor alpha [Chain I source organism]=Mus musculus [Chain I UniProt accession]=P63248 [Chain I UniProt boundaries]=6-25 [Chain I UniProt coverage]=26.3% [Chain I UniRef90 accession]=UniRef90_P63248 [Chain I UniRef90 boundaries]=6-25 [Chain E name]=cAMP-dependent protein kinase catalytic subunit alpha [Chain E source organism]=Mus musculus [Chain E UniProt accession]=P05132 [Chain E UniProt boundaries]=11-351 [Chain E UniProt coverage]=97.2% [Chain E UniRef90 accession]=UniRef90_P17612 [Chain E UniRef90 boundaries]=11-351 [Related structures]=1atp,2cpk,2gnf,2gng,2qur,3fjq,3ow3,3qal,3qam,4dfx,4dfz,4dg0,4dg2,4dg3,4dh1,4dh3,4dh5,4dh7,4dh8,1l3r,1q8u,1svh,1yds,1ydt [Entry] [Accession]=DI1200002 [Disorder status]=Confirmed [Kd]=9.20E-07 [Name]=TolB in complex with a peptide of the colicin E9 T-domain [Source organism]=Escherichia coli [PDB ID]=2ivz [PDB chain IDs]=E:A [PDB note]=Chains B, C, D, F, G and H were removed as chains A and E represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=WD40 [Type chain E]=Disordered [Evidence chain E]=The 1-83 region described in DisProt entry DP00342 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The WD40-like beta propeller repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF07676). A solved monomeric structure of the domain is represented by PDB ID 1crz. [Chain E name]=Colicin-E9 [Chain E source organism]=Escherichia coli [Chain E UniProt accession]=P09883 [Chain E UniProt boundaries]=32-46 [Chain E UniProt coverage]=2.6% [Chain E UniRef90 accession]=UniRef90_P09883 [Chain E UniRef90 boundaries]=32-46 [Chain A name]=Protein TolB [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=P0A855 [Chain A UniProt boundaries]=34-431 [Chain A UniProt coverage]=92.6% [Chain A UniRef90 accession]=UniRef90_Q83MM7 [Chain A UniRef90 boundaries]=34-431 [Entry] [Accession]=DI1000130 [Disorder status]=Confirmed [Kd]=7.66E-08 (PMID:19920178) [Name]=Tandem SH2 domains of ZAP-70 with 19-mer zeta1 peptide [Source organism]=Homo sapiens [PDB ID]=2oq1 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The 52-134 region described in DisProt entry DP00200 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (ITAM - PF02189). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1m61. [Modified residues chain B]=phosphotyrosine#Y#304|phosphotyrosine#Y#315 [Chain B name]=T-cell surface glycoprotein CD3 zeta chain [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P20963 [Chain B UniProt boundaries]=69-87 [Chain B UniProt coverage]=11.6% [Chain B UniRef90 accession]=UniRef90_P20963 [Chain B UniRef90 boundaries]=69-87 [Chain A name]=Tyrosine-protein kinase ZAP-70 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P43403 [Chain A UniProt boundaries]=3-256 [Chain A UniProt coverage]=41% [Chain A UniRef90 accession]=UniRef90_P43403 [Chain A UniRef90 boundaries]=3-256 [Related structures]=4xz1 [Entry] [Accession]=DI1000131 [Disorder status]=Confirmed [Kd]=7.70E-08 (PMID:9660763) [Name]=Cdc42 in complex with the GTPase-binding domain of WASP [Source organism]=Homo sapiens [PDB ID]=1cee [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Ras [Type chain B]=Disordered [Evidence chain B]=The interacting region of WASP (GBD/CRIB motif - PF00786) has been shown to be intrinsically disordered (PMID:9660763 and PMID:15821030). The 230-310 region described in IDEAL entry IID00269 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The ras domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00071). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1aje. [Chain B name]=Wiskott-Aldrich syndrome protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P42768 [Chain B UniProt boundaries]=230-288 [Chain B UniProt coverage]=11.8% [Chain B UniRef90 accession]=UniRef90_P42768 [Chain B UniRef90 boundaries]=230-288 [Chain A name]=Cell division control protein 42 homolog [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P60953 [Chain A UniProt boundaries]=1-179 [Chain A UniProt coverage]=93.7% [Chain A UniRef90 accession]=UniRef90_P60953 [Chain A UniRef90 boundaries]=1-179 [Entry] [Accession]=DI1010047 [Disorder status]=Inferred from homology [Kd]=7.70E-08 (PMID:9660763) [Name]=Beta-catenin:Tcf complex [Source organism]=Xenopus laevis / Homo sapiens [PDB ID]=1g3j [PDB chain IDs]=B:A [PDB note]=Chains C and D was removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=Armadillo repeat [Type chain B]=Disordered [Evidence chain B]=The corresponding region of a closely homologous protein has been shown to be intrinsically disordered (PMID:11237626). [Type chain A]=Ordered [Evidence chain A]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain is represented by PDB ID 2z6h. [Chain B name]=Transcription factor 7-like 1-A [Chain B source organism]=Xenopus laevis [Chain B UniProt accession]=P70062 [Chain B UniProt boundaries]=2-52 [Chain B UniProt coverage]=9.2% [Chain B UniRef90 accession]=UniRef90_P70062 [Chain B UniRef90 boundaries]=2-52 [Chain A name]=Catenin beta-1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P35222 [Chain A UniProt boundaries]=134-664 [Chain A UniProt coverage]=68% [Chain A UniRef90 accession]=UniRef90_Q02248 [Chain A UniRef90 boundaries]=134-664 [Entry] [Accession]=DI1100032 [Disorder status]=Confirmed [Kd]=5.20E-11 [Name]=Beta-catenin:phosphorylated E-cadherin complex [Source organism]=Mus musculus [PDB ID]=1i7w [PDB chain IDs]=B:A [PDB note]=Chains C and D was removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Armadillo repeat [Type chain B]=Disordered [Evidence chain B]=The 812-884 region described in DisProt entry DP00159 and the 773-884 region described in IDEAL entry IID50003 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain is represented by PDB ID 2bct. [Modified residues chain B]=phosphoserine#S#684|phosphoserine#S#686|phosphoserine#S#692 [Chain B name]=Cadherin-1 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=P09803 [Chain B UniProt boundaries]=817-878 [Chain B UniProt coverage]=7% [Chain B UniRef90 accession]=UniRef90_P09803 [Chain B UniRef90 boundaries]=817-878 [Chain A name]=Catenin beta-1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q02248 [Chain A UniProt boundaries]=149-662 [Chain A UniProt coverage]=65.8% [Chain A UniRef90 accession]=UniRef90_Q02248 [Chain A UniRef90 boundaries]=149-662 [Entry] [Accession]=DI1010048 [Disorder status]=Confirmed [Kd]=1.10E-06 [Name]=GGA1 GAT N-terminal region in complex with ARF1 GTP form [Source organism]=Homo sapiens / Mus musculus [PDB ID]=1j2j [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.60 [Domain]=Arf [Type chain B]=Disordered [Evidence chain B]=The interacting region of GGA1 has been shown to be largely intrinsically disordered (PMID:12679809).The 166-089 region described in DisProt entry DP00314 cover 60% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Arf (ADP-ribosylation factor) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00025). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1o3y. [Chain B name]=ADP-ribosylation factor-binding protein GGA1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9UJY5 [Chain B UniProt boundaries]=168-208 [Chain B UniProt coverage]=6.4% [Chain B UniRef90 accession]=UniRef90_Q9UJY5 [Chain B UniRef90 boundaries]=168-208 [Chain A name]=ADP-ribosylation factor 2 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q8BSL7 [Chain A UniProt boundaries]=18-180 [Chain A UniProt coverage]=90.1% [Chain A UniRef90 accession]=UniRef90_Q8BSL7 [Chain A UniRef90 boundaries]=18-180 [Entry] [Accession]=DI1100033 [Disorder status]=Confirmed [Kd]=3.00E-09 (PMID:14675538) [Name]=Yeast translation initiation factor eIF4E in complex with m7GDP and eIF4GI [Source organism]=Saccharomyces cerevisiae [PDB ID]=1rf8 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=IF4E [Type chain B]=Disordered [Evidence chain B]=The 391-488 region described in DisProt entry DP00082 cover 98% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_eIF4E_1). [Type chain A]=Ordered [Evidence chain A]=The IF4E domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01652). A solved monomeric structure of the domain is represented by PDB ID 1ap8. [Chain B name]=Eukaryotic initiation factor 4F subunit p150 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P39935 [Chain B UniProt boundaries]=391-488 [Chain B UniProt coverage]=10.3% [Chain B UniRef90 accession]=UniRef90_P39935 [Chain B UniRef90 boundaries]=391-488 [Chain A name]=Eukaryotic translation initiation factor 4E [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P07260 [Chain A UniProt boundaries]=1-213 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P07260 [Chain A UniRef90 boundaries]=1-213 [Entry] [Accession]=DI1020012 [Disorder status]=Inferred from homology [Kd]=3.00E-09 (PMID:14675538) [Name]=Neurotoxin BoNT/A complexed with Synaptosomal-associated protein 25 [Source organism]=Homo sapiens / Clostridium botulinum [PDB ID]=1xtg [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=Peptidase_M27 [Type chain B]=Disordered [Evidence chain B]=The corresponding region of a closely homologous protein has been shown to be disordered in the 1-206 region described in DisProt entry DP00068 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=Peptidase_M27 domain of neurotoxin BoNT/A is known to adopt a stable structure in isolation (see Pfam domain PF01742). A solved monomeric structure of the domain is represented by PDB ID 4ej5. [Chain B name]=Synaptosomal-associated protein 25 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P60880 [Chain B UniProt boundaries]=146-204 [Chain B UniProt coverage]=28.6% [Chain B UniRef90 accession]=UniRef90_P60880 [Chain B UniRef90 boundaries]=146-204 [Chain A name]=Botulinum neurotoxin type A [Chain A source organism]=Clostridium botulinum [Chain A UniProt accession]=P10845 [Chain A UniProt boundaries]=2-420 [Chain A UniProt coverage]=32.3% [Chain A UniRef90 accession]=UniRef90_P10845 [Chain A UniRef90 boundaries]=2-420 [Related structures]=3dda,3ddb,3zur [Entry] [Accession]=DI1000132 [Disorder status]=Confirmed [Kd]=3.00E-09 (PMID:14675538) [Name]=Grb14 BPS region in complex with the insulin receptor tyrosine kinase [Source organism]=Homo sapiens [PDB ID]=2auh [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=3.20 [Domain]=Protein tyrosine kinase [Type chain B]=Disordered [Evidence chain B]=The 361-435 region described in DisProt entry DP00230 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The protein tyrosine kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF07714). A solved monomeric structure of the domain is represented by PDB ID 1irk. [Chain B name]=Growth factor receptor-bound protein 14 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q14449 [Chain B UniProt boundaries]=373-409 [Chain B UniProt coverage]=6.9% [Chain B UniRef90 accession]=UniRef90_Q14449 [Chain B UniRef90 boundaries]=373-409 [Chain A name]=Insulin receptor [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P06213 [Chain A UniProt boundaries]=1011-1310 [Chain A UniProt coverage]=21.7% [Chain A UniRef90 accession]=UniRef90_P06213 [Chain A UniRef90 boundaries]=1011-1310 [Entry] [Accession]=DI1110011 [Disorder status]=Confirmed [Kd]=2.00E-09 (PMID:17636256) [Name]=Rat PP1-gamma complexed with mouse protein phosphatase inhibitor-2 [Source organism]=Mus musculus / Rattus norvegicus [PDB ID]=2o8a [PDB chain IDs]=I:A [PDB note]=Chains B and J were removed as chains A and I represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.61 [Domain]=Calcineurin-like phosphoesterase [Type chain I]=Disordered [Evidence chain I]=The 1-206 region described in DisProt entry DP00815 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The calcineurin-like phosphoesterase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00149). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4ut2. [Chain I name]=Protein phosphatase inhibitor 2 [Chain I source organism]=Mus musculus [Chain I UniProt accession]=Q9DCL8 [Chain I UniProt boundaries]=12-169 [Chain I UniProt coverage]=76.7% [Chain I UniRef90 accession]=UniRef90_Q9DCL8 [Chain I UniRef90 boundaries]=12-169 [Chain A name]=Serine/threonine-protein phosphatase PP1-gamma catalytic subunit [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=P63088 [Chain A UniProt boundaries]=6-300 [Chain A UniProt coverage]=91.3% [Chain A UniRef90 accession]=UniRef90_P63087 [Chain A UniRef90 boundaries]=6-300 [Related structures]=2o8g [Entry] [Accession]=DI3000004 [Disorder status]=Confirmed [Kd]=8.80E-08 (PMID:15681588) [Name]=C-terminal region of p21(WAF1/CIP1) complexed with human PCNA. [Source organism]=Homo sapiens [PDB ID]=1axc [PDB chain IDs]=B:ACE [PDB note]=Chains D and F were removed as chains A, B, C and E represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=PCNA [Type chain B]=Disordered [Evidence chain B]=The 1-164 region described in DisProt entry DP00016 and in IDEAL entry IID00043 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains four known functional linear motifs (DEG_CRL4_CDT2_1, DOC_CYCLIN_1, LIG_PCNA_PIPBox_1, TRG_NLS_Bipartite_1) and a known modification site (MOD_PKB_1). [Type chain A]=Ordered component [Evidence chain A]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60. [Type chain C]=Ordered component [Evidence chain C]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60. [Type chain E]=Ordered component [Evidence chain E]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60. [Chain B name]=Cyclin-dependent kinase inhibitor 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P38936 [Chain B UniProt boundaries]=143-160 [Chain B UniProt coverage]=11% [Chain B UniRef90 accession]=UniRef90_P38936 [Chain B UniRef90 boundaries]=143-160 [Chain A name]=Proliferating cell nuclear antigen [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P12004 [Chain A UniProt boundaries]=1-255 [Chain A UniProt coverage]=97.7% [Chain A UniRef90 accession]=UniRef90_P12004 [Chain A UniRef90 boundaries]=1-255 [Chain C name]=Proliferating cell nuclear antigen [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P12004 [Chain C UniProt boundaries]=1-255 [Chain C UniProt coverage]=97.7% [Chain C UniRef90 accession]=UniRef90_P12004 [Chain C UniRef90 boundaries]=1-255 [Chain E name]=Proliferating cell nuclear antigen [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P12004 [Chain E UniProt boundaries]=1-255 [Chain E UniProt coverage]=97.7% [Chain E UniRef90 accession]=UniRef90_P12004 [Chain E UniRef90 boundaries]=1-255 [Related structures]=4rjf,5e0u [Entry] [Accession]=DI1000133 [Disorder status]=Confirmed [Kd]=8.80E-08 (PMID:15681588) [Name]=LARG PDZ domain in complex with C-terminal octa-peptide of Plexin B1 [Source organism]=Homo sapiens [PDB ID]=2os6 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PDZ [Type chain B]=Disordered [Evidence chain B]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 3hm6, 3su8, 3sua). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 2omj. [Chain B name]=Plexin-B1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O43157 [Chain B UniProt boundaries]=2128-2135 [Chain B UniProt coverage]=0.4% [Chain B UniRef90 accession]=UniRef90_O43157 [Chain B UniRef90 boundaries]=2128-2135 [Chain A name]=Rho guanine nucleotide exchange factor 12 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9NZN5 [Chain A UniProt boundaries]=63-151 [Chain A UniProt coverage]=5.8% [Chain A UniRef90 accession]=UniRef90_Q9NZN5 [Chain A UniRef90 boundaries]=67-151 [Entry] [Accession]=DI2010003 [Disorder status]=Confirmed [Kd]=8.80E-08 (PMID:15681588) [Name]=Double SPOP MATH domain in complex with a MacroH2A peptide [Source organism]=Homo sapiens / Pongo abelii [PDB ID]=3hsv [PDB chain IDs]=M:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.43 [Domain]=MATH [Type chain M]=Disordered [Evidence chain M]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 1zr5, 3iid, 3iif, 1zr3, 2fxk). The protein region involved in the interaction contains a known functional linear motif (DEG_SPOP_SBC_1). [Type chain A]=Ordered [Evidence chain A]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00917). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2f1w. [Type chain B]=Ordered [Evidence chain B]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00917). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2f1w. [Chain M name]=Core histone macro-H2A.1 [Chain M source organism]=Homo sapiens [Chain M UniProt accession]=O75367 [Chain M UniProt boundaries]=171-186 [Chain M UniProt coverage]=4.3% [Chain M UniRef90 accession]=UniRef90_O75367 [Chain M UniRef90 boundaries]=172-186 [Chain A name]=Speckle-type POZ protein [Chain A source organism]=Pongo abelii [Chain A UniProt accession]=Q5NVK7 [Chain A UniProt boundaries]=22-166 [Chain A UniProt coverage]=38.8% [Chain A UniRef90 accession]=UniRef90_O43791 [Chain A UniRef90 boundaries]=28-166 [Chain B name]=Speckle-type POZ protein [Chain B source organism]=Pongo abelii [Chain B UniProt accession]=Q5NVK7 [Chain B UniProt boundaries]=22-166 [Chain B UniProt coverage]=38.8% [Chain B UniRef90 accession]=UniRef90_O43791 [Chain B UniRef90 boundaries]=28-166 [Entry] [Accession]=DI1000134 [Disorder status]=Confirmed [Kd]=9.30E-06 (PMID:22000412) [Name]=Kinetochore-BUBR1 kinase complex [Source organism]=Homo sapiens [PDB ID]=3si5 [PDB chain IDs]=Y:B [PDB note]=Chains A and X were removed as chains B and Y represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=BUB1 N-terminal [Type chain Y]=Disordered [Evidence chain Y]=The interacting region of the protein has been shown to undergo a disorder-to-order transition upon binding (PMID:22000412). The protein region involved in the interaction contains a Blinkin motif (IxFxxFIxRL) to bind BUBR1 (PMID:22000412). [Type chain B]=Ordered [Evidence chain B]=The BUB1 N-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF08311). A solved monomeric structure of the domain represented by PDB ID 2wvi. [Chain Y name]=Protein CASC5 [Chain Y source organism]=Homo sapiens [Chain Y UniProt accession]=Q8NG31 [Chain Y UniProt boundaries]=232-252 [Chain Y UniProt coverage]=0.9% [Chain Y UniRef90 accession]=UniRef90_Q8NG31 [Chain Y UniRef90 boundaries]=232-252 [Chain B name]=Mitotic checkpoint serine/threonine-protein kinase BUB1 beta [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O60566 [Chain B UniProt boundaries]=45-220 [Chain B UniProt coverage]=16.8% [Chain B UniRef90 accession]=UniRef90_O60566 [Chain B UniRef90 boundaries]=49-208 [Entry] [Accession]=DI1000135 [Disorder status]=Inferred from motif [Kd]=9.30E-06 (PMID:22000412) [Name]=Second bromodomain of Brd4 with di-acetylated Twist peptide [Source organism]=Homo sapiens [PDB ID]=2mjv [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Bromodomain [Type chain A]=Disordered [Evidence chain A]=The protein region involved in the interaction contains a known functional GK-X-GK linear motif (PMID:24525235). [Type chain B]=Ordered [Evidence chain B]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 2i8n. [Modified residues chain A]=N(6)-acetyllysine#K#6|N(6)-acetyllysine#K#9 [Chain A name]=Twist-related protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q15672 [Chain A UniProt boundaries]=68-79 [Chain A UniProt coverage]=5.9% [Chain A UniRef90 accession]=UniRef90_P26687 [Chain A UniRef90 boundaries]=68-74 [Chain B name]=Bromodomain-containing protein 4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O60885 [Chain B UniProt boundaries]=333-460 [Chain B UniProt coverage]=9.4% [Chain B UniRef90 accession]=UniRef90_O60885 [Chain B UniRef90 boundaries]=333-460 [Entry] [Accession]=DI1000136 [Disorder status]=Confirmed [Kd]=1.60E-06 (PMID:26245978) [Name]=LEDGF/p75 IBD in complex with POGZ peptide (1389-1404) [Source organism]=Homo sapiens [PDB ID]=2n3a [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=LEDGF [Type chain A]=Disordered [Evidence chain A]=The interacting region of the protein has been shown to undergo a disorder-to-order transition upon binding (PMID:22000412). The protein region involved in the interaction contains a IBD-binding motif [ED]xExFxGF that is common to LEDGF/p75 partners. [Type chain B]=Ordered [Evidence chain B]=The Lens epithelium-derived growth factor (LEDGF) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF11467). A solved monomeric structure of the domain is represented by PDB ID 1z9e. [Chain A name]=Pogo transposable element with ZNF domain [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q7Z3K3 [Chain A UniProt boundaries]=1389-1404 [Chain A UniProt coverage]=1.1% [Chain A UniRef90 accession]=UniRef90_Q7Z3K3 [Chain A UniRef90 boundaries]=1389-1404 [Chain B name]=PC4 and SFRS1-interacting protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O75475 [Chain B UniProt boundaries]=348-426 [Chain B UniProt coverage]=14.9% [Chain B UniRef90 accession]=UniRef90_O75475 [Chain B UniRef90 boundaries]=348-426 [Entry] [Accession]=DI1000137 [Disorder status]=Confirmed [Kd]=1.60E-06 (PMID:26245978) [Name]=Human spliceosomal protein complex p14-SF3b155 (unmodified) [Source organism]=Homo sapiens [PDB ID]=2fho [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=RRM [Type chain A]=Disordered [Evidence chain A]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB ID: 5ife). [Type chain B]=Ordered [Evidence chain B]=The RRM domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00076). A solved monomeric structure of a homologue is represented by PDB ID 2m52. [Chain A name]=Splicing factor 3B subunit 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O75533 [Chain A UniProt boundaries]=378-424 [Chain A UniProt coverage]=3.6% [Chain A UniRef90 accession]=UniRef90_O75533 [Chain A UniRef90 boundaries]=379-424 [Chain B name]=Splicing factor 3B subunit 6 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9Y3B4 [Chain B UniProt boundaries]=7-93 [Chain B UniProt coverage]=69.6% [Chain B UniRef90 accession]=UniRef90_Q9Y3B4 [Chain B UniRef90 boundaries]=8-93 [Related structures]=3lqv,2f9j [Entry] [Accession]=DI1000138 [Disorder status]=Inferred from motif [Kd]=2.03E-05 (PMID:17190833) [Name]=EIF3B-RRM bound to EIF3J peptide [Source organism]=Homo sapiens [PDB ID]=2krb [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=RRM [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional N-terminal acidic (NTA) linear motif (PMID:20060839). [Type chain A]=Ordered [Evidence chain A]=The RRM domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00076). A solved monomeric structure of a homologue is represented by PDB ID 2m52. [Chain B name]=Eukaryotic translation initiation factor 3 subunit J [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O75822 [Chain B UniProt boundaries]=45-55 [Chain B UniProt coverage]=4.3% [Chain B UniRef90 accession]=UniRef90_O75822 [Chain B UniRef90 boundaries]=45-55 [Chain A name]=Eukaryotic translation initiation factor 3 subunit B [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P55884 [Chain A UniProt boundaries]=184-264 [Chain A UniProt coverage]=10% [Chain A UniRef90 accession]=UniRef90_P55884 [Chain A UniRef90 boundaries]=184-264 [Entry] [Accession]=DI1200003 [Disorder status]=Confirmed [Kd]=2.03E-05 (PMID:17190833) [Name]=Glutaredoxin 1 in complex with a C-terminal peptide from ribonucleoside-diphosphate reductase 1 [Source organism]=Escherichia coli [PDB ID]=1qfn [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Glutaredoxin [Type chain B]=Disordered [Evidence chain B]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 4erm, 4erp, 5cns, 5cnt, 5cnu, 5cnv, 1r1r, 2r1r, 2x0x, 2xak, 2xap, 2xav, 2xaw, 2xax, 2xay, 2xaz, 2xo4, 2xo5, 3r1r, 3uus, 4r1r, 5r1r, 6r1r, 7r1r, 1rlr). [Type chain A]=Ordered [Evidence chain A]=The glutaredoxin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00462). A solved monomeric structure of the domain is represented by PDB ID 1ego. [Chain B name]=Ribonucleoside-diphosphate reductase 1 subunit alpha [Chain B source organism]=Escherichia coli [Chain B UniProt accession]=P00452 [Chain B UniProt boundaries]=737-761 [Chain B UniProt coverage]=3.3% [Chain B UniRef90 accession]=UniRef90_P00452 [Chain B UniRef90 boundaries]=737-761 [Chain A name]=Glutaredoxin 1 [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=P68688 [Chain A UniProt boundaries]=1-85 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P68688 [Chain A UniRef90 boundaries]=1-85 [Entry] [Accession]=DI1100034 [Disorder status]=Inferred from homology [Kd]=1.48E-05 [Name]=RBM39 in complex with fragment of splicing factor U2AF [Source organism]=Mus musculus [PDB ID]=5cxt [PDB chain IDs]=B:A [PDB note]=Chains C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q and R were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=RRM [Type chain B]=Disordered [Evidence chain B]=The 85-89 region described in IDEAL entry IID00147 covers 71% of the binding sequence in a homologous protein. The protein region involved in the interaction contains a known functional UHM-ligand motif (ULM) (PMID:27050129). [Type chain A]=Ordered [Evidence chain A]=The RRM domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 2lq5. [Chain B name]=Splicing factor U2AF 65 kDa subunit [Chain B source organism]=Mus musculus [Chain B UniProt accession]=P26369 [Chain B UniProt boundaries]=84-112 [Chain B UniProt coverage]=6.1% [Chain B UniRef90 accession]=UniRef90_P26368 [Chain B UniRef90 boundaries]=85-112 [Chain A name]=RNA-binding protein 39 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q8VH51 [Chain A UniProt boundaries]=417-530 [Chain A UniProt coverage]=21.5% [Chain A UniRef90 accession]=UniRef90_Q14498 [Chain A UniRef90 boundaries]=418-530 [Related structures]=4ru2,1jmt [Entry] [Accession]=DI2010004 [Disorder status]=Confirmed [Kd]=1.30E-06 (PMID:16725153) [Name]=SDF1 (constitutively dimeric form) in complex with the CXCR4 N-terminus containing a sulfotyrosine at postition 21 [Source organism]=Pan troglodytes / Homo sapiens [PDB ID]=2k03 [PDB chain IDs]=B:AC [PDB note]=Chain D was removed as chains A, B and C highlight the biologically relevant interaction. [PDB experimental technique]=NMR [Domain]=IL8 [Type chain B]=Disordered [Evidence chain B]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 4rws, 3oe0, 3odu, 3oe8, 3oe9, 3oe6). [Type chain A]=Ordered [Evidence chain A]=The IL8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00048). A solved monomeric structure of the domain is represented by PDB ID 1sdf. [Type chain C]=Ordered [Evidence chain C]=The IL8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00048). A solved monomeric structure of the domain is represented by PDB ID 1sdf. [Modified residues chain B]=O-sulfo-L-tyrosine#Y#121 [Chain B name]=C-X-C chemokine receptor type 4 [Chain B source organism]=Pan troglodytes [Chain B UniProt accession]=P61072 [Chain B UniProt boundaries]=1-38 [Chain B UniProt coverage]=10.8% [Chain B UniRef90 accession]=UniRef90_P61073 [Chain B UniRef90 boundaries]=1-38 [Chain A name]=Stromal cell-derived factor 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P48061 [Chain A UniProt boundaries]=20-89 [Chain A UniProt coverage]=75.3% [Chain A UniRef90 accession]=UniRef90_P48061 [Chain A UniRef90 boundaries]=22-89 [Chain C name]=Stromal cell-derived factor 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P48061 [Chain C UniProt boundaries]=20-89 [Chain C UniProt coverage]=75.3% [Chain C UniRef90 accession]=UniRef90_P48061 [Chain C UniRef90 boundaries]=22-89 [Entry] [Accession]=DI1000139 [Disorder status]=Confirmed [Kd]=9.70E-10 (PMID:28325822) [Name]=SDF1 (constitutively monomeric form) in complex with the CXCR4 N-terminus [Source organism]=Homo sapiens [PDB ID]=2n55 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=IL8 [Type chain B]=Disordered [Evidence chain B]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 4rws, 3oe0, 3odu, 3oe8, 3oe9, 3oe6). [Type chain A]=Ordered [Evidence chain A]=The IL8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00048). A solved monomeric structure of the domain is represented by PDB ID 1sdf. [Chain B name]=C-X-C chemokine receptor type 4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P61073 [Chain B UniProt boundaries]=1-38 [Chain B UniProt coverage]=10.8% [Chain B UniRef90 accession]=UniRef90_P61073 [Chain B UniRef90 boundaries]=1-38 [Chain A name]=Stromal cell-derived factor 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P48061 [Chain A UniProt boundaries]=20-89 [Chain A UniProt coverage]=75.3% [Chain A UniRef90 accession]=UniRef90_P48061 [Chain A UniRef90 boundaries]=22-89 [Entry] [Accession]=DI2010005 [Disorder status]=Confirmed [Kd]=7.40E-05 (PMID:19819244) [Name]=p53 bound to S100B dimer [Source organism]=Homo sapiens / Rattus norvegicus [PDB ID]=1dt7 [PDB chain IDs]=X:AB [PDB note]=Chain Y was removed as chains A, B and X highlight the biologically relevant interaction. [PDB experimental technique]=NMR [Domain]=S100B [Type chain X]=Disordered [Evidence chain X]=The 320-393 region described in DisProt entry DP00086 and the 364-389 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. [Type chain A]=Ordered component [Evidence chain A]=S100B is known to adopt a stable structure in isolation in dimeric form. A solved structure of the domain dimer without bound ligands is represented by PDB ID 1qlk. [Type chain B]=Ordered component [Evidence chain B]=S100B is known to adopt a stable structure in isolation in dimeric form. A solved structure of the domain dimer without bound ligands is represented by PDB ID 1qlk. [Chain X name]=Cellular tumor antigen p53 [Chain X source organism]=Homo sapiens [Chain X UniProt accession]=P04637 [Chain X UniProt boundaries]=367-388 [Chain X UniProt coverage]=5.6% [Chain X UniRef90 accession]=UniRef90_P04637 [Chain X UniRef90 boundaries]=367-388 [Chain A name]=Protein S100-B [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=P04631 [Chain A UniProt boundaries]=1-92 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P04631 [Chain A UniRef90 boundaries]=1-92 [Chain B name]=Protein S100-B [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=P04631 [Chain B UniProt boundaries]=1-92 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P04631 [Chain B UniRef90 boundaries]=1-92 [Entry] [Accession]=DI2010006 [Disorder status]=Confirmed [Kd]=2.00E-07 (PMID:12470955) [Name]=TRTK-12 peptide bound to S100B dimer [Source organism]=Homo sapiens / Rattus norvegicus [PDB ID]=1mwn [PDB chain IDs]=X:AB [PDB note]=Chain Y was removed as chains A, B and X highlight the biologically relevant interaction. [PDB experimental technique]=NMR [Domain]=S100B [Type chain X]=Disordered [Evidence chain X]=The 265-276 region described in IDEAL entry IID00122 cover 100% of the sequence present in the structure. [Type chain A]=Ordered component [Evidence chain A]=S100B is known to adopt a stable structure in isolation in dimeric form. A solved structure of the domain dimer without bound ligands is represented by PDB ID 1qlk. [Type chain B]=Ordered component [Evidence chain B]=S100B is known to adopt a stable structure in isolation in dimeric form. A solved structure of the domain dimer without bound ligands is represented by PDB ID 1qlk. [Chain X name]=F-actin-capping protein subunit alpha-1 [Chain X source organism]=Homo sapiens [Chain X UniProt accession]=P52907 [Chain X UniProt boundaries]=265-276 [Chain X UniProt coverage]=4.2% [Chain X UniRef90 accession]=UniRef90_P52907 [Chain X UniRef90 boundaries]=265-276 [Chain A name]=Protein S100-B [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=P04631 [Chain A UniProt boundaries]=1-92 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P04631 [Chain A UniRef90 boundaries]=1-92 [Chain B name]=Protein S100-B [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=P04631 [Chain B UniProt boundaries]=1-92 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P04631 [Chain B UniRef90 boundaries]=1-92 [Entry] [Accession]=DI3010001 [Disorder status]=Confirmed [Kd]=5.80E-07 [Name]=C-terminal region of p21(WAF1/CIP1) complexed with A. thaliana PCNA. [Source organism]=Homo sapiens / Arabidopsis thaliana [PDB ID]=2zvv [PDB chain IDs]=X:ACE [PDB note]=Chains B and Y were removed as chains A, C, E and X represent the biologically relevant interaction. Chains C and E were generated using the biomatrices described in the PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=PCNA [Type chain X]=Disordered [Evidence chain X]=The 1-164 region described in DisProt entry DP00016 and in IDEAL entry IID00043 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains four known functional linear motifs (DEG_CRL4_CDT2_1, DOC_CYCLIN_1, LIG_PCNA_PIPBox_1, TRG_NLS_Bipartite_1) and a known modification site (MOD_PKB_1). [Type chain A]=Ordered component [Evidence chain A]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60. [Type chain C]=Ordered component [Evidence chain C]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60. [Type chain E]=Ordered component [Evidence chain E]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60. [Chain X name]=Cyclin-dependent kinase inhibitor 1 [Chain X source organism]=Homo sapiens [Chain X UniProt accession]=P38936 [Chain X UniProt boundaries]=139-160 [Chain X UniProt coverage]=13.4% [Chain X UniRef90 accession]=UniRef90_P38936 [Chain X UniRef90 boundaries]=139-160 [Chain A name]=Proliferating cellular nuclear antigen 1 [Chain A source organism]=Arabidopsis thaliana [Chain A UniProt accession]=Q9M7Q7 [Chain A UniProt boundaries]=1-256 [Chain A UniProt coverage]=97.3% [Chain A UniRef90 accession]=UniRef90_Q9M7Q7 [Chain A UniRef90 boundaries]=1-256 [Chain C name]=Proliferating cellular nuclear antigen 1 [Chain C source organism]=Arabidopsis thaliana [Chain C UniProt accession]=Q9M7Q7 [Chain C UniProt boundaries]=1-256 [Chain C UniProt coverage]=97.3% [Chain C UniRef90 accession]=UniRef90_Q9M7Q7 [Chain C UniRef90 boundaries]=1-256 [Chain E name]=Proliferating cellular nuclear antigen 1 [Chain E source organism]=Arabidopsis thaliana [Chain E UniProt accession]=Q9M7Q7 [Chain E UniProt boundaries]=1-256 [Chain E UniProt coverage]=97.3% [Chain E UniRef90 accession]=UniRef90_Q9M7Q7 [Chain E UniRef90 boundaries]=1-256 [Related structures]=2zvw [Entry] [Accession]=DI1100035 [Disorder status]=Confirmed [Kd]=5.80E-07 [Name]=Catenin beta-1 bound to Catenin alpha-2 [Source organism]=Mus musculus [PDB ID]=4ons [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=Vinculin [Type chain B]=Disordered [Evidence chain B]=The 1-133 region described in DisProt entry DP00341 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Vinculin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01044). A solved monomeric structure of the domain is represented by PDB ID 4p9t. [Chain B name]=Catenin beta-1 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q02248 [Chain B UniProt boundaries]=78-151 [Chain B UniProt coverage]=9.5% [Chain B UniRef90 accession]=UniRef90_Q02248 [Chain B UniRef90 boundaries]=78-151 [Chain A name]=Catenin alpha-2 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q61301 [Chain A UniProt boundaries]=18-260 [Chain A UniProt coverage]=25.5% [Chain A UniRef90 accession]=UniRef90_Q61301 [Chain A UniRef90 boundaries]=18-260 [Related structures]=1dow [Entry] [Accession]=DI1400003 [Disorder status]=Confirmed [Kd]=2.89E-08 (PMID:25865894) [Name]=Ebola virus nucleoprotein N-terminal fragment bound to a peptide derived from Ebola VP35 [Source organism]=Zaire ebolavirus [PDB ID]=4ypi [PDB chain IDs]=E:A [PDB note]=Chains B, C, D, F, G and H were removed as chains A and E represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.71 [Domain]=EbolaNP [Type chain E]=Disordered [Evidence chain E]=The 20-48 region described in DisProt entry DP00998 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Ebola virus nucleoprotein N-terminal (EbolaNP) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF05505). A solved monomeric structure of the domain is represented by PDB ID 4z9p. [Chain E name]=Polymerase cofactor VP35 [Chain E source organism]=Zaire ebolavirus [Chain E UniProt accession]=Q05127 [Chain E UniProt boundaries]=20-47 [Chain E UniProt coverage]=8.2% [Chain E UniRef90 accession]=UniRef90_Q05127 [Chain E UniRef90 boundaries]=20-47 [Chain A name]=Nucleoprotein [Chain A source organism]=Zaire ebolavirus [Chain A UniProt accession]=P18272 [Chain A UniProt boundaries]=38-385 [Chain A UniProt coverage]=47.1% [Chain A UniRef90 accession]=UniRef90_P18272 [Chain A UniRef90 boundaries]=38-385 [Related structures]=4zta,4ztg,4zti [Entry] [Accession]=DI4000001 [Disorder status]=Confirmed [Kd]=3.30E-06 [Name]=Cladosporin in complex with human lysyl-tRNA synthetase [Source organism]=Homo sapiens [PDB ID]=4ycu [PDB chain IDs]=C:ABDE [PDB note]=Chains D and E were generated using the biomatrices described in the PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=tRNA synthetase [Type chain C]=Disordered [Evidence chain C]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB ID: 4ycw). The protein region involved in the interaction contains two related conserved motifs (motif 1 and 2) linked by a natural Gly linker and a conserved sequence that makes a 180 degree turn (PMID:23159739). [Type chain A]=Ordered component [Evidence chain A]=tRNA synthetase domain involved in the interaction is known to adopt a stable structure in isolation in tetrameric form (see Pfam domain PF00152). A solved structure of the domain tetramer without bound ligands is represented by PDB ID 3bju. [Type chain B]=Ordered component [Evidence chain B]=tRNA synthetase domain involved in the interaction is known to adopt a stable structure in isolation in tetrameric form (see Pfam domain PF00152). A solved structure of the domain tetramer without bound ligands is represented by PDB ID 3bju. [Type chain D]=Ordered component [Evidence chain D]=tRNA synthetase domain involved in the interaction is known to adopt a stable structure in isolation in tetrameric form (see Pfam domain PF00152). A solved structure of the domain tetramer without bound ligands is represented by PDB ID 3bju. [Type chain E]=Ordered component [Evidence chain E]=tRNA synthetase domain involved in the interaction is known to adopt a stable structure in isolation in tetrameric form (see Pfam domain PF00152). A solved structure of the domain tetramer without bound ligands is represented by PDB ID 3bju. [Chain C name]=Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q13155 [Chain C UniProt boundaries]=1-36 [Chain C UniProt coverage]=11.3% [Chain C UniRef90 accession]=UniRef90_Q13155 [Chain C UniRef90 boundaries]=1-36 [Chain A name]=Lysine--tRNA ligase [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q15046 [Chain A UniProt boundaries]=72-576 [Chain A UniProt coverage]=84.6% [Chain A UniRef90 accession]=UniRef90_Q15046 [Chain A UniRef90 boundaries]=72-576 [Chain B name]=Lysine--tRNA ligase [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q15046 [Chain B UniProt boundaries]=72-576 [Chain B UniProt coverage]=84.6% [Chain B UniRef90 accession]=UniRef90_Q15046 [Chain B UniRef90 boundaries]=72-576 [Chain D name]=Lysine--tRNA ligase [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=Q15046 [Chain D UniProt boundaries]=72-576 [Chain D UniProt coverage]=84.6% [Chain D UniRef90 accession]=UniRef90_Q15046 [Chain D UniRef90 boundaries]=72-576 [Chain E name]=Lysine--tRNA ligase [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=Q15046 [Chain E UniProt boundaries]=72-576 [Chain E UniProt coverage]=84.6% [Chain E UniRef90 accession]=UniRef90_Q15046 [Chain E UniRef90 boundaries]=72-576 [Related structures]=4dpg [Entry] [Accession]=DI1110012 [Disorder status]=Confirmed [Kd]=1.00E-06 (PMID:19008859) [Name]=MAL-RPEL1 motif complexed to actin [Source organism]=Mus musculus / Oryctolagus cuniculus [PDB ID]=2v51 [PDB chain IDs]=F:B [PDB note]=Chains D and E were removed as chains B and F represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.35 [Domain]=Actin [Type chain F]=Disordered [Evidence chain F]=The 16-142 region described in IDEAL entry IID50055 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_Actin_RPEL_3). [Type chain B]=Ordered [Evidence chain B]=Actin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00022). A solved monomeric structure of the domain is represented by PDB ID 1j6z. [Chain F name]=MKL/myocardin-like protein 1 [Chain F source organism]=Mus musculus [Chain F UniProt accession]=Q8K4J6 [Chain F UniProt boundaries]=14-41 [Chain F UniProt coverage]=2.9% [Chain F UniRef90 accession]=UniRef90_Q8K4J6 [Chain F UniRef90 boundaries]=14-41 [Chain B name]=Actin, alpha skeletal muscle [Chain B source organism]=Oryctolagus cuniculus [Chain B UniProt accession]=P68135 [Chain B UniProt boundaries]=7-373 [Chain B UniProt coverage]=97.3% [Chain B UniRef90 accession]=UniRef90_P68133 [Chain B UniRef90 boundaries]=7-373 [Related structures]=2yje,2yjf [Entry] [Accession]=DI1000140 [Disorder status]=Inferred from homology [Kd]=1.00E-06 (PMID:19008859) [Name]=Cdc42 in complex with the CRIB domain of human p21-activated kinase 6 (PAK6) [Source organism]=Homo sapiens [PDB ID]=2odb [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=Ras [Type chain B]=Disordered [Evidence chain B]=The interacting region of PAK6 (CRIB motif - PF00786) has been shown to be intrinsically disordered in homologous proteins (PMID:9660763 and PMID:15821030). The 65-123 region described in IDEAL entry IID50053 covers 100% of the binding sequence in a homologous protein. [Type chain A]=Ordered [Evidence chain A]=The ras domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00071). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1aje. [Chain B name]=Serine/threonine-protein kinase PAK 6 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9NQU5 [Chain B UniProt boundaries]=11-45 [Chain B UniProt coverage]=5.1% [Chain B UniRef90 accession]=UniRef90_Q9NQU5 [Chain B UniRef90 boundaries]=11-45 [Chain A name]=Cell division control protein 42 homolog [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P60953 [Chain A UniProt boundaries]=2-178 [Chain A UniProt coverage]=92.7% [Chain A UniRef90 accession]=UniRef90_P60953 [Chain A UniRef90 boundaries]=2-178 [Entry] [Accession]=DI1000141 [Disorder status]=Confirmed [Kd]=1.30E-05 (PMID:18046415) [Name]=EGFR kinase domain in complex with Mitogen-inducible gene 6 protein [Source organism]=Homo sapiens [PDB ID]=4zjv [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.70 [Domain]=Protein tyrosine kinase [Type chain C]=Disordered [Evidence chain C]=The regions described in IDEAL entry IID00286 covers the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The protein tyrosine kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF07714). A solved monomeric structure of the domain is represented by PDB ID 1m14. [Modified residues chain C]=phosphotyrosine#Y#394|phosphotyrosine#Y#395 [Chain C name]=ERBB receptor feedback inhibitor 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q9UJM3 [Chain C UniProt boundaries]=336-398 [Chain C UniProt coverage]=13.6% [Chain C UniRef90 accession]=UniRef90_Q9UJM3 [Chain C UniRef90 boundaries]=336-398 [Chain A name]=Epidermal growth factor receptor [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P00533 [Chain A UniProt boundaries]=703-985 [Chain A UniProt coverage]=23.4% [Chain A UniRef90 accession]=UniRef90_P00533 [Chain A UniRef90 boundaries]=703-985 [Related structures]=2rf9,2rfd,2rfe,4i21,4r3p,4r3r [Entry] [Accession]=DI1000142 [Disorder status]=Confirmed [Kd]=2.30E-06 [Name]=Syntenin PDZ2 domain in complex with a Syndecan-4 peptide [Source organism]=Homo sapiens [PDB ID]=1oby [PDB chain IDs]=P:A [PDB note]=Chains Q and B were removed as chains A and P represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.85 [Domain]=PDZ [Type chain P]=Disordered [Evidence chain P]=The interacting region of the protein has been shown to be highly flexible based on NMR spectra (PDB IDs: 1ejq, 1ejp). The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_2). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 1nte. [Chain P name]=Syndecan-4 [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=P31431 [Chain P UniProt boundaries]=193-198 [Chain P UniProt coverage]=3% [Chain P UniRef90 accession]=UniRef90_P31431 [Chain P UniRef90 boundaries]=193-198 [Chain A name]=Syntenin-1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O00560 [Chain A UniProt boundaries]=192-270 [Chain A UniProt coverage]=26.5% [Chain A UniRef90 accession]=UniRef90_O00560 [Chain A UniRef90 boundaries]=197-270 [Related structures]=1ybo [Entry] [Accession]=DI2100002 [Disorder status]=Confirmed [Kd]=2.30E-06 [Name]=Cytosolic dynein intermediate chain bound to Tctex-type dynein light chain (D. melanogaster) [Source organism]=Drosophila melanogaster [PDB ID]=3fm7 [PDB chain IDs]=C:AB [PDB note]=Chains D, E and F were removed and chain C was truncated to include residues 109-123 (according to UniProt numbering) as chains A, B and the remaining region of chain C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.50 [Domain]=Tctex-1 [Type chain C]=Disordered [Evidence chain C]=The 109-135 region described in DisProt entry DP00605 and the 84-143 region described in IDEAL entry IID50052 cover 100% of the sequence present in the structure. [Type chain A]=Ordered component [Evidence chain A]=The Tctex-1 dynein light chain domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF03645). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1ygt. [Type chain B]=Ordered component [Evidence chain B]=The Tctex-1 dynein light chain domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF03645). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1ygt. [Chain C name]=Cytoplasmic dynein 1 intermediate chain [Chain C source organism]=Drosophila melanogaster [Chain C UniProt accession]=Q24246 [Chain C UniProt boundaries]=109-123 [Chain C UniProt coverage]=2.3% [Chain C UniRef90 accession]=UniRef90_Q24246 [Chain C UniRef90 boundaries]=109-123 [Chain A name]=Dynein light chain Tctex-type [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=Q94524 [Chain A UniProt boundaries]=1-111 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q94524 [Chain A UniRef90 boundaries]=1-111 [Chain B name]=Dynein light chain Tctex-type [Chain B source organism]=Drosophila melanogaster [Chain B UniProt accession]=Q94524 [Chain B UniProt boundaries]=1-111 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_Q94524 [Chain B UniRef90 boundaries]=1-111 [Entry] [Accession]=DI2100003 [Disorder status]=Confirmed [Kd]=2.30E-06 [Name]=Cytosolic dynein intermediate chain bound to dynein light chain 1 (D. melanogaster) [Source organism]=Drosophila melanogaster [PDB ID]=3fm7 [PDB chain IDs]=C:EF [PDB note]=Chains A, B and D were removed and chain C was truncated to include residues 126-135 (according to UniProt numbering) as chains E, F and the remaining region of chain C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.50 [Domain]=Dynein light chain [Type chain C]=Disordered [Evidence chain C]=The 109-135 region described in DisProt entry DP00605 and the 84-143 region described in IDEAL entry IID50052 cover 100% of the sequence present in the structure. [Type chain E]=Ordered [Evidence chain E]=The dynein light chain domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01221). A solved monomeric structure of the domain is represented by PDB ID 1rhw. [Type chain F]=Ordered [Evidence chain F]=The dynein light chain domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01221). A solved monomeric structure of the domain is represented by PDB ID 1rhw. [Chain C name]=Cytoplasmic dynein 1 intermediate chain [Chain C source organism]=Drosophila melanogaster [Chain C UniProt accession]=Q24246 [Chain C UniProt boundaries]=126-135 [Chain C UniProt coverage]=1.5% [Chain C UniRef90 accession]=UniRef90_Q24246 [Chain C UniRef90 boundaries]=126-135 [Chain E name]=Dynein light chain 1, cytoplasmic [Chain E source organism]=Drosophila melanogaster [Chain E UniProt accession]=Q24117 [Chain E UniProt boundaries]=1-89 [Chain E UniProt coverage]=100% [Chain E UniRef90 accession]=UniRef90_Q24117 [Chain E UniRef90 boundaries]=1-89 [Chain F name]=Dynein light chain 1, cytoplasmic [Chain F source organism]=Drosophila melanogaster [Chain F UniProt accession]=Q24117 [Chain F UniProt boundaries]=1-89 [Chain F UniProt coverage]=100% [Chain F UniRef90 accession]=UniRef90_Q24117 [Chain F UniRef90 boundaries]=1-89 [Entry] [Accession]=DI1100036 [Disorder status]=Confirmed [Kd]=7.00E-08 (PMID:16905102) [Name]=SOCS3 in complex with gp130(pTyr757) phosphopeptide [Source organism]=Mus musculus [PDB ID]=2hmh [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The 128-163 region described in DisProt entry DP00446 and the 15-225 region described in IDEAL entry IID50193 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ab2. [Modified residues chain B]=phosphotyrosine#Y#757 [Chain B name]=Interleukin-6 receptor subunit beta [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q00560 [Chain B UniProt boundaries]=753-763 [Chain B UniProt coverage]=1.2% [Chain B UniRef90 accession]=UniRef90_Q00560 [Chain B UniRef90 boundaries]=753-763 [Chain A name]=Suppressor of cytokine signaling 3 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=O35718 [Chain A UniProt boundaries]=11-185 [Chain A UniProt coverage]=77.8% [Chain A UniRef90 accession]=UniRef90_O14543 [Chain A UniRef90 boundaries]=11-185 [Related structures]=4gl9,2bbu [Entry] [Accession]=DI2110001 [Disorder status]=Inferred from homology [Kd]=7.00E-08 (PMID:16905102) [Name]=Cytoplasmic dynein 1 intermediate chain 2 bound to Tctex-type dynein light chain (D. melanogaster) [Source organism]=Rattus norvegicus / Drosophila melanogaster [PDB ID]=2pg1 [PDB chain IDs]=I:FG [PDB note]=Chains A, B, C, D, E, H, J, K and L were removed and chain I was truncated to include residues 137-151 (according to UniProt numbering) as chains F, G and the remaining region of chain I highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=Tctex-1 [Type chain I]=Disordered [Evidence chain I]=The corresponding region of a homologous protein has been shown to be disordered in the 84-143 region described in DisProt entry DP00605 and the 84-143 region described in IDEAL entry IID50052 (covering 100% of the sequence present in the structure). The protein region involved in the interaction contains a known functional linear motif (LIG_Dynein_DLC8_1). [Type chain F]=Ordered component [Evidence chain F]=The Tctex-1 dynein light chain domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF03645). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1ygt. [Type chain G]=Ordered component [Evidence chain G]=The Tctex-1 dynein light chain domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF03645). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1ygt. [Chain I name]=Cytoplasmic dynein 1 intermediate chain 2 [Chain I source organism]=Rattus norvegicus [Chain I UniProt accession]=Q62871 [Chain I UniProt boundaries]=137-151 [Chain I UniProt coverage]=2.4% [Chain I UniRef90 accession]=UniRef90_Q13409 [Chain I UniRef90 boundaries]=137-151 [Chain F name]=Dynein light chain Tctex-type [Chain F source organism]=Drosophila melanogaster [Chain F UniProt accession]=Q94524 [Chain F UniProt boundaries]=1-111 [Chain F UniProt coverage]=100% [Chain F UniRef90 accession]=UniRef90_Q94524 [Chain F UniRef90 boundaries]=1-111 [Chain G name]=Dynein light chain Tctex-type [Chain G source organism]=Drosophila melanogaster [Chain G UniProt accession]=Q94524 [Chain G UniProt boundaries]=1-111 [Chain G UniProt coverage]=100% [Chain G UniRef90 accession]=UniRef90_Q94524 [Chain G UniRef90 boundaries]=1-111 [Entry] [Accession]=DI2110002 [Disorder status]=Inferred from homology [Kd]=7.00E-08 (PMID:16905102) [Name]=Cytoplasmic dynein 1 intermediate chain 2 bound to dynein light chain 1 (D. melanogaster) [Source organism]=Rattus norvegicus / Drosophila melanogaster [PDB ID]=2pg1 [PDB chain IDs]=I:AB [PDB note]=Chains C, D, E, F, G, H, J, K and L were removed and chain I was truncated to include residues 152-163 (according to UniProt numbering) as chains A, B and the remaining region of chain I highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=Dynein light chain [Type chain I]=Disordered [Evidence chain I]=The corresponding region of a homologous protein has been shown to be disordered in the 84-143 region described in DisProt entry DP00605 and the 84-143 region described in IDEAL entry IID50052 (covering 100% of the sequence present in the structure). The protein region involved in the interaction contains a known functional linear motif (LIG_Dynein_DLC8_1). [Type chain A]=Ordered [Evidence chain A]=The dynein light chain domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01221). A solved monomeric structure of the domain is represented by PDB ID 1rhw. [Type chain B]=Ordered [Evidence chain B]=The dynein light chain domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01221). A solved monomeric structure of the domain is represented by PDB ID 1rhw. [Modified residues chain B]=phosphotyrosine#Y#757 [Chain I name]=Cytoplasmic dynein 1 intermediate chain 2 [Chain I source organism]=Rattus norvegicus [Chain I UniProt accession]=Q62871 [Chain I UniProt boundaries]=152-163 [Chain I UniProt coverage]=1.9% [Chain I UniRef90 accession]=UniRef90_Q13409 [Chain I UniRef90 boundaries]=152-163 [Chain A name]=Dynein light chain 1, cytoplasmic [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=Q24117 [Chain A UniProt boundaries]=1-89 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q24117 [Chain A UniRef90 boundaries]=1-89 [Chain B name]=Dynein light chain 1, cytoplasmic [Chain B source organism]=Drosophila melanogaster [Chain B UniProt accession]=Q24117 [Chain B UniProt boundaries]=1-89 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_Q24117 [Chain B UniRef90 boundaries]=1-89 [Entry] [Accession]=DI2010007 [Disorder status]=Inferred from motif [Kd]=7.00E-08 (PMID:16905102) [Name]=Core ASAP complex [Source organism]=Drosophila melanogaster / Homo sapiens / Mus musculus [PDB ID]=4a8x [PDB chain IDs]=B:AC [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=RRM/SAP18 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (RSB motif - PF16294, http://pfam.xfam.org/protein/Q9VJ12). [Type chain A]=Ordered [Evidence chain A]=The RRM domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00076). A solved monomeric structure of a homologue is represented by PDB ID 2m52. [Type chain C]=Ordered [Evidence chain C]=The SAP18 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF06487). A solved monomeric structure of the domain is represented by PDB ID 4a6q. [Chain B name]=Acinus, isoform A [Chain B source organism]=Drosophila melanogaster [Chain B UniProt accession]=Q9VJ12 [Chain B UniProt boundaries]=648-687 [Chain B UniProt coverage]=5.4% [Chain B UniRef90 accession]=UniRef90_Q9VJ12 [Chain B UniRef90 boundaries]=648-687 [Chain A name]=RNA-binding protein with serine-rich domain 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q15287 [Chain A UniProt boundaries]=157-244 [Chain A UniProt coverage]=28.9% [Chain A UniRef90 accession]=UniRef90_Q15287 [Chain A UniRef90 boundaries]=157-244 [Chain C name]=Histone deacetylase complex subunit SAP18 [Chain C source organism]=Mus musculus [Chain C UniProt accession]=O55128 [Chain C UniProt boundaries]=14-143 [Chain C UniProt coverage]=85% [Chain C UniRef90 accession]=UniRef90_O00422 [Chain C UniRef90 boundaries]=14-143 [Entry] [Accession]=DI1000143 [Disorder status]=Inferred from motif [Kd]=6.40E-06 (PMID:19635485) [Name]=TIP-1 in complex with C-terminal of Kir2.3 [Source organism]=Homo sapiens [PDB ID]=3gj9 [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=PDZ [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_1). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 2kg2. [Chain C name]=Inward rectifier potassium channel 4 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P48050 [Chain C UniProt boundaries]=436-445 [Chain C UniProt coverage]=2.2% [Chain C UniRef90 accession]=UniRef90_P48050 [Chain C UniRef90 boundaries]=436-445 [Chain A name]=Tax1-binding protein 3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O14907 [Chain A UniProt boundaries]=1-124 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_O14907 [Chain A UniRef90 boundaries]=1-124 [Entry] [Accession]=DI2010008 [Disorder status]=Inferred from motif [Kd]=6.40E-06 (PMID:19635485) [Name]=Dynein light chain 8 (DLC8) in complex with BIM peptide [Source organism]=Homo sapiens / Rattus norvegicus [PDB ID]=1f95 [PDB chain IDs]=C:AB [PDB note]=Chain D was removed as chains A, B and C highlight the biologically relevant interaction. [PDB experimental technique]=NMR [Domain]=Dynein light chain [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_Dynein_DLC8_1). [Type chain A]=Ordered [Evidence chain A]=The dynein light chain domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01221). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1rhw. [Type chain B]=Ordered [Evidence chain B]=The dynein light chain domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01221). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1rhw. [Chain C name]=Bcl-2-like protein 11 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=O43521 [Chain C UniProt boundaries]=108-116 [Chain C UniProt coverage]=4.5% [Chain C UniRef90 accession]=UniRef90_O43521 [Chain C UniRef90 boundaries]=108-116 [Chain A name]=Dynein light chain 1, cytoplasmic [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=P63170 [Chain A UniProt boundaries]=1-89 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P63167 [Chain A UniRef90 boundaries]=1-89 [Chain B name]=Dynein light chain 1, cytoplasmic [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=P63170 [Chain B UniProt boundaries]=1-89 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P63167 [Chain B UniRef90 boundaries]=1-89 [Entry] [Accession]=DI1010049 [Disorder status]=Inferred from motif [Kd]=7.61E-05 [Name]=Protein cubitus interruptus fragment bound to the MATH domain of Speckle-type POZ protein [Source organism]=Drosophila melanogaster / Homo sapiens [PDB ID]=3hqm [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.74 [Domain]=MATH [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (DEG_SPOP_SBC_1). [Type chain A]=Ordered [Evidence chain A]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00917). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2f1w. [Chain C name]=Transcriptional activator cubitus interruptus [Chain C source organism]=Drosophila melanogaster [Chain C UniProt accession]=P19538 [Chain C UniProt boundaries]=1356-1367 [Chain C UniProt coverage]=0.9% [Chain C UniRef90 accession]=UniRef90_P19538 [Chain C UniRef90 boundaries]=1356-1367 [Chain A name]=Speckle-type POZ protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O43791 [Chain A UniProt boundaries]=22-166 [Chain A UniProt coverage]=38.8% [Chain A UniRef90 accession]=UniRef90_O43791 [Chain A UniRef90 boundaries]=28-166 [Entry] [Accession]=DI1010050 [Disorder status]=Inferred from motif [Kd]=3.70E-06 [Name]=Puckered fragment bound to the MATH domain of Speckle-type POZ protein [Source organism]=Drosophila melanogaster / Homo sapiens [PDB ID]=3hql [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.66 [Domain]=MATH [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (DEG_SPOP_SBC_1). [Type chain A]=Ordered [Evidence chain A]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00917). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2f1w. [Chain C name]=Puckered, isoform A [Chain C source organism]=Drosophila melanogaster [Chain C UniProt accession]=Q9VHV8 [Chain C UniProt boundaries]=91-106 [Chain C UniProt coverage]=3.4% [Chain C UniRef90 accession]=UniRef90_Q9VHV8 [Chain C UniRef90 boundaries]=91-106 [Chain A name]=Speckle-type POZ protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O43791 [Chain A UniProt boundaries]=22-166 [Chain A UniProt coverage]=38.8% [Chain A UniRef90 accession]=UniRef90_O43791 [Chain A UniRef90 boundaries]=28-166 [Entry] [Accession]=DI2100004 [Disorder status]=Inferred from motif [Kd]=8.90E-07 (PMID:18334479) [Name]=SpCia1/Asf1 complex with Hip1 [Source organism]=Schizosaccharomyces pombe [PDB ID]=2z34 [PDB chain IDs]=C:AB [PDB note]=Chain D was removed as chains A, B and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=ASF1 like histone chaperone [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (HirA B motif - PF09453, http://pfam.xfam.org/protein/P87314). [Type chain A]=Ordered [Evidence chain A]=The ASF1 like histone chaperone domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04729). A solved monomeric structure of the domain is represented by PDB ID 2cu9. [Type chain B]=Ordered [Evidence chain B]=The ASF1 like histone chaperone domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04729). A solved monomeric structure of the domain is represented by PDB ID 2cu9. [Chain C name]=Protein hir1 [Chain C source organism]=Schizosaccharomyces pombe [Chain C UniProt accession]=P87314 [Chain C UniProt boundaries]=469-497 [Chain C UniProt coverage]=3.1% [Chain C UniRef90 accession]=UniRef90_P87314 [Chain C UniRef90 boundaries]=469-497 [Chain A name]=Histone chaperone cia1 [Chain A source organism]=Schizosaccharomyces pombe [Chain A UniProt accession]=O74515 [Chain A UniProt boundaries]=2-160 [Chain A UniProt coverage]=60.7% [Chain A UniRef90 accession]=UniRef90_O74515 [Chain A UniRef90 boundaries]=2-160 [Chain B name]=Histone chaperone cia1 [Chain B source organism]=Schizosaccharomyces pombe [Chain B UniProt accession]=O74515 [Chain B UniProt boundaries]=1-161 [Chain B UniProt coverage]=61.5% [Chain B UniRef90 accession]=UniRef90_O74515 [Chain B UniRef90 boundaries]=1-161 [Entry] [Accession]=DI1100037 [Disorder status]=Inferred from motif [Kd]=3.40E-05 (PMID:7664083) [Name]=ABL tyrosine kinase SH3 domain with 3BP-1 peptide [Source organism]=Mus musculus [PDB ID]=1abo [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=SH3 [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains the known functional SH3 domin binding linear motif (http://www.uniprot.org/uniprot/P55194#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00018). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2a36. [Chain C name]=SH3 domain-binding protein 1 [Chain C source organism]=Mus musculus [Chain C UniProt accession]=P55194 [Chain C UniProt boundaries]=528-537 [Chain C UniProt coverage]=1.7% [Chain C UniRef90 accession]=UniRef90_P55194 [Chain C UniRef90 boundaries]=485-493 [Chain A name]=Tyrosine-protein kinase ABL1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P00520 [Chain A UniProt boundaries]=60-121 [Chain A UniProt coverage]=5.5% [Chain A UniRef90 accession]=UniRef90_P00520 [Chain A UniRef90 boundaries]=61-121 [Entry] [Accession]=DI1000144 [Disorder status]=Inferred from motif [Kd]=3.40E-05 (PMID:7664083) [Name]=human Grb7-SH2 domain in complex with an erbB-2 peptide [Source organism]=Homo sapiens [PDB ID]=1mw4 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_SH2_GRB2). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ab2. [Modified residues chain B]=phosphotyrosine#Y#1139 [Chain B name]=Receptor tyrosine-protein kinase erbB-2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04626 [Chain B UniProt boundaries]=1135-1144 [Chain B UniProt coverage]=0.8% [Chain B UniRef90 accession]=UniRef90_P04626 [Chain B UniRef90 boundaries]=1135-1144 [Chain A name]=Growth factor receptor-bound protein 7 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q14451 [Chain A UniProt boundaries]=413-532 [Chain A UniProt coverage]=22.6% [Chain A UniRef90 accession]=UniRef90_Q14451 [Chain A UniRef90 boundaries]=415-532 [Related structures]=2l4k [Entry] [Accession]=DI1120007 [Disorder status]=Inferred from motif [Kd]=3.40E-05 (PMID:7664083) [Name]=Sap97 PDZ2 bound to the C-terminal peptide of HPV18 E6 [Source organism]=Human papillomavirus type 18 / Rattus norvegicus [PDB ID]=2i0l [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.31 [Domain]=PDZ [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_1). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2kpk. [Chain C name]=Protein E6 [Chain C source organism]=Human papillomavirus type 18 [Chain C UniProt accession]=P06463 [Chain C UniProt boundaries]=152-158 [Chain C UniProt coverage]=4.4% [Chain C UniRef90 accession]=UniRef90_P06463 [Chain C UniRef90 boundaries]=152-158 [Chain A name]=Disks large homolog 1 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=Q62696 [Chain A UniProt boundaries]=318-401 [Chain A UniProt coverage]=9.2% [Chain A UniRef90 accession]=UniRef90_Q12959 [Chain A UniRef90 boundaries]=319-401 [Entry] [Accession]=DI1000145 [Disorder status]=Confirmed [Kd]=5.25E-04 [Name]=Filamin A repeat 21 complexed with the integrin beta2 cytoplasmic tail peptide [Source organism]=Homo sapiens [PDB ID]=2jf1 [PDB chain IDs]=T:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.2 [Domain]=Filamin repeat [Type chain T]=Disordered [Evidence chain T]=The cytoplasmic tail of integrins have been shown to be intrinsically unstructured (PMID:21421922). [Type chain A]=Ordered [Evidence chain A]=The filamin repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00630). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2nqc. [Chain T name]=Integrin beta-2 [Chain T source organism]=Homo sapiens [Chain T UniProt accession]=P05107 [Chain T UniProt boundaries]=735-769 [Chain T UniProt coverage]=4.6% [Chain T UniRef90 accession]=UniRef90_P05107 [Chain T UniRef90 boundaries]=735-769 [Chain A name]=Filamin-A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P21333 [Chain A UniProt boundaries]=2233-2329 [Chain A UniProt coverage]=3.7% [Chain A UniRef90 accession]=UniRef90_P21333 [Chain A UniRef90 boundaries]=2236-2329 [Entry] [Accession]=DI2110003 [Disorder status]=Confirmed [Kd]=3.00E-12 (PMID:2295615) [Name]=Complex of bovine alpha-thrombin and recombinant hirudin [Source organism]=Hirudo medicinalis / Bos taurus [PDB ID]=1hrt [PDB chain IDs]=I:HL [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=Trypsin [Type chain I]=Disordered [Evidence chain I]=The interacting region of hirudin has been shown to be intrinsically disordered (PMID:1335515). The 50-65 region described in DisProt entry DP00137 covers 25% of the sequence present in the structure. [Type chain H]=Ordered component [Evidence chain H]=Thrombin consists of a large and a small subunit. Trypsin domain of the large subunit involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00089). A solved structure of the thrombin dimer is represented by PDB ID 3pmb. [Type chain L]=Ordered component [Evidence chain L]=Thrombin consists of a large and a small subunit. Trypsin domain of the large subunit involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00089). A solved structure of the thrombin dimer is represented by PDB ID 3pmb. [Modified residues chain L]=phosphotyrosine#Y#474 [Chain I name]=Hirudin variant-1 [Chain I source organism]=Hirudo medicinalis [Chain I UniProt accession]=P01050 [Chain I UniProt boundaries]=1-65 [Chain I UniProt coverage]=100% [Chain I UniRef90 accession]=UniRef90_P01050 [Chain I UniRef90 boundaries]=1-65 [Chain H name]=Prothrombin [Chain H source organism]=Bos taurus [Chain H UniProt accession]=P00735 [Chain H UniProt boundaries]=367-625 [Chain H UniProt coverage]=41.4% [Chain H UniRef90 accession]=UniRef90_P00735 [Chain H UniRef90 boundaries]=367-625 [Chain L name]=Prothrombin [Chain L source organism]=Bos taurus [Chain L UniProt accession]=P00735 [Chain L UniProt boundaries]=318-366 [Chain L UniProt coverage]=7.8% [Chain L UniRef90 accession]=UniRef90_P00735 [Chain L UniRef90 boundaries]=318-366 [Related structures]=1vit [Entry] [Accession]=DI1000146 [Disorder status]=Confirmed [Kd]=3.00E-12 (PMID:2295615) [Name]=Factor inhibiting Hif-1 alpha in complex with Hif-1 alpha fragment peptide [Source organism]=Homo sapiens [PDB ID]=1h2k [PDB chain IDs]=S:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.15 [Domain]=Cupin-like [Type chain S]=Disordered [Evidence chain S]=The 776-826 region described in DisProt entry DP00262 and the 775-826 region described in IDEAL entry IID00085 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The cupin-like domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13621). A solved structure of the domain is represented by PDB ID 1h2n. [Chain S name]=Hypoxia-inducible factor 1-alpha [Chain S source organism]=Homo sapiens [Chain S UniProt accession]=Q16665 [Chain S UniProt boundaries]=786-826 [Chain S UniProt coverage]=5% [Chain S UniRef90 accession]=UniRef90_Q16665 [Chain S UniRef90 boundaries]=786-826 [Chain A name]=Hypoxia-inducible factor 1-alpha inhibitor [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9NWT6 [Chain A UniProt boundaries]=1-349 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q9NWT6 [Chain A UniRef90 boundaries]=1-349 [Related structures]=1h2m,1h2l,2ilm,5jwp [Entry] [Accession]=DI2000008 [Disorder status]=Inferred from homology [Kd]=4.80E-07 (PMID:12820959) [Name]=Beta-TrCP1-Skp1 dimer in complex with beta-catenin peptide [Source organism]=Homo sapiens [PDB ID]=1p22 [PDB chain IDs]=C:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.95 [Domain]=WD40 [Type chain C]=Disordered [Evidence chain C]=The corresponding region of a closely homologous protein has been shown to be disordered in the 17-48 region described in DisProt entry DP00341 (covers 100% of the sequence present in the structure). The protein region involved in the interaction contains a DpSGZXpS motif, Z representing hydrophobic residues (PMID:12820959). [Type chain A]=Ordered component [Evidence chain A]=Disordered peptide of beta-catenin binds to WD40 domain of beta-TrCP1 from the beta-TrCP1-Skp1 dimer (PMID:12820959). The WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00400). A solved structure of beta-TrCP1-Skp1 dimer is represented by PDB ID 2ovp. [Type chain B]=Ordered component [Evidence chain B]=Skp1 part of the beta-TrCP1-Skp1 dimer does not interact directly with the disordered beta-catenin peptide (PMID:12820959). A solved structure of beta-TrCP1-Skp1 dimer is represented by PDB ID 2ovp. [Modified residues chain C]=phosphoserine#S#33|phosphoserine#S#37 [Modified residues chain B]=phosphotyrosine#Y#1139 [Chain C name]=Catenin beta-1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P35222 [Chain C UniProt boundaries]=19-44 [Chain C UniProt coverage]=3.3% [Chain C UniRef90 accession]=UniRef90_Q02248 [Chain C UniRef90 boundaries]=19-44 [Chain A name]=F-box/WD repeat-containing protein 1A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9Y297 [Chain A UniProt boundaries]=175-605 [Chain A UniProt coverage]=71.2% [Chain A UniRef90 accession]=UniRef90_Q9Y297 [Chain A UniRef90 boundaries]=175-605 [Chain B name]=S-phase kinase-associated protein 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P63208 [Chain B UniProt boundaries]=1-163 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P63208 [Chain B UniRef90 boundaries]=1-163 [Entry] [Accession]=DI2100005 [Disorder status]=Inferred from homology [Kd]=3.10E-08 (PMID:7698360) [Name]=Calpain Domain VI Complexed with Calpastatin Inhibitory Domain C [Source organism]=Sus scrofa [PDB ID]=1nx1 [PDB chain IDs]=C:AB [PDB note]=Chains D was removed as chains A, B and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=EF-hand [Type chain C]=Disordered [Evidence chain C]=The corresponding region of a closely homologous protein has been shown to be disordered in the 137-277 region described in DisProt entry DP00196 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered component [Evidence chain A]=The EF-hand domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13833). Calpain domain VI forms a stable homodimer represented by PDB ID 1nx2. [Type chain B]=Ordered component [Evidence chain B]=The EF-hand domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13833). Calpain domain VI forms a stable homodimer represented by PDB ID 1nx2. [Modified residues chain B]=phosphotyrosine#Y#1139 [Chain C name]=Calpastatin [Chain C source organism]=Sus scrofa [Chain C UniProt accession]=P12675 [Chain C UniProt boundaries]=231-241 [Chain C UniProt coverage]=1.5% [Chain C UniRef90 accession]=UniRef90_P12675 [Chain C UniRef90 boundaries]=231-241 [Chain A name]=Calpain small subunit 1 [Chain A source organism]=Sus scrofa [Chain A UniProt accession]=P04574 [Chain A UniProt boundaries]=94-266 [Chain A UniProt coverage]=65% [Chain A UniRef90 accession]=UniRef90_P04632 [Chain A UniRef90 boundaries]=94-266 [Chain B name]=Calpain small subunit 1 [Chain B source organism]=Sus scrofa [Chain B UniProt accession]=P04574 [Chain B UniProt boundaries]=94-266 [Chain B UniProt coverage]=65% [Chain B UniRef90 accession]=UniRef90_P04632 [Chain B UniRef90 boundaries]=94-266 [Related structures]=1nx0 [Entry] [Accession]=DI1000147 [Disorder status]=Confirmed [Kd]=2.40E-07 (PMID:15231848) [Name]=Smad MH2 domain bound to the Smad-binding domain of SARA [Source organism]=Homo sapiens [PDB ID]=1dev [PDB chain IDs]=B:A [PDB note]=Chains C and D was removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=MH2 [Type chain B]=Disordered [Evidence chain B]=The interacting region of SARA (Smad Binding Domain) has been shown to be intrinsically disordered (PMID:15231848; DisProt entry DP00141). The 765-853 region described in IDEAL entry IID00112 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The MH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03166). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1mjs. [Chain B name]=Zinc finger FYVE domain-containing protein 9 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O95405 [Chain B UniProt boundaries]=771-811 [Chain B UniProt coverage]=2.9% [Chain B UniRef90 accession]=UniRef90_O95405 [Chain B UniRef90 boundaries]=771-811 [Chain A name]=Mothers against decapentaplegic homolog 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q15796 [Chain A UniProt boundaries]=261-456 [Chain A UniProt coverage]=42% [Chain A UniRef90 accession]=UniRef90_Q15796 [Chain A UniRef90 boundaries]=261-456 [Entry] [Accession]=DI1200004 [Disorder status]=Confirmed [Kd]=2.40E-07 (PMID:15231848) [Name]=Sigma-28(FliA) - FlgM complex [Source organism]=Aquifex aeolicus [PDB ID]=1sc5 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=3.26 [Domain]=Compact pack of sigma domains [Type chain B]=Disordered [Evidence chain B]=The interacting region of FlgM has been shown to be largely intrinsically disordered (PMID:9095196). The 5-88 region described in DisProt entry DP01092 covers 98% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The structures of the individual sigma-28 domains (sigma-28-2, sigma-28-3 and sigma-28-4) are essentially identical to those observed in structures of other sigma-70 family members. (PMID:15068809) A solved monomeric structure of a sigma-70 domain is represented by PDB ID 1sig. [Chain B name]=Anti sigma factor FlgM [Chain B source organism]=Aquifex aeolicus [Chain B UniProt accession]=O66683 [Chain B UniProt boundaries]=1-88 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_O66683 [Chain B UniRef90 boundaries]=1-88 [Chain A name]=RNA polymerase sigma factor FliA [Chain A source organism]=Aquifex aeolicus [Chain A UniProt accession]=O67268 [Chain A UniProt boundaries]=1-236 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_O67268 [Chain A UniRef90 boundaries]=1-236 [Related structures]=1rp3 [Entry] [Accession]=DI1110013 [Disorder status]=Confirmed [Kd]=1.00E-09 [Name]=TBP-TAFII230 complex [Source organism]=Drosophila melanogaster / Saccharomyces cerevisiae [PDB ID]=1tba [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=TATA-binding protein (TBP) [Type chain A]=Disordered [Evidence chain A]=The 11-77 region described in DisProt entry DP00081 covers 100% of the sequence present in the structure. [Type chain B]=Ordered [Evidence chain B]=TATA-binding protein domain of TBP involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00352). A solved structure of the domain is represented by PDB ID 1tbp. [Chain A name]=Transcription initiation factor TFIID subunit 1 [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=P51123 [Chain A UniProt boundaries]=11-77 [Chain A UniProt coverage]=3.1% [Chain A UniRef90 accession]=UniRef90_P51123 [Chain A UniRef90 boundaries]=11-77 [Chain B name]=TATA-box-binding protein [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P13393 [Chain B UniProt boundaries]=61-240 [Chain B UniProt coverage]=75% [Chain B UniRef90 accession]=UniRef90_P13393 [Chain B UniRef90 boundaries]=61-240 [Entry] [Accession]=DI1010051 [Disorder status]=Confirmed [Kd]=3.10E-09 [Name]=Beta-catenin armadillo repeat domain bound to ICAT [Source organism]=Homo sapiens / Mus musculus [PDB ID]=1m1e [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=Armadillo repeat [Type chain B]=Disordered [Evidence chain B]=ICAT consists of two regions that interact directly with beta-catenin, a helical N-terminal domain and an extended acidic C-terminal region that are connected by a flexible tether. It is shown that, unlike cadherins, Tcf-4 and APC, ICAT contains some folded structure in the absence of beta-catenin (PMID:12408825) [Type chain A]=Ordered [Evidence chain A]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain is represented by PDB ID 2bct. [Chain B name]=Beta-catenin-interacting protein 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9NSA3 [Chain B UniProt boundaries]=1-81 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_Q9NSA3 [Chain B UniRef90 boundaries]=1-81 [Chain A name]=Catenin beta-1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q02248 [Chain A UniProt boundaries]=134-671 [Chain A UniProt coverage]=68.9% [Chain A UniRef90 accession]=UniRef90_Q02248 [Chain A UniRef90 boundaries]=134-671 [Entry] [Accession]=DI1000148 [Disorder status]=Confirmed [Kd]=1.90E-07 [Name]=Rb tumor suppressor bound to the transactivation domain of E2F-2 [Source organism]=Homo sapiens [PDB ID]=1n4m [PDB chain IDs]=C:A [PDB note]=Chains B, D and E were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=Rb pocket [Type chain C]=Disordered [Evidence chain C]=It was shown that the flexibility in the middle of the E2F-2 peptide is essential for the tight association of E2F to the Rb pocket (PMID:12502741). The protein region involved in the interaction contains a known functional linear motif (LIG_Rb_pABgroove_1). [Type chain A]=Ordered [Evidence chain A]=The Rb pocket domain (consist of Rb_A and Rb_B) involved in the interaction is known to adopt a stable structure in isolation (see Pfam domains PF01858 and PF01857). A solved monomeric structure of the domain is represented by DPB ID 3pom. [Chain C name]=Transcription factor E2F2 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q14209 [Chain C UniProt boundaries]=410-427 [Chain C UniProt coverage]=4.1% [Chain C UniRef90 accession]=UniRef90_Q14209 [Chain C UniRef90 boundaries]=410-427 [Chain A name]=Retinoblastoma-associated protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P06400 [Chain A UniProt boundaries]=380-785 [Chain A UniProt coverage]=43.8% [Chain A UniRef90 accession]=UniRef90_P06400 [Chain A UniRef90 boundaries]=380-785 [Entry] [Accession]=DI1100038 [Disorder status]=Inferred from homology [Kd]=1.10E-09 (PMID:16222336) [Name]=Nup50:importin-alpha complex [Source organism]=Mus musculus [PDB ID]=2c1m [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.2 [Domain]=Armadillo repeat [Type chain B]=Disordered [Evidence chain B]=The corresponding region of a closely homologous protein has been shown to be disordered in the 1-720 region described in DisProt entry DP00222 and in IDEAL entry IID50007 (cover 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain is represented by PDB ID 1ial. [Chain B name]=Nuclear pore complex protein Nup50 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q9JIH2 [Chain B UniProt boundaries]=1-46 [Chain B UniProt coverage]=9.9% [Chain B UniRef90 accession]=UniRef90_Q9JIH2 [Chain B UniRef90 boundaries]=1-46 [Chain A name]=Importin subunit alpha-1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P52293 [Chain A UniProt boundaries]=75-498 [Chain A UniProt coverage]=80.2% [Chain A UniRef90 accession]=UniRef90_P52293 [Chain A UniRef90 boundaries]=75-498 [Entry] [Accession]=DI2000009 [Disorder status]=Confirmed [Kd]=1.12E-08 (PMID:16458085) [Name]=The p27 Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A:Cdk2 complex [Source organism]=Homo sapiens [PDB ID]=1jsu [PDB chain IDs]=C:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=Cyclin A:Cdk2 [Type chain C]=Disordered [Evidence chain C]=The 1-198 region described in DisProt entry DP00018 and in IDEAL entry IID00049 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (DOC_CYCLIN_1). [Type chain A]=Ordered component [Evidence chain A]=The cyclin A:Cdk2 complex involved in the interaction is known to form an ordered dimer, represented by PDB ID 1jst. [Type chain B]=Ordered component [Evidence chain B]=The cyclin A:Cdk2 complex involved in the interaction is known to form an ordered dimer, represented by PDB ID 1jst. [Chain C name]=Cyclin-dependent kinase inhibitor 1B [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P46527 [Chain C UniProt boundaries]=23-106 [Chain C UniProt coverage]=42.4% [Chain C UniRef90 accession]=UniRef90_P46527 [Chain C UniRef90 boundaries]=23-106 [Chain A name]=Cyclin-dependent kinase 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P24941 [Chain A UniProt boundaries]=1-298 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P24941 [Chain A UniRef90 boundaries]=1-298 [Chain B name]=Cyclin-A2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P20248 [Chain B UniProt boundaries]=173-432 [Chain B UniProt coverage]=60.2% [Chain B UniRef90 accession]=UniRef90_P20248 [Chain B UniRef90 boundaries]=173-432 [Related structures]=1h27 [Entry] [Accession]=DI1000149 [Disorder status]=Inferred from homology [Kd]=6.02E-06 (PMID:27302953) [Name]=IRF-3 in complex with CBP [Source organism]=Homo sapiens [PDB ID]=1zoq [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.37 [Domain]=IRF-3 [Type chain C]=Disordered [Evidence chain C]=The corresponding region of a closely homologous protein has been shown to be disordered in the 2059-2117 region described in DisProt entry DP00348 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The IRF-3 (Interferon-regulatory factor 3) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF10401). A solved monomeric structure of the domain is represented by PDB ID 1j2f. [Chain C name]=CREB-binding protein [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q92793 [Chain C UniProt boundaries]=2065-2111 [Chain C UniProt coverage]=1.9% [Chain C UniRef90 accession]=UniRef90_Q92793 [Chain C UniRef90 boundaries]=2065-2111 [Chain A name]=Interferon regulatory factor 3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q14653 [Chain A UniProt boundaries]=196-386 [Chain A UniProt coverage]=44.7% [Chain A UniRef90 accession]=UniRef90_Q14653 [Chain A UniRef90 boundaries]=196-386 [Related structures]=5jem [Entry] [Accession]=DI1000150 [Disorder status]=Inferred from motif [Kd]=6.02E-06 (PMID:27302953) [Name]=PI3K p85 C-terminal SH2 domain/CD28-derived peptide complex [Source organism]=Homo sapiens [PDB ID]=5aul [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.10 [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The interacting region of CD28 contains a known functional YMNM motif (PMID:27927989). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ab2. [Modified residues chain B]=phosphotyrosine#Y#191 [Chain B name]=T-cell-specific surface glycoprotein CD28 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P10747 [Chain B UniProt boundaries]=189-196 [Chain B UniProt coverage]=3.6% [Chain B UniRef90 accession]=UniRef90_P10747 [Chain B UniRef90 boundaries]=189-196 [Chain A name]=Phosphatidylinositol 3-kinase regulatory subunit alpha [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P27986 [Chain A UniProt boundaries]=612-720 [Chain A UniProt coverage]=15.1% [Chain A UniRef90 accession]=UniRef90_P27986 [Chain A UniRef90 boundaries]=614-720 [Entry] [Accession]=DI2010009 [Disorder status]=Confirmed [Kd]=6.02E-06 (PMID:27302953) [Name]=Autoimmune MHC class II I-Au complexed with myelin basic protein 1-11 [Source organism]=Homo sapiens / Mus musculus [PDB ID]=1k2d [PDB chain IDs]=P:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=MHC [Type chain P]=Disordered [Evidence chain P]=The 134-304 region described in DisProt entry DP00236 covers 100% of the sequence present in the structure. [Type chain A]=Ordered component [Evidence chain A]=The H-2 class II histocompatibility antigen, A-U alpha and beta chains involved in the interaction are known to form an ordered dimer, represented by PDB ID 2p24. [Type chain B]=Ordered component [Evidence chain B]=The H-2 class II histocompatibility antigen, A-U alpha and beta chains involved in the interaction are known to form an ordered dimer, represented by PDB ID 2p24. [Modified residues chain B]=phosphotyrosine#Y#191 [Chain P name]=Myelin basic protein [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=P02686 [Chain P UniProt boundaries]=134-144 [Chain P UniProt coverage]=3.6% [Chain P UniRef90 accession]=UniRef90_P02686 [Chain P UniRef90 boundaries]=134-144 [Chain A name]=H-2 class II histocompatibility antigen, A-U alpha chain (Fragment) [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P14438 [Chain A UniProt boundaries]=1-179 [Chain A UniProt coverage]=78.9% [Chain A UniRef90 accession]=UniRef90_P14434 [Chain A UniRef90 boundaries]=1-179 [Chain B name]=H-2 class II histocompatibility antigen, A-U beta chain [Chain B source organism]=Mus musculus [Chain B UniProt accession]=P06344 [Chain B UniProt boundaries]=28-216 [Chain B UniProt coverage]=71.9% [Chain B UniRef90 accession]=UniRef90_P14483 [Chain B UniRef90 boundaries]=28-216 [Entry] [Accession]=DI2000010 [Disorder status]=Confirmed [Kd]=4.00E-08 (PMID:11163233) [Name]=Binding of MHC complex to a myelin basic protein peptide [Source organism]=Homo sapiens [PDB ID]=1fv1 [PDB chain IDs]=C:AB [PDB note]=Chains D, E and F were removed as chains A, B and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=MHC7 [Type chain C]=Disordered [Evidence chain C]=The 134-304 region described in DisProt entry DP00236 covers 100% of the sequence present in the structure. [Type chain A]=Ordered component [Evidence chain A]=HLA class II histocompatibility antigen, DR alpha and beta chains involved in the interaction are known to form an ordered dimer. A solved structure of an MHC complex using a closely homologous beta chain is represented by PDB ID 4x5x. [Type chain B]=Ordered component [Evidence chain B]=HLA class II histocompatibility antigen, DR alpha and beta chains involved in the interaction are known to form an ordered dimer. A solved structure of an MHC complex using a closely homologous beta chain is represented by PDB ID 4x5x. [Modified residues chain B]=phosphotyrosine#Y#191 [Chain C name]=Myelin basic protein [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P02686 [Chain C UniProt boundaries]=218-237 [Chain C UniProt coverage]=6.6% [Chain C UniRef90 accession]=UniRef90_P02686 [Chain C UniRef90 boundaries]=218-237 [Chain A name]=HLA class II histocompatibility antigen, DR alpha chain [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P01903 [Chain A UniProt boundaries]=26-206 [Chain A UniProt coverage]=71.3% [Chain A UniRef90 accession]=UniRef90_P01903 [Chain A UniRef90 boundaries]=26-206 [Chain B name]=HLA class II histocompatibility antigen, DR beta 5 chain [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q30154 [Chain B UniProt boundaries]=30-219 [Chain B UniProt coverage]=71.4% [Chain B UniRef90 accession]=UniRef90_Q30154 [Chain B UniRef90 boundaries]=30-219 [Related structures]=1bx2,1hqr,1zgl [Entry] [Accession]=DI2200003 [Disorder status]=Confirmed [Kd]=4.00E-08 (PMID:11163233) [Name]=E. coli enolase complexed with the minimal binding segment of RNase E. [Source organism]=Escherichia coli [PDB ID]=2fym [PDB chain IDs]=B:AC [PDB note]=Chains D, E and F were removed as chains A, B and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.60 [Domain]=Enolase_N [Type chain B]=Disordered [Evidence chain B]=The 628-843 region described in DisProt entry DP00207 covers 61% of the sequence present in the structure. The protein region involved in the interaction contains a enolase-binding motif (PMID:25432321). [Type chain A]=Ordered component [Evidence chain A]=The Enolase_N domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF03952). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1e9i. [Type chain C]=Ordered component [Evidence chain C]=The Enolase_N domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF03952). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1e9i. [Chain B name]=Ribonuclease E [Chain B source organism]=Escherichia coli [Chain B UniProt accession]=P21513 [Chain B UniProt boundaries]=833-850 [Chain B UniProt coverage]=1.7% [Chain B UniRef90 accession]=UniRef90_P21513 [Chain B UniRef90 boundaries]=833-850 [Chain A name]=Enolase [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=P0A6P9 [Chain A UniProt boundaries]=2-432 [Chain A UniProt coverage]=99.8% [Chain A UniRef90 accession]=UniRef90_Q7N835 [Chain A UniRef90 boundaries]=2-432 [Chain C name]=Enolase [Chain C source organism]=Escherichia coli [Chain C UniProt accession]=P0A6P9 [Chain C UniProt boundaries]=2-432 [Chain C UniProt coverage]=99.8% [Chain C UniRef90 accession]=UniRef90_Q7N835 [Chain C UniRef90 boundaries]=2-432 [Related structures]=3h8a [Entry] [Accession]=DI1000151 [Disorder status]=Confirmed [Kd]=2.79E-04 [Name]=CTD-specific phosphatase Scp1 in complex with a double phosporylated CTD peptide of RNA polymerase II [Source organism]=Homo sapiens [PDB ID]=2ghq [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.05 [Domain]=NIF [Type chain C]=Disordered [Evidence chain C]=The 1593-1960 region described in IDEAL entry IID00126 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The NIF (NLI interacting factor-like phosphatase) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03031). A solved monomeric structure of the domain is represented by PDB ID 1t9z. [Modified residues chain C]=phosphoserine#S#171|phosphoserine#S#174 [Chain C name]=DNA-directed RNA polymerase II subunit RPB1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P24928 [Chain C UniProt boundaries]=1795-1803 [Chain C UniProt coverage]=0.5% [Chain C UniRef90 accession]=UniRef90_P24928 [Chain C UniRef90 boundaries]=1795-1803 [Chain A name]=Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9GZU7 [Chain A UniProt boundaries]=77-256 [Chain A UniProt coverage]=69% [Chain A UniRef90 accession]=UniRef90_Q9GZU7 [Chain A UniRef90 boundaries]=77-256 [Entry] [Accession]=DI1000152 [Disorder status]=Confirmed [Kd]=4.20E-08 [Name]=Karyopherin Beta2/Transportin-M9NLS [Source organism]=Homo sapiens [PDB ID]=2h4m [PDB chain IDs]=D:B [PDB note]=Chains A and C were removed as chains B and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.05 [Domain]=HEAT-like repeat [Type chain D]=Disordered [Evidence chain D]=The NLS region of hnRNP has been shown to be intrinsically disordered (PMID:16901787). The protein region involved in the interaction contains a known functional linear motif, the PY-NLS motif (PMID:16901787). [Type chain B]=Ordered [Evidence chain B]=The HEAT-like repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13513). A solved monomeric structure of the domain is represented by PDB ID 2z5j. [Chain D name]=Heterogeneous nuclear ribonucleoprotein A1 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P09651 [Chain D UniProt boundaries]=309-357 [Chain D UniProt coverage]=13.2% [Chain D UniRef90 accession]=UniRef90_P09651 [Chain D UniRef90 boundaries]=309-357 [Chain B name]=Transportin-1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q92973 [Chain B UniProt boundaries]=9-898 [Chain B UniProt coverage]=99.1% [Chain B UniRef90 accession]=UniRef90_Q92973 [Chain B UniRef90 boundaries]=9-898 [Entry] [Accession]=DI1000153 [Disorder status]=Confirmed [Kd]=1.50E-07 [Name]=Spry Domain-and Socs Box-Containing Protein1 in complex with a PAR-4 peptide [Source organism]=Homo sapiens [PDB ID]=2jk9 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.79 [Domain]=SPRY [Type chain B]=Disordered [Evidence chain B]=The 59-77 region described in IDEAL entry IID00177 covers 73% of the sequence present in the structure. The corresponding region of a closely homologous protein has been shown to be disordered in the 1-332 region described in DisProt entry DP00940 (covers 100% of the sequence present in the structure). The protein region involved in the interaction contains a known functional linear motif (LIG_SPRY_1). [Type chain A]=Ordered [Evidence chain A]=The SPRY domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00622). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3ek9. [Chain B name]=PRKC apoptosis WT1 regulator protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q96IZ0 [Chain B UniProt boundaries]=67-81 [Chain B UniProt coverage]=4.4% [Chain B UniRef90 accession]=UniRef90_Q96IZ0 [Chain B UniRef90 boundaries]=67-81 [Chain A name]=SPRY domain-containing SOCS box protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96BD6 [Chain A UniProt boundaries]=24-233 [Chain A UniProt coverage]=76.9% [Chain A UniRef90 accession]=UniRef90_Q96BD6 [Chain A UniRef90 boundaries]=24-233 [Entry] [Accession]=DI1020013 [Disorder status]=Confirmed [Kd]=9.00E-07 [Name]=Retinoblastoma protein pocket domain in complex with adenovirus E1A CR1 domain [Source organism]=Human adenovirus C serotype 5 / Homo sapiens [PDB ID]=2r7g [PDB chain IDs]=B:A [PDB note]=Chains C, D and E were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.67 [Domain]=Rb pocket [Type chain B]=Disordered [Evidence chain B]=The 1-139 region described in IDEAL entry IID90003 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_Rb_pABgroove_1). [Type chain A]=Ordered [Evidence chain A]=The Rb pocket domain (consist of Rb_A and Rb_B) involved in the interaction is known to adopt a stable structure in isolation (see Pfam domains PF01858 and PF01857). A solved monomeric structure of the domain is represented by DPB ID 3pom. [Chain B name]=Early E1A 32 kDa protein [Chain B source organism]=Human adenovirus C serotype 5 [Chain B UniProt accession]=P03255 [Chain B UniProt boundaries]=40-49 [Chain B UniProt coverage]=3.5% [Chain B UniRef90 accession]=UniRef90_P03255 [Chain B UniRef90 boundaries]=40-49 [Chain A name]=Retinoblastoma-associated protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P06400 [Chain A UniProt boundaries]=380-787 [Chain A UniProt coverage]=44% [Chain A UniRef90 accession]=UniRef90_P06400 [Chain A UniRef90 boundaries]=380-787 [Entry] [Accession]=DI1100039 [Disorder status]=Confirmed [Kd]=5.60E-06 [Name]=WDR5 in complex with an RbBP5 peptide [Source organism]=Mus musculus [PDB ID]=2xl2 [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=WD40 [Type chain C]=Disordered [Evidence chain C]=The interacting region of RbBP5 was shown to be intrinsically disordered (PMID:20716525): RbBP5 consists of a predicted beta-propeller domain followed by a long, apparently unstructured “tail” of about 200 residues. The protein region involved in the interaction contains a known functional linear motif (LIG_WD40_WDR5_VDV_1). [Type chain A]=Ordered [Evidence chain A]=The WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00400). A solved monomeric structure from a homologous protein is represented by PDB ID 2h14. [Chain C name]=Retinoblastoma-binding protein 5 [Chain C source organism]=Mus musculus [Chain C UniProt accession]=Q8BX09 [Chain C UniProt boundaries]=369-381 [Chain C UniProt coverage]=2.4% [Chain C UniRef90 accession]=UniRef90_Q15291 [Chain C UniRef90 boundaries]=369-381 [Chain A name]=WD repeat-containing protein 5 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P61965 [Chain A UniProt boundaries]=1-334 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P61964 [Chain A UniRef90 boundaries]=1-334 [Related structures]=2xl3,3p4f [Entry] [Accession]=DI1100040 [Disorder status]=Confirmed [Kd]=3.00E-06 [Name]=Yeast poly(A) polymerase in complex with Fip1 residues 80-105 [Source organism]=Saccharomyces cerevisiae [PDB ID]=3c66 [PDB chain IDs]=D:B [PDB note]=Chains A and C were removed as chains B and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=PAP RNA-binding domain [Type chain D]=Disordered [Evidence chain D]=The 80-195 region described in DisProt entry DP00625 covers 100% of the sequence present in the structure. [Type chain B]=Ordered [Evidence chain B]=The PAP RNA-binding domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04926). A solved monomeric structure of the domain is represented by PDB ID 2hhp. [Chain D name]=Pre-mRNA polyadenylation factor FIP1 [Chain D source organism]=Saccharomyces cerevisiae [Chain D UniProt accession]=P45976 [Chain D UniProt boundaries]=80-105 [Chain D UniProt coverage]=8% [Chain D UniRef90 accession]=UniRef90_P45976 [Chain D UniRef90 boundaries]=80-105 [Chain B name]=Poly(A) polymerase [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P29468 [Chain B UniProt boundaries]=1-526 [Chain B UniProt coverage]=92.6% [Chain B UniRef90 accession]=UniRef90_P29468 [Chain B UniRef90 boundaries]=1-526 [Entry] [Accession]=DI1020014 [Disorder status]=Confirmed [Kd]=3.80E-05 (PMID:15737988) [Name]=The third fibronectin F1 module in complex with a fragment of BBK32 from Borrelia burgdorferi [Source organism]=Borrelia burgdorferi / Homo sapiens [PDB ID]=4pz5 [PDB chain IDs]=B:A [PDB note]=Chain A was truncated to only include residues 94-138 (according to UniProt numbering) to highlight the fibronectin domain directly involved in the interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.96 [Domain]=Fibronectin type I domain [Type chain B]=Disordered [Evidence chain B]=The 56-205 region described in DisProt entry DP01047 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a non-canonical EEE fibronectin-binding motif (PMID:24962582). [Type chain A]=Ordered [Evidence chain A]=The Fibronectin type I domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00039). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1tpm. [Chain B name]=Fibronectin-binding protein BBK32 [Chain B source organism]=Borrelia burgdorferi [Chain B UniProt accession]=O50835 [Chain B UniProt boundaries]=174-189 [Chain B UniProt coverage]=4.5% [Chain B UniRef90 accession]=UniRef90_Q8RNW3 [Chain B UniRef90 boundaries]=175-187 [Chain A name]=Fibronectin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O50835 [Chain A UniProt boundaries]=94-138 [Chain A UniProt coverage]=1.9% [Chain A UniRef90 accession]=UniRef90_P02751 [Chain A UniRef90 boundaries]=94-138 [Entry] [Accession]=DI1020015 [Disorder status]=Inferred from homology [Kd]=3.80E-05 (PMID:15737988) [Name]=The first fibronectin F1 module in complex with a fragment of Fnbp from Streptococcus dysgalactiae [Source organism]=Streptococcus dysgalactiae / Homo sapiens [PDB ID]=1o9a [PDB chain IDs]=B:A [PDB note]=Chains A and B were truncated to only include residues 48-93 and 1052-1066 (according to UniProt numbering) to highlight the interaction. [PDB experimental technique]=NMR [Domain]=Fibronectin type I domain [Type chain B]=Disordered [Evidence chain B]=The corresponding region of a homologous protein has been shown to be disordered in the 56-205 region described in DisProt entry DP01047 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The Fibronectin type I domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00039). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1tpm. [Chain B name]=Fibronectin binding protein [Chain B source organism]=Streptococcus dysgalactiae [Chain B UniProt accession]=Q53971 [Chain B UniProt boundaries]=1052-1066 [Chain B UniProt coverage]=1.3% [Chain B UniRef90 accession]=UniRef90_Q53971 [Chain B UniRef90 boundaries]=1052-1066 [Chain A name]=Fibronectin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P02751 [Chain A UniProt boundaries]=48-93 [Chain A UniProt coverage]=1.9% [Chain A UniRef90 accession]=UniRef90_P02751 [Chain A UniRef90 boundaries]=48-93 [Entry] [Accession]=DI1020016 [Disorder status]=Inferred from homology [Kd]=3.80E-05 (PMID:15737988) [Name]=The second fibronectin F1 module in complex with a fragment of Fnbp from Streptococcus dysgalactiae [Source organism]=Streptococcus dysgalactiae / Homo sapiens [PDB ID]=1o9a [PDB chain IDs]=B:A [PDB note]=Chains A and B were truncated to only include residues 94-140 and 1043-1051 (according to UniProt numbering) to highlight the interaction. [PDB experimental technique]=NMR [Domain]=Fibronectin type I domain [Type chain B]=Disordered [Evidence chain B]=The corresponding region of a homologous protein has been shown to be disordered in the 56-205 region described in DisProt entry DP01047 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The Fibronectin type I domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00039). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1tpm. [Chain B name]=Fibronectin binding protein [Chain B source organism]=Streptococcus dysgalactiae [Chain B UniProt accession]=Q53971 [Chain B UniProt boundaries]=1043-1051 [Chain B UniProt coverage]=0.8% [Chain B UniRef90 accession]=UniRef90_Q53971 [Chain B UniRef90 boundaries]=1043-1051 [Chain A name]=Fibronectin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P02751 [Chain A UniProt boundaries]=94-140 [Chain A UniProt coverage]=2% [Chain A UniRef90 accession]=UniRef90_P02751 [Chain A UniRef90 boundaries]=94-140 [Entry] [Accession]=DI1000154 [Disorder status]=Inferred from motif [Kd]=4.20E-05 (PMID:22000519) [Name]=PTPN4 PDZ domain complexed with the C-terminus of the GluN2A NMDA receptor subunit [Source organism]=Homo sapiens [PDB ID]=3nfl [PDB chain IDs]=E:A [PDB note]=Chains B, C, D, F, G and H were removed as chains A and E represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.91 [Domain]=PDZ [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a functional PDZ-binding linear motif (PMID:22000519). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2ev8. [Chain E name]=Glutamate receptor ionotropic, NMDA 2A [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=Q12879 [Chain E UniProt boundaries]=1449-1464 [Chain E UniProt coverage]=1.1% [Chain E UniRef90 accession]=UniRef90_Q12879 [Chain E UniRef90 boundaries]=1449-1464 [Chain A name]=Tyrosine-protein phosphatase non-receptor type 4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P29074 [Chain A UniProt boundaries]=498-604 [Chain A UniProt coverage]=11.6% [Chain A UniRef90 accession]=UniRef90_P29074 [Chain A UniRef90 boundaries]=499-604 [Entry] [Accession]=DI1210001 [Disorder status]=Confirmed [Kd]=1.60E-06 [Name]=Colicin A (9-20) peptide in complex with TolB [Source organism]=Citrobacter freundii / Escherichia coli [PDB ID]=3iax [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=WD40 [Type chain B]=Disordered [Evidence chain B]=The interacting region of colicin A was shown to adopt a stable conformation via the interaction (PMID:19627502). [Type chain A]=Ordered [Evidence chain A]=The WD40-like beta propeller repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF07676). A solved monomeric structure of the domain is represented by PDB ID 1c5k. [Chain B name]=Colicin-A [Chain B source organism]=Citrobacter freundii [Chain B UniProt accession]=P04480 [Chain B UniProt boundaries]=1-107 [Chain B UniProt coverage]=18.1% [Chain B UniRef90 accession]=UniRef90_P04480 [Chain B UniRef90 boundaries]=1-107 [Chain A name]=Protein TolB [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=P0A855 [Chain A UniProt boundaries]=1-430 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q83MM7 [Chain A UniRef90 boundaries]=1-430 [Entry] [Accession]=DI1210002 [Disorder status]=Confirmed [Kd]=1.34E-06 [Name]=Colicin A (57-105) peptide in complex with domain III of TolA [Source organism]=Citrobacter freundii / Escherichia coli [PDB ID]=3qdr [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.65 [Domain]=TolA C-terminal [Type chain B]=Disordered [Evidence chain B]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 3iax). [Type chain A]=Ordered [Evidence chain A]=The TolA C-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF06519). A solved monomeric structure of the domain is represented by PDB ID 1s62. [Chain B name]=Colicin-A [Chain B source organism]=Citrobacter freundii [Chain B UniProt accession]=P04480 [Chain B UniProt boundaries]=53-107 [Chain B UniProt coverage]=9.3% [Chain B UniRef90 accession]=UniRef90_P04480 [Chain B UniRef90 boundaries]=53-107 [Chain A name]=Protein TolA [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=P19934 [Chain A UniProt boundaries]=295-421 [Chain A UniProt coverage]=30.2% [Chain A UniRef90 accession]=UniRef90_P19934 [Chain A UniRef90 boundaries]=300-421 [Entry] [Accession]=DI1000155 [Disorder status]=Confirmed [Kd]=2.48E-04 (PMID:24878663) [Name]=The second SH3 domain from CAP/Ponsin in complex with proline rich peptide from Vinculin [Source organism]=Homo sapiens [PDB ID]=4ln2 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.00 [Domain]=SH3 [Type chain B]=Disordered [Evidence chain B]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 1tr2, 3vf0, 3jbk, 3jbi). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00018). A solved monomeric structure of the domain is represented by PDB ID 2ecz. [Chain B name]=Vinculin [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P18206 [Chain B UniProt boundaries]=857-867 [Chain B UniProt coverage]=1% [Chain B UniRef90 accession]=UniRef90_P18206 [Chain B UniRef90 boundaries]=857-865 [Chain A name]=Sorbin and SH3 domain-containing protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9BX66 [Chain A UniProt boundaries]=863-930 [Chain A UniProt coverage]=5.3% [Chain A UniRef90 accession]=UniRef90_Q9BX66 [Chain A UniRef90 boundaries]=866-930 [Entry] [Accession]=DI1000156 [Disorder status]=Confirmed [Kd]=2.14E-04 (PMID:24878663) [Name]=The first SH3 domain from CAP/Ponsin in complex with proline rich peptide from Vinculin [Source organism]=Homo sapiens [PDB ID]=4lnp [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.41 [Domain]=SH3 [Type chain B]=Disordered [Evidence chain B]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 1tr2, 3vf0, 3jbk, 3jbi). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00018). A solved monomeric structure of the domain is represented by PDB ID 2dl3. [Chain B name]=Vinculin [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P18206 [Chain B UniProt boundaries]=870-879 [Chain B UniProt coverage]=0.9% [Chain B UniRef90 accession]=UniRef90_P18206 [Chain B UniRef90 boundaries]=860-864 [Chain A name]=Sorbin and SH3 domain-containing protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9BX66 [Chain A UniProt boundaries]=794-854 [Chain A UniProt coverage]=4.7% [Chain A UniRef90 accession]=UniRef90_Q9BX66 [Chain A UniRef90 boundaries]=794-854 [Entry] [Accession]=DI1100041 [Disorder status]=Confirmed [Kd]=2.14E-04 (PMID:24878663) [Name]=Auto-inhibition and phosphorylation-induced activation of PLC-gamma isozymes [Source organism]=Rattus norvegicus [PDB ID]=4k45 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.50 [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The interacting protein segment is an auto-inhibitory region of the PLC-gamma isozyme that is located in a flexible linker region connecting an SH2 and an SH3 domain (PMID:23777354). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ab2. [Modified residues chain B]=phosphotyrosine#Y#783 [Chain B name]=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=P10686 [Chain B UniProt boundaries]=770-787 [Chain B UniProt coverage]=1.4% [Chain B UniRef90 accession]=UniRef90_P19174 [Chain B UniRef90 boundaries]=770-787 [Chain A name]=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=P10686 [Chain A UniProt boundaries]=661-766 [Chain A UniProt coverage]=8.2% [Chain A UniRef90 accession]=UniRef90_P19174 [Chain A UniRef90 boundaries]=664-766 [Related structures]=4ey0,4fbn [Entry] [Accession]=DI1000157 [Disorder status]=Confirmed [Kd]=6.80E-05 (PMID:18550522) [Name]=RNA processing factor SCAF8 bound to the mono-phosphorylated CTD peptide of RNA Polymerase II [Source organism]=Homo sapiens [PDB ID]=3d9k [PDB chain IDs]=Y:A [PDB note]=Chains Z and B were removed as chains A and Y represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=CID [Type chain Y]=Disordered [Evidence chain Y]=The C terminal domain of RNA polymerase II subunit RPB1 has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 5iy7). [Type chain A]=Ordered [Evidence chain A]=The CID domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04818). A solved monomeric structure of the domain is represented by PDB ID 2diw. [Modified residues chain Y]=phosphoserine#S#2 [Chain Y name]=DNA-directed RNA polymerase II subunit RPB1 [Chain Y source organism]=Homo sapiens [Chain Y UniProt accession]=P24928 [Chain Y UniProt boundaries]=1790-1803 [Chain Y UniProt coverage]=0.7% [Chain Y UniRef90 accession]=UniRef90_P24928 [Chain Y UniRef90 boundaries]=1790-1803 [Chain A name]=Protein SCAF8 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UPN6 [Chain A UniProt boundaries]=1-145 [Chain A UniProt coverage]=11.4% [Chain A UniRef90 accession]=UniRef90_Q9UPN6 [Chain A UniRef90 boundaries]=1-138 [Related structures]=3d9l,3d9p [Entry] [Accession]=DI1000158 [Disorder status]=Confirmed [Kd]=3.12E-06 (PMID:17563362) [Name]=Cytoskeletal protein Restin in complex with tubulin tail [Source organism]=Homo sapiens [PDB ID]=2e4h [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=CAP-Gly domain [Type chain B]=Disordered [Evidence chain B]=The C terminal domain of Tubulin alpha-ubiquitous chain has been shown to be highly flexible corresponding to missing coordinates in electron microscopy structure (PDB ID: 5ij0). The protein region involved in the interaction contains a known functional linear motif EExEE(Y/F)$ (PMID:17563362). [Type chain A]=Ordered [Evidence chain A]=The CAP-Gly domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01302). A solved monomeric structure of the domain is represented by PDB ID 2e3h. [Chain B name]=Tubulin alpha-1B chain [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68363 [Chain B UniProt boundaries]=416-451 [Chain B UniProt coverage]=8% [Chain B UniRef90 accession]=UniRef90_P68363 [Chain B UniRef90 boundaries]=416-440 [Chain A name]=CAP-Gly domain-containing linker protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P30622 [Chain A UniProt boundaries]=203-300 [Chain A UniProt coverage]=6.8% [Chain A UniRef90 accession]=UniRef90_P30622 [Chain A UniRef90 boundaries]=203-300 [Entry] [Accession]=DI1000159 [Disorder status]=Confirmed [Kd]=3.00E-04 (PMID:24139988) [Name]=EKLF TAD in complex with ubiquitin [Source organism]=Homo sapiens [PDB ID]=2mbh [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Ubiquitin [Type chain B]=Disordered [Evidence chain B]=The TAD region of Klf1 has been shown to be disordered and to only adopt a stable structure upon interaction (PMID:24139988). [Type chain A]=Ordered [Evidence chain A]=The ubiquitin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00240). A solved monomeric structure of a close homologue is represented by PDB ID 2k39. [Chain B name]=Krueppel-like factor 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q13351 [Chain B UniProt boundaries]=1-40 [Chain B UniProt coverage]=11% [Chain B UniRef90 accession]=UniRef90_Q13351 [Chain B UniRef90 boundaries]=2-40 [Chain A name]=Polyubiquitin-B (Fragment) [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=J3QS39 [Chain A UniProt boundaries]=1-76 [Chain A UniProt coverage]=81.7% [Chain A UniRef90 accession]=UniRef90_P62972 [Chain A UniRef90 boundaries]=16-91 [Entry] [Accession]=DI1010052 [Disorder status]=Confirmed [Kd]=3.00E-04 (PMID:24139988) [Name]=Complex between the PH domain of the Tfb1 subunit from TFIIH and the N-terminal activation domain of EKLF (TAD1) [Source organism]=Homo sapiens / Saccharomyces cerevisiae [PDB ID]=2n23 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PH [Type chain B]=Disordered [Evidence chain B]=The TAD region of Klf1 has been shown to be disordered and to only adopt a stable structure upon interaction (PMID:24139988). [Type chain A]=Ordered [Evidence chain A]=The PH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF08567). A solved monomeric structure of the domain is represented by PDB ID 1pfj. [Chain B name]=Krueppel-like factor 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q13351 [Chain B UniProt boundaries]=22-40 [Chain B UniProt coverage]=5.2% [Chain B UniRef90 accession]=UniRef90_Q13351 [Chain B UniRef90 boundaries]=22-40 [Chain A name]=RNA polymerase II transcription factor B subunit 1 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P32776 [Chain A UniProt boundaries]=1-115 [Chain A UniProt coverage]=17.9% [Chain A UniRef90 accession]=UniRef90_P32776 [Chain A UniRef90 boundaries]=2-115 [Entry] [Accession]=DI1100042 [Disorder status]=Confirmed [Kd]=3.00E-04 (PMID:24139988) [Name]=Atg7 C-terminal region bound to Atg8 [Source organism]=Saccharomyces cerevisiae [PDB ID]=2li5 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Atg8 [Type chain B]=Disordered [Evidence chain B]=The C terminal region of Atg7 has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 3vh3). [Type chain A]=Ordered [Evidence chain A]=The Atg8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02991). A solved monomeric structure of the domain is represented by PDB ID 2kwc. [Chain B name]=Ubiquitin-like modifier-activating enzyme ATG7 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P38862 [Chain B UniProt boundaries]=601-630 [Chain B UniProt coverage]=4.8% [Chain B UniRef90 accession]=UniRef90_P38862 [Chain B UniRef90 boundaries]=601-630 [Chain A name]=Autophagy-related protein 8 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P38182 [Chain A UniProt boundaries]=1-116 [Chain A UniProt coverage]=99.1% [Chain A UniRef90 accession]=UniRef90_Q6FXR8 [Chain A UniRef90 boundaries]=1-116 [Related structures]=3rui,3vh4 [Entry] [Accession]=DI1100043 [Disorder status]=Confirmed [Kd]=7.50E-09 (PMID:25160624) [Name]=Bud13 C-terminal peptide bound to Snu17 RRM domain [Source organism]=Saccharomyces cerevisiae [PDB ID]=4uqt [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=RRM [Type chain B]=Disordered [Evidence chain B]=The interacting region of Bud13 was shown using NMR to adopt a partially ordered structure as a result of the interaction (PMID:25160624). [Type chain A]=Ordered [Evidence chain A]=The RRM domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00076). A solved monomeric structure of a close homologue is represented by PDB ID 2m52. [Chain B name]=Pre-mRNA-splicing factor CWC26 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P46947 [Chain B UniProt boundaries]=218-256 [Chain B UniProt coverage]=14.7% [Chain B UniRef90 accession]=UniRef90_P46947 [Chain B UniRef90 boundaries]=222-256 [Chain A name]=U2 snRNP component IST3 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P40565 [Chain A UniProt boundaries]=21-113 [Chain A UniProt coverage]=62.8% [Chain A UniRef90 accession]=UniRef90_P40565 [Chain A UniRef90 boundaries]=22-113 [Related structures]=2my2,5lqw [Entry] [Accession]=DI1000160 [Disorder status]=Confirmed [Kd]=1.00E-05 (PMID:12970176) [Name]=HHR23A ubiquitin-like domain and the C-terminal ubiquitin-interacting motif of proteasome subunit S5a [Source organism]=Homo sapiens [PDB ID]=1p9d [PDB chain IDs]=S:U [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Ubiquitin [Type chain S]=Disordered [Evidence chain S]=The region of interest contains alpha-helical elements connected with flexible, randomly coiled linker regions. These unstructured regions prevent the structured regions from being defined relative to each other and allow S5a to be highly adaptive for binding polyubiquitin chains (PMID:15826667). The interacting region of the protein conatins a known functional ubiquitin-interacting motif (UIM) (PMID:12970176). [Type chain U]=Ordered [Evidence chain U]=The ubiquitin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00240). A solved monomeric structure of the domain is represented by PDB ID 1p98. [Chain S name]=26S proteasome non-ATPase regulatory subunit 4 [Chain S source organism]=Homo sapiens [Chain S UniProt accession]=P55036 [Chain S UniProt boundaries]=263-307 [Chain S UniProt coverage]=11.9% [Chain S UniRef90 accession]=UniRef90_P55036 [Chain S UniRef90 boundaries]=263-307 [Chain U name]=UV excision repair protein RAD23 homolog A [Chain U source organism]=Homo sapiens [Chain U UniProt accession]=P54725 [Chain U UniProt boundaries]=1-78 [Chain U UniProt coverage]=21.5% [Chain U UniRef90 accession]=UniRef90_P54725 [Chain U UniRef90 boundaries]=1-78 [Entry] [Accession]=DI1000161 [Disorder status]=Confirmed [Kd]=1.00E-05 (PMID:12970176) [Name]=Cdt1 bound to DNA replication licensing factor MCM6 [Source organism]=Homo sapiens [PDB ID]=2le8 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=MCM C-terminal [Type chain B]=Disordered [Evidence chain B]=The interacting region of Cdt1 has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 2wvr). [Type chain A]=Ordered [Evidence chain A]=The MCM C-terminal domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 2klq. [Chain B name]=DNA replication factor Cdt1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9H211 [Chain B UniProt boundaries]=413-441 [Chain B UniProt coverage]=5.3% [Chain B UniRef90 accession]=UniRef90_Q9H211 [Chain B UniRef90 boundaries]=415-441 [Chain A name]=DNA replication licensing factor MCM6 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q14566 [Chain A UniProt boundaries]=708-821 [Chain A UniProt coverage]=13.9% [Chain A UniRef90 accession]=UniRef90_Q14566 [Chain A UniRef90 boundaries]=708-821 [Entry] [Accession]=DI1000162 [Disorder status]=Confirmed [Kd]=2.30E-06 (PMID:26982350) [Name]=C-terminal domain of human polymerase Rev1 in complex with PolD3 RIR-motif [Source organism]=Homo sapiens [PDB ID]=2n1g [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=REV1 C-terminal [Type chain B]=Disordered [Evidence chain B]=The 144-466 region of PolD3 has been shown to be intrinsically disordered (PMID:26982350). The protein region involved in the interaction contains a Rev1-interacting region (RIR) motif (PMID:26982350). [Type chain A]=Ordered [Evidence chain A]=The REV1 C-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF16727). A solved monomeric structure of the domain is represented by PDB ID 2lsy. [Chain B name]=DNA polymerase delta subunit 3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q15054 [Chain B UniProt boundaries]=231-246 [Chain B UniProt coverage]=3.4% [Chain B UniRef90 accession]=UniRef90_Q15054 [Chain B UniRef90 boundaries]=231-246 [Chain A name]=DNA repair protein REV1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UBZ9 [Chain A UniProt boundaries]=1158-1251 [Chain A UniProt coverage]=7.5% [Chain A UniRef90 accession]=UniRef90_Q9UBZ9 [Chain A UniRef90 boundaries]=1158-1251 [Entry] [Accession]=DI3000005 [Disorder status]=Confirmed [Kd]=1.56E-05 [Name]=Human PCNA bound to residues 452-466 of the DNA polymerase-delta-p66 subunit [Source organism]=Homo sapiens [PDB ID]=1u76 [PDB chain IDs]=B:ACE [PDB note]=Chains D and F were removed as chains A, B, C and E represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=PCNA [Type chain B]=Disordered [Evidence chain B]=The 144-466 region of PolD3 has been shown to be intrinsically disordered (PMID:26982350). The protein region involved in the interaction contains a known functional linear motif (LIG_PCNA_PIPBox_1). [Type chain A]=Ordered component [Evidence chain A]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60. [Type chain C]=Ordered component [Evidence chain C]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60. [Type chain E]=Ordered component [Evidence chain E]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60. [Chain B name]=DNA polymerase delta subunit 3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q15054 [Chain B UniProt boundaries]=452-466 [Chain B UniProt coverage]=3.2% [Chain B UniRef90 accession]=UniRef90_Q15054 [Chain B UniRef90 boundaries]=452-466 [Chain A name]=Proliferating cell nuclear antigen [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P12004 [Chain A UniProt boundaries]=1-261 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P12004 [Chain A UniRef90 boundaries]=1-261 [Chain C name]=Proliferating cell nuclear antigen [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P12004 [Chain C UniProt boundaries]=1-261 [Chain C UniProt coverage]=100% [Chain C UniRef90 accession]=UniRef90_P12004 [Chain C UniRef90 boundaries]=1-261 [Chain E name]=Proliferating cell nuclear antigen [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P12004 [Chain E UniProt boundaries]=1-261 [Chain E UniProt coverage]=100% [Chain E UniRef90 accession]=UniRef90_P12004 [Chain E UniRef90 boundaries]=1-261 [Entry] [Accession]=DI1210003 [Disorder status]=Confirmed [Kd]=1.20E-07 [Name]=E.coli F-ATPase delta subunit N-terminal domain in complex with alpha subunit N-terminal peptide [Source organism]=Shigella flexneri / Escherichia coli [PDB ID]=2a7u [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=OSCP [Type chain A]=Disordered [Evidence chain A]=The N-terminal interacting region of the ATP synthase alpha subunit has been shown to be intrinsically disordered as evidenced by missing electron density in X-ray structures (PDB ID: 5t4o, 5t4p, 5t4q, 3oaa). [Type chain B]=Ordered [Evidence chain B]=The OSCP domain (or ATP synthase delta subunit domain) involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00213). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1abv. [Chain A name]=ATP synthase subunit alpha [Chain A source organism]=Shigella flexneri [Chain A UniProt accession]=P0ABB3 [Chain A UniProt boundaries]=1-22 [Chain A UniProt coverage]=4.3% [Chain A UniRef90 accession]=UniRef90_A1JTC8 [Chain A UniRef90 boundaries]=1-22 [Chain B name]=ATP synthase subunit delta [Chain B source organism]=Escherichia coli [Chain B UniProt accession]=P0ABA4 [Chain B UniProt boundaries]=2-135 [Chain B UniProt coverage]=75.7% [Chain B UniRef90 accession]=UniRef90_Q83PJ9 [Chain B UniRef90 boundaries]=2-135 [Entry] [Accession]=DI1100044 [Disorder status]=Confirmed [Kd]=7.60E-06 (PMID:19170759) [Name]=Mouse Rev1 CTD in complex with the Rev1-interacting Region (RIR)of Pol Kappa [Source organism]=Mus musculus [PDB ID]=2lsj [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=REV1 C-terminal [Type chain B]=Disordered [Evidence chain B]=Binding of the mouse Pol Kappa RIR to the Rev1 CTD induces folding of the disordered RIR peptide (PMID:22700975). The protein region involved in the interaction contains a Rev1-interacting region (RIR) motif (consensous sequence: xSFFyyKy; S is a helix cap residue that is predominantly serine but can be replaced by proline, y is any residue but not proline) (PMID:19170759). [Type chain A]=Ordered [Evidence chain A]=The REV1 C-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF16727). A solved monomeric structure of the domain is represented by PDB ID 2lsg. [Chain B name]=DNA polymerase kappa [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q9QUG2 [Chain B UniProt boundaries]=558-582 [Chain B UniProt coverage]=2.9% [Chain B UniRef90 accession]=UniRef90_Q9QUG2 [Chain B UniRef90 boundaries]=559-582 [Chain A name]=DNA repair protein REV1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q920Q2 [Chain A UniProt boundaries]=1131-1249 [Chain A UniProt coverage]=9.5% [Chain A UniRef90 accession]=UniRef90_Q920Q2 [Chain A UniRef90 boundaries]=1131-1249 [Related structures]=2lsi,4fjo [Entry] [Accession]=DI1000163 [Disorder status]=Confirmed [Kd]=1.30E-05 (PMID:23805866) [Name]=Optineurin peptide bound to microtubule-associated proteins 1A/1B light chain 3B [Source organism]=Homo sapiens [PDB ID]=2lue [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Atg8 [Type chain B]=Disordered [Evidence chain B]=The interacting region of optineurin has been shown to be disordered in IDEAL entry IID00348 and contains a known functional LIR linear motif (http://www.uniprot.org/uniprot/Q96CV9#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The Atg8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02991). A solved monomeric structure of the domain is represented by PDB ID 1v49. [Modified residues chain B]=phosphoserine#S#170|phosphoserine#S#171|phosphoserine#S#173|phosphoserine#S#174|phosphoserine#S#177 [Chain B name]=Optineurin [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q96CV9 [Chain B UniProt boundaries]=169-185 [Chain B UniProt coverage]=2.9% [Chain B UniRef90 accession]=UniRef90_Q96CV9 [Chain B UniRef90 boundaries]=169-185 [Chain A name]=Microtubule-associated proteins 1A/1B light chain 3B [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9GZQ8 [Chain A UniProt boundaries]=1-119 [Chain A UniProt coverage]=95.2% [Chain A UniRef90 accession]=UniRef90_Q9GZQ8 [Chain A UniRef90 boundaries]=5-119 [Related structures]=3vtv,3vtw [Entry] [Accession]=DI1000164 [Disorder status]=Inferred from motif [Kd]=5.80E-06 (PMID:18606141) [Name]=The MIT-interaction motif of CHMP6 bound to VPS4A MIT domain [Source organism]=Homo sapiens [PDB ID]=2k3w [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=MIT [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (MIT-interacting motif - http://www.uniprot.org/uniprot/Q96FZ7#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The MIT domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04212). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2jqh. [Chain B name]=Charged multivesicular body protein 6 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q96FZ7 [Chain B UniProt boundaries]=166-181 [Chain B UniProt coverage]=8% [Chain B UniRef90 accession]=UniRef90_Q96FZ7 [Chain B UniRef90 boundaries]=166-181 [Chain A name]=Vacuolar protein sorting-associated protein 4A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UN37 [Chain A UniProt boundaries]=1-84 [Chain A UniProt coverage]=19.2% [Chain A UniRef90 accession]=UniRef90_Q9UN37 [Chain A UniRef90 boundaries]=1-84 [Entry] [Accession]=DI1110014 [Disorder status]=Confirmed [Kd]=5.80E-06 (PMID:18606141) [Name]=C-terminal peptide from peroxiredoxin-4 bound to disulfide-isomerase A6 [Source organism]=Mus musculus / Pongo abelii [PDB ID]=3w8j [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=Thioredoxin [Type chain C]=Disordered [Evidence chain C]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 3vwu, 3tkq). [Type chain A]=Ordered [Evidence chain A]=The thioredoxin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00085). A solved monomeric structure of the domain is represented by PDB ID 3vww. [Chain C name]=Peroxiredoxin-4 [Chain C source organism]=Mus musculus [Chain C UniProt accession]=O08807 [Chain C UniProt boundaries]=244-263 [Chain C UniProt coverage]=7.3% [Chain C UniRef90 accession]=UniRef90_O08807 [Chain C UniRef90 boundaries]=244-263 [Chain A name]=Protein disulfide-isomerase A6 [Chain A source organism]=Pongo abelii [Chain A UniProt accession]=Q5R6T1 [Chain A UniProt boundaries]=20-139 [Chain A UniProt coverage]=27.3% [Chain A UniRef90 accession]=UniRef90_Q15084 [Chain A UniRef90 boundaries]=20-139 [Entry] [Accession]=DI1010053 [Disorder status]=Confirmed [Kd]=5.80E-06 (PMID:18606141) [Name]=C-terminal peptide from peroxiredoxin-4 bound to thioredoxin domain-containing protein 5 [Source organism]=Mus musculus / Homo sapiens [PDB ID]=3wgx [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=0.92 [Domain]=Thioredoxin [Type chain C]=Disordered [Evidence chain C]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 3vwu, 3tkq). [Type chain A]=Ordered [Evidence chain A]=The thioredoxin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00085). A solved monomeric structure of the domain is represented by PDB ID 3wge. [Chain C name]=Peroxiredoxin-4 [Chain C source organism]=Mus musculus [Chain C UniProt accession]=O08807 [Chain C UniProt boundaries]=244-263 [Chain C UniProt coverage]=7.3% [Chain C UniRef90 accession]=UniRef90_O08807 [Chain C UniRef90 boundaries]=244-263 [Chain A name]=Thioredoxin domain-containing protein 5 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q8NBS9 [Chain A UniProt boundaries]=186-298 [Chain A UniProt coverage]=26.2% [Chain A UniRef90 accession]=UniRef90_Q8NBS9 [Chain A UniRef90 boundaries]=190-298 [Entry] [Accession]=DI1110015 [Disorder status]=Confirmed [Kd]=5.80E-06 (PMID:18606141) [Name]=Alpha-cobratoxin complexed with a cognate peptide from acetylcholine receptor protein, alpha chain [Source organism]=Torpedo californica / Naja kaouthia [PDB ID]=1lxg [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Snake toxin [Type chain B]=Disordered [Evidence chain B]=The interacting region of acetylcholine receptor alpha1 subunit hsa been shown to be unstructured in its unbound form (PMID:12133834). [Type chain A]=Ordered [Evidence chain A]=The snake toxin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00087). A solved monomeric structure of the domain is represented by PDB ID 1ctx. [Chain B name]=Acetylcholine receptor subunit alpha [Chain B source organism]=Torpedo californica [Chain B UniProt accession]=P02710 [Chain B UniProt boundaries]=205-223 [Chain B UniProt coverage]=4.1% [Chain B UniRef90 accession]=UniRef90_P02710 [Chain B UniRef90 boundaries]=205-222 [Chain A name]=Alpha-elapitoxin-Nk2a [Chain A source organism]=Naja kaouthia [Chain A UniProt accession]=P01391 [Chain A UniProt boundaries]=1-71 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P01391 [Chain A UniRef90 boundaries]=1-71 [Related structures]=1lxh [Entry] [Accession]=DI1110016 [Disorder status]=Confirmed [Kd]=6.50E-08 (PMID:1979446) [Name]=Alpha-bungarotoxin complexed with a cognate peptide from acetylcholine receptor protein, alpha chain [Source organism]=Torpedo californica / Bungarus multicinctus [PDB ID]=1abt [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Snake toxin [Type chain B]=Disordered [Evidence chain B]=The interacting region of acetylcholine receptor alpha1 subunit hsa been shown to be unstructured in its unbound form (PMID:12133834). [Type chain A]=Ordered [Evidence chain A]=The snake toxin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00087). A solved monomeric structure of the domain is represented by PDB ID 1idi. [Chain B name]=Acetylcholine receptor subunit alpha [Chain B source organism]=Torpedo californica [Chain B UniProt accession]=P02710 [Chain B UniProt boundaries]=209-220 [Chain B UniProt coverage]=2.6% [Chain B UniRef90 accession]=UniRef90_P02710 [Chain B UniRef90 boundaries]=209-220 [Chain A name]=Alpha-bungarotoxin isoform A31 [Chain A source organism]=Bungarus multicinctus [Chain A UniProt accession]=P60615 [Chain A UniProt boundaries]=22-95 [Chain A UniProt coverage]=77.9% [Chain A UniRef90 accession]=UniRef90_P60615 [Chain A UniRef90 boundaries]=22-95 [Related structures]=1idg,1idh,1l4w,1ljz [Entry] [Accession]=DI1000165 [Disorder status]=Confirmed [Kd]=1.00E-06 (PMID:8961927) [Name]=SH3 domain from Fyn complexed with the proline-rich binding site on the p85 subunit of PI3-kinase [Source organism]=Homo sapiens [PDB ID]=1a0n [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH3 [Type chain A]=Disordered [Evidence chain A]=Circular dichroism spectroscopic studies reveal that in the unbound state the peptide exhibits no structure (PMID:8961927). The protein region involved in the interaction contains a known functional linear motif (LIG_SH3_1). [Type chain B]=Ordered [Evidence chain B]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00018). A solved monomeric structure of the domain is represented by PDB ID 1nyf. [Chain A name]=Phosphatidylinositol 3-kinase regulatory subunit alpha [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P27986 [Chain A UniProt boundaries]=91-104 [Chain A UniProt coverage]=1.9% [Chain A UniRef90 accession]=UniRef90_P27986 [Chain A UniRef90 boundaries]=91-104 [Chain B name]=Tyrosine-protein kinase Fyn [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P06241 [Chain B UniProt boundaries]=80-148 [Chain B UniProt coverage]=12.8% [Chain B UniRef90 accession]=UniRef90_P06241 [Chain B UniRef90 boundaries]=80-148 [Related structures]=1azg [Entry] [Accession]=DI1020017 [Disorder status]=Confirmed [Kd]=2.30E-06 (PMID:24889612) [Name]=O-glycan attached to herpes simplex virus type 1 glycoprotein gB bound to Ig V-set domain of human paired immunoglobulin-like type 2 receptor alpha [Source organism]=Human herpesvirus 1 / Homo sapiens [PDB ID]=3wv0 [PDB chain IDs]=X:A [PDB note]=Chains B and Y were removed as chains A and X represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=V-set [Type chain X]=Disordered [Evidence chain X]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 3nwf, 3nw8, 3nwa, 4hsi, 4l1r, 3nwd). [Type chain A]=Ordered [Evidence chain A]=The V-set domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF07686). A solved monomeric structure of the domain is represented by PDB ID 3wuz. [Chain X name]=Envelope glycoprotein B [Chain X source organism]=Human herpesvirus 1 [Chain X UniProt accession]=P06437 [Chain X UniProt boundaries]=50-56 [Chain X UniProt coverage]=0.8% [Chain X UniRef90 accession]=UniRef90_P06437 [Chain X UniRef90 boundaries]=50-56 [Chain A name]=Paired immunoglobulin-like type 2 receptor alpha (Fragment) [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=C9JGG1 [Chain A UniProt boundaries]=31-150 [Chain A UniProt coverage]=72.3% [Chain A UniRef90 accession]=UniRef90_Q9UKJ1-3 [Chain A UniRef90 boundaries]=32-150 [Entry] [Accession]=DI1010054 [Disorder status]=Confirmed [Kd]=5.90E-06 (PMID:25945584) [Name]=Tah1 bound to HSP90 peptide [Source organism]=Homo sapiens / Saccharomyces cerevisiae [PDB ID]=4cgq [PDB chain IDs]=Q:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Tetratricopeptide [Type chain Q]=Disordered [Evidence chain Q]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 3q6n, 3q6m). The protein region involved in the interaction contains a known functional linear motif (LIG_TPR). [Type chain A]=Ordered [Evidence chain A]=The tetratricopeptide domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF14559). A solved monomeric structure of the domain is represented by PDB ID 2lsu. [Chain Q name]=Heat shock protein HSP 90-alpha [Chain Q source organism]=Homo sapiens [Chain Q UniProt accession]=P07900 [Chain Q UniProt boundaries]=726-732 [Chain Q UniProt coverage]=1% [Chain Q UniRef90 accession]=UniRef90_P07900 [Chain Q UniRef90 boundaries]=726-732 [Chain A name]=TPR repeat-containing protein associated with Hsp90 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P25638 [Chain A UniProt boundaries]=1-111 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P25638 [Chain A UniRef90 boundaries]=1-111 [Related structures]=4cgu [Entry] [Accession]=DI1000166 [Disorder status]=Confirmed [Kd]=9.70E-06 (PMID:24794838) [Name]=Second TPR of Spaghetti (RPAP3) bound to HSP90 peptide [Source organism]=Homo sapiens [PDB ID]=4cgw [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.00 [Domain]=Tetratricopeptide [Type chain C]=Disordered [Evidence chain C]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 3q6n, 3q6m). The protein region involved in the interaction contains a known functional linear motif (LIG_TPR). [Type chain A]=Ordered [Evidence chain A]=The tetratricopeptide domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13176/PF13181). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2lsu. [Chain C name]=Heat shock protein HSP 90-alpha [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P07900 [Chain C UniProt boundaries]=726-732 [Chain C UniProt coverage]=1% [Chain C UniRef90 accession]=UniRef90_P07900 [Chain C UniRef90 boundaries]=726-732 [Chain A name]=RNA polymerase II-associated protein 3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9H6T3 [Chain A UniProt boundaries]=265-381 [Chain A UniProt coverage]=17.6% [Chain A UniRef90 accession]=UniRef90_Q9H6T3 [Chain A UniRef90 boundaries]=265-381 [Entry] [Accession]=DI2000011 [Disorder status]=Confirmed [Kd]=9.40E-07 (PMID:24794838) [Name]=First TPR of Spaghetti (RPAP3) bound to HSP90 peptide [Source organism]=Homo sapiens [PDB ID]=4cgv [PDB chain IDs]=F:AB [PDB note]=Chains C, D and E were removed as chains A, B and F represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.54 [Domain]=Tetratricopeptide [Type chain F]=Disordered [Evidence chain F]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 3q6n, 3q6m). The protein region involved in the interaction contains a known functional linear motif (LIG_TPR). [Type chain A]=Ordered [Evidence chain A]=The tetratricopeptide domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00515). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1a17. [Type chain B]=Ordered [Evidence chain B]=The tetratricopeptide domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00515). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1a17. [Chain F name]=Heat shock protein HSP 90-alpha [Chain F source organism]=Homo sapiens [Chain F UniProt accession]=P07900 [Chain F UniProt boundaries]=726-732 [Chain F UniProt coverage]=1% [Chain F UniRef90 accession]=UniRef90_P07900 [Chain F UniRef90 boundaries]=726-732 [Chain A name]=RNA polymerase II-associated protein 3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9H6T3 [Chain A UniProt boundaries]=120-255 [Chain A UniProt coverage]=20.5% [Chain A UniRef90 accession]=UniRef90_Q9H6T3 [Chain A UniRef90 boundaries]=120-255 [Chain B name]=RNA polymerase II-associated protein 3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9H6T3 [Chain B UniProt boundaries]=120-255 [Chain B UniProt coverage]=20.5% [Chain B UniRef90 accession]=UniRef90_Q9H6T3 [Chain B UniRef90 boundaries]=120-255 [Entry] [Accession]=DI1000167 [Disorder status]=Confirmed [Kd]=5.60E-08 (PMID:15713458) [Name]=TPR domain from protein phosphatase 5 bound to HSP90 peptide [Source organism]=Homo sapiens [PDB ID]=2bug [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Tetratricopeptide [Type chain B]=Disordered [Evidence chain B]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 3q6n, 3q6m). The protein region involved in the interaction contains a known functional linear motif (LIG_TPR). [Type chain A]=Ordered [Evidence chain A]=The tetratricopeptide domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00515). A solved monomeric structure of the domain is represented by PDB ID 1a17. [Chain B name]=Heat shock protein HSP 90-alpha [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P07900 [Chain B UniProt boundaries]=728-732 [Chain B UniProt coverage]=0.7% [Chain B UniRef90 accession]=UniRef90_P07900 [Chain B UniRef90 boundaries]=728-732 [Chain A name]=Serine/threonine-protein phosphatase 5 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P53041 [Chain A UniProt boundaries]=8-147 [Chain A UniProt coverage]=28.1% [Chain A UniRef90 accession]=UniRef90_P53042 [Chain A UniRef90 boundaries]=18-147 [Entry] [Accession]=DI1120008 [Disorder status]=Inferred from motif [Kd]=5.60E-08 (PMID:15713458) [Name]=MAGI-1 PDZ1 bound to the C-terminal peptide of HPV18 E6 [Source organism]=Human papillomavirus type 18 / Mus musculus [PDB ID]=2i04 [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.15 [Domain]=PDZ [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_1). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2kpk. [Chain C name]=Protein E6 [Chain C source organism]=Human papillomavirus type 18 [Chain C UniProt accession]=P06463 [Chain C UniProt boundaries]=152-158 [Chain C UniProt coverage]=4.4% [Chain C UniRef90 accession]=UniRef90_P06463 [Chain C UniRef90 boundaries]=152-158 [Chain A name]=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q6RHR9 [Chain A UniProt boundaries]=462-546 [Chain A UniProt coverage]=5.8% [Chain A UniRef90 accession]=UniRef90_Q6RHR9 [Chain A UniRef90 boundaries]=463-546 [Entry] [Accession]=DI1000168 [Disorder status]=Inferred from motif [Kd]=5.60E-08 (PMID:15713458) [Name]=VHS domain of human GGA1 complexed with cation-independent M6PR C-terminal peptide [Source organism]=Homo sapiens [PDB ID]=1jwg [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=VHS [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (TRG_LysEnd_GGAAcLL_1). [Type chain A]=Ordered [Evidence chain A]=The VHS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00790). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1jwf. [Chain C name]=Cation-independent mannose-6-phosphate receptor [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P11717 [Chain C UniProt boundaries]=2479-2491 [Chain C UniProt coverage]=0.5% [Chain C UniRef90 accession]=UniRef90_P11717 [Chain C UniRef90 boundaries]=2479-2491 [Chain A name]=ADP-ribosylation factor-binding protein GGA1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UJY5 [Chain A UniProt boundaries]=1-147 [Chain A UniProt coverage]=23% [Chain A UniRef90 accession]=UniRef90_Q9UJY5 [Chain A UniRef90 boundaries]=1-147 [Entry] [Accession]=DI1000169 [Disorder status]=Inferred from motif [Kd]=2.20E-05 (PMID:21098120) [Name]=MLLE domain of poly(A) binding protein in complex with PAM2 motif of La-related protein 4 (LARP4) [Source organism]=Homo sapiens [PDB ID]=3pkn [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=PABP [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_PAM2_1). [Type chain A]=Ordered [Evidence chain A]=The PABP domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00658). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1i2t. [Chain B name]=La-related protein 4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q71RC2 [Chain B UniProt boundaries]=13-26 [Chain B UniProt coverage]=1.9% [Chain B UniRef90 accession]=UniRef90_Q71RC2 [Chain B UniRef90 boundaries]=13-26 [Chain A name]=Polyadenylate-binding protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P11940 [Chain A UniProt boundaries]=539-626 [Chain A UniProt coverage]=13.8% [Chain A UniRef90 accession]=UniRef90_P11940 [Chain A UniRef90 boundaries]=544-626 [Entry] [Accession]=DI1000170 [Disorder status]=Inferred from motif [Kd]=2.00E-04 (PMID:15657040) [Name]=SH3 domain of p40phox complexed with C-terminal polyproline region of p47phox [Source organism]=Homo sapiens [PDB ID]=1w70 [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.46 [Domain]=SH3 [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_SH3_2). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00018). A solved monomeric structure of the domain is represented by PDB ID 1z9q. [Chain C name]=Neutrophil cytosol factor 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P14598 [Chain C UniProt boundaries]=359-372 [Chain C UniProt coverage]=3.6% [Chain C UniRef90 accession]=UniRef90_P14598 [Chain C UniRef90 boundaries]=360-372 [Chain A name]=Neutrophil cytosol factor 4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q15080 [Chain A UniProt boundaries]=169-228 [Chain A UniProt coverage]=17.7% [Chain A UniRef90 accession]=UniRef90_Q15080 [Chain A UniRef90 boundaries]=174-228 [Entry] [Accession]=DI1000171 [Disorder status]=Confirmed [Kd]=1.23E-06 (PMID:19155274) [Name]=Human PNKP FHA domain in complex with an XRCC1-derived phosphopeptide [Source organism]=Homo sapiens [PDB ID]=2w3o [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.85 [Domain]=FHA [Type chain C]=Disordered [Evidence chain C]=The region of interest is located in the C-terminal end of the second unstructured linker region (XL2) of XRCC1 (PMID:25795425). The protein region involved in the interaction contains a known functional linear motif (MOD_CK2_1). [Type chain A]=Ordered [Evidence chain A]=The FHA domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00498). A solved monomeric structure of the domain is represented by PDB ID 2brf. [Modified residues chain C]=phosphoserine#S#518|phosphothreonine#T#519 [Chain C name]=DNA repair protein XRCC1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P18887 [Chain C UniProt boundaries]=515-522 [Chain C UniProt coverage]=1.3% [Chain C UniRef90 accession]=UniRef90_P18887 [Chain C UniRef90 boundaries]=515-522 [Chain A name]=Bifunctional polynucleotide phosphatase/kinase [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96T60 [Chain A UniProt boundaries]=1-110 [Chain A UniProt coverage]=21.1% [Chain A UniRef90 accession]=UniRef90_Q96T60 [Chain A UniRef90 boundaries]=1-110 [Entry] [Accession]=DI1000172 [Disorder status]=Inferred from motif [Kd]=1.20E-06 (PMID:25497731) [Name]=SUMO1 in complex with phosphorylated PML [Source organism]=Homo sapiens [PDB ID]=4wjn [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.50 [Domain]=SUMO [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains two known functional linear motifs (LIG_SUMO_SIM_anti_2, LIG_SUMO_SIM_par_1). [Type chain A]=Ordered [Evidence chain A]=The SUMO domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF11976). A solved monomeric structure of the domain is represented by PDB ID 1a5r. [Modified residues chain B]=phosphoserine#S#15|phosphoserine#S#16|phosphoserine#S#17 [Chain B name]=Protein PML [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P29590 [Chain B UniProt boundaries]=546-574 [Chain B UniProt coverage]=3.3% [Chain B UniRef90 accession]=UniRef90_P29590 [Chain B UniRef90 boundaries]=546-573 [Chain A name]=Small ubiquitin-related modifier 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63165 [Chain A UniProt boundaries]=15-97 [Chain A UniProt coverage]=82.2% [Chain A UniRef90 accession]=UniRef90_P63165 [Chain A UniRef90 boundaries]=17-97 [Entry] [Accession]=DI1100045 [Disorder status]=Inferred from motif [Kd]=1.20E-06 (PMID:25497731) [Name]=Homer EVH1 domain with bound Mglur peptide [Source organism]=Rattus norvegicus [PDB ID]=1ddv [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=WH1 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_EVH1_2). [Type chain A]=Ordered [Evidence chain A]=The WH1 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00568). A solved monomeric structure of the domain is represented by PDB ID 1ddw. [Chain B name]=Metabotropic glutamate receptor 5 [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=P31424 [Chain B UniProt boundaries]=1155-1160 [Chain B UniProt coverage]=0.5% [Chain B UniRef90 accession]=UniRef90_P31424 [Chain B UniRef90 boundaries]=1155-1160 [Chain A name]=Homer protein homolog 1 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=Q9Z214 [Chain A UniProt boundaries]=1-111 [Chain A UniProt coverage]=30.3% [Chain A UniRef90 accession]=UniRef90_Q9Z214 [Chain A UniRef90 boundaries]=1-111 [Entry] [Accession]=DI1100046 [Disorder status]=Inferred from motif [Kd]=3.20E-06 (PMID:14607833) [Name]=RET peptide in complex with the Dok1 phosphotyrosine binding domain [Source organism]=Mus musculus [PDB ID]=1uef [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=IRS-type PTB [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_PTB_Phospho_1). [Type chain A]=Ordered [Evidence chain A]=The IRS-type PTB domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02174). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2dlw. [Modified residues chain C]=phosphotyrosine#Y#9 [Chain C name]=Proto-oncogene tyrosine-protein kinase receptor Ret [Chain C source organism]=Mus musculus [Chain C UniProt accession]=P35546 [Chain C UniProt boundaries]=1055-1067 [Chain C UniProt coverage]=1.2% [Chain C UniRef90 accession]=UniRef90_P35546 [Chain C UniRef90 boundaries]=1055-1067 [Chain A name]=Docking protein 1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P97465 [Chain A UniProt boundaries]=148-274 [Chain A UniProt coverage]=26.3% [Chain A UniRef90 accession]=UniRef90_P97465 [Chain A UniRef90 boundaries]=152-271 [Entry] [Accession]=DI1000173 [Disorder status]=Inferred from motif [Kd]=3.20E-06 (PMID:14607833) [Name]=Osr1 kinase C-terminal domain recognizing a WNK4 kinase peptide [Source organism]=Homo sapiens [PDB ID]=2v3s [PDB chain IDs]=D:A [PDB note]=Chains B and C were removed as chains A and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=OSR1 C-terminal [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a known functional linear motif (DOC_SPAK_OSR1_1). [Type chain A]=Ordered [Evidence chain A]=The OSR1 C-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF12202). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2lru. [Chain D name]=Serine/threonine-protein kinase WNK4 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=Q96J92 [Chain D UniProt boundaries]=1015-1020 [Chain D UniProt coverage]=0.5% [Chain D UniRef90 accession]=UniRef90_Q96J92 [Chain D UniRef90 boundaries]=1015-1020 [Chain A name]=Serine/threonine-protein kinase OSR1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O95747 [Chain A UniProt boundaries]=432-527 [Chain A UniProt coverage]=18.2% [Chain A UniRef90 accession]=UniRef90_O95747 [Chain A UniRef90 boundaries]=433-527 [Entry] [Accession]=DI1000174 [Disorder status]=Inferred from motif [Kd]=5.90E-07 (PMID:27757847) [Name]=Phosphorylated FUNDC1 in complex with LC3BLC3B [Source organism]=Homo sapiens [PDB ID]=5gmv [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.25 [Domain]=Atg8 [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (YxxL motif: http://www.uniprot.org/uniprot/Q8IVP5#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The Atg8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02991). A solved monomeric structure of the domain is represented by PDB ID 1v49. [Modified residues chain C]=phosphoserine#S#17 [Chain C name]=FUN14 domain-containing protein 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q8IVP5 [Chain C UniProt boundaries]=16-23 [Chain C UniProt coverage]=5.2% [Chain C UniRef90 accession]=UniRef90_Q8IVP5 [Chain C UniRef90 boundaries]=16-23 [Chain A name]=Microtubule-associated proteins 1A/1B light chain 3B [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9GZQ8 [Chain A UniProt boundaries]=1-125 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q9GZQ8 [Chain A UniRef90 boundaries]=1-125 [Entry] [Accession]=DI1000175 [Disorder status]=Confirmed [Kd]=5.70E-06 (PMID:20015111) [Name]=VHS domain of human GGA1 complexed with an autoinhibitory DXXLL hinge peptide [Source organism]=Homo sapiens [PDB ID]=3g2w [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=VHS [Type chain C]=Disordered [Evidence chain C]=The interacting autoinhibitory peptide region of GGA1 is unstructured in isolation (PMID:20015111), and contains a known functional linear motif (TRG_LysEnd_GGAAcLL_2). [Type chain A]=Ordered [Evidence chain A]=The VHS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00790). A solved monomeric structure of the domain is represented by PDB ID 1jwf. [Chain C name]=ADP-ribosylation factor-binding protein GGA1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q9UJY5 [Chain C UniProt boundaries]=351-364 [Chain C UniProt coverage]=2.2% [Chain C UniRef90 accession]=UniRef90_Q9UJY5 [Chain C UniRef90 boundaries]=351-364 [Chain A name]=ADP-ribosylation factor-binding protein GGA1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UJY5 [Chain A UniProt boundaries]=1-147 [Chain A UniProt coverage]=23% [Chain A UniRef90 accession]=UniRef90_Q9UJY5 [Chain A UniRef90 boundaries]=1-147 [Entry] [Accession]=DI1000176 [Disorder status]=Confirmed [Kd]=2.20E-06 [Name]=Pyk2-FAT domain in complex with leupaxin LD4 motif [Source organism]=Homo sapiens [PDB ID]=4xek [PDB chain IDs]=C:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.79 [Domain]=Focal adhesion targeting region [Type chain C]=Disordered [Evidence chain C]=The LD motifs of leupaxin reside in an unstructured protein region (PMID:26866573). The interacting segment contains a known functional LD motif (LD motif 3: http://www.uniprot.org/uniprot/O60711#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The Focal adhesion targeting region domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03623). A solved monomeric structure of the domain is represented by PDB ID 2lk4. [Chain C name]=Leupaxin [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=O60711 [Chain C UniProt boundaries]=86-104 [Chain C UniProt coverage]=4.9% [Chain C UniRef90 accession]=UniRef90_O60711 [Chain C UniRef90 boundaries]=86-104 [Chain A name]=Protein-tyrosine kinase 2-beta [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q14289 [Chain A UniProt boundaries]=867-1005 [Chain A UniProt coverage]=13.8% [Chain A UniRef90 accession]=UniRef90_Q14289 [Chain A UniRef90 boundaries]=871-1005 [Related structures]=4xev [Entry] [Accession]=DI1010055 [Disorder status]=Confirmed [Kd]=2.80E-06 [Name]=Pyk2-FAT domain in complex with leupaxin LD1 motif (site 1) [Source organism]=Oryctolagus cuniculus / Homo sapiens [PDB ID]=4xef [PDB chain IDs]=B:A [PDB note]=Chains C, D, E and F were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=Focal adhesion targeting region [Type chain B]=Disordered [Evidence chain B]=The LD motifs of leupaxin reside in an unstructured protein region (PMID:26866573). The interacting segment contains a known functional LD motif (LD motif 1: http://www.uniprot.org/uniprot/O60711#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The Focal adhesion targeting region domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03623). A solved monomeric structure of the domain is represented by PDB ID 2lk4. [Chain B name]=Leupaxin [Chain B source organism]=Oryctolagus cuniculus [Chain B UniProt accession]=Q9N261 [Chain B UniProt boundaries]=1-20 [Chain B UniProt coverage]=5.2% [Chain B UniRef90 accession]=UniRef90_Q9N261 [Chain B UniRef90 boundaries]=1-20 [Chain A name]=Protein-tyrosine kinase 2-beta [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q14289 [Chain A UniProt boundaries]=867-1005 [Chain A UniProt coverage]=13.8% [Chain A UniRef90 accession]=UniRef90_Q14289 [Chain A UniRef90 boundaries]=871-1005 [Entry] [Accession]=DI1010056 [Disorder status]=Confirmed [Kd]=5.20E-05 [Name]=Pyk2-FAT domain in complex with leupaxin LD1 motif (site 2) [Source organism]=Oryctolagus cuniculus / Homo sapiens [PDB ID]=4xef [PDB chain IDs]=C:A [PDB note]=Chains B, D, E and F were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=Focal adhesion targeting region [Type chain C]=Disordered [Evidence chain C]=The LD motifs of leupaxin reside in an unstructured protein region (PMID:26866573). The interacting segment contains a known functional LD motif (LD motif 1: http://www.uniprot.org/uniprot/O60711#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The Focal adhesion targeting region domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03623). A solved monomeric structure of the domain is represented by PDB ID 2lk4. [Chain C name]=Leupaxin [Chain C source organism]=Oryctolagus cuniculus [Chain C UniProt accession]=Q9N261 [Chain C UniProt boundaries]=1-20 [Chain C UniProt coverage]=5.2% [Chain C UniRef90 accession]=UniRef90_Q9N261 [Chain C UniRef90 boundaries]=1-20 [Chain A name]=Protein-tyrosine kinase 2-beta [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q14289 [Chain A UniProt boundaries]=867-1005 [Chain A UniProt coverage]=13.8% [Chain A UniRef90 accession]=UniRef90_Q14289 [Chain A UniRef90 boundaries]=871-1005 [Entry] [Accession]=DI1020018 [Disorder status]=Inferred from motif [Kd]=5.20E-05 [Name]=CFTR Associated Ligand (CAL) PDZ domain bound to HPV18 E6 oncoprotein C-terminal peptide [Source organism]=Human papillomavirus type 18 / Homo sapiens [PDB ID]=4jor [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.34 [Domain]=PDZ [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_1). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 2kpk. [Chain C name]=Protein E6 [Chain C source organism]=Human papillomavirus type 18 [Chain C UniProt accession]=P06463 [Chain C UniProt boundaries]=149-158 [Chain C UniProt coverage]=6.3% [Chain C UniRef90 accession]=UniRef90_P06463 [Chain C UniRef90 boundaries]=149-158 [Chain A name]=Golgi-associated PDZ and coiled-coil motif-containing protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9HD26 [Chain A UniProt boundaries]=284-370 [Chain A UniProt coverage]=18.8% [Chain A UniRef90 accession]=UniRef90_Q9HD26 [Chain A UniRef90 boundaries]=284-370 [Entry] [Accession]=DI1000177 [Disorder status]=Inferred from motif [Kd]=5.60E-05 (PMID:11859375) [Name]=GGA3 VHS domain complexed with C-terminal peptide from cation-dependent Mannose 6-phosphate receptor [Source organism]=Homo sapiens [PDB ID]=1juq [PDB chain IDs]=E:A [PDB note]=Chains B, C, D, F, G and H were removed as chains A and E represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=VHS [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (TRG_LysEnd_GGAAcLL_1). [Type chain A]=Ordered [Evidence chain A]=The VHS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00790). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1jwf. [Chain E name]=Cation-dependent mannose-6-phosphate receptor [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P20645 [Chain E UniProt boundaries]=265-277 [Chain E UniProt coverage]=4.7% [Chain E UniRef90 accession]=UniRef90_P20645 [Chain E UniRef90 boundaries]=265-277 [Chain A name]=ADP-ribosylation factor-binding protein GGA3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9NZ52 [Chain A UniProt boundaries]=1-166 [Chain A UniProt coverage]=23% [Chain A UniRef90 accession]=UniRef90_Q9NZ52 [Chain A UniRef90 boundaries]=1-157 [Entry] [Accession]=DI1010057 [Disorder status]=Confirmed [Kd]=8.00E-07 (PMID:27321669) [Name]=The third PDZ domain from the synaptic protein PSD-95 in complex with a C-terminal peptide derived from CRIPT [Source organism]=Rattus norvegicus / Homo sapiens [PDB ID]=5heb [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.65 [Domain]=PDZ [Type chain B]=Disordered [Evidence chain B]=The interacting region of CRIPT has been shown to be intrinsically disordered (PMID:8674113). The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_1). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 1tq3. [Chain B name]=Cysteine-rich PDZ-binding protein [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=Q792Q4 [Chain B UniProt boundaries]=93-101 [Chain B UniProt coverage]=8.9% [Chain B UniRef90 accession]=UniRef90_O70333 [Chain B UniRef90 boundaries]=93-101 [Chain A name]=Disks large homolog 4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P78352 [Chain A UniProt boundaries]=300-403 [Chain A UniProt coverage]=14.4% [Chain A UniRef90 accession]=UniRef90_P31016 [Chain A UniRef90 boundaries]=300-403 [Related structures]=1be9,5hey,5hfb,5hfe,5hed,5hf1,5hfc,5hff [Entry] [Accession]=DI1010058 [Disorder status]=Inferred from homology [Kd]=3.40E-06 (PMID:26224628) [Name]=Structure of the MLLE domain of EDD in complex with a PAM2 peptide from Paip1 [Source organism]=Homo sapiens / Rattus norvegicus [PDB ID]=3ntw [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=PABP [Type chain B]=Disordered [Evidence chain B]=The corresponding region of a closely homologous protein has been shown to be disordered in the 106-127 region described in IDEAL entry IID00582 (covers 100% of the sequence present in the structure). The protein region involved in the interaction contains a known functional linear motif (LIG_PAM2_1). [Type chain A]=Ordered [Evidence chain A]=The PABP domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00658). A solved monomeric structure of the domain from a closely homologous protein is represented by PDB ID 1i2t. [Chain B name]=Polyadenylate-binding protein-interacting protein 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9H074 [Chain B UniProt boundaries]=123-144 [Chain B UniProt coverage]=4.6% [Chain B UniRef90 accession]=UniRef90_Q9H074 [Chain B UniRef90 boundaries]=123-144 [Chain A name]=E3 ubiquitin-protein ligase UBR5 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=Q62671 [Chain A UniProt boundaries]=2378-2442 [Chain A UniProt coverage]=2.3% [Chain A UniRef90 accession]=UniRef90_O95071 [Chain A UniRef90 boundaries]=2389-2452 [Entry] [Accession]=DI1410001 [Disorder status]=Confirmed [Kd]=5.00E-09 (PMID:7680960) [Name]=High affinity phosphotyrosyl peptide from Middle T antigen of Hamster polyomavirus bound to the Src SH2 domain [Source organism]=Hamster polyomavirus / Avian leukosis virus RSA [PDB ID]=1sps [PDB chain IDs]=D:A [PDB note]=Chains B, C, E and F were removed as chains A and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.70 [Domain]=SH2 [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a known functional linear motif (LIG_SH2_SRC). The motif is embedded in an unstructured protein region (PMID:7680960). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ab2. [Modified residues chain D]=phosphotyrosine#Y#0 [Chain D name]=Middle T antigen [Chain D source organism]=Hamster polyomavirus [Chain D UniProt accession]=P03079 [Chain D UniProt boundaries]=321-331 [Chain D UniProt coverage]=2.7% [Chain D UniRef90 accession]=UniRef90_P03079 [Chain D UniRef90 boundaries]=321-331 [Chain A name]=Tyrosine-protein kinase transforming protein Src [Chain A source organism]=Avian leukosis virus RSA [Chain A UniProt accession]=P00524 [Chain A UniProt boundaries]=144-247 [Chain A UniProt coverage]=19.8% [Chain A UniRef90 accession]=UniRef90_P00524 [Chain A UniRef90 boundaries]=144-247 [Entry] [Accession]=DI1120009 [Disorder status]=Inferred from motif [Kd]=5.00E-09 (PMID:7680960) [Name]=Sap97 PDZ3 bound to the C-terminal peptide of HPV18 E6 [Source organism]=Human papillomavirus type 18 / Rattus norvegicus [PDB ID]=2i0i [PDB chain IDs]=D:A [PDB note]=Chains B, C, E and F were removed as chains A and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=PDZ [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_1). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1tq3. [Chain D name]=Protein E6 [Chain D source organism]=Human papillomavirus type 18 [Chain D UniProt accession]=P06463 [Chain D UniProt boundaries]=152-158 [Chain D UniProt coverage]=4.4% [Chain D UniRef90 accession]=UniRef90_P06463 [Chain D UniRef90 boundaries]=152-158 [Chain A name]=Disks large homolog 1 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=Q62696 [Chain A UniProt boundaries]=459-543 [Chain A UniProt coverage]=9.3% [Chain A UniRef90 accession]=UniRef90_Q12959 [Chain A UniRef90 boundaries]=460-544 [Entry] [Accession]=DI1000178 [Disorder status]=Inferred from motif [Kd]=1.90E-05 (PMID:23395182) [Name]=T-cell Lymphoma Invasion and Metastasis-1 PDZ in complex with phosphorylated Syndecan1 peptide [Source organism]=Homo sapiens [PDB ID]=4gvc [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.54 [Domain]=PDZ [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_2). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 3kzd. [Modified residues chain B]=phosphotyrosine#Y#7 [Chain B name]=Syndecan-1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P18827 [Chain B UniProt boundaries]=303-310 [Chain B UniProt coverage]=2.6% [Chain B UniRef90 accession]=UniRef90_P18827 [Chain B UniRef90 boundaries]=303-310 [Chain A name]=T-lymphoma invasion and metastasis-inducing protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q13009 [Chain A UniProt boundaries]=837-930 [Chain A UniProt coverage]=5.9% [Chain A UniRef90 accession]=UniRef90_Q13009 [Chain A UniRef90 boundaries]=841-928 [Entry] [Accession]=DI1000179 [Disorder status]=Inferred from motif [Kd]=1.23E-05 [Name]=CAP-Gly domain-containing linker protein 1 in complex with SLAIN motif-containing protein 2 [Source organism]=Homo sapiens [PDB ID]=3rdv [PDB chain IDs]=E:A [PDB note]=Chains B, C, D, F, G and H were removed as chains A and E represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.75 [Domain]=CAP-Gly domain [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (LIG_CAP-Gly_2). [Type chain A]=Ordered [Evidence chain A]=The CAP-Gly domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01302). A solved monomeric structure of the domain is represented by PDB ID 2e3h. [Chain E name]=SLAIN motif-containing protein 2 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=Q9P270 [Chain E UniProt boundaries]=574-581 [Chain E UniProt coverage]=1.4% [Chain E UniRef90 accession]=UniRef90_Q9P270 [Chain E UniRef90 boundaries]=574-581 [Chain A name]=CAP-Gly domain-containing linker protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P30622 [Chain A UniProt boundaries]=56-127 [Chain A UniProt coverage]=5% [Chain A UniRef90 accession]=UniRef90_P30622 [Chain A UniRef90 boundaries]=56-127 [Entry] [Accession]=DI1000180 [Disorder status]=Inferred from motif [Kd]=1.23E-05 [Name]=PLEKHM1 LIR in complex with human LC3C [Source organism]=Homo sapiens [PDB ID]=5dpw [PDB chain IDs]=B:A [PDB note]=Chains C, D, E, F, G, H, I, J, K, L, M, N, O and P were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.19 [Domain]=Atg8 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIR motif: http://www.uniprot.org/uniprot/Q9Y4G2#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The Atg8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02991). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1gnu. [Chain B name]=Pleckstrin homology domain-containing family M member 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9Y4G2 [Chain B UniProt boundaries]=629-642 [Chain B UniProt coverage]=1.3% [Chain B UniRef90 accession]=UniRef90_Q9Y4G2 [Chain B UniRef90 boundaries]=629-642 [Chain A name]=Microtubule-associated proteins 1A/1B light chain 3C [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9BXW4 [Chain A UniProt boundaries]=8-125 [Chain A UniProt coverage]=80.3% [Chain A UniRef90 accession]=UniRef90_Q9BXW4 [Chain A UniRef90 boundaries]=8-125 [Entry] [Accession]=DI1100047 [Disorder status]=Confirmed [Kd]=4.40E-05 (PMID:12453410) [Name]=Pex13p SH3 domain in complex with a peptide of Pex14p [Source organism]=Saccharomyces cerevisiae [PDB ID]=1n5z [PDB chain IDs]=P:A [PDB note]=Chains B and Q were removed as chains A and P represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.70 [Domain]=SH3 [Type chain P]=Disordered [Evidence chain P]=The protein region involved in the interaction contains a known functional linear motif (LIG_SH2_SRC) and is unstructured in its unbound form (PMID:12453410). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00018). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2a36. [Chain P name]=Peroxisomal membrane protein PEX14 [Chain P source organism]=Saccharomyces cerevisiae [Chain P UniProt accession]=P53112 [Chain P UniProt boundaries]=83-96 [Chain P UniProt coverage]=4.1% [Chain P UniRef90 accession]=UniRef90_P53112 [Chain P UniRef90 boundaries]=83-96 [Chain A name]=Peroxisomal membrane protein PAS20 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P80667 [Chain A UniProt boundaries]=295-386 [Chain A UniProt coverage]=23.8% [Chain A UniRef90 accession]=UniRef90_P80667 [Chain A UniRef90 boundaries]=299-386 [Related structures]=2v1r [Entry] [Accession]=DI1100048 [Disorder status]=Inferred from motif [Kd]=4.40E-05 (PMID:12453410) [Name]=PDZ domain of sorting nexin 27 (SNX27) in complex with the C-terminal tail of GIRK3 [Source organism]=Rattus norvegicus [PDB ID]=3qgl [PDB chain IDs]=F:A [PDB note]=Chains B, C, D, E, G, H, I and J were removed as chains A and F represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.31 [Domain]=PDZ [Type chain F]=Disordered [Evidence chain F]=The protein region involved in the interaction contains a known functional linear motif (PDZ-binding: http://www.uniprot.org/uniprot/Q63511#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2kpk. [Chain F name]=G protein-activated inward rectifier potassium channel 3 [Chain F source organism]=Rattus norvegicus [Chain F UniProt accession]=Q63511 [Chain F UniProt boundaries]=388-393 [Chain F UniProt coverage]=1.5% [Chain F UniRef90 accession]=UniRef90_Q63511 [Chain F UniRef90 boundaries]=388-393 [Chain A name]=Sorting nexin-27 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=Q8K4V4 [Chain A UniProt boundaries]=33-133 [Chain A UniProt coverage]=18.7% [Chain A UniRef90 accession]=UniRef90_Q96L92 [Chain A UniRef90 boundaries]=41-135 [Entry] [Accession]=DI1000181 [Disorder status]=Inferred from motif [Kd]=6.50E-07 (PMID:10549287) [Name]=XLP protein SAP SH2 domain in complex with an unmodified SLAM peptide [Source organism]=Homo sapiens [PDB ID]=1d4t [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.10 [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_TYR_ITSM). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ab2. [Chain B name]=Signaling lymphocytic activation molecule [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q13291 [Chain B UniProt boundaries]=276-286 [Chain B UniProt coverage]=3.3% [Chain B UniRef90 accession]=UniRef90_Q13291 [Chain B UniRef90 boundaries]=276-286 [Chain A name]=SH2 domain-containing protein 1A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O60880 [Chain A UniProt boundaries]=1-104 [Chain A UniProt coverage]=81.3% [Chain A UniRef90 accession]=UniRef90_O60880 [Chain A UniRef90 boundaries]=1-104 [Related structures]=1ka7,1m27 [Entry] [Accession]=DI1000182 [Disorder status]=Inferred from motif [Kd]=5.40E-06 (PMID:20015111) [Name]=VHS Domain of human GGA1 complexed with unmodified sortilin C-terminal peptide [Source organism]=Homo sapiens [PDB ID]=3g2u [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=VHS [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (TRG_LysEnd_GGAAcLL_1). [Type chain A]=Ordered [Evidence chain A]=The VHS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00790). A solved monomeric structure of the domain is represented by PDB ID 1jwf. [Chain C name]=Sortilin [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q99523 [Chain C UniProt boundaries]=819-831 [Chain C UniProt coverage]=1.6% [Chain C UniRef90 accession]=UniRef90_Q99523 [Chain C UniRef90 boundaries]=819-831 [Chain A name]=ADP-ribosylation factor-binding protein GGA1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UJY5 [Chain A UniProt boundaries]=1-147 [Chain A UniProt coverage]=23% [Chain A UniRef90 accession]=UniRef90_Q9UJY5 [Chain A UniRef90 boundaries]=1-147 [Entry] [Accession]=DI1000183 [Disorder status]=Inferred from motif [Kd]=4.00E-05 (PMID:14567678) [Name]=VHS Domain of human GGA1 complexed with beta-secretase C-terminal phosphopeptide [Source organism]=Homo sapiens [PDB ID]=1py1 [PDB chain IDs]=E:A [PDB note]=Chains B, C, D, F, G and H were removed as chains A and E represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=VHS [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (TRG_LysEnd_APsAcLL_1). [Type chain A]=Ordered [Evidence chain A]=The VHS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00790). A solved monomeric structure of the domain is represented by PDB ID 1jwf. [Modified residues chain E]=phosphoserine#S#5 [Chain E name]=Beta-secretase 1 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P56817 [Chain E UniProt boundaries]=494-501 [Chain E UniProt coverage]=1.6% [Chain E UniRef90 accession]=UniRef90_P56817 [Chain E UniRef90 boundaries]=494-501 [Chain A name]=ADP-ribosylation factor-binding protein GGA1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UJY5 [Chain A UniProt boundaries]=1-157 [Chain A UniProt coverage]=24.6% [Chain A UniRef90 accession]=UniRef90_Q9UJY5 [Chain A UniRef90 boundaries]=2-157 [Related structures]=1ujk [Entry] [Accession]=DI1010059 [Disorder status]=Inferred from motif [Kd]=1.50E-08 (PMID:21060336) [Name]=Bcl-2 in complex with the Bh3 Domain of Bax [Source organism]=Mus musculus / Homo sapiens [PDB ID]=2xa0 [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.70 [Domain]=Bcl-2 homology [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_BH_BH3_1). [Type chain A]=Ordered [Evidence chain A]=Bcl-2 homology (BH) domains, such as the one involved in the interaction, are known to adopt a stable structure in isolation (see Pfam domain PF00452). A solved monomeric structure of the domain is represented by PDB ID 4lxd. [Chain C name]=Apoptosis regulator BAX [Chain C source organism]=Mus musculus [Chain C UniProt accession]=Q07813 [Chain C UniProt boundaries]=52-82 [Chain C UniProt coverage]=16.1% [Chain C UniRef90 accession]=UniRef90_Q07813 [Chain C UniRef90 boundaries]=52-82 [Chain A name]=Apoptosis regulator Bcl-2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P10415 [Chain A UniProt boundaries]=1-207 [Chain A UniProt coverage]=86.6% [Chain A UniRef90 accession]=UniRef90_P10417 [Chain A UniRef90 boundaries]=1-204 [Entry] [Accession]=DI1000184 [Disorder status]=Inferred from motif [Kd]=5.10E-07 (PMID:25657007) [Name]=IST1 MIM peptide bound to Spartin MIT domain [Source organism]=Homo sapiens [PDB ID]=4u7i [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.79 [Domain]=MIT [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (MIT-interacting motif - http://www.uniprot.org/uniprot/P53990#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The MIT domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04212). A solved monomeric structure of the domain is represented by PDB ID 2dl1. [Chain B name]=IST1 homolog [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P53990 [Chain B UniProt boundaries]=341-364 [Chain B UniProt coverage]=6.6% [Chain B UniRef90 accession]=UniRef90_P53990 [Chain B UniRef90 boundaries]=341-364 [Chain A name]=Spartin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q8N0X7 [Chain A UniProt boundaries]=7-101 [Chain A UniProt coverage]=14.3% [Chain A UniRef90 accession]=UniRef90_Q8N0X7 [Chain A UniRef90 boundaries]=7-101 [Entry] [Accession]=DI1100049 [Disorder status]=Inferred from motif [Kd]=5.10E-07 (PMID:25657007) [Name]=Protein swallow peptide bound to dynein light chain 1 [Source organism]=Drosophila melanogaster [PDB ID]=3brl [PDB chain IDs]=C:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=Dynein light chain [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_Dynein_DLC8_1). [Type chain A]=Ordered [Evidence chain A]=The dynein light chain domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01221). A solved monomeric structure of the domain is represented by PDB ID 1rhw. [Chain C name]=Protein swallow [Chain C source organism]=Drosophila melanogaster [Chain C UniProt accession]=P40688 [Chain C UniProt boundaries]=287-296 [Chain C UniProt coverage]=1.8% [Chain C UniRef90 accession]=UniRef90_P40688 [Chain C UniRef90 boundaries]=287-296 [Chain A name]=Dynein light chain 1, cytoplasmic [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=Q24117 [Chain A UniProt boundaries]=1-89 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q24117 [Chain A UniRef90 boundaries]=1-89 [Related structures]=3e2b [Entry] [Accession]=DI1000185 [Disorder status]=Inferred from motif [Kd]=1.00E-05 (PMID:20839809) [Name]=Second PDZ domain from human PTP1E in complex with RA-GEF2 peptide [Source organism]=Homo sapiens [PDB ID]=3lny [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.30 [Domain]=PDZ [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_1). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 1q7x. [Chain B name]=Rap guanine nucleotide exchange factor 6 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q8TEU7 [Chain B UniProt boundaries]=1596-1601 [Chain B UniProt coverage]=0.4% [Chain B UniRef90 accession]=UniRef90_Q8TEU7 [Chain B UniRef90 boundaries]=1596-1601 [Chain A name]=Tyrosine-protein phosphatase non-receptor type 13 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q12923 [Chain A UniProt boundaries]=1361-1456 [Chain A UniProt coverage]=3.9% [Chain A UniRef90 accession]=UniRef90_Q12923 [Chain A UniRef90 boundaries]=1361-1456 [Entry] [Accession]=DI1100050 [Disorder status]=Inferred from motif [Kd]=1.00E-05 (PMID:20839809) [Name]=Rat VAP-A MSP homology domain in complex with the rat ORP1 FFAT motif [Source organism]=Rattus norvegicus [PDB ID]=1z9o [PDB chain IDs]=J:D [PDB note]=Chains A, B, C, E, F, G, H, I, K and L were removed as chains D and J represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=MSP [Type chain J]=Disordered [Evidence chain J]=The protein region involved in the interaction contains a known functional linear motif (TRG_ER_FFAT_1). [Type chain D]=Ordered [Evidence chain D]=The MSP domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00635). A solved monomeric structure of the domain is represented by PDB ID 1z9l. [Chain J name]=Oxysterol-binding protein-related protein 1 [Chain J source organism]=Rattus norvegicus [Chain J UniProt accession]=Q8K4M9 [Chain J UniProt boundaries]=472-481 [Chain J UniProt coverage]=1.1% [Chain J UniRef90 accession]=UniRef90_Q9BXW6 [Chain J UniRef90 boundaries]=472-481 [Chain D name]=Vesicle-associated membrane protein-associated protein A [Chain D source organism]=Rattus norvegicus [Chain D UniProt accession]=Q9Z270 [Chain D UniProt boundaries]=8-132 [Chain D UniProt coverage]=50.2% [Chain D UniRef90 accession]=UniRef90_Q9WV55 [Chain D UniRef90 boundaries]=8-132 [Entry] [Accession]=DI1000186 [Disorder status]=Inferred from motif [Kd]=6.21E-05 (PMID:22921829) [Name]=YAP WW2 domain in complex with a Smad7 derived peptide [Source organism]=Homo sapiens [PDB ID]=2ltv [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=WW [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (PY-motif, PMID:22921829, http://www.uniprot.org/uniprot/O15105#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1yiu. [Chain B name]=Mothers against decapentaplegic homolog 7 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O15105 [Chain B UniProt boundaries]=206-217 [Chain B UniProt coverage]=2.8% [Chain B UniRef90 accession]=UniRef90_O15105 [Chain B UniRef90 boundaries]=206-217 [Chain A name]=Transcriptional coactivator YAP1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P46937 [Chain A UniProt boundaries]=230-265 [Chain A UniProt coverage]=7.1% [Chain A UniRef90 accession]=UniRef90_P46937 [Chain A UniRef90 boundaries]=230-265 [Entry] [Accession]=DI1000187 [Disorder status]=Inferred from motif [Kd]=6.90E-06 (PMID:22921829) [Name]=YAP WW1 domain in complex with a Smad7 derived peptide [Source organism]=Homo sapiens [PDB ID]=2ltw [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=WW [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (PY-motif, PMID:22921829, http://www.uniprot.org/uniprot/O15105#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1yiu. [Chain B name]=Mothers against decapentaplegic homolog 7 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O15105 [Chain B UniProt boundaries]=204-217 [Chain B UniProt coverage]=3.3% [Chain B UniRef90 accession]=UniRef90_O15105 [Chain B UniRef90 boundaries]=205-217 [Chain A name]=Transcriptional coactivator YAP1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P46937 [Chain A UniProt boundaries]=170-205 [Chain A UniProt coverage]=7.1% [Chain A UniRef90 accession]=UniRef90_P46937 [Chain A UniRef90 boundaries]=170-205 [Entry] [Accession]=DI1000188 [Disorder status]=Inferred from motif [Kd]=6.00E-06 (PMID:22921829) [Name]=SMURF1 WW2 domain in complex with a Smad7 derived peptide [Source organism]=Homo sapiens [PDB ID]=2ltx [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=WW [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (PY-motif, PMID:22921829, http://www.uniprot.org/uniprot/O15105#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1yiu. [Chain B name]=Mothers against decapentaplegic homolog 7 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O15105 [Chain B UniProt boundaries]=203-217 [Chain B UniProt coverage]=3.5% [Chain B UniRef90 accession]=UniRef90_O15105 [Chain B UniRef90 boundaries]=203-217 [Chain A name]=E3 ubiquitin-protein ligase SMURF1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9HCE7 [Chain A UniProt boundaries]=306-340 [Chain A UniProt coverage]=4.6% [Chain A UniRef90 accession]=UniRef90_Q9HCE7 [Chain A UniRef90 boundaries]=306-340 [Entry] [Accession]=DI1000189 [Disorder status]=Inferred from motif [Kd]=4.20E-06 (PMID:22921829) [Name]=NEDD4L WW2 domain in complex with a Smad7 derived peptide [Source organism]=Homo sapiens [PDB ID]=2lty [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=WW [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (PY-motif, PMID:22921829, http://www.uniprot.org/uniprot/O15105#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1yiu. [Chain B name]=Mothers against decapentaplegic homolog 7 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O15105 [Chain B UniProt boundaries]=203-217 [Chain B UniProt coverage]=3.5% [Chain B UniRef90 accession]=UniRef90_O15105 [Chain B UniRef90 boundaries]=203-217 [Chain A name]=E3 ubiquitin-protein ligase NEDD4-like [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96PU5 [Chain A UniProt boundaries]=385-418 [Chain A UniProt coverage]=3.5% [Chain A UniRef90 accession]=UniRef90_Q96PU5 [Chain A UniRef90 boundaries]=385-417 [Entry] [Accession]=DI1000190 [Disorder status]=Inferred from motif [Kd]=3.40E-06 (PMID:22921829) [Name]=SMURF2 WW3 domain in complex with a Smad7 derived peptide [Source organism]=Homo sapiens [PDB ID]=2ltz [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=WW [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (PY-motif, PMID:22921829, http://www.uniprot.org/uniprot/O15105#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1yiu. [Chain B name]=Mothers against decapentaplegic homolog 7 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O15105 [Chain B UniProt boundaries]=203-217 [Chain B UniProt coverage]=3.5% [Chain B UniRef90 accession]=UniRef90_O15105 [Chain B UniRef90 boundaries]=203-217 [Chain A name]=E3 ubiquitin-protein ligase SMURF2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9HAU4 [Chain A UniProt boundaries]=297-333 [Chain A UniProt coverage]=4.9% [Chain A UniRef90 accession]=UniRef90_Q9HAU4 [Chain A UniRef90 boundaries]=297-333 [Related structures]=2djy,2kxq [Entry] [Accession]=DI1000191 [Disorder status]=Confirmed [Kd]=9.00E-06 (PMID:19197237) [Name]=Pex14 in complex with Pex19 [Source organism]=Homo sapiens [PDB ID]=2w85 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Pex14 (N-terminal) [Type chain B]=Disordered [Evidence chain B]=It is known that the N-terminal half (region of interest) of Pex19 is structurally disordered (PMID:15252024, PMID:25062251). The protein region involved in the interaction contains a known functional linear motif (LIG_Pex14_2). [Type chain A]=Ordered [Evidence chain A]=The N-terminal domain of Pex14 (see Pfam domain PF04695) has been shown by NMR to be ordered in its monomeric form (PMID:19197237). [Chain B name]=Peroxisomal biogenesis factor 19 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P40855 [Chain B UniProt boundaries]=66-77 [Chain B UniProt coverage]=4% [Chain B UniRef90 accession]=UniRef90_P40855 [Chain B UniRef90 boundaries]=66-77 [Chain A name]=Peroxisomal membrane protein PEX14 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O75381 [Chain A UniProt boundaries]=12-81 [Chain A UniProt coverage]=18.6% [Chain A UniRef90 accession]=UniRef90_O75381 [Chain A UniRef90 boundaries]=15-80 [Entry] [Accession]=DI1010060 [Disorder status]=Confirmed [Kd]=4.00E-05 [Name]=MDC1 FHA domain complexed with CHK2 pThr68 peptide [Source organism]=Homo sapiens / Mus musculus [PDB ID]=3va4 [PDB chain IDs]=C:B [PDB note]=Chain A was removed as chains B and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.54 [Domain]=FHA [Type chain C]=Disordered [Evidence chain C]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 1gxc, 3i6w). The protein region involved in the interaction contains a known functional linear motif (LIG_FHA_1) and a known modification site (MOD_PIKK_1). [Type chain B]=Ordered [Evidence chain B]=The FHA domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00498). A solved monomeric structure of the domain is represented by PDB ID 3va1. [Modified residues chain C]=phosphothreonine#T#1 [Chain C name]=Serine/threonine-protein kinase Chk2 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=O96017 [Chain C UniProt boundaries]=63-73 [Chain C UniProt coverage]=2% [Chain C UniRef90 accession]=UniRef90_O96017 [Chain C UniRef90 boundaries]=63-73 [Chain B name]=Mediator of DNA damage checkpoint protein 1 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q5PSV9 [Chain B UniProt boundaries]=25-139 [Chain B UniProt coverage]=6.7% [Chain B UniRef90 accession]=UniRef90_Q5PSV9 [Chain B UniRef90 boundaries]=25-139 [Entry] [Accession]=DI1020019 [Disorder status]=Inferred from motif [Kd]=4.00E-05 [Name]=Human NEDD4 3RD WW domain in complex with human T-cell leukemia virus 1 GAG-Pro poliprotein derived peptide [Source organism]=Human T-cell leukemia virus 1 / Homo sapiens [PDB ID]=2kpz [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=WW [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (PPXY motif: http://www.uniprot.org/uniprot/P0C210#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain is represented by PDB ID 5aht. [Chain B name]=Gag-Pro polyprotein [Chain B source organism]=Human T-cell leukemia virus 1 [Chain B UniProt accession]=P0C210 [Chain B UniProt boundaries]=113-124 [Chain B UniProt coverage]=1.8% [Chain B UniRef90 accession]=UniRef90_P10274 [Chain B UniRef90 boundaries]=113-124 [Chain A name]=E3 ubiquitin-protein ligase NEDD4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P46934 [Chain A UniProt boundaries]=830-878 [Chain A UniProt coverage]=3.7% [Chain A UniRef90 accession]=UniRef90_P46934 [Chain A UniRef90 boundaries]=834-878 [Entry] [Accession]=DI1000192 [Disorder status]=Inferred from motif [Kd]=3.30E-06 (PMID:24379409) [Name]=Complex of the 3rd WW domain of human Nedd4 and 1st PPXY Motif of ARRDC3 [Source organism]=Homo sapiens [PDB ID]=4n7h [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=WW [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (PPXY motif, PMID:24379409, http://www.uniprot.org/uniprot/Q96B67#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain is represented by PDB ID 5aht. [Chain B name]=Arrestin domain-containing protein 3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q96B67 [Chain B UniProt boundaries]=342-354 [Chain B UniProt coverage]=3.1% [Chain B UniRef90 accession]=UniRef90_Q96B67 [Chain B UniRef90 boundaries]=342-354 [Chain A name]=E3 ubiquitin-protein ligase NEDD4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P46934 [Chain A UniProt boundaries]=840-872 [Chain A UniProt coverage]=2.5% [Chain A UniRef90 accession]=UniRef90_P46934 [Chain A UniRef90 boundaries]=840-872 [Entry] [Accession]=DI1000193 [Disorder status]=Inferred from motif [Kd]=4.60E-06 (PMID:11802777) [Name]=Complex of the 3rd WW domain of human Nedd4 and alpha ENaC PY peptide [Source organism]=Homo sapiens [PDB ID]=2m3o [PDB chain IDs]=P:W [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=WW [Type chain P]=Disordered [Evidence chain P]=The protein region involved in the interaction contains a known functional linear motif (LIG_WW_1). [Type chain W]=Ordered [Evidence chain W]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain is represented by PDB ID 5aht. [Chain P name]=Amiloride-sensitive sodium channel subunit alpha [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=P37088 [Chain P UniProt boundaries]=638-648 [Chain P UniProt coverage]=1.6% [Chain P UniRef90 accession]=UniRef90_P37088 [Chain P UniRef90 boundaries]=638-648 [Chain W name]=E3 ubiquitin-protein ligase NEDD4 [Chain W source organism]=Homo sapiens [Chain W UniProt accession]=P46934 [Chain W UniProt boundaries]=835-877 [Chain W UniProt coverage]=3.3% [Chain W UniRef90 accession]=UniRef90_P46934 [Chain W UniRef90 boundaries]=837-877 [Entry] [Accession]=DI1020020 [Disorder status]=Inferred from motif [Kd]=4.60E-06 (PMID:11802777) [Name]=Complex of the 3rd WW domain of human Nedd4 and ebola Zaire virus matrix protein VP40 derived peptide [Source organism]=Zaire ebolavirus / Homo sapiens [PDB ID]=2kq0 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=WW [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains two known functional linear motifs (LIG_PTAP_UEV_1 and LIG_WW_1). [Type chain A]=Ordered [Evidence chain A]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain is represented by PDB ID 5aht. [Chain B name]=Matrix protein VP40 [Chain B source organism]=Zaire ebolavirus [Chain B UniProt accession]=Q05128 [Chain B UniProt boundaries]=5-16 [Chain B UniProt coverage]=3.7% [Chain B UniRef90 accession]=UniRef90_Q2PDK5 [Chain B UniRef90 boundaries]=5-16 [Chain A name]=E3 ubiquitin-protein ligase NEDD4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P46934 [Chain A UniProt boundaries]=830-878 [Chain A UniProt coverage]=3.7% [Chain A UniRef90 accession]=UniRef90_P46934 [Chain A UniRef90 boundaries]=834-878 [Entry] [Accession]=DI2000012 [Disorder status]=Confirmed [Kd]=4.00E-08 [Name]=RSK1 bound to S100B dimer (site 1) [Source organism]=Homo sapiens [PDB ID]=5csf [PDB chain IDs]=C:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=S100B [Type chain C]=Disordered [Evidence chain C]=The interacting region of RSK1 has been shown to be unstructured in isolation (PMID:26527685). [Type chain A]=Ordered component [Evidence chain A]=S100B is known to adopt a stable structure in isolation in dimeric form. A solved structure of the domain dimer without bound ligands is represented by PDB ID 1qlk. [Type chain B]=Ordered component [Evidence chain B]=S100B is known to adopt a stable structure in isolation in dimeric form. A solved structure of the domain dimer without bound ligands is represented by PDB ID 1qlk. [Chain C name]=Ribosomal protein S6 kinase alpha-1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q15418 [Chain C UniProt boundaries]=681-735 [Chain C UniProt coverage]=7.5% [Chain C UniRef90 accession]=UniRef90_Q15418 [Chain C UniRef90 boundaries]=683-735 [Chain A name]=Protein S100-B [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P04271 [Chain A UniProt boundaries]=1-92 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P04271 [Chain A UniRef90 boundaries]=1-92 [Chain B name]=Protein S100-B [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04271 [Chain B UniProt boundaries]=1-92 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P04271 [Chain B UniRef90 boundaries]=1-92 [Related structures]=5csi,5csj [Entry] [Accession]=DI2000013 [Disorder status]=Confirmed [Kd]=9.60E-06 [Name]=RSK1 bound to S100B dimer (site 2) [Source organism]=Homo sapiens [PDB ID]=5csn [PDB chain IDs]=C:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.95 [Domain]=S100B [Type chain C]=Disordered [Evidence chain C]=The interacting region of RSK1 has been shown to be unstructured in isolation (PMID:26527685). [Type chain A]=Ordered component [Evidence chain A]=S100B is known to adopt a stable structure in isolation in dimeric form. A solved structure of the domain dimer without bound ligands is represented by PDB ID 1qlk. [Type chain B]=Ordered component [Evidence chain B]=S100B is known to adopt a stable structure in isolation in dimeric form. A solved structure of the domain dimer without bound ligands is represented by PDB ID 1qlk. [Chain C name]=Ribosomal protein S6 kinase alpha-1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q15418 [Chain C UniProt boundaries]=681-720 [Chain C UniProt coverage]=5.4% [Chain C UniRef90 accession]=UniRef90_Q15418 [Chain C UniRef90 boundaries]=683-720 [Chain A name]=Protein S100-B [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P04271 [Chain A UniProt boundaries]=1-92 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P04271 [Chain A UniRef90 boundaries]=1-92 [Chain B name]=Protein S100-B [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04271 [Chain B UniProt boundaries]=1-92 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P04271 [Chain B UniRef90 boundaries]=1-92 [Entry] [Accession]=DI1000194 [Disorder status]=Confirmed [Kd]=2.00E-07 (PMID:25730857) [Name]=Human ERK2 complexed with a MAPK docking peptide [Source organism]=Homo sapiens [PDB ID]=4h3p [PDB chain IDs]=B:A [PDB note]=Chains D and E were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=Protein kinase [Type chain B]=Disordered [Evidence chain B]=The interacting region of RSK1 has been shown to be unstructured in isolation (PMID:26527685). The protein region involved in the interaction contains a known functional linear motif (DOC_MAPK_RevD_3). [Type chain A]=Ordered [Evidence chain A]=The protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 1tvo. [Chain B name]=Ribosomal protein S6 kinase alpha-1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q15418 [Chain B UniProt boundaries]=712-735 [Chain B UniProt coverage]=3.3% [Chain B UniRef90 accession]=UniRef90_Q15418 [Chain B UniRef90 boundaries]=712-735 [Chain A name]=Mitogen-activated protein kinase 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P28482 [Chain A UniProt boundaries]=1-360 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P28482 [Chain A UniRef90 boundaries]=1-360 [Related structures]=3tei,4nif [Entry] [Accession]=DI1000195 [Disorder status]=Confirmed [Kd]=9.20E-09 (PMID:18616292) [Name]=Ring1B C-terminal domain/Cbx7 Cbox Complex [Source organism]=Homo sapiens [PDB ID]=3gs2 [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=RAWUL [Type chain B]=Disordered [Evidence chain B]=The interacting Cbox region has been shown to be unstructured in isolation (PMID:15386022). [Type chain A]=Ordered [Evidence chain A]=The RAWUL domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF16207). A solved monomeric structure of the domain represented by PDB ID 3h8h. [Chain B name]=Chromobox protein homolog 7 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O95931 [Chain B UniProt boundaries]=219-248 [Chain B UniProt coverage]=12% [Chain B UniRef90 accession]=UniRef90_O95931 [Chain B UniRef90 boundaries]=219-248 [Chain A name]=E3 ubiquitin-protein ligase RING2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q99496 [Chain A UniProt boundaries]=223-333 [Chain A UniProt coverage]=33% [Chain A UniRef90 accession]=UniRef90_Q99496 [Chain A UniRef90 boundaries]=223-333 [Entry] [Accession]=DI1000196 [Disorder status]=Inferred from motif [Kd]=2.30E-04 [Name]=PIN1 WW domain complexed with human Tau phosphothreonine peptide [Source organism]=Homo sapiens [PDB ID]=1i8h [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=WW [Type chain A]=Disordered [Evidence chain A]=The protein region involved in the interaction contains a known functional linear motif (LIG_SH3_1). [Type chain B]=Ordered [Evidence chain B]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain is represented by PDB ID 1yiu. [Modified residues chain A]=phosphothreonine#T#7 [Chain A name]=Microtubule-associated protein tau [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P10636 [Chain A UniProt boundaries]=542-554 [Chain A UniProt coverage]=1.7% [Chain A UniRef90 accession]=UniRef90_P10636 [Chain A UniRef90 boundaries]=542-554 [Chain B name]=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q13526 [Chain B UniProt boundaries]=6-44 [Chain B UniProt coverage]=23.9% [Chain B UniRef90 accession]=UniRef90_Q13526 [Chain B UniRef90 boundaries]=6-44 [Entry] [Accession]=DI1000197 [Disorder status]=Inferred from motif [Kd]=8.00E-07 [Name]=Ncoa-1/Src-1 Pas-B domain bound to the LxxLL motif of the Stat6 transactivation domain [Source organism]=Homo sapiens [PDB ID]=1oj5 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.2 [Domain]=PAS [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LxxLL motif, PMID:14757047, http://www.uniprot.org/uniprot/P42226#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The PAS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF14598). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1x0o. [Modified residues chain A]=phosphothreonine#T#7 [Chain B name]=Signal transducer and activator of transcription 6 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P42226 [Chain B UniProt boundaries]=795-808 [Chain B UniProt coverage]=1.7% [Chain B UniRef90 accession]=UniRef90_P42226 [Chain B UniRef90 boundaries]=795-808 [Chain A name]=Nuclear receptor coactivator 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q15788 [Chain A UniProt boundaries]=256-385 [Chain A UniProt coverage]=9% [Chain A UniRef90 accession]=UniRef90_Q15788 [Chain A UniRef90 boundaries]=256-385 [Entry] [Accession]=DI1020021 [Disorder status]=Inferred from motif [Kd]=8.00E-07 [Name]=BCL-2 homologous antagonist peptide in complex with M11L [Source organism]=Homo sapiens / Myxoma virus [PDB ID]=2jby [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.41 [Domain]=M11L [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_BH_BH3_1). [Type chain A]=Ordered [Evidence chain A]=The M11L (Apoptosis regulator M11L like) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF11099). A solved structure of the domain without bound ligands is represented by PDB ID 2jbx. [Modified residues chain A]=phosphothreonine#T#7 [Chain B name]=Bcl-2 homologous antagonist/killer [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q16611 [Chain B UniProt boundaries]=67-92 [Chain B UniProt coverage]=12.3% [Chain B UniRef90 accession]=UniRef90_Q16611 [Chain B UniRef90 boundaries]=67-92 [Chain A name]=Apoptosis regulator M11L [Chain A source organism]=Myxoma virus [Chain A UniProt accession]=Q85295 [Chain A UniProt boundaries]=1-132 [Chain A UniProt coverage]=79.5% [Chain A UniRef90 accession]=UniRef90_Q85295 [Chain A UniRef90 boundaries]=1-132 [Entry] [Accession]=DI1000198 [Disorder status]=Confirmed [Kd]=2.40E-05 [Name]=Siah1 SBD bound to a SIP peptide [Source organism]=Homo sapiens [PDB ID]=2a25 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=Sina [Type chain B]=Disordered [Evidence chain B]=The interacting region of SIP has been shown to be unstructured in isolation (PMID:16085652). The protein region involved in the interaction contains a PXAXVXP linear motif that is common to a family of Siah-binding proteins (PMID:16085652). [Type chain A]=Ordered [Evidence chain A]=The Sina domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03145). A solved structure of the domain without bound ligands is represented by PDB ID 4c9z. [Modified residues chain A]=phosphothreonine#T#7 [Chain B name]=Calcyclin-binding protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9HB71 [Chain B UniProt boundaries]=58-70 [Chain B UniProt coverage]=5.7% [Chain B UniRef90 accession]=UniRef90_Q9HB71 [Chain B UniRef90 boundaries]=58-70 [Chain A name]=E3 ubiquitin-protein ligase SIAH1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q8IUQ4 [Chain A UniProt boundaries]=90-282 [Chain A UniProt coverage]=68.4% [Chain A UniRef90 accession]=UniRef90_Q8IUQ4 [Chain A UniRef90 boundaries]=90-282 [Entry] [Accession]=DI1000199 [Disorder status]=Inferred from motif [Kd]=2.66E-06 (PMID:27776223) [Name]=SIAH1 SINA domain in complex with a USP19 peptide [Source organism]=Homo sapiens [PDB ID]=4x3g [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.34 [Domain]=Sina [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional SIAH-binding linear motif (PMID:23500468). [Type chain A]=Ordered [Evidence chain A]=The Sina domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03145). A solved structure of the domain without bound ligands is represented by PDB ID 4c9z. [Modified residues chain A]=phosphothreonine#T#7 [Chain C name]=Ubiquitin carboxyl-terminal hydrolase 19 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=O94966 [Chain C UniProt boundaries]=461-474 [Chain C UniProt coverage]=1.1% [Chain C UniRef90 accession]=UniRef90_O94966 [Chain C UniRef90 boundaries]=461-474 [Chain A name]=E3 ubiquitin-protein ligase SIAH1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q8IUQ4 [Chain A UniProt boundaries]=91-282 [Chain A UniProt coverage]=68.1% [Chain A UniRef90 accession]=UniRef90_Q8IUQ4 [Chain A UniRef90 boundaries]=91-282 [Entry] [Accession]=DI1100051 [Disorder status]=Inferred from motif [Kd]=3.10E-06 [Name]=Nedd4 WW3 Domain:Comm LPSY peptide complex [Source organism]=Drosophila melanogaster [PDB ID]=2ez5 [PDB chain IDs]=P:W [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=WW [Type chain P]=Disordered [Evidence chain P]=The protein region involved in the interaction contains a known functional linear motif (PY-motif, PMID:12165468, http://www.uniprot.org/uniprot/Q24139#family_and_domains). [Type chain W]=Ordered [Evidence chain W]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1yiu. [Chain P name]=Protein commissureless 1 [Chain P source organism]=Drosophila melanogaster [Chain P UniProt accession]=Q24139 [Chain P UniProt boundaries]=227-237 [Chain P UniProt coverage]=3% [Chain P UniRef90 accession]=UniRef90_Q24139 [Chain P UniRef90 boundaries]=227-237 [Chain W name]=E3 ubiquitin-protein ligase Nedd-4 [Chain W source organism]=Drosophila melanogaster [Chain W UniProt accession]=Q9VVI3 [Chain W UniProt boundaries]=526-566 [Chain W UniProt coverage]=4.1% [Chain W UniRef90 accession]=UniRef90_Q9VVI3 [Chain W UniRef90 boundaries]=526-566 [Entry] [Accession]=DI1000200 [Disorder status]=Confirmed [Kd]=3.10E-06 [Name]=Peptide from SMAC/DIABLO complexed to the BIR domain of IAP-like protein 2 [Source organism]=Homo sapiens [PDB ID]=1xb0 [PDB chain IDs]=G:A [PDB note]=Chains B, C, D, E, F, H, I, J, K and L were removed as chains A and G represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=BIR [Type chain G]=Disordered [Evidence chain G]=The protein region involved in the interaction contains a known functional linear motif (IAP-binding motif - http://www.uniprot.org/uniprot/Q9NR28#family_and_domains). The N terminal region of Smac has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 1few). [Type chain A]=Ordered [Evidence chain A]=The BIR domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00653). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1f9x. [Modified residues chain A]=phosphothreonine#T#7 [Chain G name]=Diablo homolog, mitochondrial [Chain G source organism]=Homo sapiens [Chain G UniProt accession]=Q9NR28 [Chain G UniProt boundaries]=56-62 [Chain G UniProt coverage]=2.9% [Chain G UniRef90 accession]=UniRef90_Q9NR28 [Chain G UniRef90 boundaries]=56-62 [Chain A name]=Baculoviral IAP repeat-containing protein 8 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96P09 [Chain A UniProt boundaries]=1-95 [Chain A UniProt coverage]=40.3% [Chain A UniRef90 accession]=UniRef90_Q96P09 [Chain A UniRef90 boundaries]=1-95 [Related structures]=1xb1 [Entry] [Accession]=DI1000201 [Disorder status]=Confirmed [Kd]=8.50E-08 [Name]=Peptide from SMAC/DIABLO complexed to the BIR3 domain of cIAP1 [Source organism]=Homo sapiens [PDB ID]=3d9u [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=BIR [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (IAP-binding motif - http://www.uniprot.org/uniprot/Q9NR28#family_and_domains). The N terminal region of Smac has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 1few). [Type chain A]=Ordered [Evidence chain A]=The BIR domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00653). A solved monomeric structure of the domain is represented by PDB ID 1qbh. [Modified residues chain A]=phosphothreonine#T#7 [Chain B name]=Diablo homolog, mitochondrial [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9NR28 [Chain B UniProt boundaries]=56-61 [Chain B UniProt coverage]=2.5% [Chain B UniRef90 accession]=UniRef90_Q9NR28 [Chain B UniRef90 boundaries]=56-61 [Chain A name]=Baculoviral IAP repeat-containing protein 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q13490 [Chain A UniProt boundaries]=260-352 [Chain A UniProt coverage]=15% [Chain A UniRef90 accession]=UniRef90_Q13490 [Chain A UniRef90 boundaries]=260-352 [Entry] [Accession]=DI2000014 [Disorder status]=Confirmed [Kd]=1.21E-04 (PMID:22244766) [Name]=Peptide from SMAC/DIABLO complexed to the BIR3 domain of Survivin [Source organism]=Homo sapiens [PDB ID]=3uih [PDB chain IDs]=P:AB [PDB note]=Chain Q was removed as chains A, B and P represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=BIR [Type chain P]=Disordered [Evidence chain P]=The protein region involved in the interaction contains a known functional linear motif (IAP-binding motif - http://www.uniprot.org/uniprot/Q9NR28#family_and_domains). The N terminal region of Smac has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 1few). [Type chain A]=Ordered component [Evidence chain A]=The BIR domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00653). A solved structure of the BIR dimer of survivin is represented by PDB ID 1e31. [Type chain B]=Ordered component [Evidence chain B]=The BIR domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00653). A solved structure of the BIR dimer of survivin is represented by PDB ID 1e31. [Modified residues chain A]=phosphothreonine#T#7 [Chain P name]=Diablo homolog, mitochondrial [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=Q9NR28 [Chain P UniProt boundaries]=56-70 [Chain P UniProt coverage]=6.3% [Chain P UniRef90 accession]=UniRef90_Q9NR28 [Chain P UniRef90 boundaries]=56-70 [Chain A name]=Baculoviral IAP repeat-containing protein 5 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O15392 [Chain A UniProt boundaries]=1-142 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_O15392 [Chain A UniRef90 boundaries]=1-142 [Chain B name]=Baculoviral IAP repeat-containing protein 5 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O15392 [Chain B UniProt boundaries]=1-142 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_O15392 [Chain B UniRef90 boundaries]=1-142 [Related structures]=3uij [Entry] [Accession]=DI1010061 [Disorder status]=Confirmed [Kd]=7.40E-07 [Name]=Histone H3 (Xenopus laevis) tail bound to lysine-specific histone demethylase 1B [Source organism]=Xenopus laevis / Homo sapiens [PDB ID]=4hsu [PDB chain IDs]=C:A [PDB note]=Chain B was removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.99 [Domain]=Lysine-specific histone demethylase [Type chain C]=Disordered [Evidence chain C]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The lysine-specific histone demethylase domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4fwe. [Modified residues chain A]=phosphothreonine#T#7 [Chain C name]=Histone H3 [Chain C source organism]=Xenopus laevis [Chain C UniProt accession]=Q92133 [Chain C UniProt boundaries]=2-31 [Chain C UniProt coverage]=22.1% [Chain C UniRef90 accession]=UniRef90_Q16695 [Chain C UniRef90 boundaries]=2-31 [Chain A name]=Lysine-specific histone demethylase 1B [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q8NB78 [Chain A UniProt boundaries]=51-822 [Chain A UniProt coverage]=93.9% [Chain A UniRef90 accession]=UniRef90_Q8NB78 [Chain A UniRef90 boundaries]=51-822 [Entry] [Accession]=DI1000202 [Disorder status]=Confirmed [Kd]=9.90E-07 [Name]=Histone H3.3 (human) tail bound to lysine-specific histone demethylase 1B [Source organism]=Homo sapiens [PDB ID]=4gur [PDB chain IDs]=C:A [PDB note]=Chain B was removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.51 [Domain]=Lysine-specific histone demethylase [Type chain C]=Disordered [Evidence chain C]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The lysine-specific histone demethylase domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4fwe. [Modified residues chain A]=phosphothreonine#T#7 [Chain C name]=Histone H3.3 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P84243 [Chain C UniProt boundaries]=2-22 [Chain C UniProt coverage]=15.4% [Chain C UniRef90 accession]=UniRef90_P84243 [Chain C UniRef90 boundaries]=2-22 [Chain A name]=Lysine-specific histone demethylase 1B [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q8NB78 [Chain A UniProt boundaries]=51-822 [Chain A UniProt coverage]=93.9% [Chain A UniRef90 accession]=UniRef90_Q8NB78 [Chain A UniRef90 boundaries]=51-822 [Related structures]=4gu0,4gus [Entry] [Accession]=DI2110004 [Disorder status]=Confirmed [Kd]=4.90E-06 [Name]=S100A6 bound to C-terminal Siah-1 interacting protein [Source organism]=Mus musculus / Oryctolagus cuniculus [PDB ID]=2jtt [PDB chain IDs]=C:AB [PDB note]=Chain D was removed as chains A, B and C highlight the biologically relevant interaction. [PDB experimental technique]=NMR [Domain]=S100B [Type chain C]=Disordered [Evidence chain C]=The 178-229 region described in DisProt entry DP00226 covers 100% of the sequence present in the structure. [Type chain A]=Ordered component [Evidence chain A]=S100B is known to adopt a stable structure in isolation in dimeric form. A solved structure of the domain dimer without bound ligands is represented by PDB ID 1jwd. [Type chain B]=Ordered component [Evidence chain B]=S100B is known to adopt a stable structure in isolation in dimeric form. A solved structure of the domain dimer without bound ligands is represented by PDB ID 1jwd. [Modified residues chain A]=phosphothreonine#T#7 [Chain C name]=Calcyclin-binding protein [Chain C source organism]=Mus musculus [Chain C UniProt accession]=Q9CXW3 [Chain C UniProt boundaries]=189-219 [Chain C UniProt coverage]=13.5% [Chain C UniRef90 accession]=UniRef90_Q9HB71-3 [Chain C UniRef90 boundaries]=145-175 [Chain A name]=Protein S100-A6 [Chain A source organism]=Oryctolagus cuniculus [Chain A UniProt accession]=P30801 [Chain A UniProt boundaries]=1-90 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P30801 [Chain A UniRef90 boundaries]=1-90 [Chain B name]=Protein S100-A6 [Chain B source organism]=Oryctolagus cuniculus [Chain B UniProt accession]=P30801 [Chain B UniProt boundaries]=1-90 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P30801 [Chain B UniRef90 boundaries]=1-90 [Entry] [Accession]=DI1010062 [Disorder status]=Confirmed [Kd]=7.40E-06 [Name]=Vav1 SH2 domain complexed with a Syk-derived doubly phosphorylated peptide [Source organism]=Mus musculus / Homo sapiens [PDB ID]=2lct [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 4wnm). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2crh. [Modified residues chain B]=phosphotyrosine#Y#342|phosphotyrosine#Y#346 [Modified residues chain A]=phosphothreonine#T#7 [Chain B name]=Tyrosine-protein kinase SYK [Chain B source organism]=Mus musculus [Chain B UniProt accession]=P48025 [Chain B UniProt boundaries]=338-350 [Chain B UniProt coverage]=2.1% [Chain B UniRef90 accession]=UniRef90_P48025 [Chain B UniRef90 boundaries]=338-350 [Chain A name]=Proto-oncogene vav [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P15498 [Chain A UniProt boundaries]=661-767 [Chain A UniProt coverage]=12.7% [Chain A UniRef90 accession]=UniRef90_P15498 [Chain A UniRef90 boundaries]=661-767 [Entry] [Accession]=DI1000203 [Disorder status]=Confirmed [Kd]=2.00E-07 [Name]=Complex between the Nonsense-Mediated Decay Factors, Upf1 and Upf2. [Source organism]=Homo sapiens [PDB ID]=2wjv [PDB chain IDs]=D:A [PDB note]=Chains B and E were removed as chains A and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.85 [Domain]=UPF2 interacting domain [Type chain D]=Disordered [Evidence chain D]=The 1105-1207 region described in DisProt entry DP00949 and the 1105-1227 region in IDEAL entry IID00252 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The UPF2 interacting domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF09416). A solved monomeric structure of the UPF2 interacting domain is represented by DPB ID 2wjy. [Modified residues chain A]=phosphothreonine#T#7 [Chain D name]=Regulator of nonsense transcripts 2 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=Q9HAU5 [Chain D UniProt boundaries]=1105-1198 [Chain D UniProt coverage]=7.4% [Chain D UniRef90 accession]=UniRef90_Q9HAU5 [Chain D UniRef90 boundaries]=1105-1198 [Chain A name]=Regulator of nonsense transcripts 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q92900 [Chain A UniProt boundaries]=115-925 [Chain A UniProt coverage]=71.8% [Chain A UniRef90 accession]=UniRef90_Q92900 [Chain A UniRef90 boundaries]=115-925 [Entry] [Accession]=DI1010063 [Disorder status]=Confirmed [Kd]=6.00E-07 (PMID:17513864) [Name]=Myo5a globular tail domain in complex with melanophilin GTBD [Source organism]=Mus musculus / Homo sapiens [PDB ID]=4lx2 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.50 [Domain]=DIL [Type chain B]=Disordered [Evidence chain B]=The 147-403 region described in DisProt entry DP00541 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The DIL (Dilute) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01843). A solved monomeric structure is represented by DPB ID 4lx1. [Modified residues chain A]=phosphothreonine#T#7 [Chain B name]=Melanophilin [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q91V27 [Chain B UniProt boundaries]=176-201 [Chain B UniProt coverage]=4.4% [Chain B UniRef90 accession]=UniRef90_Q91V27 [Chain B UniRef90 boundaries]=176-201 [Chain A name]=Unconventional myosin-Va [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9Y4I1 [Chain A UniProt boundaries]=1464-1855 [Chain A UniProt coverage]=21.1% [Chain A UniRef90 accession]=UniRef90_Q99104 [Chain A UniRef90 boundaries]=1464-1855 [Related structures]=4kp3 [Entry] [Accession]=DI2010010 [Disorder status]=Confirmed [Kd]=3.65E-09 [Name]=Salivary anti-thrombin peptide anophelin in complex with thrombin [Source organism]=Anopheles albimanus / Homo sapiens [PDB ID]=4e05 [PDB chain IDs]=I:HL [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=Trypsin [Type chain I]=Disordered [Evidence chain I]=The 23-83 region described in DisProt entry DP00824 cover 100% of the sequence present in the structure. [Type chain H]=Ordered component [Evidence chain H]=Thrombin consists of a large and a small subunit. Trypsin domain of the large subunit involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00089). A solved structure of the thrombin dimer is represented by PDB ID 1abj. [Type chain L]=Ordered component [Evidence chain L]=Thrombin consists of a large and a small subunit. Trypsin domain of the large subunit involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00089). A solved structure of the thrombin dimer is represented by PDB ID 1abj. [Modified residues chain L]=phosphotyrosine#Y#474 [Chain I name]=Salivary anti-thrombin peptide anophelin [Chain I source organism]=Anopheles albimanus [Chain I UniProt accession]=Q9NJS1 [Chain I UniProt boundaries]=23-83 [Chain I UniProt coverage]=73.5% [Chain I UniRef90 accession]=UniRef90_Q9NJS1 [Chain I UniRef90 boundaries]=23-83 [Chain H name]=Prothrombin [Chain H source organism]=Homo sapiens [Chain H UniProt accession]=P00734 [Chain H UniProt boundaries]=364-622 [Chain H UniProt coverage]=41.6% [Chain H UniRef90 accession]=UniRef90_P00734 [Chain H UniRef90 boundaries]=364-622 [Chain L name]=Prothrombin [Chain L source organism]=Homo sapiens [Chain L UniProt accession]=P00734 [Chain L UniProt boundaries]=328-363 [Chain L UniProt coverage]=5.8% [Chain L UniRef90 accession]=UniRef90_P00734 [Chain L UniRef90 boundaries]=328-363 [Related structures]=4e06 [Entry] [Accession]=DI4100001 [Disorder status]=Confirmed [Kd]=1.80E-07 (PMID:17947231) [Name]=Binary complex of photosyntetic A4 glyceraldehyde 3-phosphate dehydrogenase (GAPDH) with cp12-2 [Source organism]=Arabidopsis thaliana [PDB ID]=3qv1 [PDB chain IDs]=G:ABCD [PDB note]=Chains E, F, H and I were removed as chains A, B, C, D and E represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=GAPDH [Type chain G]=Disordered [Evidence chain G]=The 1-131 region described in DisProt entry DP00534 cover 100% of the sequence present in the structure. [Type chain A]=Ordered component [Evidence chain A]=GAPDH is known to adopt a stable structure in isolation in tetrameric form (see Pfam domains PF00044 and PF02800). A solved structure of the homotetramer without bound ligands is represented by PDB ID 3k2b. One CP12 bounds to each pair of GAPDH subunits. [Type chain B]=Ordered component [Evidence chain B]=GAPDH is known to adopt a stable structure in isolation in tetrameric form (see Pfam domains PF00044 and PF02800). A solved structure of the homotetramer without bound ligands is represented by PDB ID 3k2b. One CP12 bounds to each pair of GAPDH subunits. [Type chain C]=Ordered component [Evidence chain C]=GAPDH is known to adopt a stable structure in isolation in tetrameric form (see Pfam domains PF00044 and PF02800). A solved structure of the homotetramer without bound ligands is represented by PDB ID 3k2b. One CP12 bounds to each pair of GAPDH subunits. [Type chain D]=Ordered component [Evidence chain D]=GAPDH is known to adopt a stable structure in isolation in tetrameric form (see Pfam domains PF00044 and PF02800). A solved structure of the homotetramer without bound ligands is represented by PDB ID 3k2b. One CP12 bounds to each pair of GAPDH subunits. [Modified residues chain A]=phosphothreonine#T#7 [Chain G name]=Calvin cycle protein CP12-2, chloroplastic [Chain G source organism]=Arabidopsis thaliana [Chain G UniProt accession]=Q9LZP9 [Chain G UniProt boundaries]=54-131 [Chain G UniProt coverage]=59.5% [Chain G UniRef90 accession]=UniRef90_Q9LZP9 [Chain G UniRef90 boundaries]=54-131 [Chain A name]=Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic [Chain A source organism]=Arabidopsis thaliana [Chain A UniProt accession]=P25856 [Chain A UniProt boundaries]=60-396 [Chain A UniProt coverage]=85.1% [Chain A UniRef90 accession]=UniRef90_P25856 [Chain A UniRef90 boundaries]=60-396 [Chain B name]=Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic [Chain B source organism]=Arabidopsis thaliana [Chain B UniProt accession]=P25856 [Chain B UniProt boundaries]=60-396 [Chain B UniProt coverage]=85.1% [Chain B UniRef90 accession]=UniRef90_P25856 [Chain B UniRef90 boundaries]=60-396 [Chain C name]=Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic [Chain C source organism]=Arabidopsis thaliana [Chain C UniProt accession]=P25856 [Chain C UniProt boundaries]=60-396 [Chain C UniProt coverage]=85.1% [Chain C UniRef90 accession]=UniRef90_P25856 [Chain C UniRef90 boundaries]=60-396 [Chain D name]=Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic [Chain D source organism]=Arabidopsis thaliana [Chain D UniProt accession]=P25856 [Chain D UniProt boundaries]=60-396 [Chain D UniProt coverage]=85.1% [Chain D UniRef90 accession]=UniRef90_P25856 [Chain D UniRef90 boundaries]=60-396 [Related structures]=3rvd [Entry] [Accession]=DI1100052 [Disorder status]=Confirmed [Kd]=1.00E-09 [Name]=Mouse prosurvival protein A1 bound to the Puma BH3-domain [Source organism]=Mus musculus [PDB ID]=2vof [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.8 [Domain]=Bcl-2 [Type chain B]=Disordered [Evidence chain B]=The interacting region of Puma was shown to be intrinsically disordered (PMID:23301700): the BH3 region of the intrinsically disordered protein Puma forms a single, contiguous alpha-helix upon binding the folded protein Mcl-1. The protein region involved in the interaction contains a known functional linear motif (LIG_BH_BH3_1). [Type chain A]=Ordered [Evidence chain A]=Bcl-2 domains, such as the one involved in the interaction, are known to adopt a stable structure in isolation (see Pfam domain PF00452). A solved monomeric structure from a homologous protein is represented by PDB ID 2mhs. [Modified residues chain A]=phosphothreonine#T#7 [Chain B name]=Bcl-2-binding component 3 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q99ML1 [Chain B UniProt boundaries]=130-155 [Chain B UniProt coverage]=13.5% [Chain B UniRef90 accession]=UniRef90_Q99ML1 [Chain B UniRef90 boundaries]=130-155 [Chain A name]=Bcl-2-related protein A1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q07440 [Chain A UniProt boundaries]=1-152 [Chain A UniProt coverage]=88.4% [Chain A UniRef90 accession]=UniRef90_Q07440 [Chain A UniRef90 boundaries]=1-152 [Entry] [Accession]=DI1100053 [Disorder status]=Confirmed [Kd]=1.80E-09 [Name]=Mcl-1 complexed with Puma [Source organism]=Mus musculus [PDB ID]=2roc [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Bcl-2 [Type chain B]=Disordered [Evidence chain B]=The interacting region of Puma was shown to be intrinsically disordered (PMID:23301700): the BH3 region of the intrinsically disordered protein Puma forms a single, contiguous alpha-helix upon binding the folded protein Mcl-1. The protein region involved in the interaction contains a known functional linear motif (LIG_BH_BH3_1). [Type chain A]=Ordered [Evidence chain A]=Bcl-2 domains, such as the one involved in the interaction, are known to adopt a stable structure in isolation (see Pfam domain PF00452). A solved monomeric structure of the protein is represented by PDB ID 1wsx. [Modified residues chain A]=phosphothreonine#T#7 [Chain B name]=Bcl-2-binding component 3 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q99ML1 [Chain B UniProt boundaries]=130-155 [Chain B UniProt coverage]=13.5% [Chain B UniRef90 accession]=UniRef90_Q99ML1 [Chain B UniRef90 boundaries]=130-155 [Chain A name]=Induced myeloid leukemia cell differentiation protein Mcl-1 homolog [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P97287 [Chain A UniProt boundaries]=152-308 [Chain A UniProt coverage]=47.4% [Chain A UniRef90 accession]=UniRef90_P97287 [Chain A UniRef90 boundaries]=152-308 [Entry] [Accession]=DI1100054 [Disorder status]=Confirmed [Kd]=3.95E-08 [Name]=Mcl-1 complexed with NoxaA [Source organism]=Mus musculus [PDB ID]=2rod [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Bcl-2 [Type chain B]=Disordered [Evidence chain B]=The first BH3 domain of Noxa has been shown to be intrinsically disordered in solution, but form well-ordered alpha-helices upon binding to Mcl-1 (PMID:18589438). The protein region involved in the interaction contains a known functional linear motif (LIG_BH_BH3_1). [Type chain A]=Ordered [Evidence chain A]=Bcl-2 domains, such as the one involved in the interaction, are known to adopt a stable structure in isolation (see Pfam domain PF00452). A solved monomeric structure of the protein is represented by PDB ID 1wsx. [Modified residues chain A]=phosphothreonine#T#7 [Chain B name]=Phorbol-12-myristate-13-acetate-induced protein 1 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q9JM54 [Chain B UniProt boundaries]=17-42 [Chain B UniProt coverage]=25.2% [Chain B UniRef90 accession]=UniRef90_Q9JM54 [Chain B UniRef90 boundaries]=17-42 [Chain A name]=Induced myeloid leukemia cell differentiation protein Mcl-1 homolog [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P97287 [Chain A UniProt boundaries]=152-308 [Chain A UniProt coverage]=47.4% [Chain A UniRef90 accession]=UniRef90_P97287 [Chain A UniRef90 boundaries]=152-308 [Entry] [Accession]=DI1100055 [Disorder status]=Confirmed [Kd]=1.90E-08 [Name]=Mcl-1 complexed with NoxaB [Source organism]=Mus musculus [PDB ID]=2jm6 [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Bcl-2 [Type chain A]=Disordered [Evidence chain A]=The second BH3 domain of Noxa has been shown to be intrinsically disordered in solution (PMID:18589438). The protein region involved in the interaction contains a known functional linear motif (LIG_BH_BH3_1). [Type chain B]=Ordered [Evidence chain B]=Bcl-2 domains, such as the one involved in the interaction, are known to adopt a stable structure in isolation (see Pfam domain PF00452). A solved monomeric structure of the protein is represented by PDB ID 1wsx. [Chain A name]=Phorbol-12-myristate-13-acetate-induced protein 1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q9JM54 [Chain A UniProt boundaries]=68-93 [Chain A UniProt coverage]=25.2% [Chain A UniRef90 accession]=UniRef90_Q9JM54 [Chain A UniRef90 boundaries]=68-93 [Chain B name]=Induced myeloid leukemia cell differentiation protein Mcl-1 homolog [Chain B source organism]=Mus musculus [Chain B UniProt accession]=P97287 [Chain B UniProt boundaries]=152-308 [Chain B UniProt coverage]=47.4% [Chain B UniRef90 accession]=UniRef90_P97287 [Chain B UniRef90 boundaries]=152-308 [Related structures]=2nla [Entry] [Accession]=DI4200001 [Disorder status]=Confirmed [Kd]=1.90E-08 [Name]=Glyceraldehyde-3-Phosphate Dehydrogenase complexed with CP12 from Synechococcus elongatus [Source organism]=Synechococcus elongatus [PDB ID]=3b1k [PDB chain IDs]=D:ABGH [PDB note]=Chains J, C and I were removed as chains A, B, G, H and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.30 [Domain]=GAPDH [Type chain D]=Disordered [Evidence chain D]=CP12 has been shown to be intrinsically disordered in solution (PMID:22153507). The intrinsically disordered CP12 becomes partially structured upon GAPDH binding. [Type chain A]=Ordered component [Evidence chain A]=GAPDH is known to adopt a stable structure in isolation in tetrameric form (see Pfam domains PF00044 and PF02800). A solved structure of the homotetramer without bound ligands is represented by PDB ID 3b20. One GAPDH tetramer bounds four CP12. [Type chain B]=Ordered component [Evidence chain B]=GAPDH is known to adopt a stable structure in isolation in tetrameric form (see Pfam domains PF00044 and PF02800). A solved structure of the homotetramer without bound ligands is represented by PDB ID 3b20. One GAPDH tetramer bounds four CP12. [Type chain G]=Ordered component [Evidence chain G]=GAPDH is known to adopt a stable structure in isolation in tetrameric form (see Pfam domains PF00044 and PF02800). A solved structure of the homotetramer without bound ligands is represented by PDB ID 3b20. One GAPDH tetramer bounds four CP12. [Type chain H]=Ordered component [Evidence chain H]=GAPDH is known to adopt a stable structure in isolation in tetrameric form (see Pfam domains PF00044 and PF02800). A solved structure of the homotetramer without bound ligands is represented by PDB ID 3b20. One GAPDH tetramer bounds four CP12. [Chain D name]=CP12 [Chain D source organism]=Synechococcus elongatus [Chain D UniProt accession]=Q6BBK3 [Chain D UniProt boundaries]=51-75 [Chain D UniProt coverage]=33.3% [Chain D UniRef90 accession]=UniRef90_Q6BBK3 [Chain D UniRef90 boundaries]=51-75 [Chain A name]=Glyceraldehyde-3-phosphate dehydrogenase [Chain A source organism]=Synechococcus elongatus [Chain A UniProt accession]=Q9R6W2 [Chain A UniProt boundaries]=1-339 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q9R6W2 [Chain A UniRef90 boundaries]=1-339 [Chain B name]=Glyceraldehyde-3-phosphate dehydrogenase [Chain B source organism]=Synechococcus elongatus [Chain B UniProt accession]=Q9R6W2 [Chain B UniProt boundaries]=1-339 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_Q9R6W2 [Chain B UniRef90 boundaries]=1-339 [Chain G name]=Glyceraldehyde-3-phosphate dehydrogenase [Chain G source organism]=Synechococcus elongatus [Chain G UniProt accession]=Q9R6W2 [Chain G UniProt boundaries]=1-339 [Chain G UniProt coverage]=100% [Chain G UniRef90 accession]=UniRef90_Q9R6W2 [Chain G UniRef90 boundaries]=1-339 [Chain H name]=Glyceraldehyde-3-phosphate dehydrogenase [Chain H source organism]=Synechococcus elongatus [Chain H UniProt accession]=Q9R6W2 [Chain H UniProt boundaries]=1-339 [Chain H UniProt coverage]=100% [Chain H UniRef90 accession]=UniRef90_Q9R6W2 [Chain H UniRef90 boundaries]=1-339 [Related structures]=3b1j [Entry] [Accession]=DI2200004 [Disorder status]=Confirmed [Kd]=1.90E-08 [Name]=Prokaryotic ubiquitin-like protein (Pup) complexed with the amino terminal coiled coil of the Mycobacterium tuberculosis proteasomal ATPase Mpa [Source organism]=Mycobacterium tuberculosis [PDB ID]=3m91 [PDB chain IDs]=B:AC [PDB note]=Chain D was removed as chains A, B and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=Coiled coil domain [Type chain B]=Disordered [Evidence chain B]=The 1-64 region described in DisProt entry DP00877 cover 100% of the sequence present in the structure. [Type chain A]=Ordered component [Evidence chain A]=Mpa coiled coil domain is known to adopt stable, two-stranded parallel coiled-coil structure in isolation represented by PDB ID 3m9h. Upon binding Pup interacts with the Mpa coiled-coil domain with a 1:1 stoichiometry. In the context of the Mpa hexamer only one Pup binds to one coiled coil pair. (PMID:20953180). [Type chain C]=Ordered component [Evidence chain C]=Mpa coiled coil domain is known to adopt stable, two-stranded parallel coiled-coil structure in isolation represented by PDB ID 3m9h. Upon binding Pup interacts with the Mpa coiled-coil domain with a 1:1 stoichiometry. (PMID:20953180). [Chain B name]=Prokaryotic ubiquitin-like protein Pup [Chain B source organism]=Mycobacterium tuberculosis [Chain B UniProt accession]=P9WHN5 [Chain B UniProt boundaries]=21-64 [Chain B UniProt coverage]=68.8% [Chain B UniRef90 accession]=UniRef90_A0QZ48 [Chain B UniRef90 boundaries]=21-64 [Chain A name]=Proteasome-associated ATPase [Chain A source organism]=Mycobacterium tuberculosis [Chain A UniProt accession]=P9WQN5 [Chain A UniProt boundaries]=46-96 [Chain A UniProt coverage]=8.4% [Chain A UniRef90 accession]=UniRef90_A0QZ54 [Chain A UniRef90 boundaries]=55-100 [Chain C name]=Proteasome-associated ATPase [Chain C source organism]=Mycobacterium tuberculosis [Chain C UniProt accession]=P9WQN5 [Chain C UniProt boundaries]=46-96 [Chain C UniProt coverage]=8.4% [Chain C UniRef90 accession]=UniRef90_A0QZ54 [Chain C UniRef90 boundaries]=55-100 [Related structures]=3m9d [Entry] [Accession]=DI1010064 [Disorder status]=Inferred from motif [Kd]=7.38E-06 [Name]=SH3 domain of betaPIX in complex with an AIP4 peptide [Source organism]=Homo sapiens / Rattus norvegicus [PDB ID]=2p4r [PDB chain IDs]=T:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=SH3 [Type chain T]=Disordered [Evidence chain T]=The protein region involved in the interaction contains a known functional linear motif (atypical SH3-binding motif PxxxPR, PMID:17652093). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF07653). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1shg. [Chain T name]=E3 ubiquitin-protein ligase Itchy homolog [Chain T source organism]=Homo sapiens [Chain T UniProt accession]=Q96J02 [Chain T UniProt boundaries]=246-270 [Chain T UniProt coverage]=2.8% [Chain T UniRef90 accession]=UniRef90_Q96J02 [Chain T UniRef90 boundaries]=356-367 [Chain A name]=Rho guanine nucleotide exchange factor 7 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=O55043 [Chain A UniProt boundaries]=5-63 [Chain A UniProt coverage]=9.1% [Chain A UniRef90 accession]=UniRef90_Q9ES28-4 [Chain A UniRef90 boundaries]=115-168 [Entry] [Accession]=DI1000204 [Disorder status]=Confirmed [Kd]=8.00E-07 [Name]=Filamin A repeat 21 complexed with the integrin beta7 cytoplasmic tail peptide [Source organism]=Homo sapiens [PDB ID]=2brq [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=Filamin repeat [Type chain C]=Disordered [Evidence chain C]=The cytoplasmic tail of integrins have been shown to be intrinsically unstructured (PMID:21421922). [Type chain A]=Ordered [Evidence chain A]=The filamin repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00630). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2nqc. [Chain C name]=Integrin beta-7 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P26010 [Chain C UniProt boundaries]=768-798 [Chain C UniProt coverage]=3.9% [Chain C UniRef90 accession]=UniRef90_P26010 [Chain C UniRef90 boundaries]=768-798 [Chain A name]=Filamin-A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P21333 [Chain A UniProt boundaries]=2233-2329 [Chain A UniProt coverage]=3.7% [Chain A UniRef90 accession]=UniRef90_P21333 [Chain A UniRef90 boundaries]=2236-2329 [Entry] [Accession]=DI1000205 [Disorder status]=Confirmed [Kd]=4.80E-08 [Name]=CIAP1-BIR3 in complex with N-terminal peptide from Caspase-9 [Source organism]=Homo sapiens [PDB ID]=3d9t [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.50 [Domain]=BIR [Type chain C]=Disordered [Evidence chain C]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 2ar9, 1jxq, 3v3k). [Type chain A]=Ordered [Evidence chain A]=The BIR domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00653). A solved monomeric structure of the domain is represented by PDB ID 1qbh. [Chain C name]=Caspase-9 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P55211 [Chain C UniProt boundaries]=316-321 [Chain C UniProt coverage]=1.4% [Chain C UniRef90 accession]=UniRef90_P55211 [Chain C UniRef90 boundaries]=316-321 [Chain A name]=Baculoviral IAP repeat-containing protein 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q13490 [Chain A UniProt boundaries]=256-352 [Chain A UniProt coverage]=15.7% [Chain A UniRef90 accession]=UniRef90_Q13490 [Chain A UniRef90 boundaries]=260-352 [Entry] [Accession]=DI1010065 [Disorder status]=Confirmed [Kd]=1.40E-04 (PMID:20709061) [Name]=BRD2 second bromodomain in complex with acetylated histone H4 peptide [Source organism]=Saccharomyces cerevisiae / Homo sapiens [PDB ID]=2e3k [PDB chain IDs]=R:D [PDB note]=Chains A, B, C and Q were removed as chains D and R highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=Bromodomain [Type chain R]=Disordered [Evidence chain R]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain D]=Ordered [Evidence chain D]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 2dvv. [Modified residues chain R]=N(6)-acetyllysine#K#5|N(6)-acetyllysine#K#12 [Chain R name]=Histone H4 [Chain R source organism]=Saccharomyces cerevisiae [Chain R UniProt accession]=P02309 [Chain R UniProt boundaries]=2-16 [Chain R UniProt coverage]=14.6% [Chain R UniRef90 accession]=UniRef90_P02309 [Chain R UniRef90 boundaries]=2-16 [Chain D name]=Bromodomain-containing protein 2 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P25440 [Chain D UniProt boundaries]=344-455 [Chain D UniProt coverage]=14% [Chain D UniRef90 accession]=UniRef90_P25440 [Chain D UniRef90 boundaries]=344-455 [Entry] [Accession]=DI1200005 [Disorder status]=Confirmed [Kd]=4.80E-06 [Name]=The N-degron of E. coli Dps bound to the Clpap Adaptor Protein Clps [Source organism]=Escherichia coli [PDB ID]=2w9r [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=ClpS [Type chain B]=Disordered [Evidence chain B]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 1jre, 1jts, 1l8i). [Type chain A]=Ordered [Evidence chain A]=The ClpS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain P0A8Q6). A solved monomeric structure of the domain is represented by PDB ID 3o1f. [Chain B name]=DNA protection during starvation protein [Chain B source organism]=Escherichia coli [Chain B UniProt accession]=P0ABT2 [Chain B UniProt boundaries]=6-16 [Chain B UniProt coverage]=6.6% [Chain B UniRef90 accession]=UniRef90_A7ZJM7 [Chain B UniRef90 boundaries]=6-16 [Chain A name]=ATP-dependent Clp protease adapter protein ClpS [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=P0A8Q6 [Chain A UniProt boundaries]=1-106 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_A8AIK9 [Chain A UniRef90 boundaries]=1-106 [Related structures]=3o2h [Entry] [Accession]=DI1000206 [Disorder status]=Confirmed [Kd]=1.19E-05 [Name]=Mst2 flexible linker bound to MOB kinase activator 1A [Source organism]=Homo sapiens [PDB ID]=5brm [PDB chain IDs]=G:A [PDB note]=Chains B, C, D, E, F, H, I, J, K, L, M, N and O were removed as chains A and G highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.65 [Domain]=Mob1/phocein [Type chain G]=Disordered [Evidence chain G]=The region of Mst2 involved in the interaction has been shown to be highly flexible outside the interaction (PMID:26108669). [Type chain A]=Ordered [Evidence chain A]=The Mob1/phocein domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03637). A solved monomeric structure of the domain is represented by PDB ID 1pi1. [Modified residues chain G]=phosphothreonine#T#378 [Chain G name]=Serine/threonine-protein kinase 3 [Chain G source organism]=Homo sapiens [Chain G UniProt accession]=Q13188 [Chain G UniProt boundaries]=371-401 [Chain G UniProt coverage]=6.3% [Chain G UniRef90 accession]=UniRef90_Q13188 [Chain G UniRef90 boundaries]=371-401 [Chain A name]=MOB kinase activator 1A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9H8S9 [Chain A UniProt boundaries]=41-216 [Chain A UniProt coverage]=81.5% [Chain A UniRef90 accession]=UniRef90_Q9H8S9 [Chain A UniRef90 boundaries]=41-216 [Entry] [Accession]=DI2010011 [Disorder status]=Inferred from homology [Kd]=1.19E-05 [Name]=Annexin II bound to S100A10 dimer [Source organism]=Gallus gallus / Homo sapiens [PDB ID]=1bt6 [PDB chain IDs]=C:AB [PDB note]=Chain D was removed as chains A, B and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=S100A [Type chain C]=Disordered [Evidence chain C]=The interacting region of a closely homologous protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 1w7b, 4x9p). [Type chain A]=Ordered component [Evidence chain A]=S100A is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF01023). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1a4p. [Type chain B]=Ordered component [Evidence chain B]=S100A is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF01023). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1a4p. [Chain C name]=Annexin A2 [Chain C source organism]=Gallus gallus [Chain C UniProt accession]=P17785 [Chain C UniProt boundaries]=1-14 [Chain C UniProt coverage]=4.1% [Chain C UniRef90 accession]=UniRef90_P07356 [Chain C UniRef90 boundaries]=2-14 [Chain A name]=Protein S100-A10 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P60903 [Chain A UniProt boundaries]=2-97 [Chain A UniProt coverage]=99% [Chain A UniRef90 accession]=UniRef90_P60903 [Chain A UniRef90 boundaries]=2-97 [Chain B name]=Protein S100-A10 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P60903 [Chain B UniProt boundaries]=2-97 [Chain B UniProt coverage]=99% [Chain B UniRef90 accession]=UniRef90_P60903 [Chain B UniRef90 boundaries]=2-97 [Entry] [Accession]=DI2200005 [Disorder status]=Confirmed [Kd]=1.19E-05 [Name]=C-terminal domain of the clock protein KaiA in complex with a KaiC-derived peptide [Source organism]=Thermosynechococcus elongatus [PDB ID]=1suy [PDB chain IDs]=C:AB [PDB note]=Chain D was removed as chains A, B and C highlight the biologically relevant interaction. [PDB experimental technique]=NMR [Domain]=KaiA [Type chain C]=Disordered [Evidence chain C]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 1jre, 1jts, 1l8i). [Type chain A]=Ordered component [Evidence chain A]=The C-terminal domain of KaiA is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF07688). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1q6b. [Type chain B]=Ordered component [Evidence chain B]=The C-terminal domain of KaiA is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF07688). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1q6b. [Chain C name]=Circadian clock protein kinase KaiC [Chain C source organism]=Thermosynechococcus elongatus [Chain C UniProt accession]=Q79V60 [Chain C UniProt boundaries]=485-518 [Chain C UniProt coverage]=6.6% [Chain C UniRef90 accession]=UniRef90_Q79V60 [Chain C UniRef90 boundaries]=488-518 [Chain A name]=Circadian clock protein KaiA [Chain A source organism]=Thermosynechococcus elongatus [Chain A UniProt accession]=Q79V62 [Chain A UniProt boundaries]=177-283 [Chain A UniProt coverage]=37.8% [Chain A UniRef90 accession]=UniRef90_Q79V62 [Chain A UniRef90 boundaries]=180-283 [Chain B name]=Circadian clock protein KaiA [Chain B source organism]=Thermosynechococcus elongatus [Chain B UniProt accession]=Q79V62 [Chain B UniProt boundaries]=177-283 [Chain B UniProt coverage]=37.8% [Chain B UniRef90 accession]=UniRef90_Q79V62 [Chain B UniRef90 boundaries]=180-283 [Related structures]=1sv1 [Entry] [Accession]=DI1000207 [Disorder status]=Confirmed [Kd]=1.23E-05 [Name]=AIP TPR domain in complex with human Tomm20 peptide [Source organism]=Homo sapiens [PDB ID]=4apo [PDB chain IDs]=E:A [PDB note]=Chains B and D were removed as chains A and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=Tetratricopeptide [Type chain E]=Disordered [Evidence chain E]=The interacting region of the protein has been shown to be highly flexible based on NMR spectrum (PDB ID: 1om2). The protein region involved in the interaction contains a conserved C-terminal TPR-domain binding motif EDDVE (equivalent to the conserved HSP90 motif, MEEVD) (PMID:23300914, LIG_TPR). [Type chain A]=Ordered [Evidence chain A]=A solved monomeric structure of the domain from a homologous protein involved in the interaction is represented by PDB ID 2lsu. [Chain E name]=Mitochondrial import receptor subunit TOM20 homolog [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=Q15388 [Chain E UniProt boundaries]=140-145 [Chain E UniProt coverage]=4.1% [Chain E UniRef90 accession]=UniRef90_Q15388 [Chain E UniRef90 boundaries]=140-145 [Chain A name]=AH receptor-interacting protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O00170 [Chain A UniProt boundaries]=166-330 [Chain A UniProt coverage]=50% [Chain A UniRef90 accession]=UniRef90_O00170 [Chain A UniRef90 boundaries]=166-330 [Entry] [Accession]=DI1100056 [Disorder status]=Confirmed [Kd]=1.23E-05 [Name]=Dcp2 peptide bound to Edc3 [Source organism]=Schizosaccharomyces pombe [PDB ID]=4a54 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Edc3 N-terminal [Type chain B]=Disordered [Evidence chain B]=The region of Dcp2 involved in the interaction has been shown to contain a short helical leucine-rich motif (HLM) and to be highly flexible outside the interaction (PMID:22085934). [Type chain A]=Ordered [Evidence chain A]=The N-terminal domain of Edc3 involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 4a53. [Chain B name]=mRNA decapping complex subunit 2 [Chain B source organism]=Schizosaccharomyces pombe [Chain B UniProt accession]=O13828 [Chain B UniProt boundaries]=240-291 [Chain B UniProt coverage]=7% [Chain B UniRef90 accession]=UniRef90_O13828 [Chain B UniRef90 boundaries]=242-291 [Chain A name]=Enhancer of mRNA-decapping protein 3 [Chain A source organism]=Schizosaccharomyces pombe [Chain A UniProt accession]=O94752 [Chain A UniProt boundaries]=1-94 [Chain A UniProt coverage]=20.7% [Chain A UniRef90 accession]=UniRef90_O94752 [Chain A UniRef90 boundaries]=1-94 [Entry] [Accession]=DI1000208 [Disorder status]=Confirmed [Kd]=5.00E-04 [Name]=BRD4 ET domain in complex with NSD3_3 peptide [Source organism]=Homo sapiens [PDB ID]=2nd1 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=BET [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction has been shown to be highly flexible outside the interaction (PMID:27291650). The protein region involved in the interaction contains an ET-binding motif (EBM; PMID:27291650). [Type chain A]=Ordered [Evidence chain A]=The BET (Bromodomain extra-terminal) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF17035). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2jns. [Chain B name]=Histone-lysine N-methyltransferase NSD3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9BZ95 [Chain B UniProt boundaries]=593-605 [Chain B UniProt coverage]=0.9% [Chain B UniRef90 accession]=UniRef90_Q9BZ95 [Chain B UniRef90 boundaries]=593-605 [Chain A name]=Bromodomain-containing protein 4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O60885 [Chain A UniProt boundaries]=601-683 [Chain A UniProt coverage]=6.1% [Chain A UniRef90 accession]=UniRef90_O60885 [Chain A UniRef90 boundaries]=601-683 [Entry] [Accession]=DI1020022 [Disorder status]=Confirmed [Kd]=6.35E-04 [Name]=BRD4 ET domain in complex with LANA peptide [Source organism]=Human herpesvirus 8 / Homo sapiens [PDB ID]=2nd0 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=BET [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction has been shown to be highly flexible outside the interaction (PMID:27291650). The protein region involved in the interaction contains an ET-binding motif (EBM; PMID:27291650). [Type chain A]=Ordered [Evidence chain A]=The BET (Bromodomain extra-terminal) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF17035). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2jns. [Chain B name]=LANA [Chain B source organism]=Human herpesvirus 8 [Chain B UniProt accession]=E5LC01 [Chain B UniProt boundaries]=1086-1104 [Chain B UniProt coverage]=1.7% [Chain B UniRef90 accession]=UniRef90_Q9QR71 [Chain B UniRef90 boundaries]=1098-1116 [Chain A name]=Bromodomain-containing protein 4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O60885 [Chain A UniProt boundaries]=601-683 [Chain A UniProt coverage]=6.1% [Chain A UniRef90 accession]=UniRef90_O60885 [Chain A UniRef90 boundaries]=601-683 [Entry] [Accession]=DI1000209 [Disorder status]=Confirmed [Kd]=1.41E-04 [Name]=BRD4 ET domain in complex with NSD3_1 peptide [Source organism]=Homo sapiens [PDB ID]=2ncz [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=BET [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction has been shown to be highly flexible outside the interaction (PMID:27291650). The protein region involved in the interaction contains an ET-binding motif (EBM; PMID:27291650). [Type chain A]=Ordered [Evidence chain A]=The BET (Bromodomain extra-terminal) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF17035). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2jns. [Chain B name]=Histone-lysine N-methyltransferase NSD3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9BZ95 [Chain B UniProt boundaries]=152-163 [Chain B UniProt coverage]=0.8% [Chain B UniRef90 accession]=UniRef90_Q9BZ95 [Chain B UniRef90 boundaries]=152-163 [Chain A name]=Bromodomain-containing protein 4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O60885 [Chain A UniProt boundaries]=601-683 [Chain A UniProt coverage]=6.1% [Chain A UniRef90 accession]=UniRef90_O60885 [Chain A UniRef90 boundaries]=601-683 [Entry] [Accession]=DI1020023 [Disorder status]=Confirmed [Kd]=1.59E-07 [Name]=BRD4 ET domain in complex with MLV Integrase C-terminal peptide [Source organism]=Moloney murine leukemia virus / Homo sapiens [PDB ID]=2n3k [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=BET [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction has been shown to be highly flexible outside the interaction (PMID:27291650). The protein region involved in the interaction contains an ET-binding motif (EBM; PMID:26858406). [Type chain A]=Ordered [Evidence chain A]=The BET (Bromodomain extra-terminal) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF17035). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2jns. [Chain B name]=Pr180 Gag-Pro-Pol polyprotein [Chain B source organism]=Moloney murine leukemia virus [Chain B UniProt accession]=Q8UN00 [Chain B UniProt boundaries]=1719-1735 [Chain B UniProt coverage]=1% [Chain B UniRef90 accession]=UniRef90_P03355 [Chain B UniRef90 boundaries]=1719-1735 [Chain A name]=Bromodomain-containing protein 4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O60885 [Chain A UniProt boundaries]=595-680 [Chain A UniProt coverage]=6.3% [Chain A UniRef90 accession]=UniRef90_O60885 [Chain A UniRef90 boundaries]=600-678 [Entry] [Accession]=DI1110017 [Disorder status]=Confirmed [Kd]=1.59E-07 [Name]=P-element somatic inhibitor complexed with U1-70K [Source organism]=Drosophila melanogaster / Drosophila sp. [PDB ID]=2bn5 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=DUF1897 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction has been shown to be highly flexible outside the interaction (PMID:15990112). [Type chain A]=Ordered [Evidence chain A]=The domain with unknown function involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF09005). A solved monomeric structure of the domain is represented by PDB ID 2bn6. [Chain B name]=U1 small nuclear ribonucleoprotein 70 kDa [Chain B source organism]=Drosophila melanogaster [Chain B UniProt accession]=P17133 [Chain B UniProt boundaries]=405-425 [Chain B UniProt coverage]=4.7% [Chain B UniRef90 accession]=UniRef90_P17133 [Chain B UniRef90 boundaries]=405-425 [Chain A name]=PSI [Chain A source organism]=Drosophila sp. [Chain A UniProt accession]=Q7JPS0 [Chain A UniProt boundaries]=651-683 [Chain A UniProt coverage]=4.1% [Chain A UniRef90 accession]=UniRef90_O96828 [Chain A UniRef90 boundaries]=662-691 [Entry] [Accession]=DI3010002 [Disorder status]=Confirmed [Kd]=1.59E-07 [Name]=Alpha-chain of human fibrinogen bound to bovine epsilon-thrombin [Source organism]=Homo sapiens / Bos taurus [PDB ID]=1bbr [PDB chain IDs]=F:EHL [PDB note]=Chains F, J, K, G, M, N and I were removed as chains E, F, H and L highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=Trypsin [Type chain F]=Disordered [Evidence chain F]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 3h32). [Type chain E]=Ordered component [Evidence chain E]=Thrombin consists of a large and a small subunit. Trypsin domain of the large subunit involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00089). A solved structure of a homologous thrombin domain is represented by PDB ID 3pmb. [Type chain H]=Ordered component [Evidence chain H]=Thrombin consists of a large and a small subunit. Trypsin domain of the large subunit involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00089). A solved structure of a homologous thrombin domain is represented by PDB ID 3pmb. [Type chain L]=Ordered component [Evidence chain L]=Thrombin consists of a large and a small subunit. Trypsin domain of the large subunit involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00089). A solved structure of a homologous thrombin domain is represented by PDB ID 3pmb. [Modified residues chain L]=phosphotyrosine#Y#474 [Chain F name]=Fibrinogen alpha chain [Chain F source organism]=Homo sapiens [Chain F UniProt accession]=P02671 [Chain F UniProt boundaries]=25-35 [Chain F UniProt coverage]=1.3% [Chain F UniRef90 accession]=UniRef90_P02671 [Chain F UniRef90 boundaries]=26-35 [Chain E name]=Prothrombin [Chain E source organism]=Bos taurus [Chain E UniProt accession]=P00735 [Chain E UniProt boundaries]=517-625 [Chain E UniProt coverage]=17.4% [Chain E UniRef90 accession]=UniRef90_P00735 [Chain E UniRef90 boundaries]=517-625 [Chain H name]=Prothrombin [Chain H source organism]=Bos taurus [Chain H UniProt accession]=P00735 [Chain H UniProt boundaries]=367-516 [Chain H UniProt coverage]=24% [Chain H UniRef90 accession]=UniRef90_P00735 [Chain H UniRef90 boundaries]=367-516 [Chain L name]=Prothrombin [Chain L source organism]=Bos taurus [Chain L UniProt accession]=P00735 [Chain L UniProt boundaries]=318-366 [Chain L UniProt coverage]=7.8% [Chain L UniRef90 accession]=UniRef90_P00735 [Chain L UniRef90 boundaries]=318-366 [Related structures]=1ycp [Entry] [Accession]=DI1200006 [Disorder status]=Confirmed [Kd]=1.59E-07 [Name]=BamC bound to BamD [Source organism]=Escherichia coli [PDB ID]=5d0o [PDB chain IDs]=C:D [PDB note]=Chains A, B and E were removed as chains C and D highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.90 [Domain]=BamD [Type chain C]=Disordered [Evidence chain C]=The interacting region of the protein has been shown to be highly flexible in isolation (PMID:26901871). [Type chain D]=Ordered [Evidence chain D]=The BamD domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 2yhc. [Chain C name]=Outer membrane protein assembly factor BamC [Chain C source organism]=Escherichia coli [Chain C UniProt accession]=P0A903 [Chain C UniProt boundaries]=1-344 [Chain C UniProt coverage]=100% [Chain C UniRef90 accession]=UniRef90_P0A903 [Chain C UniRef90 boundaries]=1-344 [Chain D name]=Outer membrane protein assembly factor BamD [Chain D source organism]=Escherichia coli [Chain D UniProt accession]=P0AC02 [Chain D UniProt boundaries]=1-245 [Chain D UniProt coverage]=100% [Chain D UniRef90 accession]=UniRef90_P0AC04 [Chain D UniRef90 boundaries]=1-245 [Related structures]=3tgo,5ayw,5d0q,5ekq [Entry] [Accession]=DI2210002 [Disorder status]=Confirmed [Kd]=4.50E-07 [Name]=SspB:RseA complex [Source organism]=Escherichia coli O6:H1 / Escherichia coli [PDB ID]=1yfn [PDB chain IDs]=E:AB [PDB note]=Chains C, D, F, G and H were removed as chains A, B and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=SspB [Type chain E]=Disordered [Evidence chain E]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 1or7). [Type chain A]=Ordered component [Evidence chain A]=The Stringent starvation protein B (SspB) domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF04386). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1ox8. [Type chain B]=Ordered component [Evidence chain B]=The Stringent starvation protein B (SspB) domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF04386). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1ox8. [Chain E name]=Anti-sigma-E factor RseA [Chain E source organism]=Escherichia coli O6:H1 [Chain E UniProt accession]=P0AFX8 [Chain E UniProt boundaries]=77-108 [Chain E UniProt coverage]=14.8% [Chain E UniRef90 accession]=UniRef90_P0AFX8 [Chain E UniRef90 boundaries]=77-108 [Chain A name]=Stringent starvation protein B [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=P0AFZ3 [Chain A UniProt boundaries]=1-118 [Chain A UniProt coverage]=71.5% [Chain A UniRef90 accession]=UniRef90_Q83Q08 [Chain A UniRef90 boundaries]=1-118 [Chain B name]=Stringent starvation protein B [Chain B source organism]=Escherichia coli [Chain B UniProt accession]=P0AFZ3 [Chain B UniProt boundaries]=1-118 [Chain B UniProt coverage]=71.5% [Chain B UniRef90 accession]=UniRef90_Q83Q08 [Chain B UniRef90 boundaries]=1-118 [Entry] [Accession]=DI1000210 [Disorder status]=Confirmed [Kd]=4.50E-07 [Name]=HOP TPR2A domain in complex with the non-cognate Hsc70 peptide ligand [Source organism]=Homo sapiens [PDB ID]=3esk [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.05 [Domain]=Tetratricopeptide [Type chain B]=Disordered [Evidence chain B]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 1ud0). The protein region involved in the interaction contains a conserved C-terminal TPR-domain binding motif GPTIEEVD (PMID:19586912). [Type chain A]=Ordered [Evidence chain A]=The tetratricopeptide domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13176/PF13181). A solved monomeric structure of the domain is represented by PDB ID 2nc9. [Chain B name]=Heat shock cognate 71 kDa protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P11142 [Chain B UniProt boundaries]=635-646 [Chain B UniProt coverage]=1.9% [Chain B UniRef90 accession]=UniRef90_P11142 [Chain B UniRef90 boundaries]=635-646 [Chain A name]=Stress-induced-phosphoprotein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P31948 [Chain A UniProt boundaries]=222-350 [Chain A UniProt coverage]=23.8% [Chain A UniRef90 accession]=UniRef90_P31948 [Chain A UniRef90 boundaries]=223-350 [Entry] [Accession]=DI1100057 [Disorder status]=Confirmed [Kd]=4.50E-07 [Name]=OSCP-NT (1-120) in complex with N-terminal (1-25) alpha subunit from F1-ATPase [Source organism]=Bos taurus [PDB ID]=2jmx [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=OSCP [Type chain B]=Disordered [Evidence chain B]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 2w6e, 2w6f, 2w6g, 2w6h, 2w6i, 2w6j). [Type chain A]=Ordered [Evidence chain A]=The OSCP domain (or ATP synthase delta subunit domain) involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00213). A solved monomeric structure of the domain is represented by PDB ID 2bo5. [Chain B name]=ATP synthase subunit alpha, mitochondrial [Chain B source organism]=Bos taurus [Chain B UniProt accession]=P19483 [Chain B UniProt boundaries]=44-68 [Chain B UniProt coverage]=4.5% [Chain B UniRef90 accession]=UniRef90_Q03265 [Chain B UniRef90 boundaries]=44-68 [Chain A name]=ATP synthase subunit O, mitochondrial [Chain A source organism]=Bos taurus [Chain A UniProt accession]=P13621 [Chain A UniProt boundaries]=24-143 [Chain A UniProt coverage]=56.3% [Chain A UniRef90 accession]=UniRef90_P13621 [Chain A UniRef90 boundaries]=24-143 [Related structures]=2wss,5ara,5are,5arh,5ari,5fij,5fik,5fil [Entry] [Accession]=DI1100058 [Disorder status]=Confirmed [Kd]=3.00E-07 [Name]=Yeast Dun1 FHA domain in complex with a doubly phosphorylated (pT) peptide derived from Rad53 SCD1 [Source organism]=Saccharomyces cerevisiae [PDB ID]=2jql [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=FHA [Type chain B]=Disordered [Evidence chain B]=The interacting region of the protein has been shown to be highly flexible based on NMR spectrum (PDB ID: 1g3g). [Type chain A]=Ordered [Evidence chain A]=The FHA domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00498). A solved monomeric structure of the domain is represented by PDB ID 2jqj. [Modified residues chain B]=phosphothreonine#T#5|phosphothreonine#T#8 [Chain B name]=Serine/threonine-protein kinase RAD53 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P22216 [Chain B UniProt boundaries]=3-12 [Chain B UniProt coverage]=1.2% [Chain B UniRef90 accession]=UniRef90_P22216 [Chain B UniRef90 boundaries]=3-12 [Chain A name]=DNA damage response protein kinase DUN1 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P39009 [Chain A UniProt boundaries]=17-167 [Chain A UniProt coverage]=29.4% [Chain A UniRef90 accession]=UniRef90_P39009 [Chain A UniRef90 boundaries]=19-160 [Entry] [Accession]=DI3000006 [Disorder status]=Inferred from motif [Kd]=3.00E-07 [Name]=TNF receptor associated factor 2 in complex with a peptide from TNF-R2 [Source organism]=Homo sapiens [PDB ID]=1ca9 [PDB chain IDs]=G:ABC [PDB note]=Chains D, E, F and H were removed as chains A, B, C and G highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=MATH [Type chain G]=Disordered [Evidence chain G]=The protein region involved in the interaction contains a known functional linear motif (LIG_TRAF2_1). [Type chain A]=Ordered component [Evidence chain A]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4. [Type chain B]=Ordered component [Evidence chain B]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4. [Type chain C]=Ordered component [Evidence chain C]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4. [Modified residues chain B]=phosphothreonine#T#5|phosphothreonine#T#8 [Chain G name]=Tumor necrosis factor receptor superfamily member 1B [Chain G source organism]=Homo sapiens [Chain G UniProt accession]=P20333 [Chain G UniProt boundaries]=420-428 [Chain G UniProt coverage]=2% [Chain G UniRef90 accession]=UniRef90_P20333 [Chain G UniRef90 boundaries]=420-428 [Chain A name]=TNF receptor-associated factor 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q12933 [Chain A UniProt boundaries]=310-501 [Chain A UniProt coverage]=38.3% [Chain A UniRef90 accession]=UniRef90_Q12933 [Chain A UniRef90 boundaries]=310-501 [Chain B name]=TNF receptor-associated factor 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q12933 [Chain B UniProt boundaries]=310-501 [Chain B UniProt coverage]=38.3% [Chain B UniRef90 accession]=UniRef90_Q12933 [Chain B UniRef90 boundaries]=310-501 [Chain C name]=TNF receptor-associated factor 2 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q12933 [Chain C UniProt boundaries]=310-501 [Chain C UniProt coverage]=38.3% [Chain C UniRef90 accession]=UniRef90_Q12933 [Chain C UniRef90 boundaries]=310-501 [Entry] [Accession]=DI3020001 [Disorder status]=Inferred from motif [Kd]=3.00E-07 [Name]=TNF receptor associated factor 2 in complex with a peptide from LMP1 [Source organism]=Epstein-Barr virus / Homo sapiens [PDB ID]=1czy [PDB chain IDs]=D:ABC [PDB note]=Chain E was removed as chains A, B, C and D highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=MATH [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a known functional linear motif (LIG_TRAF2_2). [Type chain A]=Ordered component [Evidence chain A]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4. [Type chain B]=Ordered component [Evidence chain B]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4. [Type chain C]=Ordered component [Evidence chain C]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4. [Modified residues chain B]=phosphothreonine#T#5|phosphothreonine#T#8 [Chain D name]=Latent membrane protein 1 [Chain D source organism]=Epstein-Barr virus [Chain D UniProt accession]=P03230 [Chain D UniProt boundaries]=204-210 [Chain D UniProt coverage]=1.8% [Chain D UniRef90 accession]=UniRef90_P03230 [Chain D UniRef90 boundaries]=204-210 [Chain A name]=TNF receptor-associated factor 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q12933 [Chain A UniProt boundaries]=334-501 [Chain A UniProt coverage]=33.5% [Chain A UniRef90 accession]=UniRef90_Q12933 [Chain A UniRef90 boundaries]=334-501 [Chain B name]=TNF receptor-associated factor 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q12933 [Chain B UniProt boundaries]=334-501 [Chain B UniProt coverage]=33.5% [Chain B UniRef90 accession]=UniRef90_Q12933 [Chain B UniRef90 boundaries]=334-501 [Chain C name]=TNF receptor-associated factor 2 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q12933 [Chain C UniProt boundaries]=334-501 [Chain C UniProt coverage]=33.5% [Chain C UniRef90 accession]=UniRef90_Q12933 [Chain C UniRef90 boundaries]=334-501 [Entry] [Accession]=DI3000007 [Disorder status]=Inferred from motif [Kd]=3.00E-07 [Name]=TNF receptor associated factor 2 in complex with a peptide from CD40 [Source organism]=Homo sapiens [PDB ID]=1czz [PDB chain IDs]=D:ABC [PDB note]=Chain E was removed as chains A, B, C and D highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.70 [Domain]=MATH [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a known functional linear motif (LIG_TRAF2_1). [Type chain A]=Ordered component [Evidence chain A]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4. [Type chain B]=Ordered component [Evidence chain B]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4. [Type chain C]=Ordered component [Evidence chain C]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4. [Modified residues chain B]=phosphothreonine#T#5|phosphothreonine#T#8 [Chain D name]=Tumor necrosis factor receptor superfamily member 5 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P25942 [Chain D UniProt boundaries]=250-258 [Chain D UniProt coverage]=3.2% [Chain D UniRef90 accession]=UniRef90_P25942 [Chain D UniRef90 boundaries]=250-258 [Chain A name]=TNF receptor-associated factor 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q12933 [Chain A UniProt boundaries]=315-501 [Chain A UniProt coverage]=37.3% [Chain A UniRef90 accession]=UniRef90_Q12933 [Chain A UniRef90 boundaries]=315-501 [Chain B name]=TNF receptor-associated factor 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q12933 [Chain B UniProt boundaries]=315-501 [Chain B UniProt coverage]=37.3% [Chain B UniRef90 accession]=UniRef90_Q12933 [Chain B UniRef90 boundaries]=315-501 [Chain C name]=TNF receptor-associated factor 2 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q12933 [Chain C UniProt boundaries]=315-501 [Chain C UniProt coverage]=37.3% [Chain C UniRef90 accession]=UniRef90_Q12933 [Chain C UniRef90 boundaries]=315-501 [Related structures]=1d00 [Entry] [Accession]=DI3000008 [Disorder status]=Inferred from motif [Kd]=3.00E-07 [Name]=TNF receptor associated factor 2 in complex with a peptide from CD30 [Source organism]=Homo sapiens [PDB ID]=1d01 [PDB chain IDs]=G:DEF [PDB note]=Chains A, B, C, H and I were removed as chains D, E, F and G highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=MATH [Type chain G]=Disordered [Evidence chain G]=The protein region involved in the interaction contains a known functional linear motif (LIG_TRAF2_1). [Type chain D]=Ordered component [Evidence chain D]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4. [Type chain E]=Ordered component [Evidence chain E]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4. [Type chain F]=Ordered component [Evidence chain F]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4. [Chain G name]=Tumor necrosis factor receptor superfamily member 8 [Chain G source organism]=Homo sapiens [Chain G UniProt accession]=P28908 [Chain G UniProt boundaries]=576-583 [Chain G UniProt coverage]=1.3% [Chain G UniRef90 accession]=UniRef90_P28908 [Chain G UniRef90 boundaries]=576-583 [Chain D name]=TNF receptor-associated factor 2 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=Q12933 [Chain D UniProt boundaries]=334-501 [Chain D UniProt coverage]=33.5% [Chain D UniRef90 accession]=UniRef90_Q12933 [Chain D UniRef90 boundaries]=334-501 [Chain E name]=TNF receptor-associated factor 2 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=Q12933 [Chain E UniProt boundaries]=334-501 [Chain E UniProt coverage]=33.5% [Chain E UniRef90 accession]=UniRef90_Q12933 [Chain E UniRef90 boundaries]=334-501 [Chain F name]=TNF receptor-associated factor 2 [Chain F source organism]=Homo sapiens [Chain F UniProt accession]=Q12933 [Chain F UniProt boundaries]=334-501 [Chain F UniProt coverage]=33.5% [Chain F UniRef90 accession]=UniRef90_Q12933 [Chain F UniRef90 boundaries]=334-501 [Entry] [Accession]=DI3000009 [Disorder status]=Inferred from motif [Kd]=3.00E-07 [Name]=TNF receptor associated factor 2 in complex with a peptide from OX40 [Source organism]=Homo sapiens [PDB ID]=1d0a [PDB chain IDs]=G:ABC [PDB note]=Chains D, E, F, H, I, J, K and L were removed as chains A, B, C and G highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=MATH [Type chain G]=Disordered [Evidence chain G]=The protein region involved in the interaction contains a known functional linear motif (LIG_TRAF2_1). [Type chain A]=Ordered component [Evidence chain A]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4. [Type chain B]=Ordered component [Evidence chain B]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4. [Type chain C]=Ordered component [Evidence chain C]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4. [Modified residues chain B]=phosphothreonine#T#5|phosphothreonine#T#8 [Chain G name]=Tumor necrosis factor receptor superfamily member 4 [Chain G source organism]=Homo sapiens [Chain G UniProt accession]=P43489 [Chain G UniProt boundaries]=261-266 [Chain G UniProt coverage]=2.2% [Chain G UniRef90 accession]=UniRef90_P43489 [Chain G UniRef90 boundaries]=261-266 [Chain A name]=TNF receptor-associated factor 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q12933 [Chain A UniProt boundaries]=334-501 [Chain A UniProt coverage]=33.5% [Chain A UniRef90 accession]=UniRef90_Q12933 [Chain A UniRef90 boundaries]=334-501 [Chain B name]=TNF receptor-associated factor 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q12933 [Chain B UniProt boundaries]=334-501 [Chain B UniProt coverage]=33.5% [Chain B UniRef90 accession]=UniRef90_Q12933 [Chain B UniRef90 boundaries]=334-501 [Chain C name]=TNF receptor-associated factor 2 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q12933 [Chain C UniProt boundaries]=334-501 [Chain C UniProt coverage]=33.5% [Chain C UniRef90 accession]=UniRef90_Q12933 [Chain C UniRef90 boundaries]=334-501 [Entry] [Accession]=DI2100006 [Disorder status]=Confirmed [Kd]=1.30E-06 [Name]=Rrp6 and Rrp47 dimer in complex with a Mtr4 helicase peptide [Source organism]=Saccharomyces cerevisiae [PDB ID]=4wfd [PDB chain IDs]=C:AB [PDB note]=Chains D, E, F, G, H and I were removed as chains A, B and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=Rrp6:Rrp47 [Type chain C]=Disordered [Evidence chain C]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 4qu4). [Type chain A]=Ordered component [Evidence chain A]=Rrp6 forms an ordered complex together with Rrp47 serving as a platform for binding Mtr4 (PMID:25319414). The structure of the Rrp6:Rrp47 dimer is represented by PDB ID 4wfc. [Type chain B]=Ordered component [Evidence chain B]=Rrp6 forms an ordered complex together with Rrp47 serving as a platform for binding Mtr4 (PMID:25319414). The structure of the Rrp6:Rrp47 dimer is represented by PDB ID 4wfc. [Modified residues chain B]=phosphothreonine#T#5|phosphothreonine#T#8 [Chain C name]=ATP-dependent RNA helicase DOB1 [Chain C source organism]=Saccharomyces cerevisiae [Chain C UniProt accession]=P47047 [Chain C UniProt boundaries]=1-20 [Chain C UniProt coverage]=1.9% [Chain C UniRef90 accession]=UniRef90_P47047 [Chain C UniRef90 boundaries]=1-19 [Chain A name]=Exosome complex exonuclease RRP6 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=Q12149 [Chain A UniProt boundaries]=1-111 [Chain A UniProt coverage]=15.1% [Chain A UniRef90 accession]=UniRef90_Q12149 [Chain A UniRef90 boundaries]=1-111 [Chain B name]=Exosome complex protein LRP1 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P38801 [Chain B UniProt boundaries]=1-103 [Chain B UniProt coverage]=56% [Chain B UniRef90 accession]=UniRef90_P38801 [Chain B UniRef90 boundaries]=1-103 [Entry] [Accession]=DI1010066 [Disorder status]=Inferred from motif [Kd]=1.30E-06 [Name]=Yeast karyopherin (importin) alpha in complex with a c-Myc NLS peptide [Source organism]=Homo sapiens / Saccharomyces cerevisiae [PDB ID]=1ee4 [PDB chain IDs]=C:A [PDB note]=Chains D, B, E and F were removed as chains C and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=Armadillo repeat [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains 2 known functional linear motifs (TRG_NLS_MonoExtC_3, TRG_NLS_MonoExtN_4). [Type chain A]=Ordered [Evidence chain A]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain is represented by PDB ID 1bk5. [Chain C name]=Myc proto-oncogene protein [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P01106 [Chain C UniProt boundaries]=320-328 [Chain C UniProt coverage]=2.1% [Chain C UniRef90 accession]=UniRef90_P01106 [Chain C UniRef90 boundaries]=320-328 [Chain A name]=Importin subunit alpha [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=Q02821 [Chain A UniProt boundaries]=87-509 [Chain A UniProt coverage]=78% [Chain A UniRef90 accession]=UniRef90_Q02821 [Chain A UniRef90 boundaries]=87-509 [Entry] [Accession]=DI2010012 [Disorder status]=Inferred from motif [Kd]=1.30E-06 [Name]=Domain-swapped GRB2-SH2 bound to HGFR peptide [Source organism]=Homo sapiens / Rattus norvegicus [PDB ID]=1fyr [PDB chain IDs]=I:AB [PDB note]=Chains C, D, J, K and L were removed as chains A, B and I highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=SH2 [Type chain I]=Disordered [Evidence chain I]=The protein region involved in the interaction contains a known functional linear motif (LIG_SH2_GRB2). [Type chain A]=Ordered [Evidence chain A]=The domain-swapped SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain is represented by PDB ID 1fhs. [Type chain B]=Ordered [Evidence chain B]=The domain-swapped SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain is represented by PDB ID 1fhs. [Modified residues chain I]=phosphotyrosine#Y#0 [Modified residues chain B]=phosphothreonine#T#5|phosphothreonine#T#8 [Chain I name]=Hepatocyte growth factor receptor [Chain I source organism]=Homo sapiens [Chain I UniProt accession]=P08581 [Chain I UniProt boundaries]=1355-1359 [Chain I UniProt coverage]=0.4% [Chain I UniRef90 accession]=UniRef90_P08581 [Chain I UniRef90 boundaries]=1355-1359 [Chain A name]=Growth factor receptor-bound protein 2 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=P62994 [Chain A UniProt boundaries]=48-161 [Chain A UniProt coverage]=52.5% [Chain A UniRef90 accession]=UniRef90_P62993 [Chain A UniRef90 boundaries]=50-161 [Chain B name]=Growth factor receptor-bound protein 2 [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=P62994 [Chain B UniProt boundaries]=48-161 [Chain B UniProt coverage]=52.5% [Chain B UniRef90 accession]=UniRef90_P62993 [Chain B UniRef90 boundaries]=50-161 [Entry] [Accession]=DI2000015 [Disorder status]=Inferred from motif [Kd]=7.60E-08 [Name]=Human estrogen receptor alpha ligand-binding domain in complex with NCOA2 peptide [Source organism]=Homo sapiens [PDB ID]=1gwq [PDB chain IDs]=C:AB [PDB note]=Chain D was removed as chains A, B and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.45 [Domain]=Nuclear hormone receptor [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_NRBOX). [Type chain A]=Ordered component [Evidence chain A]=The nuclear hormone receptor domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form. A solved structure of the domain dimer without bound ligands is represented by PDB ID 1g50. [Type chain B]=Ordered component [Evidence chain B]=The nuclear hormone receptor domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form. A solved structure of the domain dimer without bound ligands is represented by PDB ID 1g50. [Modified residues chain B]=phosphothreonine#T#5|phosphothreonine#T#8 [Chain C name]=Nuclear receptor coactivator 2 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q15596 [Chain C UniProt boundaries]=688-696 [Chain C UniProt coverage]=0.6% [Chain C UniRef90 accession]=UniRef90_Q61026 [Chain C UniRef90 boundaries]=688-696 [Chain A name]=Estrogen receptor [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P03372 [Chain A UniProt boundaries]=301-548 [Chain A UniProt coverage]=41.7% [Chain A UniRef90 accession]=UniRef90_P03372 [Chain A UniRef90 boundaries]=301-548 [Chain B name]=Estrogen receptor [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P03372 [Chain B UniProt boundaries]=301-548 [Chain B UniProt coverage]=41.7% [Chain B UniRef90 accession]=UniRef90_P03372 [Chain B UniRef90 boundaries]=301-548 [Related structures]=1zky,2b1v,2b1z,2b23,2fai,2g44,2g5o,2p15,3erd,3q95,3q97,4iu7,4iui,4iv2,4iv4,4ivw,4ivy,4iw6,4iw8,4iwc,4iwf,4pp6,4ppp,4pps,4pxm,4zn7,4zn9,4znh,4zns,4znt,4znu,4znv,4znw,5di7,5did,5die,5dig,5dk9,5dkb,5dke,5dkg,5dks,5dl4,5dlr,5dmc,5dmf,5dp0,5drj,5drm,5dtv,5du5,5due,5dug,5duh,5dvs,5dvv,5dwe,5dwg,5dwi,5dwj,5dx3,5dxb,5dxe,5dxg,5dxk,5dxm,5dxp,5dxq,5dxr,5dy8,5dyb,5dyd,5dz0,5dz1,5dz3,5dzh,5dzi,5e0w,5e0x,5e14,5e15,5e19,5e1c,5egv,5ehj,5ei1,5eit,5hyr,5kcc,5kcd,5kce,5kcf,5kct,5kcu,5kcw,5kd9,5kr9,5kra,5krc,5krf,5krh,5kri,5krj,5krk,5krl,5krm,5kro,5tld,5tlf,5tlg,5tll,5tlm,5tlo,5tlp,5tlt,5tlu,5tlv,5tlx,5tly,5tm1,5tm2,5tm3,5tm4,5tm5,5tm6,5tm7,5tm8,5tm9,5tml,5tmm,5tmo,5tmq,5tmr,5tms,5tmt,5tmu,5tmv,5tmw,5tmz,5tn1,5tn3,5tn4,5tn5,5tn6,5tn7,5tn8,5u2d,1l2i,2q6j,2qa6,2qa8,2qab,2qgt,2qgw,2qh6,2qr9,2qse,2qxm,2qzo,3hlv,3hm1,3l03 [Entry] [Accession]=DI2000016 [Disorder status]=Inferred from motif [Kd]=5.00E-07 [Name]=Cyclin A:CDK2 in complex with an E2F peptide [Source organism]=Homo sapiens [PDB ID]=1h24 [PDB chain IDs]=E:AB [PDB note]=Chains C and D were removed as chains A, B and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.5 [Domain]=Cyclin A:Cdk2 [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (DOC_CYCLIN_1). [Type chain A]=Ordered component [Evidence chain A]=The cyclin A:Cdk2 complex involved in the interaction is known to form an ordered dimer, represented by PDB ID 1jst. [Type chain B]=Ordered component [Evidence chain B]=The cyclin A:Cdk2 complex involved in the interaction is known to form an ordered dimer, represented by PDB ID 1jst. [Modified residues chain B]=phosphothreonine#T#5|phosphothreonine#T#8 [Chain E name]=Transcription factor E2F1 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=Q01094 [Chain E UniProt boundaries]=87-95 [Chain E UniProt coverage]=2.1% [Chain E UniRef90 accession]=UniRef90_Q01094 [Chain E UniRef90 boundaries]=87-95 [Chain A name]=Cyclin-dependent kinase 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P24941 [Chain A UniProt boundaries]=1-298 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P24941 [Chain A UniRef90 boundaries]=1-298 [Chain B name]=Cyclin-A2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P20248 [Chain B UniProt boundaries]=174-432 [Chain B UniProt coverage]=60% [Chain B UniRef90 accession]=UniRef90_P20248 [Chain B UniRef90 boundaries]=174-432 [Entry] [Accession]=DI2000017 [Disorder status]=Confirmed [Kd]=2.90E-06 [Name]=Cyclin A:CDK2 in complex with a p53 peptide [Source organism]=Homo sapiens [PDB ID]=1h26 [PDB chain IDs]=E:AB [PDB note]=Chains C and D were removed as chains A, B and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.24 [Domain]=Cyclin A:Cdk2 [Type chain E]=Disordered [Evidence chain E]=The 320-393 region described in DisProt entry DP00086 and the 364-389 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a KXL motif (PMID:12501191). [Type chain A]=Ordered component [Evidence chain A]=The cyclin A:Cdk2 complex involved in the interaction is known to form an ordered dimer, represented by PDB ID 1jst. [Type chain B]=Ordered component [Evidence chain B]=The cyclin A:Cdk2 complex involved in the interaction is known to form an ordered dimer, represented by PDB ID 1jst. [Modified residues chain B]=phosphothreonine#T#5|phosphothreonine#T#8 [Chain E name]=Cellular tumor antigen p53 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P04637 [Chain E UniProt boundaries]=376-386 [Chain E UniProt coverage]=2.8% [Chain E UniRef90 accession]=UniRef90_P04637 [Chain E UniRef90 boundaries]=376-386 [Chain A name]=Cyclin-dependent kinase 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P24941 [Chain A UniProt boundaries]=1-298 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P24941 [Chain A UniRef90 boundaries]=1-298 [Chain B name]=Cyclin-A2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P20248 [Chain B UniProt boundaries]=174-432 [Chain B UniProt coverage]=60% [Chain B UniRef90 accession]=UniRef90_P20248 [Chain B UniRef90 boundaries]=174-432 [Entry] [Accession]=DI2000018 [Disorder status]=Inferred from motif [Kd]=1.80E-06 [Name]=Cyclin A:CDK2 in complex with a peptide from retinoblastoma-associated protein [Source organism]=Homo sapiens [PDB ID]=1h25 [PDB chain IDs]=E:AB [PDB note]=Chains C and D were removed as chains A, B and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.5 [Domain]=Cyclin A:Cdk2 [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (DOC_CYCLIN_1). [Type chain A]=Ordered component [Evidence chain A]=The cyclin A:Cdk2 complex involved in the interaction is known to form an ordered dimer, represented by PDB ID 1jst. [Type chain B]=Ordered component [Evidence chain B]=The cyclin A:Cdk2 complex involved in the interaction is known to form an ordered dimer, represented by PDB ID 1jst. [Modified residues chain B]=phosphothreonine#T#5|phosphothreonine#T#8 [Chain E name]=Retinoblastoma-associated protein [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P06400 [Chain E UniProt boundaries]=868-878 [Chain E UniProt coverage]=1.2% [Chain E UniRef90 accession]=UniRef90_P06400 [Chain E UniRef90 boundaries]=868-878 [Chain A name]=Cyclin-dependent kinase 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P24941 [Chain A UniProt boundaries]=1-298 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P24941 [Chain A UniRef90 boundaries]=1-298 [Chain B name]=Cyclin-A2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P20248 [Chain B UniProt boundaries]=174-432 [Chain B UniProt coverage]=60% [Chain B UniRef90 accession]=UniRef90_P20248 [Chain B UniRef90 boundaries]=174-432 [Entry] [Accession]=DI2000019 [Disorder status]=Inferred from motif [Kd]=3.00E-07 [Name]=Cyclin A:CDK2 in complex with a peptide from P107 [Source organism]=Homo sapiens [PDB ID]=1h28 [PDB chain IDs]=E:AB [PDB note]=Chains C, D and F were removed as chains A, B and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=Cyclin A:Cdk2 [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (DOC_CYCLIN_1). [Type chain A]=Ordered component [Evidence chain A]=The cyclin A:Cdk2 complex involved in the interaction is known to form an ordered dimer, represented by PDB ID 1jst. [Type chain B]=Ordered component [Evidence chain B]=The cyclin A:Cdk2 complex involved in the interaction is known to form an ordered dimer, represented by PDB ID 1jst. [Modified residues chain B]=phosphothreonine#T#5|phosphothreonine#T#8 [Chain E name]=Retinoblastoma-like protein 1 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P28749 [Chain E UniProt boundaries]=653-663 [Chain E UniProt coverage]=1% [Chain E UniRef90 accession]=UniRef90_P28749 [Chain E UniRef90 boundaries]=653-663 [Chain A name]=Cyclin-dependent kinase 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P24941 [Chain A UniProt boundaries]=1-298 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P24941 [Chain A UniRef90 boundaries]=1-298 [Chain B name]=Cyclin-A2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P20248 [Chain B UniProt boundaries]=174-432 [Chain B UniProt coverage]=60% [Chain B UniRef90 accession]=UniRef90_P20248 [Chain B UniRef90 boundaries]=174-432 [Entry] [Accession]=DI1100059 [Disorder status]=Inferred from motif [Kd]=2.40E-07 [Name]=DIAP1-BIR2/GRIM complex [Source organism]=Drosophila melanogaster [PDB ID]=1jd5 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=BIR [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_BIR_III_3). [Type chain A]=Ordered [Evidence chain A]=The BIR domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00653). A solved monomeric structure of the domain is represented by PDB ID 1jd4. [Chain B name]=Cell death protein Grim [Chain B source organism]=Drosophila melanogaster [Chain B UniProt accession]=Q24570 [Chain B UniProt boundaries]=2-11 [Chain B UniProt coverage]=7.2% [Chain B UniRef90 accession]=UniRef90_Q24570 [Chain B UniRef90 boundaries]=2-11 [Chain A name]=Death-associated inhibitor of apoptosis 1 [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=Q24306 [Chain A UniProt boundaries]=201-324 [Chain A UniProt coverage]=28.3% [Chain A UniRef90 accession]=UniRef90_Q24306 [Chain A UniRef90 boundaries]=201-323 [Entry] [Accession]=DI1100060 [Disorder status]=Inferred from motif [Kd]=4.10E-08 [Name]=DIAP1-BIR2/HID complex [Source organism]=Drosophila melanogaster [PDB ID]=1jd6 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.70 [Domain]=BIR [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_BIR_III_3). [Type chain A]=Ordered [Evidence chain A]=The BIR domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00653). A solved monomeric structure of the domain is represented by PDB ID 1jd4. [Chain B name]=Cell death protein hid [Chain B source organism]=Drosophila melanogaster [Chain B UniProt accession]=Q24106 [Chain B UniProt boundaries]=2-11 [Chain B UniProt coverage]=2.4% [Chain B UniRef90 accession]=UniRef90_Q24106 [Chain B UniRef90 boundaries]=2-11 [Chain A name]=Death-associated inhibitor of apoptosis 1 [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=Q24306 [Chain A UniProt boundaries]=201-323 [Chain A UniProt coverage]=28.1% [Chain A UniRef90 accession]=UniRef90_Q24306 [Chain A UniRef90 boundaries]=201-323 [Entry] [Accession]=DI1100061 [Disorder status]=Inferred from motif [Kd]=8.00E-07 [Name]=SH3 domain from C-terminal SRC kinase complexed with a tyrosine phosphatase PEP peptide [Source organism]=Mus musculus [PDB ID]=1jeg [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH3 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_SH3_2). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00018). A solved monomeric structure of the domain from a hologous protein is represented by PDB ID 2a36. [Chain B name]=Tyrosine-protein phosphatase non-receptor type 22 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=P29352 [Chain B UniProt boundaries]=605-629 [Chain B UniProt coverage]=3.1% [Chain B UniRef90 accession]=UniRef90_P29352 [Chain B UniRef90 boundaries]=605-629 [Chain A name]=Tyrosine-protein kinase CSK [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P41241 [Chain A UniProt boundaries]=1-83 [Chain A UniProt coverage]=18.4% [Chain A UniRef90 accession]=UniRef90_P41240 [Chain A UniRef90 boundaries]=1-83 [Entry] [Accession]=DI1100062 [Disorder status]=Inferred from motif [Kd]=1.29E-05 [Name]=FHA2 domain of RAD53 complexed with a phosphothreonyl peptide from RAD9 (599-607) [Source organism]=Saccharomyces cerevisiae [PDB ID]=1k2n [PDB chain IDs]=P:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=FHA [Type chain P]=Disordered [Evidence chain P]=The protein region involved in the interaction contains a known functional linear motif (LIG_FHA_1). [Type chain A]=Ordered [Evidence chain A]=The FHA domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00498). A solved monomeric structure of the domain is represented by PDB ID 1dmz. [Modified residues chain P]=phosphothreonine#T#603 [Chain P name]=DNA repair protein RAD9 [Chain P source organism]=Saccharomyces cerevisiae [Chain P UniProt accession]=P14737 [Chain P UniProt boundaries]=599-607 [Chain P UniProt coverage]=0.7% [Chain P UniRef90 accession]=UniRef90_P14737 [Chain P UniRef90 boundaries]=599-607 [Chain A name]=Serine/threonine-protein kinase RAD53 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P22216 [Chain A UniProt boundaries]=573-730 [Chain A UniProt coverage]=19.2% [Chain A UniRef90 accession]=UniRef90_P22216 [Chain A UniRef90 boundaries]=573-730 [Related structures]=1j4l [Entry] [Accession]=DI1100063 [Disorder status]=Inferred from motif [Kd]=3.60E-07 (PMID:11124038) [Name]=FHA1 domain of RAD53 complexed with a phosphothreonyl peptide from RAD9 (188-200) [Source organism]=Saccharomyces cerevisiae [PDB ID]=1k3q [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=FHA [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_FHA_2). [Type chain A]=Ordered [Evidence chain A]=The FHA domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00498). A solved monomeric structure of the domain is represented by PDB ID 1g3g. [Modified residues chain B]=phosphothreonine#T#169 [Chain B name]=DNA repair protein RAD9 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P14737 [Chain B UniProt boundaries]=188-200 [Chain B UniProt coverage]=1% [Chain B UniRef90 accession]=UniRef90_P14737 [Chain B UniRef90 boundaries]=188-200 [Chain A name]=Serine/threonine-protein kinase RAD53 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P22216 [Chain A UniProt boundaries]=14-164 [Chain A UniProt coverage]=18.4% [Chain A UniRef90 accession]=UniRef90_P22216 [Chain A UniRef90 boundaries]=14-164 [Related structures]=1j4q [Entry] [Accession]=DI1000211 [Disorder status]=Inferred from motif [Kd]=3.60E-07 (PMID:11124038) [Name]=Human PPAR-alpha ligand-binding domain in complex with a SMRT corepressor motif [Source organism]=Homo sapiens [PDB ID]=1kkq [PDB chain IDs]=E:A [PDB note]=Chains B, C, D, F, G and H were removed as chains A and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.00 [Domain]=Nuclear hormone receptor [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (LIG_CORNRBOX). [Type chain A]=Ordered [Evidence chain A]=The nuclear hormone receptor domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00104). A solved monomeric structure of the domain is represented by PDB ID 1i7g. [Chain E name]=Nuclear receptor corepressor 2 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=Q9Y618 [Chain E UniProt boundaries]=2347-2365 [Chain E UniProt coverage]=0.8% [Chain E UniRef90 accession]=UniRef90_Q9Y618 [Chain E UniRef90 boundaries]=2347-2365 [Chain A name]=Peroxisome proliferator-activated receptor alpha [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q07869 [Chain A UniProt boundaries]=200-468 [Chain A UniProt coverage]=57.5% [Chain A UniRef90 accession]=UniRef90_Q07869 [Chain A UniRef90 boundaries]=200-468 [Entry] [Accession]=DI1110018 [Disorder status]=Confirmed [Kd]=3.60E-07 (PMID:11124038) [Name]=AP-2 clathrin adaptor alpha-appendage in comple with Epsin DPW peptide [Source organism]=Rattus norvegicus / Mus musculus [PDB ID]=1ky6 [PDB chain IDs]=P:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Adaptin C-terminal domain [Type chain P]=Disordered [Evidence chain P]=The 144-575 region described in DisProt entry DP00251 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_AP2alpha_2). [Type chain A]=Ordered [Evidence chain A]=The adaptin C-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02883/PF02296). A solved monomeric structure of the domain is represented by PDB ID 1b9k. [Chain P name]=Epsin-1 [Chain P source organism]=Rattus norvegicus [Chain P UniProt accession]=O88339 [Chain P UniProt boundaries]=375-381 [Chain P UniProt coverage]=1.2% [Chain P UniRef90 accession]=UniRef90_O88339 [Chain P UniRef90 boundaries]=375-381 [Chain A name]=AP-2 complex subunit alpha-2 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P17427 [Chain A UniProt boundaries]=701-938 [Chain A UniProt coverage]=25.4% [Chain A UniRef90 accession]=UniRef90_P17427 [Chain A UniRef90 boundaries]=701-938 [Entry] [Accession]=DI1010067 [Disorder status]=Inferred from motif [Kd]=3.60E-07 (PMID:11124038) [Name]=AP-2 clathrin adaptor alpha-appendage in complex with amphiphysin peptide [Source organism]=Homo sapiens / Mus musculus [PDB ID]=1ky7 [PDB chain IDs]=P:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.15 [Domain]=Adaptin C-terminal domain [Type chain P]=Disordered [Evidence chain P]=The protein region involved in the interaction contains a known functional linear motif (LIG_AP2alpha_1). [Type chain A]=Ordered [Evidence chain A]=The adaptin C-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02883/PF02296). A solved monomeric structure of the domain is represented by PDB ID 1b9k. [Chain P name]=Amphiphysin [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=P49418 [Chain P UniProt boundaries]=322-331 [Chain P UniProt coverage]=1.4% [Chain P UniRef90 accession]=UniRef90_P49418 [Chain P UniRef90 boundaries]=322-331 [Chain A name]=AP-2 complex subunit alpha-2 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P17427 [Chain A UniProt boundaries]=701-938 [Chain A UniProt coverage]=25.4% [Chain A UniRef90 accession]=UniRef90_P17427 [Chain A UniRef90 boundaries]=701-938 [Entry] [Accession]=DI1100064 [Disorder status]=Inferred from motif [Kd]=3.60E-07 (PMID:11124038) [Name]=AP-2 clathrin adaptor alpha-appendage in comple with EPS15 DPF peptide [Source organism]=Mus musculus [PDB ID]=1kyu [PDB chain IDs]=P:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=Adaptin C-terminal domain [Type chain P]=Disordered [Evidence chain P]=The protein region involved in the interaction contains a known functional linear motif (LIG_AP2alpha_2). [Type chain A]=Ordered [Evidence chain A]=The adaptin C-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02883/PF02296). A solved monomeric structure of the domain is represented by PDB ID 1b9k. [Chain P name]=Epidermal growth factor receptor substrate 15 [Chain P source organism]=Mus musculus [Chain P UniProt accession]=P42567 [Chain P UniProt boundaries]=627-632 [Chain P UniProt coverage]=0.7% [Chain P UniRef90 accession]=UniRef90_P42567 [Chain P UniRef90 boundaries]=627-632 [Chain A name]=AP-2 complex subunit alpha-2 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P17427 [Chain A UniProt boundaries]=701-938 [Chain A UniProt coverage]=25.4% [Chain A UniRef90 accession]=UniRef90_P17427 [Chain A UniRef90 boundaries]=701-938 [Related structures]=1kyf [Entry] [Accession]=DI1000212 [Disorder status]=Inferred from motif [Kd]=3.60E-07 (PMID:11124038) [Name]=Human glucocorticoid receptor ligand-binding domain bound to a TIF2 coactivator motif [Source organism]=Homo sapiens [PDB ID]=1m2z [PDB chain IDs]=B:A [PDB note]=Chains D and E were removed as chains B and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=Nuclear hormone receptor [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_NRBOX). [Type chain A]=Ordered [Evidence chain A]=The nuclear hormone receptor domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00104). A solved monomeric structure of the domain is represented by PDB ID 1nhz. [Chain B name]=Nuclear receptor coactivator 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q15596 [Chain B UniProt boundaries]=734-754 [Chain B UniProt coverage]=1.4% [Chain B UniRef90 accession]=UniRef90_Q61026 [Chain B UniRef90 boundaries]=734-754 [Chain A name]=Glucocorticoid receptor [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P04150 [Chain A UniProt boundaries]=521-777 [Chain A UniProt coverage]=33.1% [Chain A UniRef90 accession]=UniRef90_P04150 [Chain A UniRef90 boundaries]=521-777 [Related structures]=1p93,3cld,3e7c,3k22,3k23,4csj,4p6w,4p6x,4udc,4udd,5g3j,5g5w [Entry] [Accession]=DI1110019 [Disorder status]=Inferred from motif [Kd]=3.60E-07 (PMID:11124038) [Name]=Phosphotyrosine binding domain (PTB) of mouse Disabled 2 (Dab2) in complex with an amyloid beta A4 peptide [Source organism]=Rattus norvegicus / Mus musculus [PDB ID]=1m7e [PDB chain IDs]=D:A [PDB note]=Chains B, C, E and F were removed as chains D and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.45 [Domain]=PID [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a known functional linear motif (LIG_PTB_Apo_2). [Type chain A]=Ordered [Evidence chain A]=The PID domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00640). A solved monomeric structure of the domain is represented by PDB ID 1p3r. [Chain D name]=Amyloid beta A4 protein [Chain D source organism]=Rattus norvegicus [Chain D UniProt accession]=P08592 [Chain D UniProt boundaries]=755-763 [Chain D UniProt coverage]=1.2% [Chain D UniRef90 accession]=UniRef90_P05067 [Chain D UniRef90 boundaries]=755-763 [Chain A name]=Disabled homolog 2 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P98078 [Chain A UniProt boundaries]=33-191 [Chain A UniProt coverage]=20.8% [Chain A UniRef90 accession]=UniRef90_P98078 [Chain A UniRef90 boundaries]=33-191 [Entry] [Accession]=DI1000213 [Disorder status]=Inferred from motif [Kd]=5.00E-05 [Name]=ERBIN PDZ domain bound to the C-terminal tail of the ErbB2 receptor [Source organism]=Homo sapiens [PDB ID]=1mfg [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.25 [Domain]=PDZ [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_2). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 2h3l. [Chain B name]=Receptor tyrosine-protein kinase erbB-2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04626 [Chain B UniProt boundaries]=1247-1255 [Chain B UniProt coverage]=0.7% [Chain B UniRef90 accession]=UniRef90_P04626 [Chain B UniRef90 boundaries]=1247-1255 [Chain A name]=Erbin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96RT1 [Chain A UniProt boundaries]=1321-1412 [Chain A UniProt coverage]=6.5% [Chain A UniRef90 accession]=UniRef90_Q96RT1 [Chain A UniRef90 boundaries]=1321-1412 [Related structures]=1mfl [Entry] [Accession]=DI1010068 [Disorder status]=Inferred from motif [Kd]=5.00E-05 [Name]=Sixth PDZ domain of GRIP1 in complex with liprin C-terminal peptide [Source organism]=Homo sapiens / Rattus norvegicus [PDB ID]=1n7f [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains C and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=PDZ [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_2). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 1n7e. [Chain C name]=Liprin-alpha-1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q13136 [Chain C UniProt boundaries]=1195-1202 [Chain C UniProt coverage]=0.7% [Chain C UniRef90 accession]=UniRef90_Q13136 [Chain C UniRef90 boundaries]=1195-1202 [Chain A name]=Glutamate receptor-interacting protein 1 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=P97879 [Chain A UniProt boundaries]=665-761 [Chain A UniProt coverage]=8.7% [Chain A UniRef90 accession]=UniRef90_Q9Y3R0 [Chain A UniRef90 boundaries]=665-761 [Entry] [Accession]=DI1000214 [Disorder status]=Confirmed [Kd]=5.00E-05 [Name]=Akt/Protein Kinase B in complex with Gsk-3 peptide [Source organism]=Homo sapiens [PDB ID]=1o6l [PDB chain IDs]=C:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.6 [Domain]=Protein kinase [Type chain C]=Disordered [Evidence chain C]=The 1-34 region described in DisProt entry DP00385 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (DOC_AGCK_PIF_1). [Type chain A]=Ordered [Evidence chain A]=The protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 1gzn. [Chain C name]=Glycogen synthase kinase-3 beta [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P49841 [Chain C UniProt boundaries]=3-12 [Chain C UniProt coverage]=2.4% [Chain C UniRef90 accession]=UniRef90_P49841 [Chain C UniRef90 boundaries]=3-12 [Chain A name]=RAC-beta serine/threonine-protein kinase [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P31751 [Chain A UniProt boundaries]=146-469 [Chain A UniProt coverage]=67.4% [Chain A UniRef90 accession]=UniRef90_P31751 [Chain A UniRef90 boundaries]=146-469 [Related structures]=1o6k,2jdo,2jdr,2uw9,2x39,2xh5,3e87,3e88,3e8d [Entry] [Accession]=DI1000215 [Disorder status]=Inferred from motif [Kd]=1.90E-06 [Name]=PDZ2 of sytenin with an interleukin 5 receptor alpha peptide [Source organism]=Homo sapiens [PDB ID]=1obx [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.35 [Domain]=PDZ [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_1). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 1nte. [Chain B name]=Interleukin-5 receptor subunit alpha [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q01344 [Chain B UniProt boundaries]=413-420 [Chain B UniProt coverage]=1.9% [Chain B UniRef90 accession]=UniRef90_Q01344 [Chain B UniRef90 boundaries]=413-420 [Chain A name]=Syntenin-1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O00560 [Chain A UniProt boundaries]=192-270 [Chain A UniProt coverage]=26.5% [Chain A UniRef90 accession]=UniRef90_O00560 [Chain A UniRef90 boundaries]=197-270 [Related structures]=1obz [Entry] [Accession]=DI1010069 [Disorder status]=Inferred from motif [Kd]=1.80E-07 [Name]=Retinoblastoma-associated protein peptide bound to importin alpha-2 subunit [Source organism]=Homo sapiens / Mus musculus [PDB ID]=1pjm [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=Armadillo repeat [Type chain A]=Disordered [Evidence chain A]=The protein region involved in the interaction contains a known functional linear motif (TRG_NLS_Bipartite_1). [Type chain B]=Ordered [Evidence chain B]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain is represented by PDB ID 1ial. [Chain A name]=Retinoblastoma-associated protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P06400 [Chain A UniProt boundaries]=858-877 [Chain A UniProt coverage]=2.2% [Chain A UniRef90 accession]=UniRef90_P06400 [Chain A UniRef90 boundaries]=858-877 [Chain B name]=Importin subunit alpha-1 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=P52293 [Chain B UniProt boundaries]=70-529 [Chain B UniProt coverage]=87% [Chain B UniRef90 accession]=UniRef90_P52293 [Chain B UniRef90 boundaries]=70-529 [Entry] [Accession]=DI1110020 [Disorder status]=Inferred from motif [Kd]=2.20E-08 [Name]=NLS from histone-binding protein N1/N2 bound to importin alpha-2 subunit [Source organism]=Xenopus laevis / Mus musculus [PDB ID]=1pjn [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=Armadillo repeat [Type chain A]=Disordered [Evidence chain A]=The protein region involved in the interaction contains a known functional linear motif (TRG_NLS_Bipartite_1). [Type chain B]=Ordered [Evidence chain B]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain is represented by PDB ID 1ial. [Chain A name]=Histone-binding protein N1/N2 [Chain A source organism]=Xenopus laevis [Chain A UniProt accession]=P06180 [Chain A UniProt boundaries]=532-553 [Chain A UniProt coverage]=3.7% [Chain A UniRef90 accession]=UniRef90_P06180 [Chain A UniRef90 boundaries]=532-553 [Chain B name]=Importin subunit alpha-1 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=P52293 [Chain B UniProt boundaries]=70-529 [Chain B UniProt coverage]=87% [Chain B UniRef90 accession]=UniRef90_P52293 [Chain B UniRef90 boundaries]=70-529 [Entry] [Accession]=DI1120010 [Disorder status]=Inferred from motif [Kd]=1.00E-08 [Name]=Non-phosphorylated SV40 CN peptide bound to importin alpha-2 subunit [Source organism]=Simian virus 40 / Mus musculus [PDB ID]=1q1t [PDB chain IDs]=A:C [PDB note]=Chain B was removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=Armadillo repeat [Type chain A]=Disordered [Evidence chain A]=The protein region involved in the interaction contains 3 known functional linear motifs (TRG_NLS_MonoCore_2, TRG_NLS_MonoExtC_3, TRG_NLS_MonoExtN_4). [Type chain C]=Ordered [Evidence chain C]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain is represented by PDB ID 1ial. [Chain A name]=Large T antigen [Chain A source organism]=Simian virus 40 [Chain A UniProt accession]=P03070 [Chain A UniProt boundaries]=110-134 [Chain A UniProt coverage]=3.5% [Chain A UniRef90 accession]=UniRef90_P03070 [Chain A UniRef90 boundaries]=110-134 [Chain C name]=Importin subunit alpha-1 [Chain C source organism]=Mus musculus [Chain C UniProt accession]=P52293 [Chain C UniProt boundaries]=70-529 [Chain C UniProt coverage]=87% [Chain C UniRef90 accession]=UniRef90_P52293 [Chain C UniRef90 boundaries]=70-529 [Related structures]=1ejl,1q1s [Entry] [Accession]=DI1100065 [Disorder status]=Inferred from motif [Kd]=1.05E-06 [Name]=SH3 domain of betaPIX in complex with a high affinity peptide from PAK2 [Source organism]=Rattus norvegicus [PDB ID]=2df6 [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.30 [Domain]=SH3 [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (atypical SH3-binding motif PxxxPR, PMID:16527308). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF07653). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1shg. [Chain C name]=Serine/threonine-protein kinase PAK 3 [Chain C source organism]=Rattus norvegicus [Chain C UniProt accession]=Q62829 [Chain C UniProt boundaries]=188-205 [Chain C UniProt coverage]=3.3% [Chain C UniRef90 accession]=UniRef90_Q62829 [Chain C UniRef90 boundaries]=188-205 [Chain A name]=Rho guanine nucleotide exchange factor 7 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=O55043 [Chain A UniProt boundaries]=5-63 [Chain A UniProt coverage]=9.1% [Chain A UniRef90 accession]=UniRef90_Q9ES28-4 [Chain A UniRef90 boundaries]=115-168 [Entry] [Accession]=DI2100007 [Disorder status]=Confirmed [Kd]=1.05E-06 [Name]=RbcX-IIa from Chlamydomonas reinhardtii in complex with RbcL C-terminal tail [Source organism]=Chlamydomonas reinhardtii [PDB ID]=5bs2 [PDB chain IDs]=R:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.97 [Domain]=RcbX [Type chain R]=Disordered [Evidence chain R]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 2v69). [Type chain A]=Ordered component [Evidence chain A]=The RcbX domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF02341). A solved structure of the domain dimer without bound ligands is represented by PDB ID 5bs1. [Type chain B]=Ordered component [Evidence chain B]=The RcbX domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF02341). A solved structure of the domain dimer without bound ligands is represented by PDB ID 5bs1. [Chain R name]=Ribulose bisphosphate carboxylase large chain [Chain R source organism]=Chlamydomonas reinhardtii [Chain R UniProt accession]=P00877 [Chain R UniProt boundaries]=462-467 [Chain R UniProt coverage]=1.3% [Chain R UniRef90 accession]=UniRef90_P00877 [Chain R UniRef90 boundaries]=462-467 [Chain A name]=Predicted protein (Fragment) [Chain A source organism]=Chlamydomonas reinhardtii [Chain A UniProt accession]=A8HQH2 [Chain A UniProt boundaries]=25-156 [Chain A UniProt coverage]=65.7% [Chain A UniRef90 accession]=UniRef90_A8HQH2 [Chain A UniRef90 boundaries]=37-156 [Chain B name]=Predicted protein (Fragment) [Chain B source organism]=Chlamydomonas reinhardtii [Chain B UniProt accession]=A8HQH2 [Chain B UniProt boundaries]=25-156 [Chain B UniProt coverage]=65.7% [Chain B UniRef90 accession]=UniRef90_A8HQH2 [Chain B UniRef90 boundaries]=37-156 [Related structures]=1gk8,1ir2,1uw9,1uwa,1uzd,1uzh,2v63,2v67,2v68,2v6a,2vdh,2vdi [Entry] [Accession]=DI1200007 [Disorder status]=Confirmed [Kd]=1.00E-06 [Name]=VirB9 C-terminal domain in complex with VirB7 N-terminal domain from Xanthomonas citri's T4SS [Source organism]=Xanthomonas axonopodis pv. citri [PDB ID]=2n01 [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=CagX [Type chain A]=Disordered [Evidence chain A]=The interacting region of the protein has been shown to be highly flexible based on NMR spectrum (PDB ID: 2l4w). [Type chain B]=Ordered [Evidence chain B]=The CagX domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03524). A solved structure of the domain without the bound peptide from a homologous protein is represented by PDB ID 2ypw. [Chain A name]=Uncharacterized protein [Chain A source organism]=Xanthomonas axonopodis pv. citri [Chain A UniProt accession]=Q8PJB3 [Chain A UniProt boundaries]=23-47 [Chain A UniProt coverage]=18% [Chain A UniRef90 accession]=UniRef90_U4M802 [Chain A UniRef90 boundaries]=24-46 [Chain B name]=VirB9 protein [Chain B source organism]=Xanthomonas axonopodis pv. citri [Chain B UniProt accession]=Q8PJB5 [Chain B UniProt boundaries]=150-255 [Chain B UniProt coverage]=41.6% [Chain B UniRef90 accession]=UniRef90_B0RRE4 [Chain B UniRef90 boundaries]=150-255 [Entry] [Accession]=DI1000216 [Disorder status]=Confirmed [Kd]=1.44E-05 [Name]=AIP TPR domain in complex with human Hsp90 peptide [Source organism]=Homo sapiens [PDB ID]=4aif [PDB chain IDs]=D:A [PDB note]=Chains B and E were removed as chains A and D highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.01 [Domain]=Tetratricopeptide [Type chain D]=Disordered [Evidence chain D]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 3q6n, 3q6m). The protein region involved in the interaction contains a known functional linear motif (LIG_TPR). [Type chain A]=Ordered [Evidence chain A]=The tetratricopeptide domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF08311). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2lah. [Chain D name]=Heat shock protein HSP 90-alpha [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P07900 [Chain D UniProt boundaries]=726-732 [Chain D UniProt coverage]=1% [Chain D UniRef90 accession]=UniRef90_P07900 [Chain D UniRef90 boundaries]=726-732 [Chain A name]=AH receptor-interacting protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O00170 [Chain A UniProt boundaries]=172-315 [Chain A UniProt coverage]=43.6% [Chain A UniRef90 accession]=UniRef90_O00170 [Chain A UniRef90 boundaries]=173-315 [Entry] [Accession]=DI1000217 [Disorder status]=Inferred from motif [Kd]=1.24E-06 (PMID:23317506) [Name]=ICAP1 PTB domain in complex with a KRIT1 peptide [Source organism]=Homo sapiens [PDB ID]=4jif [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=PID [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (NPXY motif, PMID:23695561). [Type chain A]=Ordered [Evidence chain A]=The PID domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4dbb. [Chain B name]=Krev interaction trapped protein 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O00522 [Chain B UniProt boundaries]=169-198 [Chain B UniProt coverage]=4.1% [Chain B UniRef90 accession]=UniRef90_O00522 [Chain B UniRef90 boundaries]=169-198 [Chain A name]=Integrin beta-1-binding protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O14713 [Chain A UniProt boundaries]=47-200 [Chain A UniProt coverage]=77% [Chain A UniRef90 accession]=UniRef90_O14713 [Chain A UniRef90 boundaries]=49-200 [Related structures]=4dx8 [Entry] [Accession]=DI1000218 [Disorder status]=Confirmed [Kd]=5.00E-06 [Name]=ICAP1 in complex with integrin beta 1 cytoplasmic tail [Source organism]=Homo sapiens [PDB ID]=4dx9 [PDB chain IDs]=B:A [PDB note]=All chains except for A and B were removed as chains A and B highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.99 [Domain]=PID [Type chain B]=Disordered [Evidence chain B]=The cytoplasmic tail of integrins have been shown to be intrinsically unstructured (PMID:21421922). [Type chain A]=Ordered [Evidence chain A]=The PID domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4dbb. [Chain B name]=Integrin beta-1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P05556 [Chain B UniProt boundaries]=784-798 [Chain B UniProt coverage]=1.9% [Chain B UniRef90 accession]=UniRef90_P05556 [Chain B UniRef90 boundaries]=784-798 [Chain A name]=Integrin beta-1-binding protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O14713 [Chain A UniProt boundaries]=49-200 [Chain A UniProt coverage]=76% [Chain A UniRef90 accession]=UniRef90_O14713 [Chain A UniRef90 boundaries]=49-200 [Entry] [Accession]=DI2010013 [Disorder status]=Confirmed [Kd]=2.61E-07 [Name]=14-3-3 protein zeta in complex with Thr758 phosphorylated integrin beta2 peptide [Source organism]=Homo sapiens / Bos taurus [PDB ID]=2v7d [PDB chain IDs]=P:AB [PDB note]=Chains C, D, Q, R and S were removed as chains A, B and P highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.5 [Domain]=14-3-3 [Type chain P]=Disordered [Evidence chain P]=The cytoplasmic tail of integrins have been shown to be intrinsically unstructured (PMID:21421922). [Type chain A]=Ordered component [Evidence chain A]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1a4o. [Type chain B]=Ordered component [Evidence chain B]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1a4o. [Modified residues chain P]=phosphothreonine#T#758 [Chain P name]=Integrin beta-2 [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=P05107 [Chain P UniProt boundaries]=755-764 [Chain P UniProt coverage]=1.3% [Chain P UniRef90 accession]=UniRef90_P05107 [Chain P UniRef90 boundaries]=755-764 [Chain A name]=14-3-3 protein zeta/delta [Chain A source organism]=Bos taurus [Chain A UniProt accession]=P63103 [Chain A UniProt boundaries]=1-245 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P63104 [Chain A UniRef90 boundaries]=1-245 [Chain B name]=14-3-3 protein zeta/delta [Chain B source organism]=Bos taurus [Chain B UniProt accession]=P63103 [Chain B UniProt boundaries]=1-245 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P63104 [Chain B UniRef90 boundaries]=1-245 [Entry] [Accession]=DI2020002 [Disorder status]=Inferred from motif [Kd]=2.61E-07 [Name]=14-3-3 zeta in complex with a middle T antigen peptide [Source organism]=Murine polyomavirus / Homo sapiens [PDB ID]=1qjb [PDB chain IDs]=Q:AB [PDB note]=Chain S was removed as chains A, B and Q highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.0 [Domain]=14-3-3 [Type chain Q]=Disordered [Evidence chain Q]=The protein region involved in the interaction contains a known functional linear motif (LIG_14-3-3_CanoR_1). [Type chain A]=Ordered component [Evidence chain A]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 3rdh. [Type chain B]=Ordered component [Evidence chain B]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 3rdh. [Modified residues chain Q]=phosphoserine#S#7 [Chain Q name]=Middle T antigen [Chain Q source organism]=Murine polyomavirus [Chain Q UniProt accession]=P03076 [Chain Q UniProt boundaries]=254-259 [Chain Q UniProt coverage]=1.4% [Chain Q UniRef90 accession]=UniRef90_P03077 [Chain Q UniRef90 boundaries]=254-259 [Chain A name]=14-3-3 protein zeta/delta [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63104 [Chain A UniProt boundaries]=1-245 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P63104 [Chain A UniRef90 boundaries]=1-245 [Chain B name]=14-3-3 protein zeta/delta [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P63104 [Chain B UniProt boundaries]=1-245 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P63104 [Chain B UniRef90 boundaries]=1-245 [Entry] [Accession]=DI2000020 [Disorder status]=Inferred from motif [Kd]=1.55E-06 [Name]=14-3-3 epsilon with Mlf1 peptide [Source organism]=Homo sapiens [PDB ID]=3ual [PDB chain IDs]=P:AB [PDB note]=Chain B was generated using the biomatrix described in the PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=14-3-3 [Type chain P]=Disordered [Evidence chain P]=The protein region involved in the interaction contains a known functional linear motif (LIG_14-3-3_CanoR_1). [Type chain A]=Ordered component [Evidence chain A]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer from a homologous protein without bound ligands is represented by PDB ID 1yz5. [Type chain B]=Ordered component [Evidence chain B]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer from a homologous protein without bound ligands is represented by PDB ID 1yz5. [Modified residues chain P]=phosphoserine#S#38 [Chain P name]=Myeloid leukemia factor 1 [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=P58340 [Chain P UniProt boundaries]=29-42 [Chain P UniProt coverage]=5.2% [Chain P UniRef90 accession]=UniRef90_P58340 [Chain P UniRef90 boundaries]=29-42 [Chain A name]=14-3-3 protein epsilon [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P62258 [Chain A UniProt boundaries]=1-232 [Chain A UniProt coverage]=91% [Chain A UniRef90 accession]=UniRef90_P62258 [Chain A UniRef90 boundaries]=1-232 [Chain B name]=14-3-3 protein epsilon [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P62258 [Chain B UniProt boundaries]=1-232 [Chain B UniProt coverage]=91% [Chain B UniRef90 accession]=UniRef90_P62258 [Chain B UniRef90 boundaries]=1-232 [Related structures]=3ubw [Entry] [Accession]=DI2000021 [Disorder status]=Confirmed [Kd]=9.17E-05 [Name]=14-3-3 zeta in complex with phosphoacetylated histone H3 tail [Source organism]=Homo sapiens [PDB ID]=2c1j [PDB chain IDs]=C:AB [PDB note]=Chain D was removed as chains A, B and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=14-3-3 [Type chain C]=Disordered [Evidence chain C]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered component [Evidence chain A]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 3rdh. [Type chain B]=Ordered component [Evidence chain B]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 3rdh. [Modified residues chain C]=N(6)-acetyllysine#K#9|phosphoserine#S#10 [Chain C name]=Histone H3.1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P68431 [Chain C UniProt boundaries]=8-15 [Chain C UniProt coverage]=5.9% [Chain C UniRef90 accession]=UniRef90_P68431 [Chain C UniRef90 boundaries]=8-15 [Chain A name]=14-3-3 protein zeta/delta [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63104 [Chain A UniProt boundaries]=1-245 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P63104 [Chain A UniRef90 boundaries]=1-245 [Chain B name]=14-3-3 protein zeta/delta [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P63104 [Chain B UniProt boundaries]=1-245 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P63104 [Chain B UniRef90 boundaries]=1-245 [Entry] [Accession]=DI3000010 [Disorder status]=Inferred from motif [Kd]=9.17E-05 [Name]=Peptide from lymphotoxin-B receptor bound to TRAF3 [Source organism]=Homo sapiens [PDB ID]=1rf3 [PDB chain IDs]=B:ACE [PDB note]=Chains C and E were generated using the biomatrices described in the PDB file. [PDB experimental technique]=X-ray [PDB resolution]=3.50 [Domain]=MATH [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_TRAF2_1). [Type chain A]=Ordered component [Evidence chain A]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1flk. [Type chain C]=Ordered component [Evidence chain C]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1flk. [Type chain E]=Ordered component [Evidence chain E]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1flk. [Modified residues chain C]=N(6)-acetyllysine#K#9|phosphoserine#S#10 [Chain B name]=Tumor necrosis factor receptor superfamily member 3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P36941 [Chain B UniProt boundaries]=385-408 [Chain B UniProt coverage]=5.5% [Chain B UniRef90 accession]=UniRef90_P36941 [Chain B UniRef90 boundaries]=385-408 [Chain A name]=TNF receptor-associated factor 3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q13114 [Chain A UniProt boundaries]=377-568 [Chain A UniProt coverage]=33.8% [Chain A UniRef90 accession]=UniRef90_Q13114 [Chain A UniRef90 boundaries]=377-568 [Chain C name]=TNF receptor-associated factor 3 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q13114 [Chain C UniProt boundaries]=377-568 [Chain C UniProt coverage]=33.8% [Chain C UniRef90 accession]=UniRef90_Q13114 [Chain C UniRef90 boundaries]=377-568 [Chain E name]=TNF receptor-associated factor 3 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=Q13114 [Chain E UniProt boundaries]=377-568 [Chain E UniProt coverage]=33.8% [Chain E UniRef90 accession]=UniRef90_Q13114 [Chain E UniRef90 boundaries]=377-568 [Entry] [Accession]=DI2010014 [Disorder status]=Inferred from motif [Kd]=9.17E-05 [Name]=Rat vitamin D receptor ligand binding domain complexed with the NR2 box of DRIP 205 [Source organism]=Homo sapiens / Rattus norvegicus [PDB ID]=1rjk [PDB chain IDs]=C:AB [PDB note]=Chain B was generated using the biomatrix described in the PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.99 [Domain]=Nuclear hormone receptor [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_NRBOX). [Type chain A]=Ordered component [Evidence chain A]=The nuclear hormone receptor domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form. A solved structure of the domain dimer from a homologous protein without bound ligands is represented by PDB ID 1g50. [Type chain B]=Ordered component [Evidence chain B]=The nuclear hormone receptor domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form. A solved structure of the domain dimer from a homologous protein without bound ligands is represented by PDB ID 1g50. [Chain C name]=Mediator of RNA polymerase II transcription subunit 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q15648 [Chain C UniProt boundaries]=640-652 [Chain C UniProt coverage]=0.8% [Chain C UniRef90 accession]=UniRef90_Q15648 [Chain C UniRef90 boundaries]=640-652 [Chain A name]=Vitamin D3 receptor [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=P13053 [Chain A UniProt boundaries]=116-423 [Chain A UniProt coverage]=72.8% [Chain A UniRef90 accession]=UniRef90_P13053 [Chain A UniRef90 boundaries]=116-423 [Chain B name]=Vitamin D3 receptor [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=P13053 [Chain B UniProt boundaries]=116-423 [Chain B UniProt coverage]=72.8% [Chain B UniRef90 accession]=UniRef90_P13053 [Chain B UniRef90 boundaries]=116-423 [Related structures]=1rk3,1rkg,1rkh,2o4j,2o4r,2zfx,3a2h,3aun,3vjs,3vjt,3vrt,3vru,3vrv,3vrw,3w0g,3w0h,3w0i,3w0j,3w5p,3w5q,3w5r,3w5t,3wt5,3wt6,3wt7,3wtq,4ynk,5awj,5awk,5b41,5b5b,5gic,5gid,5gie [Entry] [Accession]=DI1100066 [Disorder status]=Inferred from motif [Kd]=1.20E-07 [Name]=DIAP1 BIR1 bound to a GRIM peptide [Source organism]=Drosophila melanogaster [PDB ID]=1se0 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.75 [Domain]=BIR [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_BIR_III_3). [Type chain A]=Ordered [Evidence chain A]=The BIR domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00653). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1f9x. [Chain B name]=Cell death protein Grim [Chain B source organism]=Drosophila melanogaster [Chain B UniProt accession]=Q24570 [Chain B UniProt boundaries]=2-11 [Chain B UniProt coverage]=7.2% [Chain B UniRef90 accession]=UniRef90_Q24570 [Chain B UniRef90 boundaries]=2-11 [Chain A name]=Death-associated inhibitor of apoptosis 1 [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=Q24306 [Chain A UniProt boundaries]=30-145 [Chain A UniProt coverage]=26.5% [Chain A UniRef90 accession]=UniRef90_Q24306 [Chain A UniRef90 boundaries]=30-145 [Entry] [Accession]=DI1000219 [Disorder status]=Inferred from motif [Kd]=5.30E-08 [Name]=SHC PTB domain complexed with a TRKA receptor phosphopeptide [Source organism]=Homo sapiens [PDB ID]=1shc [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PID [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_PTB_Phospho_1). [Type chain A]=Ordered [Evidence chain A]=The PID domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00640). A solved monomeric structure of the domain is represented by PDB ID 1n3h. [Modified residues chain B]=phosphotyrosine#Y#490 [Chain B name]=High affinity nerve growth factor receptor [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04629 [Chain B UniProt boundaries]=489-500 [Chain B UniProt coverage]=1.5% [Chain B UniRef90 accession]=UniRef90_P04629 [Chain B UniRef90 boundaries]=489-500 [Chain A name]=SHC-transforming protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P29353 [Chain A UniProt boundaries]=125-317 [Chain A UniProt coverage]=33.1% [Chain A UniRef90 accession]=UniRef90_P29353 [Chain A UniRef90 boundaries]=125-317 [Entry] [Accession]=DI1000220 [Disorder status]=Confirmed [Kd]=5.30E-08 [Name]=Shc-PTB:biphosphorylated integrin beta3 cytoplasmic tail complex [Source organism]=Homo sapiens [PDB ID]=2l1c [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PID [Type chain B]=Disordered [Evidence chain B]=The cytoplasmic tail of integrins have been shown to be intrinsically unstructured (PMID:21421922). The protein region involved in the interaction contains 2 known functional linear motifs (LIG_PTB_Phospho_1, LIG_PTB_Phospho_1). [Type chain A]=Ordered [Evidence chain A]=The PID domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00640). A solved monomeric structure of the domain is represented by PDB ID 1n3h. [Modified residues chain B]=phosphotyrosine#Y#747|phosphotyrosine#Y#759 [Chain B name]=Integrin beta-3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P05106 [Chain B UniProt boundaries]=762-788 [Chain B UniProt coverage]=3.4% [Chain B UniRef90 accession]=UniRef90_P05106 [Chain B UniRef90 boundaries]=762-788 [Chain A name]=SHC-transforming protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P29353 [Chain A UniProt boundaries]=127-317 [Chain A UniProt coverage]=32.8% [Chain A UniRef90 accession]=UniRef90_P29353 [Chain A UniRef90 boundaries]=127-317 [Entry] [Accession]=DI1000221 [Disorder status]=Inferred from motif [Kd]=9.00E-07 (PMID:15125843) [Name]=Brca1 BRCT domains in complex with the phosphorylated interacting region from Bach1 helicase [Source organism]=Homo sapiens [PDB ID]=1t15 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.85 [Domain]=BRCT [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_BRCT_BRCA1_1). [Type chain A]=Ordered [Evidence chain A]=The BRCT domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00533). A solved monomeric structure of the domain is represented by PDB ID 1jnx. [Modified residues chain B]=phosphoserine#S#8 [Chain B name]=Fanconi anemia group J protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9BX63 [Chain B UniProt boundaries]=988-995 [Chain B UniProt coverage]=0.6% [Chain B UniRef90 accession]=UniRef90_Q9BX63 [Chain B UniRef90 boundaries]=988-995 [Chain A name]=Breast cancer type 1 susceptibility protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P38398 [Chain A UniProt boundaries]=1646-1859 [Chain A UniProt coverage]=11.5% [Chain A UniRef90 accession]=UniRef90_P38398 [Chain A UniRef90 boundaries]=1646-1859 [Related structures]=1t29 [Entry] [Accession]=DI1010070 [Disorder status]=Confirmed [Kd]=2.12E-08 [Name]=Complex between PP1 and the PP1-binding domain of PNUTS [Source organism]=Rattus norvegicus / Homo sapiens [PDB ID]=4moy [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=Calcineurin-like phosphoesterase [Type chain B]=Disordered [Evidence chain B]=PNUTS is known to be an intrinsically disordered protein in its free state, uses both the RVxF motif and the recently identified ΦΦ motif binding pockets to bind PP1 (PMID:24591642). [Type chain A]=Ordered [Evidence chain A]=The calcineurin-like phosphoesterase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00149). A solved monomeric structure of the domain is represented by PDB ID 4mov. [Chain B name]=Serine/threonine-protein phosphatase 1 regulatory subunit 10 [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=O55000 [Chain B UniProt boundaries]=393-433 [Chain B UniProt coverage]=4.7% [Chain B UniRef90 accession]=UniRef90_O55000 [Chain B UniRef90 boundaries]=393-433 [Chain A name]=Serine/threonine-protein phosphatase PP1-alpha catalytic subunit [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P62136 [Chain A UniProt boundaries]=7-300 [Chain A UniProt coverage]=89.1% [Chain A UniRef90 accession]=UniRef90_P62136 [Chain A UniRef90 boundaries]=7-300 [Related structures]=4mp0 [Entry] [Accession]=DI1100067 [Disorder status]=Inferred from motif [Kd]=6.40E-09 [Name]=CED-9 in complex with the proapoptotic protein Egl-1 [Source organism]=Caenorhabditis elegans [PDB ID]=1ty4 [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=Bcl-2 homology [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_BH_BH3_1). [Type chain A]=Ordered [Evidence chain A]=Bcl-2 homology (BH) domains, such as the one involved in the interaction, are known to adopt a stable structure in isolation (see Pfam domain PF00452). A solved monomeric structure of the domain is represented by PDB ID 1ohu. [Modified residues chain C]=selenomethionine#M#61|selenomethionine#M#69|selenomethionine#M#70 [Chain C name]=Programmed cell death activator egl-1 [Chain C source organism]=Caenorhabditis elegans [Chain C UniProt accession]=O61667 [Chain C UniProt boundaries]=46-102 [Chain C UniProt coverage]=53.8% [Chain C UniRef90 accession]=UniRef90_O61667 [Chain C UniRef90 boundaries]=46-102 [Chain A name]=Apoptosis regulator ced-9 [Chain A source organism]=Caenorhabditis elegans [Chain A UniProt accession]=P41958 [Chain A UniProt boundaries]=68-237 [Chain A UniProt coverage]=60.7% [Chain A UniRef90 accession]=UniRef90_P41958 [Chain A UniRef90 boundaries]=68-237 [Entry] [Accession]=DI1010071 [Disorder status]=Confirmed [Kd]=2.80E-05 [Name]=Clathrin terminal domain in complex with human amphiphysin peptide (379-385) [Source organism]=Homo sapiens / Bos taurus [PDB ID]=1utc [PDB chain IDs]=P:A [PDB note]=Chains B and Q were removed as chains A and P highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=Clathrin propeller repeat [Type chain P]=Disordered [Evidence chain P]=The protein region involved in the interaction corresponds to an intrinsically disordered protein segment (PMID:27813245) and contains a known functional linear motif (LIG_Clathr_ClatBox_2). [Type chain A]=Ordered [Evidence chain A]=The clathrin propeller repeat involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01394). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1bpo. [Chain P name]=Amphiphysin [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=P49418 [Chain P UniProt boundaries]=379-387 [Chain P UniProt coverage]=1.3% [Chain P UniRef90 accession]=UniRef90_P49418 [Chain P UniRef90 boundaries]=379-387 [Chain A name]=Clathrin heavy chain 1 [Chain A source organism]=Bos taurus [Chain A UniProt accession]=P49951 [Chain A UniProt boundaries]=1-363 [Chain A UniProt coverage]=21.7% [Chain A UniRef90 accession]=UniRef90_Q00610-2 [Chain A UniRef90 boundaries]=1-363 [Entry] [Accession]=DI1010072 [Disorder status]=Confirmed [Kd]=2.80E-05 [Name]=Clathrin terminal domain in complex with beta2 adaptin clathrin box motif [Source organism]=Homo sapiens / Bos taurus [PDB ID]=5m5r [PDB chain IDs]=C:A [PDB note]=Chain D was removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.76 [Domain]=Clathrin propeller repeat [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction corresponds to an intrinsically disordered protein segment (PMID:27813245). The protein region involved in the interaction contains a known functional linear motif (LIG_Clathr_ClatBox_1). [Type chain A]=Ordered [Evidence chain A]=The clathrin propeller repeat involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01394). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1bpo. [Chain C name]=AP-2 complex subunit beta [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P63010 [Chain C UniProt boundaries]=629-637 [Chain C UniProt coverage]=1% [Chain C UniRef90 accession]=UniRef90_P63010 [Chain C UniRef90 boundaries]=629-637 [Chain A name]=Clathrin heavy chain 1 [Chain A source organism]=Bos taurus [Chain A UniProt accession]=P49951 [Chain A UniProt boundaries]=1-363 [Chain A UniProt coverage]=21.7% [Chain A UniRef90 accession]=UniRef90_Q00610-2 [Chain A UniRef90 boundaries]=1-363 [Entry] [Accession]=DI1010073 [Disorder status]=Confirmed [Kd]=2.20E-05 (PMID:14981508) [Name]=Clathrin terminal domain in complex with human amphiphysin peptide (349-355) [Source organism]=Homo sapiens / Bos taurus [PDB ID]=5m5s [PDB chain IDs]=E:A [PDB note]=Chains B, F, G and H were removed as chains A and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.88 [Domain]=Clathrin propeller repeat [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction corresponds to an intrinsically disordered protein segment (PMID:27813245). The protein region involved in the interaction contains a known functional linear motif (LIG_Clathr_ClatBox_1). [Type chain A]=Ordered [Evidence chain A]=The clathrin propeller repeat involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01394). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1bpo. [Chain E name]=Amphiphysin [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P49418 [Chain E UniProt boundaries]=349-358 [Chain E UniProt coverage]=1.4% [Chain E UniRef90 accession]=UniRef90_P49418 [Chain E UniRef90 boundaries]=349-358 [Chain A name]=Clathrin heavy chain 1 [Chain A source organism]=Bos taurus [Chain A UniProt accession]=P49951 [Chain A UniProt boundaries]=1-363 [Chain A UniProt coverage]=21.7% [Chain A UniRef90 accession]=UniRef90_Q00610-2 [Chain A UniRef90 boundaries]=1-363 [Related structures]=5m61,5m5t [Entry] [Accession]=DI1120011 [Disorder status]=Confirmed [Kd]=2.20E-05 (PMID:14981508) [Name]=Clathrin terminal domain in complex with clathrin-box motif from hepatitis D virus large antigen (clade 1) [Source organism]=Hepatitis delta virus genotype I / Bos taurus [PDB ID]=5m5u [PDB chain IDs]=E:A [PDB note]=Chains B, F, G and H were removed as chains A and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.15 [Domain]=Clathrin propeller repeat [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction corresponds to an intrinsically disordered protein segment (PMID:27813245). The protein region involved in the interaction contains a known functional linear motif (LIG_Clathr_ClatBox_1). [Type chain A]=Ordered [Evidence chain A]=The clathrin propeller repeat involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01394). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1bpo. [Chain E name]=Large delta antigen [Chain E source organism]=Hepatitis delta virus genotype I [Chain E UniProt accession]=P0C6L6 [Chain E UniProt boundaries]=196-204 [Chain E UniProt coverage]=4.2% [Chain E UniRef90 accession]=UniRef90_P29996 [Chain E UniRef90 boundaries]=196-204 [Chain A name]=Clathrin heavy chain 1 [Chain A source organism]=Bos taurus [Chain A UniProt accession]=P49951 [Chain A UniProt boundaries]=1-363 [Chain A UniProt coverage]=21.7% [Chain A UniRef90 accession]=UniRef90_Q00610-2 [Chain A UniRef90 boundaries]=1-363 [Entry] [Accession]=DI1120012 [Disorder status]=Confirmed [Kd]=2.20E-05 (PMID:14981508) [Name]=Clathrin terminal domain in complex with clathrin-box motif from hepatitis D virus large antigen (clade 2) [Source organism]=Hepatitis delta virus / Bos taurus [PDB ID]=5m5v [PDB chain IDs]=E:A [PDB note]=Chains B, F, G and H were removed as chains A and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.96 [Domain]=Clathrin propeller repeat [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction corresponds to an intrinsically disordered protein segment (PMID:27813245). The protein region involved in the interaction contains a known functional linear motif (LIG_Clathr_ClatBox_1). [Type chain A]=Ordered [Evidence chain A]=The clathrin propeller repeat involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01394). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1bpo. [Chain E name]=Large delta antigen [Chain E source organism]=Hepatitis delta virus [Chain E UniProt accession]=A4ZNG7 [Chain E UniProt boundaries]=202-210 [Chain E UniProt coverage]=4.2% [Chain E UniRef90 accession]=UniRef90_A4ZNG7 [Chain E UniRef90 boundaries]=202-210 [Chain A name]=Clathrin heavy chain 1 [Chain A source organism]=Bos taurus [Chain A UniProt accession]=P49951 [Chain A UniProt boundaries]=1-363 [Chain A UniProt coverage]=21.7% [Chain A UniRef90 accession]=UniRef90_Q00610-2 [Chain A UniRef90 boundaries]=1-363 [Entry] [Accession]=DI1100068 [Disorder status]=Confirmed [Kd]=2.63E-08 (PMID:24366543) [Name]=Second Nrf2 degron bound to Kelch-like ECH-associated protein 1 (Keap1) (mouse) [Source organism]=Mus musculus [PDB ID]=1x2r [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=Kelch [Type chain B]=Disordered [Evidence chain B]=The interacting region of Nrf2 is presumed to acquire a conformation that is induced by its binding with Keap1. The Nrf2 region involved in the interaction contains a known functional linear motif (DEG_Kelch_Keap1_1). [Type chain A]=Ordered [Evidence chain A]=The Kelch domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01344). A solved monomeric structure of the domain is represented by PDB ID 1x2j. [Chain B name]=Nuclear factor erythroid 2-related factor 2 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q60795 [Chain B UniProt boundaries]=76-84 [Chain B UniProt coverage]=1.5% [Chain B UniRef90 accession]=UniRef90_Q60795 [Chain B UniRef90 boundaries]=76-84 [Chain A name]=Kelch-like ECH-associated protein 1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q9Z2X8 [Chain A UniProt boundaries]=309-624 [Chain A UniProt coverage]=50.6% [Chain A UniRef90 accession]=UniRef90_Q14145 [Chain A UniRef90 boundaries]=309-624 [Entry] [Accession]=DI1100069 [Disorder status]=Confirmed [Kd]=5.26E-07 (PMID:24366543) [Name]=First Nrf2 degron bound to Kelch-like ECH-associated protein 1 (Keap1) (mouse) [Source organism]=Mus musculus [PDB ID]=2dyh [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=Kelch [Type chain B]=Disordered [Evidence chain B]=The interacting region of Nrf2 is presumed to acquire a conformation that is induced by its binding with Keap1. The Nrf2 region involved in the interaction contains a known functional linear motif (DEG_Kelch_Keap1_2). [Type chain A]=Ordered [Evidence chain A]=The Kelch domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01344). A solved monomeric structure of the domain is represented by PDB ID 1x2j. [Chain B name]=Nuclear factor erythroid 2-related factor 2 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q60795 [Chain B UniProt boundaries]=22-36 [Chain B UniProt coverage]=2.5% [Chain B UniRef90 accession]=UniRef90_Q60795 [Chain B UniRef90 boundaries]=22-36 [Chain A name]=Kelch-like ECH-associated protein 1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q9Z2X8 [Chain A UniProt boundaries]=308-624 [Chain A UniProt coverage]=50.8% [Chain A UniRef90 accession]=UniRef90_Q14145 [Chain A UniRef90 boundaries]=308-624 [Related structures]=3wn7 [Entry] [Accession]=DI3000011 [Disorder status]=Inferred from motif [Kd]=5.99E-05 [Name]=Residues 331-350 of the flap endonuclease-1 (FEN1) complexed with human PCNA [Source organism]=Homo sapiens [PDB ID]=1u7b [PDB chain IDs]=B:ACE [PDB note]=Chains C and E were generated using the biomatrices described in the PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.88 [Domain]=PCNA [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_PCNA_PIPBox_1). [Type chain A]=Ordered component [Evidence chain A]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60. [Type chain C]=Ordered component [Evidence chain C]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60. [Type chain E]=Ordered component [Evidence chain E]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60. [Chain B name]=Flap endonuclease 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P39748 [Chain B UniProt boundaries]=331-350 [Chain B UniProt coverage]=5.3% [Chain B UniRef90 accession]=UniRef90_P39748 [Chain B UniRef90 boundaries]=331-350 [Chain A name]=Proliferating cell nuclear antigen [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P12004 [Chain A UniProt boundaries]=1-261 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P12004 [Chain A UniRef90 boundaries]=1-261 [Chain C name]=Proliferating cell nuclear antigen [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P12004 [Chain C UniProt boundaries]=1-261 [Chain C UniProt coverage]=100% [Chain C UniRef90 accession]=UniRef90_P12004 [Chain C UniRef90 boundaries]=1-261 [Chain E name]=Proliferating cell nuclear antigen [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P12004 [Chain E UniProt boundaries]=1-261 [Chain E UniProt coverage]=100% [Chain E UniRef90 accession]=UniRef90_P12004 [Chain E UniRef90 boundaries]=1-261 [Related structures]=5e0v,1ul1 [Entry] [Accession]=DI1020024 [Disorder status]=Inferred from motif [Kd]=8.60E-07 [Name]=N-terminal domain of HAUSP/USP7 complexed with an EBNA1 peptide [Source organism]=Epstein-Barr virus / Homo sapiens [PDB ID]=1yy6 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=MATH [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (DOC_USP7_MATH_2). [Type chain A]=Ordered [Evidence chain A]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00917). A solved monomeric structure of the domain is represented by PDB ID 1yze. [Chain B name]=Epstein-Barr nuclear antigen 1 [Chain B source organism]=Epstein-Barr virus [Chain B UniProt accession]=P03211 [Chain B UniProt boundaries]=441-450 [Chain B UniProt coverage]=1.6% [Chain B UniRef90 accession]=UniRef90_P03211 [Chain B UniRef90 boundaries]=441-450 [Chain A name]=Ubiquitin carboxyl-terminal hydrolase 7 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q93009 [Chain A UniProt boundaries]=51-205 [Chain A UniProt coverage]=14.1% [Chain A UniRef90 accession]=UniRef90_Q93009 [Chain A UniRef90 boundaries]=51-205 [Entry] [Accession]=DI1100070 [Disorder status]=Inferred from motif [Kd]=1.50E-05 [Name]=FHA1 domain of Rad53 in complex with a biological relevant phosphopeptide derived from Madt1 [Source organism]=Saccharomyces cerevisiae [PDB ID]=2a0t [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=FHA [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_FHA_1). [Type chain A]=Ordered [Evidence chain A]=The FHA domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00498). A solved monomeric structure of the domain is represented by PDB ID 1g3g. [Modified residues chain B]=phosphothreonine#T#169 [Chain B name]=RNA-binding protein PIN4 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P34217 [Chain B UniProt boundaries]=301-310 [Chain B UniProt coverage]=1.5% [Chain B UniRef90 accession]=UniRef90_P34217 [Chain B UniRef90 boundaries]=301-310 [Chain A name]=Serine/threonine-protein kinase RAD53 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P22216 [Chain A UniProt boundaries]=14-164 [Chain A UniProt coverage]=18.4% [Chain A UniRef90 accession]=UniRef90_P22216 [Chain A UniRef90 boundaries]=14-164 [Entry] [Accession]=DI1010074 [Disorder status]=Inferred from homology [Kd]=2.50E-07 [Name]=WH2 domain of WASP complexed with actin [Source organism]=Homo sapiens / Oryctolagus cuniculus [PDB ID]=2a3z [PDB chain IDs]=C:A [PDB note]=Chain B was removed as chains C and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.08 [Domain]=Actin [Type chain C]=Disordered [Evidence chain C]=The interacting region contains a WH2 domain (Pfam motif PF02205) that is known to be disordered (PMID:19260013, PMID:11911886). The protein region involved in the interaction contains a known functional linear motif (LIG_Actin_WH2_1). [Type chain A]=Ordered [Evidence chain A]=The actin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00022). A solved monomeric structure of the domain is represented by PDB ID 1j6z. [Chain C name]=Wiskott-Aldrich syndrome protein [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P42768 [Chain C UniProt boundaries]=430-458 [Chain C UniProt coverage]=5.8% [Chain C UniRef90 accession]=UniRef90_P42768 [Chain C UniRef90 boundaries]=430-458 [Chain A name]=Actin, alpha skeletal muscle [Chain A source organism]=Oryctolagus cuniculus [Chain A UniProt accession]=P68135 [Chain A UniProt boundaries]=3-377 [Chain A UniProt coverage]=99.5% [Chain A UniRef90 accession]=UniRef90_P68133 [Chain A UniRef90 boundaries]=3-377 [Entry] [Accession]=DI1010075 [Disorder status]=Inferred from homology [Kd]=5.20E-08 [Name]=WH2 domain of WAVE complexed with actin [Source organism]=Homo sapiens / Oryctolagus cuniculus [PDB ID]=2a40 [PDB chain IDs]=C:A [PDB note]=Chains B, D, E and F were removed as chains C and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=Actin [Type chain C]=Disordered [Evidence chain C]=The interacting region contains a WH2 domain (Pfam motif PF02205) that is known to be disordered (PMID:19260013, PMID:11911886). The protein region involved in the interaction contains a known functional linear motif (LIG_Actin_WH2_1). [Type chain A]=Ordered [Evidence chain A]=The Actin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00022). A solved monomeric structure of the domain is represented by PDB ID 1j6z. [Chain C name]=Wiskott-Aldrich syndrome protein family member 2 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q9Y6W5 [Chain C UniProt boundaries]=433-464 [Chain C UniProt coverage]=6.4% [Chain C UniRef90 accession]=UniRef90_Q9Y6W5 [Chain C UniRef90 boundaries]=433-464 [Chain A name]=Actin, alpha skeletal muscle [Chain A source organism]=Oryctolagus cuniculus [Chain A UniProt accession]=P68135 [Chain A UniProt boundaries]=3-377 [Chain A UniProt coverage]=99.5% [Chain A UniRef90 accession]=UniRef90_P68133 [Chain A UniRef90 boundaries]=3-377 [Entry] [Accession]=DI1010076 [Disorder status]=Inferred from homology [Kd]=1.60E-07 [Name]=WH2 domain of WIP complexed with actin [Source organism]=Homo sapiens / Oryctolagus cuniculus [PDB ID]=2a41 [PDB chain IDs]=C:A [PDB note]=Chain B was removed as chains C and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=Actin [Type chain C]=Disordered [Evidence chain C]=The interacting region contains a WH2 domain (Pfam motif PF02205) that is known to be disordered (PMID:19260013, PMID:11911886). The protein region involved in the interaction contains a known functional linear motif (LIG_Actin_WH2_1). [Type chain A]=Ordered [Evidence chain A]=The Actin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00022). A solved monomeric structure of the domain is represented by PDB ID 1j6z. [Chain C name]=WAS/WASL-interacting protein family member 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=O43516 [Chain C UniProt boundaries]=29-60 [Chain C UniProt coverage]=6.4% [Chain C UniRef90 accession]=UniRef90_O43516 [Chain C UniRef90 boundaries]=29-60 [Chain A name]=Actin, alpha skeletal muscle [Chain A source organism]=Oryctolagus cuniculus [Chain A UniProt accession]=P68135 [Chain A UniProt boundaries]=3-377 [Chain A UniProt coverage]=99.5% [Chain A UniRef90 accession]=UniRef90_P68133 [Chain A UniRef90 boundaries]=3-377 [Entry] [Accession]=DI1100071 [Disorder status]=Inferred from motif [Kd]=5.98E-06 (PMID:16634638) [Name]=Synapse associated protein 97 PDZ2 domain with C-terminal GluR-A peptide [Source organism]=Rattus norvegicus [PDB ID]=2g2l [PDB chain IDs]=C:A [PDB note]=Chain B and D were removed as chains C and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.35 [Domain]=PDZ [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_1). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 2awx. [Chain C name]=Glutamate receptor 1 [Chain C source organism]=Rattus norvegicus [Chain C UniProt accession]=M0R9A7 [Chain C UniProt boundaries]=795-812 [Chain C UniProt coverage]=2.2% [Chain C UniRef90 accession]=UniRef90_M0R9A7 [Chain C UniRef90 boundaries]=795-812 [Chain A name]=Disks large homolog 1 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=Q62696 [Chain A UniProt boundaries]=313-409 [Chain A UniProt coverage]=10.6% [Chain A UniRef90 accession]=UniRef90_Q12959 [Chain A UniRef90 boundaries]=313-409 [Related structures]=2aww [Entry] [Accession]=DI1000222 [Disorder status]=Inferred from motif [Kd]=2.00E-06 [Name]=MDC1 BRCT repeat in complex with the histone tail of gamma-H2AX [Source organism]=Homo sapiens [PDB ID]=2azm [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.41 [Domain]=BRCT [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_BRCT_MDC1_1). [Type chain A]=Ordered [Evidence chain A]=The BRCT domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF16770). A solved monomeric structure of the domain is represented by PDB ID 2ado. [Modified residues chain C]=phosphoserine#S#139 [Chain C name]=Histone H2AX [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P16104 [Chain C UniProt boundaries]=134-143 [Chain C UniProt coverage]=7% [Chain C UniRef90 accession]=UniRef90_P16104 [Chain C UniRef90 boundaries]=134-143 [Chain A name]=Mediator of DNA damage checkpoint protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q14676 [Chain A UniProt boundaries]=1883-2089 [Chain A UniProt coverage]=9.9% [Chain A UniRef90 accession]=UniRef90_Q14676 [Chain A UniRef90 boundaries]=1883-2089 [Entry] [Accession]=DI1000223 [Disorder status]=Inferred from motif [Kd]=5.20E-06 [Name]=BRCT domains of human BRCA1 in complex with a phosphorylated peptide from human acetyl-CoA carboxylase 1 [Source organism]=Homo sapiens [PDB ID]=3coj [PDB chain IDs]=I:A [PDB note]=Chains B, C, D, E, F, G, H, J, K, L, M, N, O and X were removed as chains A and I highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.21 [Domain]=BRCT [Type chain I]=Disordered [Evidence chain I]=The protein region involved in the interaction contains a known functional linear motif (LIG_BRCT_BRCA1_1). [Type chain A]=Ordered [Evidence chain A]=The BRCT domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00533). A solved monomeric structure of the domain is represented by PDB ID 1jnx. [Modified residues chain I]=phosphoserine#S#1263 [Chain I name]=Acetyl-CoA carboxylase 1 [Chain I source organism]=Homo sapiens [Chain I UniProt accession]=Q13085 [Chain I UniProt boundaries]=1258-1270 [Chain I UniProt coverage]=0.6% [Chain I UniRef90 accession]=UniRef90_Q13085 [Chain I UniRef90 boundaries]=1258-1270 [Chain A name]=Breast cancer type 1 susceptibility protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P38398 [Chain A UniProt boundaries]=1646-1859 [Chain A UniProt coverage]=11.5% [Chain A UniRef90 accession]=UniRef90_P38398 [Chain A UniRef90 boundaries]=1646-1859 [Entry] [Accession]=DI2000022 [Disorder status]=Inferred from motif [Kd]=2.30E-08 [Name]=CDC6 derived peptide bound to CDK2:CyclinA [Source organism]=Homo sapiens [PDB ID]=2cch [PDB chain IDs]=E:AB [PDB note]=Chains C, D and F were removed as chains A, B and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.7 [Domain]=Cyclin A:Cdk2 [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (DOC_CYCLIN_1). [Type chain A]=Ordered component [Evidence chain A]=The cyclin A:Cdk2 complex involved in the interaction is known to form an ordered dimer, represented by PDB ID 1jst. [Type chain B]=Ordered component [Evidence chain B]=The cyclin A:Cdk2 complex involved in the interaction is known to form an ordered dimer, represented by PDB ID 1jst. [Modified residues chain B]=phosphothreonine#T#169 [Chain E name]=Cell division control protein 6 homolog [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=Q99741 [Chain E UniProt boundaries]=89-100 [Chain E UniProt coverage]=2.1% [Chain E UniRef90 accession]=UniRef90_Q99741 [Chain E UniRef90 boundaries]=89-100 [Chain A name]=Cyclin-dependent kinase 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P24941 [Chain A UniProt boundaries]=1-298 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P24941 [Chain A UniRef90 boundaries]=1-298 [Chain B name]=Cyclin-A2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P20248 [Chain B UniProt boundaries]=173-432 [Chain B UniProt coverage]=60.2% [Chain B UniRef90 accession]=UniRef90_P20248 [Chain B UniRef90 boundaries]=173-432 [Related structures]=2cci [Entry] [Accession]=DI2000023 [Disorder status]=Inferred from motif [Kd]=5.90E-08 [Name]=Pkc Epsilon peptide bound to a tandem 14-3-3 binding site [Source organism]=Homo sapiens [PDB ID]=2wh0 [PDB chain IDs]=Q:AB [PDB note]=Chains C, D and R were removed as chains Q, A and B highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.25 [Domain]=14-3-3 [Type chain Q]=Disordered [Evidence chain Q]=The protein region involved in the interaction contains a known functional linear motif (LIG_14-3-3_CanoR_1). [Type chain A]=Ordered component [Evidence chain A]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1a4o. [Type chain B]=Ordered component [Evidence chain B]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1a4o. [Modified residues chain Q]=phosphoserine#S#346|phosphoserine#S#368 [Modified residues chain B]=phosphothreonine#T#169 [Chain Q name]=Protein kinase C epsilon type [Chain Q source organism]=Homo sapiens [Chain Q UniProt accession]=Q02156 [Chain Q UniProt boundaries]=342-372 [Chain Q UniProt coverage]=4.2% [Chain Q UniRef90 accession]=UniRef90_P16054 [Chain Q UniRef90 boundaries]=342-372 [Chain A name]=14-3-3 protein zeta/delta [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63104 [Chain A UniProt boundaries]=1-245 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P63104 [Chain A UniRef90 boundaries]=1-245 [Chain B name]=14-3-3 protein zeta/delta [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P63104 [Chain B UniProt boundaries]=1-245 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P63104 [Chain B UniRef90 boundaries]=1-245 [Entry] [Accession]=DI2000024 [Disorder status]=Confirmed [Kd]=1.17E-05 [Name]=Human 14-3-3 sigma in complex with Raf1 peptide (255-262) [Source organism]=Homo sapiens [PDB ID]=3iqj [PDB chain IDs]=P:AB [PDB note]=Chain B was generated using the biomatrix described in the PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.15 [Domain]=14-3-3 [Type chain P]=Disordered [Evidence chain P]=The 255-260 region described in DisProt entry DP00171 covers 60% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_14-3-3_CanoR_1). [Type chain A]=Ordered component [Evidence chain A]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1yz5. [Type chain B]=Ordered component [Evidence chain B]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1yz5. [Modified residues chain P]=phosphoserine#S#259 [Modified residues chain B]=phosphothreonine#T#169 [Chain P name]=RAF proto-oncogene serine/threonine-protein kinase [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=P04049 [Chain P UniProt boundaries]=255-264 [Chain P UniProt coverage]=1.5% [Chain P UniRef90 accession]=UniRef90_P04049 [Chain P UniRef90 boundaries]=255-264 [Chain A name]=14-3-3 protein sigma [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P31947 [Chain A UniProt boundaries]=1-231 [Chain A UniProt coverage]=93.1% [Chain A UniRef90 accession]=UniRef90_P31947 [Chain A UniRef90 boundaries]=1-231 [Chain B name]=14-3-3 protein sigma [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P31947 [Chain B UniProt boundaries]=1-231 [Chain B UniProt coverage]=93.1% [Chain B UniRef90 accession]=UniRef90_P31947 [Chain B UniRef90 boundaries]=1-231 [Related structures]=3o8i,3iqu,3iqv [Entry] [Accession]=DI2000025 [Disorder status]=Inferred from motif [Kd]=4.13E-06 [Name]=Human 14-3-3 sigma in complex with TASK-3 peptide [Source organism]=Homo sapiens [PDB ID]=3p1n [PDB chain IDs]=P:AB [PDB note]=Chain B was generated using the biomatrix described in the PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.40 [Domain]=14-3-3 [Type chain P]=Disordered [Evidence chain P]=The protein region involved in the interaction contains a known functional linear motif (LIG_14-3-3_CterR_2). [Type chain A]=Ordered component [Evidence chain A]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1yz5. [Type chain B]=Ordered component [Evidence chain B]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1yz5. [Modified residues chain P]=phosphoserine#S#373 [Modified residues chain B]=phosphothreonine#T#169 [Chain P name]=Potassium channel subfamily K member 9 [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=Q9NPC2 [Chain P UniProt boundaries]=369-374 [Chain P UniProt coverage]=1.6% [Chain P UniRef90 accession]=UniRef90_Q9NPC2 [Chain P UniRef90 boundaries]=369-374 [Chain A name]=14-3-3 protein sigma [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P31947 [Chain A UniProt boundaries]=1-231 [Chain A UniProt coverage]=93.1% [Chain A UniRef90 accession]=UniRef90_P31947 [Chain A UniRef90 boundaries]=1-231 [Chain B name]=14-3-3 protein sigma [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P31947 [Chain B UniProt boundaries]=1-231 [Chain B UniProt coverage]=93.1% [Chain B UniRef90 accession]=UniRef90_P31947 [Chain B UniRef90 boundaries]=1-231 [Related structures]=3p1o,3p1p,3p1q,3p1r,3p1s,3smk,3sml,3smm,3smn,3smo,3sp5,3spr,3ux0,4fr3 [Entry] [Accession]=DI2000026 [Disorder status]=Inferred from motif [Kd]=4.13E-06 [Name]=14-3-3 sigma in complex with PADI6 14-3-3 binding motif I [Source organism]=Homo sapiens [PDB ID]=4dau [PDB chain IDs]=B:AC [PDB note]=Chain C was generated using the biomatrix described in the PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=14-3-3 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_14-3-3_CanoR_1). [Type chain A]=Ordered component [Evidence chain A]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1yz5. [Type chain C]=Ordered component [Evidence chain C]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1yz5. [Modified residues chain B]=phosphoserine#S#10 [Modified residues chain C]=phosphoserine#S#139 [Chain B name]=Protein-arginine deiminase type-6 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q6TGC4 [Chain B UniProt boundaries]=1-13 [Chain B UniProt coverage]=1.9% [Chain B UniRef90 accession]=UniRef90_Q6TGC4 [Chain B UniRef90 boundaries]=1-13 [Chain A name]=14-3-3 protein sigma [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P31947 [Chain A UniProt boundaries]=1-231 [Chain A UniProt coverage]=93.1% [Chain A UniRef90 accession]=UniRef90_P31947 [Chain A UniRef90 boundaries]=1-231 [Chain C name]=14-3-3 protein sigma [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P31947 [Chain C UniProt boundaries]=1-231 [Chain C UniProt coverage]=93.1% [Chain C UniRef90 accession]=UniRef90_P31947 [Chain C UniRef90 boundaries]=1-231 [Entry] [Accession]=DI2000027 [Disorder status]=Confirmed [Kd]=4.13E-06 [Name]=Human 14-3-3 sigma in complex with Raf1 peptide (618-625) [Source organism]=Homo sapiens [PDB ID]=4iea [PDB chain IDs]=P:AB [PDB note]=Chain B was generated using the biomatrix described in the PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=14-3-3 [Type chain P]=Disordered [Evidence chain P]=The 618-625 region described in DisProt entry DP00171 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_14-3-3_CanoR_1). [Type chain A]=Ordered component [Evidence chain A]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1yz5. [Type chain B]=Ordered component [Evidence chain B]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1yz5. [Modified residues chain P]=phosphoserine#S#621 [Modified residues chain B]=phosphoserine#S#10 [Chain P name]=RAF proto-oncogene serine/threonine-protein kinase [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=P04049 [Chain P UniProt boundaries]=618-625 [Chain P UniProt coverage]=1.2% [Chain P UniRef90 accession]=UniRef90_P04049 [Chain P UniRef90 boundaries]=618-625 [Chain A name]=14-3-3 protein sigma [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P31947 [Chain A UniProt boundaries]=1-231 [Chain A UniProt coverage]=93.1% [Chain A UniRef90 accession]=UniRef90_P31947 [Chain A UniRef90 boundaries]=1-231 [Chain B name]=14-3-3 protein sigma [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P31947 [Chain B UniProt boundaries]=1-231 [Chain B UniProt coverage]=93.1% [Chain B UniRef90 accession]=UniRef90_P31947 [Chain B UniRef90 boundaries]=1-231 [Entry] [Accession]=DI2000028 [Disorder status]=Inferred from motif [Kd]=2.00E-08 [Name]=14-3-3 zeta in complex with a diphosphorylated c-Raf peptide [Source organism]=Homo sapiens [PDB ID]=4ihl [PDB chain IDs]=P:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=14-3-3 [Type chain P]=Disordered [Evidence chain P]=The protein region involved in the interaction contains two instances of a known functional linear motif (LIG_14-3-3_CanoR_1). [Type chain A]=Ordered component [Evidence chain A]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1a4o. [Type chain B]=Ordered component [Evidence chain B]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1a4o. [Modified residues chain P]=phosphoserine#S#233|phosphoserine#S#259 [Modified residues chain B]=phosphoserine#S#10 [Chain P name]=RAF proto-oncogene serine/threonine-protein kinase [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=P04049 [Chain P UniProt boundaries]=229-264 [Chain P UniProt coverage]=5.6% [Chain P UniRef90 accession]=UniRef90_P04049 [Chain P UniRef90 boundaries]=229-264 [Chain A name]=14-3-3 protein zeta/delta [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63104 [Chain A UniProt boundaries]=1-230 [Chain A UniProt coverage]=93.9% [Chain A UniRef90 accession]=UniRef90_P63104 [Chain A UniRef90 boundaries]=1-230 [Chain B name]=14-3-3 protein zeta/delta [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P63104 [Chain B UniProt boundaries]=1-230 [Chain B UniProt coverage]=93.9% [Chain B UniRef90 accession]=UniRef90_P63104 [Chain B UniRef90 boundaries]=1-230 [Related structures]=3cu8,3nkx,4fj3 [Entry] [Accession]=DI2000029 [Disorder status]=Confirmed [Kd]=4.60E-06 [Name]=14-3-3 zeta in complex with Chibby peptide [Source organism]=Homo sapiens [PDB ID]=4wrq [PDB chain IDs]=C:AB [PDB note]=Chain D was removed as chains A, B and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.41 [Domain]=14-3-3 [Type chain C]=Disordered [Evidence chain C]=The 1-63 region described in DisProt entry DP00709 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_14-3-3_CanoR_1). [Type chain A]=Ordered component [Evidence chain A]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1a4o. [Type chain B]=Ordered component [Evidence chain B]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1a4o. [Modified residues chain C]=phosphoserine#S#20 [Modified residues chain B]=phosphoserine#S#10 [Chain C name]=Protein chibby homolog 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q9Y3M2 [Chain C UniProt boundaries]=12-29 [Chain C UniProt coverage]=14.3% [Chain C UniRef90 accession]=UniRef90_Q9Y3M2 [Chain C UniRef90 boundaries]=12-29 [Chain A name]=14-3-3 protein zeta/delta [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63104 [Chain A UniProt boundaries]=1-245 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P63104 [Chain A UniRef90 boundaries]=1-245 [Chain B name]=14-3-3 protein zeta/delta [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P63104 [Chain B UniProt boundaries]=1-245 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P63104 [Chain B UniRef90 boundaries]=1-245 [Entry] [Accession]=DI2000030 [Disorder status]=Confirmed [Kd]=7.58E-05 [Name]=14-3-3 zeta in complex with CFTR R-domain peptide [Source organism]=Homo sapiens [PDB ID]=5d2d [PDB chain IDs]=C:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=14-3-3 [Type chain C]=Disordered [Evidence chain C]=The 708-831 region described in DisProt entry DP00012 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains two instances of a known functional linear motif (LIG_14-3-3_CanoR_1). [Type chain A]=Ordered component [Evidence chain A]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1a4o. [Type chain B]=Ordered component [Evidence chain B]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1a4o. [Modified residues chain C]=phosphoserine#S#753|phosphoserine#S#768 [Modified residues chain B]=phosphoserine#S#10 [Chain C name]=Cystic fibrosis transmembrane conductance regulator [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P13569 [Chain C UniProt boundaries]=747-774 [Chain C UniProt coverage]=1.9% [Chain C UniRef90 accession]=UniRef90_P13569 [Chain C UniRef90 boundaries]=747-774 [Chain A name]=14-3-3 protein zeta/delta [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63104 [Chain A UniProt boundaries]=1-230 [Chain A UniProt coverage]=93.9% [Chain A UniRef90 accession]=UniRef90_P63104 [Chain A UniRef90 boundaries]=1-230 [Chain B name]=14-3-3 protein zeta/delta [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P63104 [Chain B UniProt boundaries]=1-230 [Chain B UniProt coverage]=93.9% [Chain B UniRef90 accession]=UniRef90_P63104 [Chain B UniRef90 boundaries]=1-230 [Related structures]=5d3f [Entry] [Accession]=DI2000031 [Disorder status]=Confirmed [Kd]=2.40E-05 [Name]=14-3-3 gamma in complex with CFTR R-domain peptide [Source organism]=Homo sapiens [PDB ID]=5d3e [PDB chain IDs]=C:AB [PDB note]=Chains E, F, G, I, J and K were removed as chains A, B and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.75 [Domain]=14-3-3 [Type chain C]=Disordered [Evidence chain C]=The 708-831 region described in DisProt entry DP00012 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains 2 known functional linear motifs (LIG_14-3-3_CanoR_1, LIG_14-3-3_CanoR_1). [Type chain A]=Ordered component [Evidence chain A]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 4e2e. [Type chain B]=Ordered component [Evidence chain B]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 4e2e. [Modified residues chain C]=phosphoserine#S#768|phosphoserine#S#795 [Modified residues chain B]=phosphoserine#S#10 [Chain C name]=Cystic fibrosis transmembrane conductance regulator [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P13569 [Chain C UniProt boundaries]=762-801 [Chain C UniProt coverage]=2.7% [Chain C UniRef90 accession]=UniRef90_P13569 [Chain C UniRef90 boundaries]=762-801 [Chain A name]=14-3-3 protein gamma [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P61981 [Chain A UniProt boundaries]=1-238 [Chain A UniProt coverage]=96.4% [Chain A UniRef90 accession]=UniRef90_P61981 [Chain A UniRef90 boundaries]=1-238 [Chain B name]=14-3-3 protein gamma [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P61981 [Chain B UniProt boundaries]=1-238 [Chain B UniProt coverage]=96.4% [Chain B UniRef90 accession]=UniRef90_P61981 [Chain B UniRef90 boundaries]=1-238 [Entry] [Accession]=DI2100008 [Disorder status]=Confirmed [Kd]=5.00E-11 (PMID:17543955) [Name]=Structure of m-calpain in complex with calpastatin inhibitory domain 4 [Source organism]=Rattus norvegicus [PDB ID]=3bow [PDB chain IDs]=C:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=EF-hand [Type chain C]=Disordered [Evidence chain C]=Calpastatin inhibitory domain 4 has been shown to be intrinsically disordered in the absence of calpain and binds as an extended polypeptide over the surface of calpain, making contact with each domain of the enzyme. (PMID:19020623). [Type chain A]=Ordered component [Evidence chain A]=The EF-hand domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13833). Calpain large and small subunits form a stable heterodimer represented by PDB ID 1df0. [Type chain B]=Ordered component [Evidence chain B]=The EF-hand domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13833). Calpain large and small subunits form a stable heterodimer represented by PDB ID 1df0. [Modified residues chain B]=phosphoserine#S#10 [Chain C name]=Calpastatin [Chain C source organism]=Rattus norvegicus [Chain C UniProt accession]=P27321 [Chain C UniProt boundaries]=571-664 [Chain C UniProt coverage]=13.2% [Chain C UniRef90 accession]=UniRef90_P27321 [Chain C UniRef90 boundaries]=571-664 [Chain A name]=Calpain-2 catalytic subunit [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=Q07009 [Chain A UniProt boundaries]=1-700 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P17655 [Chain A UniRef90 boundaries]=1-700 [Chain B name]=Calpain small subunit 1 [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=Q64537 [Chain B UniProt boundaries]=88-270 [Chain B UniProt coverage]=67.8% [Chain B UniRef90 accession]=UniRef90_P04632 [Chain B UniRef90 boundaries]=88-270 [Entry] [Accession]=DI2100009 [Disorder status]=Inferred from homology [Kd]=4.50E-12 (PMID:17543955) [Name]=Calcium-dependent complex between m-calpain and calpastatin inhibitory domain 1 [Source organism]=Rattus norvegicus [PDB ID]=3df0 [PDB chain IDs]=C:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.95 [Domain]=EF-hand [Type chain C]=Disordered [Evidence chain C]=The corresponding region of a closely homologous protein has been shown to be disordered in the 137-277 region described in DisProt entry DP00196 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered component [Evidence chain A]=The EF-hand domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13833). Calpain large and small subunits form a stable heterodimer represented by PDB ID 1df0. [Type chain B]=Ordered component [Evidence chain B]=The EF-hand domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13833). Calpain large and small subunits form a stable heterodimer represented by PDB ID 1df0. [Modified residues chain B]=phosphoserine#S#10 [Chain C name]=Calpastatin [Chain C source organism]=Rattus norvegicus [Chain C UniProt accession]=P27321 [Chain C UniProt boundaries]=193-278 [Chain C UniProt coverage]=12.1% [Chain C UniRef90 accession]=UniRef90_P27321 [Chain C UniRef90 boundaries]=193-278 [Chain A name]=Calpain-2 catalytic subunit [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=Q07009 [Chain A UniProt boundaries]=1-700 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P17655 [Chain A UniRef90 boundaries]=1-700 [Chain B name]=Calpain small subunit 1 [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=Q64537 [Chain B UniProt boundaries]=88-270 [Chain B UniProt coverage]=67.8% [Chain B UniRef90 accession]=UniRef90_P04632 [Chain B UniRef90 boundaries]=88-270 [Entry] [Accession]=DI1010077 [Disorder status]=Confirmed [Kd]=8.70E-09 [Name]=Complex between Protein Phosphatase 1 alpha (PP1) and the PP1 binding and PDZ domains of Spinophilin [Source organism]=Rattus norvegicus / Homo sapiens [PDB ID]=3egg [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.85 [Domain]=Calcineurin-like phosphoesterase [Type chain C]=Disordered [Evidence chain C]=The 417-494 region described in DisProt entry DP00943 and in IDEAL entry IID50058 cover 100% of the protein region involved in the interaction (PP1 binding domain, PMID:20305656). The protein region involved in the interaction contains a known functional linear motif (DOC_PP1_RVXF_1). [Type chain A]=Ordered [Evidence chain A]=The calcineurin-like phosphoesterase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00149). A solved monomeric structure of the domain is represented by PDB ID 4mov. [Chain C name]=Neurabin-2 [Chain C source organism]=Rattus norvegicus [Chain C UniProt accession]=O35274 [Chain C UniProt boundaries]=417-583 [Chain C UniProt coverage]=20.4% [Chain C UniRef90 accession]=UniRef90_O35274 [Chain C UniRef90 boundaries]=417-583 [Chain A name]=Serine/threonine-protein phosphatase PP1-alpha catalytic subunit [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P62136 [Chain A UniProt boundaries]=7-330 [Chain A UniProt coverage]=98.2% [Chain A UniRef90 accession]=UniRef90_P62136 [Chain A UniRef90 boundaries]=7-330 [Entry] [Accession]=DI1100072 [Disorder status]=Confirmed [Kd]=8.70E-09 [Name]=Complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (MYPT1) [Source organism]=Gallus gallus [PDB ID]=1s70 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.70 [Domain]=Calcineurin-like phosphoesterase [Type chain B]=Disordered [Evidence chain B]=The 1-299 region described in DisProt entry DP00218 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains two known functional linear motif (DOC_PP1_MyPhoNE_1 and DOC_PP1_RVXF_1). [Type chain A]=Ordered [Evidence chain A]=The calcineurin-like phosphoesterase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00149). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 4mov. [Chain B name]=Protein phosphatase 1 regulatory subunit 12A [Chain B source organism]=Gallus gallus [Chain B UniProt accession]=Q90623 [Chain B UniProt boundaries]=1-299 [Chain B UniProt coverage]=29.8% [Chain B UniRef90 accession]=UniRef90_Q90623 [Chain B UniRef90 boundaries]=1-299 [Chain A name]=Serine/threonine-protein phosphatase PP1-beta catalytic subunit [Chain A source organism]=Gallus gallus [Chain A UniProt accession]=P62207 [Chain A UniProt boundaries]=1-327 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P62140 [Chain A UniRef90 boundaries]=1-327 [Entry] [Accession]=DI1000224 [Disorder status]=Confirmed [Kd]=6.20E-08 [Name]=Protein Phosphate 1 in complex with PP1 binding domain of GADD34 [Source organism]=Homo sapiens [PDB ID]=4xpn [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.29 [Domain]=Calcineurin-like phosphoesterase [Type chain B]=Disordered [Evidence chain B]=The GADD34 PP1-binding domain is known to be intrinsically disordered and binds to PP1 alpha via PP1-binding motif RVxF [KVRF] (PMID:26095357). [Type chain A]=Ordered [Evidence chain A]=The calcineurin-like phosphoesterase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00149). A solved monomeric structure of the domain is represented by PDB ID 4mov. [Chain B name]=Protein phosphatase 1 regulatory subunit 15A [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O75807 [Chain B UniProt boundaries]=552-591 [Chain B UniProt coverage]=5.9% [Chain B UniRef90 accession]=UniRef90_O75807 [Chain B UniRef90 boundaries]=552-591 [Chain A name]=Serine/threonine-protein phosphatase PP1-alpha catalytic subunit [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P62136 [Chain A UniProt boundaries]=7-300 [Chain A UniProt coverage]=89.1% [Chain A UniRef90 accession]=UniRef90_P62136 [Chain A UniRef90 boundaries]=7-300 [Entry] [Accession]=DI1020025 [Disorder status]=Confirmed [Kd]=6.20E-08 [Name]=Second fibronectin f1 module in complex with a fragment of staphylococcus aureus fnbpa-1 [Source organism]=Staphylococcus aureus / Homo sapiens [PDB ID]=2rkz [PDB chain IDs]=M:A [PDB note]=Chains B, C, D, E, F, N, O, P, Q and R were removed as chains A and M represent the biologically relevant interaction. Chains A and M were truncated to only include residues 139-182 and 529-538 (according to UniProt numbering), respectively, to highlight the interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Fibronectin type I [Type chain M]=Disordered [Evidence chain M]=It is known that FnBPA from S. aureus, have multiple intrinsically disordered, high-affinity binding repeats (FnBRs) for Fibronectin, which undergo a disorder-to-order transition on binding to Fn. In this tandem beta-zipper interaction, the FnBR extends the triple-stranded anti-parallel beta-sheet of sequential F1 modules by forming an additional strand anti-parallel to the C-terminal strand of each F1 module (PMID:18713862). [Type chain A]=Ordered [Evidence chain A]=The Fibronectin type I domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00039). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1tpm. [Chain M name]=Fibronectin-binding protein A [Chain M source organism]=Staphylococcus aureus [Chain M UniProt accession]=P14738 [Chain M UniProt boundaries]=529-538 [Chain M UniProt coverage]=1% [Chain M UniRef90 accession]=UniRef90_P14738 [Chain M UniRef90 boundaries]=529-538 [Chain A name]=Fibronectin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P02751 [Chain A UniProt boundaries]=139-182 [Chain A UniProt coverage]=1.8% [Chain A UniRef90 accession]=UniRef90_P02751 [Chain A UniRef90 boundaries]=139-182 [Entry] [Accession]=DI1020026 [Disorder status]=Confirmed [Kd]=6.20E-08 [Name]=Third fibronectin f1 module in complex with a fragment of staphylococcus aureus fnbpa-1 [Source organism]=Staphylococcus aureus / Homo sapiens [PDB ID]=2rkz [PDB chain IDs]=N:B [PDB note]=Chains A, C, D, E, F, M, O, P, Q and R were removed as chains B and N represent the biologically relevant interaction. Chains B and N were truncated to only include residues 94-138 and 539-547 (according to UniProt numbering), respectively, to highlight the interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Fibronectin type I [Type chain N]=Disordered [Evidence chain N]=It is known that FnBPA from S. aureus, have multiple, intrinsically disordered, high-affinity binding repeats (FnBRs) for Fibronectin, that undergo a disorder-to-order transition on binding to Fn. In this tandem beta-zipper interaction, the FnBR extends the triple-stranded anti-parallel beta-sheet of sequential F1 modules by forming an additional strand anti-parallel to the C-terminal strand of each F1 module (PMID:18713862). [Type chain B]=Ordered [Evidence chain B]=The Fibronectin type I domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00039). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1tpm. [Chain N name]=Fibronectin-binding protein A [Chain N source organism]=Staphylococcus aureus [Chain N UniProt accession]=P14738 [Chain N UniProt boundaries]=539-547 [Chain N UniProt coverage]=0.9% [Chain N UniRef90 accession]=UniRef90_P14738 [Chain N UniRef90 boundaries]=539-547 [Chain B name]=Fibronectin [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P02751 [Chain B UniProt boundaries]=94-138 [Chain B UniProt coverage]=1.9% [Chain B UniRef90 accession]=UniRef90_P02751 [Chain B UniRef90 boundaries]=94-138 [Entry] [Accession]=DI1020027 [Disorder status]=Confirmed [Kd]=6.20E-08 [Name]=Fourth fibronectin f1 module in complex with a fragment of staphylococcus aureus fnbpa-1 [Source organism]=Staphylococcus aureus / Homo sapiens [PDB ID]=2rky [PDB chain IDs]=D:A [PDB note]=Chains B and C were removed as chains A and D represent the biologically relevant interaction. Chains A and D were truncated to only include residues 183-228 and 520-530 (according to UniProt numbering), respectively, to highlight the interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=Fibronectin type I [Type chain D]=Disordered [Evidence chain D]=It is known that FnBPA from S. aureus, have multiple intrinsically disordered, high-affinity binding repeats (FnBRs) for Fibronectin, which undergo a disorder-to-order transition on binding to Fn. In this tandem beta-zipper interaction, the FnBR extends the triple-stranded anti-parallel beta-sheet of sequential F1 modules by forming an additional strand anti-parallel to the C-terminal strand of each F1 module (PMID:18713862). [Type chain A]=Ordered [Evidence chain A]=The Fibronectin type I domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00039). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1tpm. [Chain D name]=Fibronectin-binding protein A [Chain D source organism]=Staphylococcus aureus [Chain D UniProt accession]=P14738 [Chain D UniProt boundaries]=520-530 [Chain D UniProt coverage]=1.1% [Chain D UniRef90 accession]=UniRef90_P14738 [Chain D UniRef90 boundaries]=520-530 [Chain A name]=Fibronectin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P02751 [Chain A UniProt boundaries]=183-228 [Chain A UniProt coverage]=1.9% [Chain A UniRef90 accession]=UniRef90_P02751 [Chain A UniRef90 boundaries]=183-228 [Entry] [Accession]=DI1020028 [Disorder status]=Confirmed [Kd]=6.20E-08 [Name]=Fifth fibronectin f1 module in complex with a fragment of staphylococcus aureus fnbpa-1 [Source organism]=Staphylococcus aureus / Homo sapiens [PDB ID]=2rky [PDB chain IDs]=B:C [PDB note]=Chains A and D were removed as chains B and C represent the biologically relevant interaction. Chains B and C were truncated to only include residues 508-519 and 229-274 (according to UniProt numbering), respectively, to highlight the interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=Fibronectin type I [Type chain B]=Disordered [Evidence chain B]=It is known that FnBPA from S. aureus, have multiple intrinsically disordered, high-affinity binding repeats (FnBRs) for Fibronectin, which undergo a disorder-to-order transition on binding to Fn. In this tandem beta-zipper interaction, the FnBR extends the triple-stranded anti-parallel beta-sheet of sequential F1 modules by forming an additional strand anti-parallel to the C-terminal strand of each F1 module (PMID:18713862). [Type chain C]=Ordered [Evidence chain C]=The Fibronectin type I domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00039). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1tpm. [Chain B name]=Fibronectin-binding protein A [Chain B source organism]=Staphylococcus aureus [Chain B UniProt accession]=P14738 [Chain B UniProt boundaries]=508-519 [Chain B UniProt coverage]=1.2% [Chain B UniRef90 accession]=UniRef90_P14738 [Chain B UniRef90 boundaries]=508-519 [Chain C name]=Fibronectin [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P02751 [Chain C UniProt boundaries]=229-274 [Chain C UniProt coverage]=1.9% [Chain C UniRef90 accession]=UniRef90_P02751 [Chain C UniRef90 boundaries]=229-274 [Entry] [Accession]=DI1020029 [Disorder status]=Confirmed [Kd]=6.20E-08 [Name]=Fourth fibronectin f1 module in complex with a fragment of staphylococcus aureus fnbpa-5 [Source organism]=Staphylococcus aureus / Homo sapiens [PDB ID]=2rl0 [PDB chain IDs]=E:D [PDB note]=Chains A, B, C, F, G, H, I, J, K and L were removed as chains D and E represent the biologically relevant interaction. Chains D and E were truncated to only include residues 184-228 and 647-654 (according to UniProt numbering) to highlight the interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Fibronectin type I [Type chain E]=Disordered [Evidence chain E]=It is known that FnBPA from S. aureus, have multiple intrinsically disordered, high-affinity binding repeats (FnBRs) for Fibronectin, which undergo a disorder-to-order transition on binding to Fn. In this tandem beta-zipper interaction, the FnBR extends the triple-stranded anti-parallel beta-sheet of sequential F1 modules by forming an additional strand anti-parallel to the C-terminal strand of each F1 module (PMID:18713862). [Type chain D]=Ordered [Evidence chain D]=The Fibronectin type I domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00039). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1tpm. [Chain E name]=Fibronectin-binding protein A [Chain E source organism]=Staphylococcus aureus [Chain E UniProt accession]=P14738 [Chain E UniProt boundaries]=647-654 [Chain E UniProt coverage]=0.8% [Chain E UniRef90 accession]=UniRef90_P14738 [Chain E UniRef90 boundaries]=647-654 [Chain D name]=Fibronectin [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P02751 [Chain D UniProt boundaries]=184-228 [Chain D UniProt coverage]=1.9% [Chain D UniRef90 accession]=UniRef90_P02751 [Chain D UniRef90 boundaries]=184-228 [Entry] [Accession]=DI1020030 [Disorder status]=Confirmed [Kd]=6.20E-08 [Name]=Fifth fibronectin f1 module in complex with a fragment of staphylococcus aureus fnbpa-5 [Source organism]=Staphylococcus aureus / Homo sapiens [PDB ID]=2rl0 [PDB chain IDs]=L:K [PDB note]=Chains A, B, C, D, E, F, G, H, I and J were removed as chains K and L represent the biologically relevant interaction. Chains K and L were truncated to only include residues 229-272 and 639-646 (according to UniProt numbering) to highlight the interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Fibronectin type I [Type chain L]=Disordered [Evidence chain L]=It is known that FnBPA from S. aureus, have multiple intrinsically disordered, high-affinity binding repeats (FnBRs) for Fibronectin, which undergo a disorder-to-order transition on binding to Fn. In this tandem beta-zipper interaction, the FnBR extends the triple-stranded anti-parallel beta-sheet of sequential F1 modules by forming an additional strand anti-parallel to the C-terminal strand of each F1 module (PMID:18713862). [Type chain K]=Ordered [Evidence chain K]=The Fibronectin type I domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00039). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1tpm. [Chain L name]=Fibronectin-binding protein A [Chain L source organism]=Staphylococcus aureus [Chain L UniProt accession]=P14738 [Chain L UniProt boundaries]=639-646 [Chain L UniProt coverage]=0.8% [Chain L UniRef90 accession]=UniRef90_P14738 [Chain L UniRef90 boundaries]=639-646 [Chain K name]=Fibronectin [Chain K source organism]=Homo sapiens [Chain K UniProt accession]=P02751 [Chain K UniProt boundaries]=229-272 [Chain K UniProt coverage]=1.8% [Chain K UniRef90 accession]=UniRef90_P02751 [Chain K UniRef90 boundaries]=229-272 [Entry] [Accession]=DI1020031 [Disorder status]=Confirmed [Kd]=6.20E-08 [Name]=Second fibronectin f1 module in complex with a fragment of staphylococcus aureus fnbpa-5 [Source organism]=Staphylococcus aureus / Homo sapiens [PDB ID]=3cal [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant interaction. Chains A and B were truncated to only include residues 94-138 and 664-672 (according to UniProt numbering) to highlight the interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=Fibronectin type I [Type chain B]=Disordered [Evidence chain B]=It is known that FnBPA from S. aureus, have multiple intrinsically disordered, high-affinity binding repeats (FnBRs) for Fibronectin, which undergo a disorder-to-order transition on binding to Fn. In this tandem beta-zipper interaction, the FnBR extends the triple-stranded anti-parallel beta-sheet of sequential F1 modules by forming an additional strand anti-parallel to the C-terminal strand of each F1 module (PMID:18713862). [Type chain A]=Ordered [Evidence chain A]=The Fibronectin type I domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00039). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1tpm. [Chain B name]=Fibronectin-binding protein A [Chain B source organism]=Staphylococcus aureus [Chain B UniProt accession]=P14738 [Chain B UniProt boundaries]=664-672 [Chain B UniProt coverage]=0.9% [Chain B UniRef90 accession]=UniRef90_P14738 [Chain B UniRef90 boundaries]=664-672 [Chain A name]=Fibronectin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P02751 [Chain A UniProt boundaries]=94-138 [Chain A UniProt coverage]=1.9% [Chain A UniRef90 accession]=UniRef90_P02751 [Chain A UniRef90 boundaries]=94-138 [Entry] [Accession]=DI1020032 [Disorder status]=Confirmed [Kd]=6.20E-08 [Name]=Third fibronectin f1 module in complex with a fragment of staphylococcus aureus fnbpa-5 [Source organism]=Staphylococcus aureus / Homo sapiens [PDB ID]=3cal [PDB chain IDs]=D:C [PDB note]=Chains A and B were removed as chains C and D represent the biologically relevant interaction. Chains C and D were truncated to only include residues 139-182 and 655-663 (according to UniProt numbering) to highlight the interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=Fibronectin type I [Type chain D]=Disordered [Evidence chain D]=It is known that FnBPA from S. aureus, have multiple intrinsically disordered, high-affinity binding repeats (FnBRs) for Fibronectin, which undergo a disorder-to-order transition on binding to Fn. In this tandem beta-zipper interaction, the FnBR extends the triple-stranded anti-parallel beta-sheet of sequential F1 modules by forming an additional strand anti-parallel to the C-terminal strand of each F1 module (PMID:18713862). [Type chain C]=Ordered [Evidence chain C]=The Fibronectin type I domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00039). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1tpm. [Chain D name]=Fibronectin-binding protein A [Chain D source organism]=Staphylococcus aureus [Chain D UniProt accession]=P14738 [Chain D UniProt boundaries]=655-663 [Chain D UniProt coverage]=0.9% [Chain D UniRef90 accession]=UniRef90_P14738 [Chain D UniRef90 boundaries]=655-663 [Chain C name]=Fibronectin [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P02751 [Chain C UniProt boundaries]=139-182 [Chain C UniProt coverage]=1.8% [Chain C UniRef90 accession]=UniRef90_P02751 [Chain C UniRef90 boundaries]=139-182 [Entry] [Accession]=DI1010078 [Disorder status]=Inferred from motif [Kd]=2.30E-07 [Name]=WH2 domain of MIM complexed with actin [Source organism]=Homo sapiens / Oryctolagus cuniculus [PDB ID]=2d1k [PDB chain IDs]=C:A [PDB note]=Chain B was removed as chains C and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=Actin [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_Actin_WH2_2). [Type chain A]=Ordered [Evidence chain A]=The actin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00022). A solved monomeric structure of the domain is represented by PDB ID 1j6z. [Chain C name]=Metastasis suppressor protein 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=O43312 [Chain C UniProt boundaries]=724-755 [Chain C UniProt coverage]=4.2% [Chain C UniRef90 accession]=UniRef90_Q8R1S4 [Chain C UniRef90 boundaries]=724-755 [Chain A name]=Actin, alpha skeletal muscle [Chain A source organism]=Oryctolagus cuniculus [Chain A UniProt accession]=P68135 [Chain A UniProt boundaries]=3-377 [Chain A UniProt coverage]=99.5% [Chain A UniRef90 accession]=UniRef90_P68133 [Chain A UniRef90 boundaries]=3-377 [Entry] [Accession]=DI1110021 [Disorder status]=Confirmed [Kd]=1.90E-06 [Name]=Mal-Rpel2 complexed to G-actin [Source organism]=Mus musculus / Oryctolagus cuniculus [PDB ID]=2v52 [PDB chain IDs]=M:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.45 [Domain]=Actin [Type chain M]=Disordered [Evidence chain M]=It was shown that the RPEL peptide is largely unstructured in solution indicating that the observed secondary structure is induced by binding actin (PMID:19008859). The 16-142 region described in IDEAL entry IID50055 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_Actin_RPEL_3). [Type chain B]=Ordered [Evidence chain B]=The Actin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00022). A solved monomeric structure of the domain is represented by PDB ID 1j6z. [Chain M name]=MKL/myocardin-like protein 1 [Chain M source organism]=Mus musculus [Chain M UniProt accession]=Q8K4J6 [Chain M UniProt boundaries]=54-85 [Chain M UniProt coverage]=3.3% [Chain M UniRef90 accession]=UniRef90_Q8K4J6 [Chain M UniRef90 boundaries]=54-85 [Chain B name]=Actin, alpha skeletal muscle [Chain B source organism]=Oryctolagus cuniculus [Chain B UniProt accession]=P68135 [Chain B UniProt boundaries]=1-377 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P68133 [Chain B UniRef90 boundaries]=1-377 [Entry] [Accession]=DI1110022 [Disorder status]=Inferred from homology [Kd]=1.90E-06 [Name]=Second WH2 domain bound to actin from Oryctolagus cuniculus [Source organism]=Drosophila melanogaster / Oryctolagus cuniculus [PDB ID]=3mn5 [PDB chain IDs]=S:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.50 [Domain]=Actin [Type chain S]=Disordered [Evidence chain S]=The interacting region contains a WH2 domain (Pfam motif PF02205) that is known to be disordered (PMID:19260013, PMID:11911886). The protein region involved in the interaction contains a known functional linear motif (LIG_Actin_WH2_1). [Type chain A]=Ordered [Evidence chain A]=The Actin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00022). A solved monomeric structure of the domain is represented by PDB ID 1j6z. [Chain S name]=Protein spire [Chain S source organism]=Drosophila melanogaster [Chain S UniProt accession]=Q9U1K1 [Chain S UniProt boundaries]=448-485 [Chain S UniProt coverage]=3.7% [Chain S UniRef90 accession]=UniRef90_Q9U1K1 [Chain S UniRef90 boundaries]=448-485 [Chain A name]=Actin, alpha skeletal muscle [Chain A source organism]=Oryctolagus cuniculus [Chain A UniProt accession]=P68135 [Chain A UniProt boundaries]=3-377 [Chain A UniProt coverage]=99.5% [Chain A UniRef90 accession]=UniRef90_P68133 [Chain A UniRef90 boundaries]=3-377 [Related structures]=3ue5 [Entry] [Accession]=DI1100073 [Disorder status]=Inferred from homology [Kd]=1.90E-06 [Name]=Second WH2 domain bound to actin from Drosophila melanogaster [Source organism]=Drosophila melanogaster [PDB ID]=3mn7 [PDB chain IDs]=S:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Actin [Type chain S]=Disordered [Evidence chain S]=The interacting region contains a WH2 domain (Pfam motif PF02205) that is known to be disordered (PMID:19260013, PMID:11911886). The protein region involved in the interaction contains a known functional linear motif (LIG_Actin_WH2_1). [Type chain A]=Ordered [Evidence chain A]=The Actin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00022). A solved monomeric structure of the domain is represented by PDB ID 2hf3. [Chain S name]=Protein spire [Chain S source organism]=Drosophila melanogaster [Chain S UniProt accession]=Q9U1K1 [Chain S UniProt boundaries]=437-483 [Chain S UniProt coverage]=4.6% [Chain S UniRef90 accession]=UniRef90_Q9U1K1 [Chain S UniRef90 boundaries]=437-483 [Chain A name]=Actin-5C [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=P10987 [Chain A UniProt boundaries]=3-376 [Chain A UniProt coverage]=99.5% [Chain A UniRef90 accession]=UniRef90_P10987 [Chain A UniRef90 boundaries]=3-376 [Entry] [Accession]=DI1100074 [Disorder status]=Inferred from motif [Kd]=2.50E-04 [Name]=Itk SH2 domain bound to a phosphopeptide lymphocyte cytosolic protein 2 [Source organism]=Mus musculus [PDB ID]=2eu0 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_SH2_SRC). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain is represented by PDB ID 1lui. [Modified residues chain B]=phosphotyrosine#Y#121 [Chain B name]=Lymphocyte cytosolic protein 2 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q60787 [Chain B UniProt boundaries]=143-148 [Chain B UniProt coverage]=1.1% [Chain B UniRef90 accession]=UniRef90_Q60787 [Chain B UniRef90 boundaries]=143-148 [Chain A name]=Tyrosine-protein kinase ITK/TSK [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q03526 [Chain A UniProt boundaries]=237-345 [Chain A UniProt coverage]=17.4% [Chain A UniRef90 accession]=UniRef90_Q08881 [Chain A UniRef90 boundaries]=232-339 [Related structures]=2etz [Entry] [Accession]=DI1000225 [Disorder status]=Confirmed [Kd]=2.00E-08 [Name]=Second Nrf2 degron bound to Kelch-like ECH-associated protein 1 (Keap1) (human) [Source organism]=Homo sapiens [PDB ID]=2flu [PDB chain IDs]=P:X [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.50 [Domain]=Kelch [Type chain P]=Disordered [Evidence chain P]=The interacting region of Nrf2 is presumed to acquire a conformation that is induced by its binding with Keap1. The Nrf2 region involved in the interaction contains a known functional linear motif (DEG_Kelch_Keap1_1). [Type chain X]=Ordered [Evidence chain X]=The Kelch domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01344). A solved monomeric structure of the domain is represented by PDB ID 1u6d. [Chain P name]=Nuclear factor erythroid 2-related factor 2 [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=Q16236 [Chain P UniProt boundaries]=69-84 [Chain P UniProt coverage]=2.6% [Chain P UniRef90 accession]=UniRef90_Q16236 [Chain P UniRef90 boundaries]=69-84 [Chain X name]=Kelch-like ECH-associated protein 1 [Chain X source organism]=Homo sapiens [Chain X UniProt accession]=Q14145 [Chain X UniProt boundaries]=321-609 [Chain X UniProt coverage]=46.3% [Chain X UniRef90 accession]=UniRef90_Q14145 [Chain X UniRef90 boundaries]=321-609 [Related structures]=3zgc,4ifl [Entry] [Accession]=DI1100075 [Disorder status]=Inferred from motif [Kd]=2.00E-08 [Name]=Keap1 complexed with prothymosin alpha [Source organism]=Mus musculus [PDB ID]=2z32 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Kelch [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (DEG_Kelch_Keap1_1). [Type chain A]=Ordered [Evidence chain A]=The Kelch domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01344). A solved monomeric structure of the domain is represented by PDB ID 1x2j. [Chain B name]=Prothymosin alpha [Chain B source organism]=Mus musculus [Chain B UniProt accession]=P26350 [Chain B UniProt boundaries]=39-54 [Chain B UniProt coverage]=14.4% [Chain B UniRef90 accession]=UniRef90_P26350 [Chain B UniRef90 boundaries]=39-54 [Chain A name]=Kelch-like ECH-associated protein 1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q9Z2X8 [Chain A UniProt boundaries]=308-624 [Chain A UniProt coverage]=50.8% [Chain A UniRef90 accession]=UniRef90_Q14145 [Chain A UniRef90 boundaries]=308-624 [Entry] [Accession]=DI1100076 [Disorder status]=Inferred from motif [Kd]=2.00E-08 [Name]=Keap1 in complex with unmodified sequestosome-1/p62 peptide [Source organism]=Mus musculus [PDB ID]=3ade [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=Kelch [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (DEG_Kelch_Keap1_1). [Type chain A]=Ordered [Evidence chain A]=The Kelch domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01344). A solved monomeric structure of the domain is represented by PDB ID 1x2j. [Chain B name]=Sequestosome-1 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q64337 [Chain B UniProt boundaries]=346-359 [Chain B UniProt coverage]=3.2% [Chain B UniRef90 accession]=UniRef90_Q13501 [Chain B UniRef90 boundaries]=346-359 [Chain A name]=Kelch-like ECH-associated protein 1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q9Z2X8 [Chain A UniProt boundaries]=309-624 [Chain A UniProt coverage]=50.6% [Chain A UniRef90 accession]=UniRef90_Q14145 [Chain A UniRef90 boundaries]=309-624 [Entry] [Accession]=DI1000226 [Disorder status]=Confirmed [Kd]=2.09E-05 [Name]=N-terminal domain of HAUSP/USP7 complexed with p53 peptide 364-367 [Source organism]=Homo sapiens [PDB ID]=2foj [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.60 [Domain]=MATH [Type chain B]=Disordered [Evidence chain B]=The 320-393 region described in DisProt entry DP00086 and the 364-389 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (DOC_USP7_MATH_1). [Type chain A]=Ordered [Evidence chain A]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00917). A solved monomeric structure of the domain is represented by PDB ID 1yze. [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=361-367 [Chain B UniProt coverage]=1.8% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=361-367 [Chain A name]=Ubiquitin carboxyl-terminal hydrolase 7 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q93009 [Chain A UniProt boundaries]=54-205 [Chain A UniProt coverage]=13.8% [Chain A UniRef90 accession]=UniRef90_Q93009 [Chain A UniRef90 boundaries]=54-205 [Entry] [Accession]=DI1000227 [Disorder status]=Confirmed [Kd]=1.85E-05 [Name]=N-terminal domain of HAUSP/USP7 complexed with p53 peptide 359-362 [Source organism]=Homo sapiens [PDB ID]=2foo [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=MATH [Type chain B]=Disordered [Evidence chain B]=The 320-393 region described in DisProt entry DP00086 and the 364-389 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (DOC_USP7_MATH_1). [Type chain A]=Ordered [Evidence chain A]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00917). A solved monomeric structure of the domain is represented by PDB ID 1yze. [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=358-363 [Chain B UniProt coverage]=1.5% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=358-363 [Chain A name]=Ubiquitin carboxyl-terminal hydrolase 7 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q93009 [Chain A UniProt boundaries]=54-205 [Chain A UniProt coverage]=13.8% [Chain A UniRef90 accession]=UniRef90_Q93009 [Chain A UniRef90 boundaries]=54-205 [Entry] [Accession]=DI1020033 [Disorder status]=Confirmed [Kd]=1.85E-05 [Name]=Sir2 in complex with an unmodified p53 peptide [Source organism]=Homo sapiens / Thermotoga maritima [PDB ID]=2h4j [PDB chain IDs]=D:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=Sirtuin [Type chain D]=Disordered [Evidence chain D]=The 320-393 region described in DisProt entry DP00086 and the 364-389 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The sirtuin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02146). A solved monomeric structure of the domain is represented by PDB ID 2h2i. [Chain D name]=Cellular tumor antigen p53 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P04637 [Chain D UniProt boundaries]=372-389 [Chain D UniProt coverage]=4.6% [Chain D UniRef90 accession]=UniRef90_P04637 [Chain D UniRef90 boundaries]=372-389 [Chain A name]=NAD-dependent protein deacetylase [Chain A source organism]=Thermotoga maritima [Chain A UniProt accession]=Q9WYW0 [Chain A UniProt boundaries]=1-246 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q9WYW0 [Chain A UniRef90 boundaries]=1-246 [Related structures]=2h59,2h2f,4bv2 [Entry] [Accession]=DI1000228 [Disorder status]=Confirmed [Kd]=2.00E-07 [Name]=Methyltransferase SET9 in complex with a p53 peptide [Source organism]=Homo sapiens [PDB ID]=1xqh [PDB chain IDs]=B:A [PDB note]=Chain E and F were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.75 [Domain]=SET [Type chain B]=Disordered [Evidence chain B]=The 320-393 region described in DisProt entry DP00086 and the 364-389 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The SET domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00856). A solved structure of the domain without bound ligands is represented by PDB ID 1mt6b. [Modified residues chain B]=N-methyl-lysine#K#372 [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=369-377 [Chain B UniProt coverage]=2.3% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=369-377 [Chain A name]=Histone-lysine N-methyltransferase SETD7 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q8WTS6 [Chain A UniProt boundaries]=108-366 [Chain A UniProt coverage]=70.8% [Chain A UniRef90 accession]=UniRef90_Q8WTS6 [Chain A UniRef90 boundaries]=108-366 [Entry] [Accession]=DI1020034 [Disorder status]=Confirmed [Kd]=2.00E-07 [Name]=Sir2 enzyme from Archaeoglobus fulgidus bound to an acetylated p53 peptide [Source organism]=Homo sapiens / Archaeoglobus fulgidus [PDB ID]=1ma3 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=SET [Type chain B]=Disordered [Evidence chain B]=The 320-393 region described in DisProt entry DP00086 and the 364-389 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The SET domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00856). A solved structure of the domain without bound ligands is represented by PDB ID 1s7g. [Modified residues chain B]=N(6)-acetyllysine#K#11 [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=372-389 [Chain B UniProt coverage]=4.6% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=372-389 [Chain A name]=NAD-dependent protein deacylase 2 [Chain A source organism]=Archaeoglobus fulgidus [Chain A UniProt accession]=O30124 [Chain A UniProt boundaries]=1-253 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_O30124 [Chain A UniRef90 boundaries]=1-253 [Entry] [Accession]=DI1000229 [Disorder status]=Confirmed [Kd]=2.00E-07 [Name]=Sirtuin 1 in complex with a p53 peptide [Source organism]=Homo sapiens [PDB ID]=4zzj [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.74 [Domain]=Sirtuin [Type chain B]=Disordered [Evidence chain B]=The 320-393 region described in DisProt entry DP00086 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The sirtuin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02146). A solved monomeric structure of the domain is represented by PDB ID 4zzh. [Modified residues chain B]=N(6)-acetyllysine#K#4|norleucine#L#6 [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=379-385 [Chain B UniProt coverage]=1.8% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=379-385 [Chain A name]=NAD-dependent protein deacetylase sirtuin-1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96EB6 [Chain A UniProt boundaries]=183-505 [Chain A UniProt coverage]=43.2% [Chain A UniRef90 accession]=UniRef90_Q96EB6 [Chain A UniRef90 boundaries]=183-505 [Entry] [Accession]=DI2000032 [Disorder status]=Confirmed [Kd]=1.63E-05 [Name]=Human 14-3-3 sigma in complex with p53 [Source organism]=Homo sapiens [PDB ID]=3lw1 [PDB chain IDs]=P:AB [PDB note]=Chain B was generated using the biomatrix described in the PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.28 [Domain]=14-3-3 [Type chain P]=Disordered [Evidence chain P]=The 320-393 region described in DisProt entry DP00086 covers 100% of the sequence present in the structure. [Type chain A]=Ordered component [Evidence chain A]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1yz5. [Type chain B]=Ordered component [Evidence chain B]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1yz5. [Modified residues chain P]=phosphothreonine#T#387 [Modified residues chain B]=N(6)-acetyllysine#K#4|norleucine#L#6 [Chain P name]=Cellular tumor antigen p53 [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=P04637 [Chain P UniProt boundaries]=385-393 [Chain P UniProt coverage]=2.3% [Chain P UniRef90 accession]=UniRef90_P04637 [Chain P UniRef90 boundaries]=385-393 [Chain A name]=14-3-3 protein sigma [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P31947 [Chain A UniProt boundaries]=1-248 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P31947 [Chain A UniRef90 boundaries]=1-248 [Chain B name]=14-3-3 protein sigma [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P31947 [Chain B UniProt boundaries]=1-248 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P31947 [Chain B UniRef90 boundaries]=1-248 [Entry] [Accession]=DI1000230 [Disorder status]=Confirmed [Kd]=2.00E-05 [Name]=SMYD2 in complex with p53 peptide [Source organism]=Homo sapiens [PDB ID]=3tg5 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=SET [Type chain B]=Disordered [Evidence chain B]=The 320-393 region described in DisProt entry DP00086 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The SET domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00856). A solved structure of the domain without bound ligands is represented by PDB ID 3s7b. [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=365-375 [Chain B UniProt coverage]=2.8% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=365-375 [Chain A name]=N-lysine methyltransferase SMYD2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9NRG4 [Chain A UniProt boundaries]=1-433 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q9NRG4 [Chain A UniRef90 boundaries]=1-433 [Entry] [Accession]=DI1000231 [Disorder status]=Inferred from motif [Kd]=7.97E-06 [Name]=N-terminal domain of HAUSP/USP7 complexed with MDM2 peptide 147-150 [Source organism]=Homo sapiens [PDB ID]=2fop [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=MATH [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (DOC_USP7_MATH_1). [Type chain A]=Ordered [Evidence chain A]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00917). A solved monomeric structure of the domain is represented by PDB ID 1yze. [Chain B name]=E3 ubiquitin-protein ligase Mdm2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q00987 [Chain B UniProt boundaries]=145-150 [Chain B UniProt coverage]=1.2% [Chain B UniRef90 accession]=UniRef90_Q00987 [Chain B UniRef90 boundaries]=145-150 [Chain A name]=Ubiquitin carboxyl-terminal hydrolase 7 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q93009 [Chain A UniProt boundaries]=54-205 [Chain A UniProt coverage]=13.8% [Chain A UniRef90 accession]=UniRef90_Q93009 [Chain A UniRef90 boundaries]=54-205 [Entry] [Accession]=DI1000232 [Disorder status]=Inferred from motif [Kd]=2.18E-05 (PMID:20713061) [Name]=N-terminal domain of HAUSP/USP7 complexed with HdmX peptide [Source organism]=Homo sapiens [PDB ID]=3mqr [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=MATH [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (DOC_USP7_MATH_1). [Type chain A]=Ordered [Evidence chain A]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00917). A solved monomeric structure of the domain is represented by PDB ID 1yze. [Chain B name]=Protein Mdm4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O15151 [Chain B UniProt boundaries]=395-404 [Chain B UniProt coverage]=2% [Chain B UniRef90 accession]=UniRef90_O15151 [Chain B UniRef90 boundaries]=395-404 [Chain A name]=Ubiquitin carboxyl-terminal hydrolase 7 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q93009 [Chain A UniProt boundaries]=54-205 [Chain A UniProt coverage]=13.8% [Chain A UniRef90 accession]=UniRef90_Q93009 [Chain A UniRef90 boundaries]=54-205 [Entry] [Accession]=DI1000233 [Disorder status]=Inferred from motif [Kd]=9.70E-06 (PMID:20713061) [Name]=N-terminal domain of HAUSP/USP7 complexed with Hdm2 peptide [Source organism]=Homo sapiens [PDB ID]=3mqs [PDB chain IDs]=D:C [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=MATH [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a known functional linear motif (DOC_USP7_MATH_1). [Type chain C]=Ordered [Evidence chain C]=The MATH domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00917). A solved monomeric structure of the domain is represented by PDB ID 1yze. [Chain D name]=E3 ubiquitin-protein ligase Mdm2 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=Q00987 [Chain D UniProt boundaries]=394-403 [Chain D UniProt coverage]=2% [Chain D UniRef90 accession]=UniRef90_Q00987 [Chain D UniRef90 boundaries]=394-403 [Chain C name]=Ubiquitin carboxyl-terminal hydrolase 7 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q93009 [Chain C UniProt boundaries]=54-205 [Chain C UniProt coverage]=13.8% [Chain C UniRef90 accession]=UniRef90_Q93009 [Chain C UniRef90 boundaries]=54-205 [Entry] [Accession]=DI1000234 [Disorder status]=Inferred from motif [Kd]=2.40E-06 [Name]=Beta appendage from Ap2 in complex with ARH peptide [Source organism]=Homo sapiens [PDB ID]=2g30 [PDB chain IDs]=P:A [PDB note]=Chain S was removed as chains P and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.60 [Domain]=Adaptin C-terminal domain [Type chain P]=Disordered [Evidence chain P]=The protein region involved in the interaction contains a known functional linear motif (TRG_AP2beta_CARGO_1). [Type chain A]=Ordered [Evidence chain A]=Adaptin C-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domains PF02883/PF09066). A solved monomeric structure of the domain is represented by PDB ID 1e42. [Chain P name]=Low density lipoprotein receptor adapter protein 1 [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=Q5SW96 [Chain P UniProt boundaries]=252-267 [Chain P UniProt coverage]=5.2% [Chain P UniRef90 accession]=UniRef90_Q5SW96 [Chain P UniRef90 boundaries]=252-267 [Chain A name]=AP-2 complex subunit beta [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63010 [Chain A UniProt boundaries]=701-937 [Chain A UniProt coverage]=25.3% [Chain A UniRef90 accession]=UniRef90_P63010 [Chain A UniRef90 boundaries]=701-937 [Entry] [Accession]=DI1110023 [Disorder status]=Inferred from motif [Kd]=2.10E-05 [Name]=Alpha-2 adaptin appendage domain in complex with an amphiphysin peptide (FXDNF) [Source organism]=Rattus norvegicus / Mus musculus [PDB ID]=2vj0 [PDB chain IDs]=Q:A [PDB note]=Chain P was removed as chains Q and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.60 [Domain]=Adaptin C-terminal domain [Type chain Q]=Disordered [Evidence chain Q]=The protein region involved in the interaction contains a known functional linear motif (LIG_AP2alpha_1). [Type chain A]=Ordered [Evidence chain A]=Adaptin C-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domains PF02883/PF09066). A solved monomeric structure of the domain is represented by PDB ID 1b9k. [Chain Q name]=Amphiphysin [Chain Q source organism]=Rattus norvegicus [Chain Q UniProt accession]=O08838 [Chain Q UniProt boundaries]=324-330 [Chain Q UniProt coverage]=1% [Chain Q UniRef90 accession]=UniRef90_O08838 [Chain Q UniRef90 boundaries]=324-330 [Chain A name]=AP-2 complex subunit alpha-2 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P17427 [Chain A UniProt boundaries]=690-938 [Chain A UniProt coverage]=26.5% [Chain A UniRef90 accession]=UniRef90_P17427 [Chain A UniRef90 boundaries]=690-938 [Entry] [Accession]=DI1100077 [Disorder status]=Inferred from motif [Kd]=3.50E-06 [Name]=Grb2 N-terminal SH3 domain complexed with a ten-residue peptide derived from SOS [Source organism]=Mus musculus [PDB ID]=2gbq [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH3 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_SH3_3). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00018). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2a36. [Chain B name]=Son of sevenless homolog 1 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q62245 [Chain B UniProt boundaries]=1135-1144 [Chain B UniProt coverage]=0.8% [Chain B UniRef90 accession]=UniRef90_Q07889 [Chain B UniRef90 boundaries]=1135-1144 [Chain A name]=Growth factor receptor-bound protein 2 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q60631 [Chain A UniProt boundaries]=1-61 [Chain A UniProt coverage]=28.1% [Chain A UniRef90 accession]=UniRef90_P62993 [Chain A UniRef90 boundaries]=1-61 [Related structures]=1gbq,3gbq,4gbq [Entry] [Accession]=DI1010079 [Disorder status]=Inferred from motif [Kd]=6.30E-06 (PMID:23047924) [Name]=Docking motif interactions in the MAP kinase ERK2 [Source organism]=Homo sapiens / Rattus norvegicus [PDB ID]=2gph [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=Protein kinase [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (DOC_MAPK_HePTP_8). [Type chain A]=Ordered [Evidence chain A]=The Protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 1erk. [Chain B name]=Tyrosine-protein phosphatase non-receptor type 7 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P35236 [Chain B UniProt boundaries]=37-52 [Chain B UniProt coverage]=4.4% [Chain B UniRef90 accession]=UniRef90_P35236 [Chain B UniRef90 boundaries]=37-52 [Chain A name]=Mitogen-activated protein kinase 1 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=P63086 [Chain A UniProt boundaries]=2-358 [Chain A UniProt coverage]=99.7% [Chain A UniRef90 accession]=UniRef90_P28482 [Chain A UniRef90 boundaries]=2-358 [Entry] [Accession]=DI1000235 [Disorder status]=Inferred from motif [Kd]=6.30E-06 (PMID:23047924) [Name]=Estrogen Related Receptor-gamma ligand binding domain complexed with a synthetic peptide from RIP140 [Source organism]=Homo sapiens [PDB ID]=2gpo [PDB chain IDs]=C:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.95 [Domain]=Nuclear hormone receptor [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_NRBOX). [Type chain A]=Ordered [Evidence chain A]=The Nuclear hormone receptor domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00104). A solved monomeric structure of the domain is represented by PDB ID 2e2r. [Chain C name]=Nuclear receptor-interacting protein 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P48552 [Chain C UniProt boundaries]=366-390 [Chain C UniProt coverage]=2.2% [Chain C UniRef90 accession]=UniRef90_P48552 [Chain C UniRef90 boundaries]=366-390 [Chain A name]=Estrogen-related receptor gamma [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P62508 [Chain A UniProt boundaries]=229-458 [Chain A UniProt coverage]=50.2% [Chain A UniRef90 accession]=UniRef90_P62508 [Chain A UniRef90 boundaries]=229-458 [Related structures]=2gpp [Entry] [Accession]=DI1000236 [Disorder status]=Inferred from motif [Kd]=6.30E-06 (PMID:23047924) [Name]=Peroxisome proliferator-activated receptor gamma bound to a PGC-1alpha peptide [Source organism]=Homo sapiens [PDB ID]=3cs8 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=Nuclear hormone receptor [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_NRBOX). [Type chain A]=Ordered [Evidence chain A]=The Nuclear hormone receptor domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00104). A solved monomeric structure of the domain is represented by PDB ID 1i7i. [Chain B name]=Peroxisome proliferator-activated receptor gamma coactivator 1-alpha [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9UBK2 [Chain B UniProt boundaries]=141-152 [Chain B UniProt coverage]=1.5% [Chain B UniRef90 accession]=UniRef90_Q9UBK2 [Chain B UniRef90 boundaries]=141-152 [Chain A name]=Peroxisome proliferator-activated receptor gamma [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P37231 [Chain A UniProt boundaries]=234-504 [Chain A UniProt coverage]=53.7% [Chain A UniRef90 accession]=UniRef90_P37231 [Chain A UniRef90 boundaries]=234-504 [Related structures]=3b1m,3u9q,3v9t,3v9v,5two [Entry] [Accession]=DI2000033 [Disorder status]=Inferred from motif [Kd]=6.00E-07 (PMID:17466438) [Name]=Human glucocorticoid receptor in complex with a Nuclear receptor corepressor 1 peptide [Source organism]=Homo sapiens [PDB ID]=3h52 [PDB chain IDs]=N:AD [PDB note]=Chains B, C and M were removed as chains A, D and N highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=Nuclear hormone receptor [Type chain N]=Disordered [Evidence chain N]=The protein region involved in the interaction contains a known functional linear motif (LIG_CORNRBOX). [Type chain A]=Ordered [Evidence chain A]=The ordered partner is a domain-swapped PDZ dimer. PDZ domains are known to adopt a stable structure in isolation, even in their monomeric form (see Pfam domain PF00104). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1nhz. [Type chain D]=Ordered [Evidence chain D]=The ordered partner is a domain-swapped PDZ dimer. PDZ domains are known to adopt a stable structure in isolation, even in their monomeric form (see Pfam domain PF00104). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1nhz. [Chain N name]=Nuclear receptor corepressor 1 [Chain N source organism]=Homo sapiens [Chain N UniProt accession]=O75376 [Chain N UniProt boundaries]=2258-2276 [Chain N UniProt coverage]=0.8% [Chain N UniRef90 accession]=UniRef90_Q60974 [Chain N UniRef90 boundaries]=2258-2276 [Chain A name]=Glucocorticoid receptor [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P04150 [Chain A UniProt boundaries]=528-777 [Chain A UniProt coverage]=32.2% [Chain A UniRef90 accession]=UniRef90_P04150 [Chain A UniRef90 boundaries]=528-777 [Chain D name]=Glucocorticoid receptor [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P04150 [Chain D UniProt boundaries]=528-777 [Chain D UniProt coverage]=32.2% [Chain D UniRef90 accession]=UniRef90_P04150 [Chain D UniRef90 boundaries]=528-777 [Related structures]=4mdd [Entry] [Accession]=DI1000237 [Disorder status]=Inferred from motif [Kd]=1.72E-05 [Name]=JNK3 in complex with a SAB peptide [Source organism]=Homo sapiens [PDB ID]=4h3b [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains B and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.08 [Domain]=Protein kinase [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (DOC_MAPK_JIP1_4). [Type chain A]=Ordered [Evidence chain A]=The Protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 1jnk. [Chain B name]=SH3 domain-binding protein 5 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O60239 [Chain B UniProt boundaries]=341-350 [Chain B UniProt coverage]=2.2% [Chain B UniRef90 accession]=UniRef90_O60239 [Chain B UniRef90 boundaries]=341-350 [Chain A name]=Mitogen-activated protein kinase 10 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P53779 [Chain A UniProt boundaries]=45-400 [Chain A UniProt coverage]=76.7% [Chain A UniRef90 accession]=UniRef90_P53779 [Chain A UniRef90 boundaries]=45-400 [Entry] [Accession]=DI1100078 [Disorder status]=Inferred from motif [Kd]=2.50E-06 [Name]=p38 (Mapk14) bound to a TAB1 peptide [Source organism]=Mus musculus [PDB ID]=4loo [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.95 [Domain]=Protein kinase [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (DOC_MAPK_MEF2A_6). [Type chain A]=Ordered [Evidence chain A]=The Protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 3py3. [Chain B name]=TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q8CF89 [Chain B UniProt boundaries]=384-412 [Chain B UniProt coverage]=5.8% [Chain B UniRef90 accession]=UniRef90_Q15750 [Chain B UniRef90 boundaries]=384-412 [Chain A name]=Mitogen-activated protein kinase 14 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P47811 [Chain A UniProt boundaries]=1-360 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P47811 [Chain A UniRef90 boundaries]=1-360 [Related structures]=4ka3,4lop,4loq [Entry] [Accession]=DI1000238 [Disorder status]=Inferred from motif [Kd]=2.00E-08 (PMID:15287722) [Name]=p38 alpha bound to a MAPKAP kinase 2 peptide [Source organism]=Homo sapiens [PDB ID]=2okr [PDB chain IDs]=C:A [PDB note]=Chains D and F were removed as chains C and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Protein kinase [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (DOC_MAPK_RevD_3). [Type chain A]=Ordered [Evidence chain A]=The Protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 1a9u. [Chain C name]=MAP kinase-activated protein kinase 2 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P49137 [Chain C UniProt boundaries]=370-393 [Chain C UniProt coverage]=6% [Chain C UniRef90 accession]=UniRef90_P49137 [Chain C UniRef90 boundaries]=370-393 [Chain A name]=Mitogen-activated protein kinase 14 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q16539 [Chain A UniProt boundaries]=2-360 [Chain A UniProt coverage]=99.7% [Chain A UniRef90 accession]=UniRef90_Q16539 [Chain A UniRef90 boundaries]=2-360 [Related structures]=2onl [Entry] [Accession]=DI1000239 [Disorder status]=Inferred from motif [Kd]=7.10E-06 [Name]=Jnk1 bound to a NFAT4 peptide [Source organism]=Homo sapiens [PDB ID]=2xs0 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=Protein kinase [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (DOC_MAPK_NFAT4_5). [Type chain A]=Ordered [Evidence chain A]=The Protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 3elj. [Chain B name]=Nuclear factor of activated T-cells, cytoplasmic 3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q12968 [Chain B UniProt boundaries]=141-154 [Chain B UniProt coverage]=1.3% [Chain B UniRef90 accession]=UniRef90_Q12968 [Chain B UniRef90 boundaries]=141-154 [Chain A name]=Mitogen-activated protein kinase 8 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P45983 [Chain A UniProt boundaries]=1-379 [Chain A UniProt coverage]=88.8% [Chain A UniRef90 accession]=UniRef90_P45983 [Chain A UniRef90 boundaries]=1-379 [Related structures]=2xrw [Entry] [Accession]=DI1000240 [Disorder status]=Inferred from motif [Kd]=7.00E-07 (PMID:23047924) [Name]=Human ERK2 complexed with a MAPK docking peptide [Source organism]=Homo sapiens [PDB ID]=2y9q [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.55 [Domain]=Protein kinase [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (DOC_MAPK_RevD_3). [Type chain A]=Ordered [Evidence chain A]=The Protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 4g6n. [Chain B name]=MAP kinase-interacting serine/threonine-protein kinase 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9BUB5 [Chain B UniProt boundaries]=434-451 [Chain B UniProt coverage]=3.9% [Chain B UniRef90 accession]=UniRef90_Q9BUB5 [Chain B UniRef90 boundaries]=434-451 [Chain A name]=Mitogen-activated protein kinase 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P28482 [Chain A UniProt boundaries]=1-360 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P28482 [Chain A UniRef90 boundaries]=1-360 [Entry] [Accession]=DI1100079 [Disorder status]=Inferred from motif [Kd]=1.70E-05 [Name]=ERK2/DCC peptide complex [Source organism]=Rattus norvegicus [PDB ID]=3o71 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.95 [Domain]=Protein kinase [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (DOC_MAPK_DCC_7). [Type chain A]=Ordered [Evidence chain A]=The Protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 1erk. [Chain B name]=Netrin receptor DCC [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=Q63155 [Chain B UniProt boundaries]=1140-1166 [Chain B UniProt coverage]=1.9% [Chain B UniRef90 accession]=UniRef90_P43146 [Chain B UniRef90 boundaries]=1140-1166 [Chain A name]=Mitogen-activated protein kinase 1 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=P63086 [Chain A UniProt boundaries]=1-358 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P28482 [Chain A UniRef90 boundaries]=1-358 [Entry] [Accession]=DI1000241 [Disorder status]=Inferred from motif [Kd]=1.40E-05 (PMID:20711187) [Name]=The first two RRM domains of FIR in the complex with FBP Nbox peptide [Source organism]=Homo sapiens [PDB ID]=2kxh [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=RRM [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_NBox_RRM_1). [Type chain A]=Ordered [Evidence chain A]=The RRM domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00076). A solved monomeric structure of the domain is represented by PDB ID 2kxf. [Chain B name]=Far upstream element-binding protein 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q96AE4 [Chain B UniProt boundaries]=27-52 [Chain B UniProt coverage]=4% [Chain B UniRef90 accession]=UniRef90_Q96AE4 [Chain B UniRef90 boundaries]=27-52 [Chain A name]=Poly(U)-binding-splicing factor PUF60 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UHX1 [Chain A UniProt boundaries]=119-314 [Chain A UniProt coverage]=35.1% [Chain A UniRef90 accession]=UniRef90_Q9UHX1 [Chain A UniRef90 boundaries]=119-314 [Entry] [Accession]=DI1100080 [Disorder status]=Inferred from motif [Kd]=3.56E-08 [Name]=B30.2/SPRY domain of GUSTAVUS in complex with a 20-residue VASA peptide [Source organism]=Drosophila melanogaster [PDB ID]=2ihs [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains C and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=SPRY [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_SPRY_1). [Type chain A]=Ordered [Evidence chain A]=The SPRY domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00622). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3ek9. [Chain C name]=ATP-dependent RNA helicase vasa, isoform A [Chain C source organism]=Drosophila melanogaster [Chain C UniProt accession]=P09052 [Chain C UniProt boundaries]=184-203 [Chain C UniProt coverage]=3% [Chain C UniRef90 accession]=UniRef90_P09052 [Chain C UniRef90 boundaries]=184-203 [Chain A name]=Protein gustavus [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=A1Z6E0 [Chain A UniProt boundaries]=27-232 [Chain A UniProt coverage]=73.8% [Chain A UniRef90 accession]=UniRef90_A1Z6E0 [Chain A UniRef90 boundaries]=27-232 [Entry] [Accession]=DI1010080 [Disorder status]=Inferred from motif [Kd]=4.00E-08 [Name]=Human splA/ryanodine receptor domain and SOCS box containing 1 (SPSB1) in complex with a 20-residue VASA peptide [Source organism]=Drosophila melanogaster / Homo sapiens [PDB ID]=3f2o [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.05 [Domain]=SPRY [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_SPRY_1). [Type chain A]=Ordered [Evidence chain A]=The SPRY domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00622). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3ek9. [Chain C name]=ATP-dependent RNA helicase vasa, isoform A [Chain C source organism]=Drosophila melanogaster [Chain C UniProt accession]=P09052 [Chain C UniProt boundaries]=184-203 [Chain C UniProt coverage]=3% [Chain C UniRef90 accession]=UniRef90_P09052 [Chain C UniRef90 boundaries]=184-203 [Chain A name]=SPRY domain-containing SOCS box protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96BD6 [Chain A UniProt boundaries]=24-233 [Chain A UniProt coverage]=76.9% [Chain A UniRef90 accession]=UniRef90_Q96BD6 [Chain A UniRef90 boundaries]=24-233 [Entry] [Accession]=DI1000242 [Disorder status]=Inferred from motif [Kd]=1.20E-06 [Name]=Rb C-terminal peptide bound to the catalytic subunit of PP1 [Source organism]=Homo sapiens [PDB ID]=3n5u [PDB chain IDs]=C:A [PDB note]=Chain B was removed as chains C and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.20 [Domain]=Calcineurin-like phosphoesterase [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (DOC_PP1_RVXF_1). [Type chain A]=Ordered [Evidence chain A]=The calcineurin-like phosphoesterase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00149). A solved monomeric structure of the domain is represented by PDB ID 4mov. [Chain C name]=Retinoblastoma-associated protein [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P06400 [Chain C UniProt boundaries]=870-882 [Chain C UniProt coverage]=1.4% [Chain C UniRef90 accession]=UniRef90_P06400 [Chain C UniRef90 boundaries]=870-882 [Chain A name]=Serine/threonine-protein phosphatase PP1-alpha catalytic subunit [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P62136 [Chain A UniProt boundaries]=1-300 [Chain A UniProt coverage]=90.9% [Chain A UniRef90 accession]=UniRef90_P62136 [Chain A UniRef90 boundaries]=1-300 [Entry] [Accession]=DI1000243 [Disorder status]=Inferred from motif [Kd]=3.00E-06 [Name]=GABARAPL-1:NBR1-LIR complex [Source organism]=Homo sapiens [PDB ID]=2l8j [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Atg8 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_LIR_Gen_1). [Type chain A]=Ordered [Evidence chain A]=The Atg8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02991). A solved monomeric structure of the domain is represented by PDB ID 2r2q. [Chain B name]=Next to BRCA1 gene 1 protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q14596 [Chain B UniProt boundaries]=726-738 [Chain B UniProt coverage]=1.3% [Chain B UniRef90 accession]=UniRef90_Q14596 [Chain B UniRef90 boundaries]=726-738 [Chain A name]=Gamma-aminobutyric acid receptor-associated protein-like 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9H0R8 [Chain A UniProt boundaries]=1-115 [Chain A UniProt coverage]=98.3% [Chain A UniRef90 accession]=UniRef90_Q9H0R8 [Chain A UniRef90 boundaries]=1-115 [Entry] [Accession]=DI1100081 [Disorder status]=Inferred from motif [Kd]=3.00E-06 [Name]=Saccharomyces cerevisiae Atg8- Atg19(412-415) complex [Source organism]=Saccharomyces cerevisiae [PDB ID]=2zpn [PDB chain IDs]=E:A [PDB note]=Chains B, C, D, F, G and H were removed as chains A and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.70 [Domain]=Atg8 [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (LIG_LIR_Gen_1). [Type chain A]=Ordered [Evidence chain A]=The Atg8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02991). A solved monomeric structure of the domain is represented by PDB ID 2kq7. [Chain E name]=Autophagy-related protein 19 [Chain E source organism]=Saccharomyces cerevisiae [Chain E UniProt accession]=P35193 [Chain E UniProt boundaries]=412-415 [Chain E UniProt coverage]=1% [Chain E UniRef90 accession]=UniRef90_P35193 [Chain E UniRef90 boundaries]=412-415 [Chain A name]=Autophagy-related protein 8 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P38182 [Chain A UniProt boundaries]=1-116 [Chain A UniProt coverage]=99.1% [Chain A UniRef90 accession]=UniRef90_Q6FXR8 [Chain A UniRef90 boundaries]=1-116 [Entry] [Accession]=DI1100082 [Disorder status]=Inferred from motif [Kd]=3.00E-06 [Name]=Plasmodium falciparum Atg8 in complex with Plasmodium falciparum Atg3 peptide [Source organism]=Plasmodium falciparum [PDB ID]=4eoy [PDB chain IDs]=D:A [PDB note]=Chains B, C, E and F were removed as chains D and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.22 [Domain]=Atg8 [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a known functional linear motif (LIG_LIR_Apic_2). [Type chain A]=Ordered [Evidence chain A]=The Atg8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02991). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2kq7. [Chain D name]=Autophagy-related protein 3 [Chain D source organism]=Plasmodium falciparum [Chain D UniProt accession]=C0H519 [Chain D UniProt boundaries]=103-110 [Chain D UniProt coverage]=2.6% [Chain D UniRef90 accession]=UniRef90_A0A060RS78 [Chain D UniRef90 boundaries]=103-110 [Chain A name]=Autophagy-related protein [Chain A source organism]=Plasmodium falciparum [Chain A UniProt accession]=Q8IJK2 [Chain A UniProt boundaries]=1-124 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q8IJK2 [Chain A UniRef90 boundaries]=1-124 [Entry] [Accession]=DI2000034 [Disorder status]=Confirmed [Kd]=1.10E-06 [Name]=Bcl-XL:Beclin 1 complex [Source organism]=Homo sapiens [PDB ID]=2p1l [PDB chain IDs]=B:AC [PDB note]=Chains D, E, F, G and H were removed as chains A, B and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=Bcl-2 homology [Type chain B]=Disordered [Evidence chain B]=The Beclin-1 BH3 domain was shown to be unstructured in the absence of other interactions and undergoes a helical transition upon binding (PMID:24115198). The protein region involved in the interaction contains a known functional linear motif (LIG_BH_BH3_1). [Type chain A]=Ordered [Evidence chain A]=The ordered partner is a domain-swapped Bcl-2 homology domain dimer. Bcl-2 homology domains are known to adopt a stable structure in isolation, even in their monomeric form (see Pfam domain PF00452). A solved monomeric structure of the domain is represented by PDB ID 1lxl. [Type chain C]=Ordered [Evidence chain C]=The ordered partner is a domain-swapped Bcl-2 homology domain dimer. Bcl-2 homology domains are known to adopt a stable structure in isolation, even in their monomeric form (see Pfam domain PF00452). A solved monomeric structure of the domain is represented by PDB ID 1lxl. [Chain B name]=Beclin-1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q14457 [Chain B UniProt boundaries]=107-135 [Chain B UniProt coverage]=6.4% [Chain B UniRef90 accession]=UniRef90_Q14457 [Chain B UniRef90 boundaries]=107-135 [Chain A name]=Bcl-2-like protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q07817 [Chain A UniProt boundaries]=1-209 [Chain A UniProt coverage]=89.7% [Chain A UniRef90 accession]=UniRef90_Q07817 [Chain A UniRef90 boundaries]=1-209 [Chain C name]=Bcl-2-like protein 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q07817 [Chain C UniProt boundaries]=1-209 [Chain C UniProt coverage]=89.7% [Chain C UniRef90 accession]=UniRef90_Q07817 [Chain C UniRef90 boundaries]=1-209 [Related structures]=2pon [Entry] [Accession]=DI1100083 [Disorder status]=Inferred from motif [Kd]=1.10E-06 [Name]=Mouse A1 bound to the BID BH3-domain [Source organism]=Mus musculus [PDB ID]=2voi [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.1 [Domain]=Bcl-2 homology [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_BH_BH3_1). [Type chain A]=Ordered [Evidence chain A]=The Bcl-2 homology domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00452). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1pq0. [Chain B name]=BH3-interacting domain death agonist [Chain B source organism]=Mus musculus [Chain B UniProt accession]=P70444 [Chain B UniProt boundaries]=76-109 [Chain B UniProt coverage]=17.4% [Chain B UniRef90 accession]=UniRef90_P70444 [Chain B UniRef90 boundaries]=76-109 [Chain A name]=Bcl-2-related protein A1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q07440 [Chain A UniProt boundaries]=1-152 [Chain A UniProt coverage]=88.4% [Chain A UniRef90 accession]=UniRef90_Q07440 [Chain A UniRef90 boundaries]=1-152 [Entry] [Accession]=DI1100084 [Disorder status]=Inferred from motif [Kd]=1.09E-06 [Name]=Nrd1p CID - Trf4p NIM complex [Source organism]=Saccharomyces cerevisiae [PDB ID]=2mow [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=CID [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_CID_NIM_1). [Type chain A]=Ordered [Evidence chain A]=The CID domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04818). A solved monomeric structure of the domain is represented by PDB ID 3clj. [Chain B name]=Poly(A) RNA polymerase protein 2 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P53632 [Chain B UniProt boundaries]=573-584 [Chain B UniProt coverage]=2.1% [Chain B UniRef90 accession]=UniRef90_P53632 [Chain B UniRef90 boundaries]=573-584 [Chain A name]=Protein NRD1 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P53617 [Chain A UniProt boundaries]=1-153 [Chain A UniProt coverage]=26.6% [Chain A UniRef90 accession]=UniRef90_P53617 [Chain A UniRef90 boundaries]=1-153 [Entry] [Accession]=DI1000244 [Disorder status]=Inferred from homology [Kd]=3.10E-06 (PMID:14685257) [Name]=C-terminal domain of PABPC1 in complex with binding region of eRF3a [Source organism]=Homo sapiens [PDB ID]=3kuj [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.40 [Domain]=PABP [Type chain B]=Disordered [Evidence chain B]=Corresponding region of a closly homologous protein (erf3a) was shown to be unstructured (PMID:23019593). The protein region involved in the interaction contains a known functional linear motif (LIG_PAM2_1). [Type chain A]=Ordered [Evidence chain A]=The PABP domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00658). A solved monomeric structure of the domain is represented by PDB ID 1g9l. [Chain B name]=Eukaryotic peptide chain release factor GTP-binding subunit ERF3B [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q8IYD1 [Chain B UniProt boundaries]=59-73 [Chain B UniProt coverage]=2.4% [Chain B UniRef90 accession]=UniRef90_Q8IYD1 [Chain B UniRef90 boundaries]=59-73 [Chain A name]=Polyadenylate-binding protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P11940 [Chain A UniProt boundaries]=544-626 [Chain A UniProt coverage]=13.1% [Chain A UniRef90 accession]=UniRef90_P11940 [Chain A UniRef90 boundaries]=544-626 [Entry] [Accession]=DI1000245 [Disorder status]=Inferred from motif [Kd]=1.50E-07 [Name]=EPS15-EH2 Stonin2 Complex [Source organism]=Homo sapiens [PDB ID]=2jxc [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=EF-hand [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains 2 known functional linear motifs (LIG_EH_1, LIG_EH_1). [Type chain A]=Ordered [Evidence chain A]=The EF-hand domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF12763). A solved monomeric structure of the domain is represented by PDB ID 1eh2. [Chain B name]=Stonin-2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q8WXE9 [Chain B UniProt boundaries]=300-340 [Chain B UniProt coverage]=4.5% [Chain B UniRef90 accession]=UniRef90_Q8WXE9 [Chain B UniRef90 boundaries]=300-340 [Chain A name]=Epidermal growth factor receptor substrate 15 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P42566 [Chain A UniProt boundaries]=116-215 [Chain A UniProt coverage]=11.2% [Chain A UniRef90 accession]=UniRef90_P42566 [Chain A UniRef90 boundaries]=121-215 [Entry] [Accession]=DI3100003 [Disorder status]=Confirmed [Kd]=1.50E-07 [Name]=Peptide derived from Cdc9 bound to PCNA [Source organism]=Saccharomyces cerevisiae [PDB ID]=2od8 [PDB chain IDs]=B:ACE [PDB note]=Chains C and E were generated using the biomatrices in the PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=PCNA [Type chain B]=Disordered [Evidence chain B]=The Cdc9 peptide encompasses the PIP box, known to reside within a flexible unstructured region (PMID:17308348). The protein region involved in the interaction contains a known functional linear motif (LIG_PCNA_PIPBox_1). [Type chain A]=Ordered component [Evidence chain A]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1plq. [Type chain C]=Ordered component [Evidence chain C]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1plq. [Type chain E]=Ordered component [Evidence chain E]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1plq. [Chain B name]=DNA ligase 1 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P04819 [Chain B UniProt boundaries]=32-53 [Chain B UniProt coverage]=2.9% [Chain B UniRef90 accession]=UniRef90_P04819 [Chain B UniRef90 boundaries]=32-53 [Chain A name]=Proliferating cell nuclear antigen [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P15873 [Chain A UniProt boundaries]=1-258 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P15873 [Chain A UniRef90 boundaries]=1-258 [Chain C name]=Proliferating cell nuclear antigen [Chain C source organism]=Saccharomyces cerevisiae [Chain C UniProt accession]=P15873 [Chain C UniProt boundaries]=1-258 [Chain C UniProt coverage]=100% [Chain C UniRef90 accession]=UniRef90_P15873 [Chain C UniRef90 boundaries]=1-258 [Chain E name]=Proliferating cell nuclear antigen [Chain E source organism]=Saccharomyces cerevisiae [Chain E UniProt accession]=P15873 [Chain E UniProt boundaries]=1-258 [Chain E UniProt coverage]=100% [Chain E UniRef90 accession]=UniRef90_P15873 [Chain E UniRef90 boundaries]=1-258 [Entry] [Accession]=DI1000246 [Disorder status]=Inferred from motif [Kd]=1.09E-04 [Name]=MYND domain from AML1-ETO complexed with SMRT, a corepressor [Source organism]=Homo sapiens [PDB ID]=2odd [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=MYND [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_MYND_2). [Type chain A]=Ordered [Evidence chain A]=The MYND domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01753). A solved monomeric structure of the domain is represented by PDB ID 2od1. [Chain B name]=Nuclear receptor corepressor 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9Y618 [Chain B UniProt boundaries]=1109-1121 [Chain B UniProt coverage]=0.5% [Chain B UniRef90 accession]=UniRef90_Q9Y618 [Chain B UniRef90 boundaries]=1109-1121 [Chain A name]=Protein CBFA2T1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q06455 [Chain A UniProt boundaries]=510-559 [Chain A UniProt coverage]=8.3% [Chain A UniRef90 accession]=UniRef90_Q06455 [Chain A UniRef90 boundaries]=510-559 [Entry] [Accession]=DI1000247 [Disorder status]=Inferred from motif [Kd]=2.40E-06 [Name]=ARC4 from human Tankyrase 2 in complex with peptide from human MCL1 [Source organism]=Homo sapiens [PDB ID]=3twu [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=Ankyrin repeat [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (DOC_ANK_TNKS_1). [Type chain A]=Ordered [Evidence chain A]=The ankyrin repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13857/PF12796). A solved monomeric structure of the domain is represented by PDB ID 3twq. [Modified residues chain B]=L-alpha-asparagine#N#16 [Chain B name]=Induced myeloid leukemia cell differentiation protein Mcl-1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q07820 [Chain B UniProt boundaries]=73-88 [Chain B UniProt coverage]=4.6% [Chain B UniRef90 accession]=UniRef90_Q07820 [Chain B UniRef90 boundaries]=73-88 [Chain A name]=Tankyrase-2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9H2K2 [Chain A UniProt boundaries]=488-649 [Chain A UniProt coverage]=13.9% [Chain A UniRef90 accession]=UniRef90_Q9H2K2 [Chain A UniRef90 boundaries]=488-649 [Entry] [Accession]=DI1000248 [Disorder status]=Inferred from motif [Kd]=1.09E-04 [Name]=PxLPxI/L motif of Histone deacetylase 4 bound by RFXANK [Source organism]=Homo sapiens [PDB ID]=3uxg [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.85 [Domain]=Ankyrin repeat [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_ANK_PxLPxL_1). [Type chain A]=Ordered [Evidence chain A]=The ankyrin repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF12796). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3twq. [Chain B name]=Histone deacetylase 4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P56524 [Chain B UniProt boundaries]=343-359 [Chain B UniProt coverage]=1.6% [Chain B UniRef90 accession]=UniRef90_P56524 [Chain B UniRef90 boundaries]=343-359 [Chain A name]=DNA-binding protein RFXANK [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O14593 [Chain A UniProt boundaries]=90-260 [Chain A UniProt coverage]=65.8% [Chain A UniRef90 accession]=UniRef90_O14593 [Chain A UniRef90 boundaries]=90-260 [Entry] [Accession]=DI1010081 [Disorder status]=Inferred from motif [Kd]=4.90E-06 [Name]=Human ANKRA2 in complex with an Lrp2 peptide [Source organism]=Rattus norvegicus / Homo sapiens [PDB ID]=3v2o [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.89 [Domain]=Ankyrin repeat [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_ANK_PxLPxL_1). [Type chain A]=Ordered [Evidence chain A]=The ankyrin repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF12796). A solved monomeric structure of the domain is represented by PDB ID 3so8. [Chain B name]=Low-density lipoprotein receptor-related protein 2 [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=P98158 [Chain B UniProt boundaries]=4448-4466 [Chain B UniProt coverage]=0.4% [Chain B UniRef90 accession]=UniRef90_P98158 [Chain B UniRef90 boundaries]=4448-4466 [Chain A name]=Ankyrin repeat family A protein 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9H9E1 [Chain A UniProt boundaries]=148-313 [Chain A UniProt coverage]=53% [Chain A UniRef90 accession]=UniRef90_Q9H9E1 [Chain A UniRef90 boundaries]=148-313 [Related structures]=3v2x [Entry] [Accession]=DI1000249 [Disorder status]=Inferred from motif [Kd]=1.84E-04 [Name]=RFXANK in complex with an RFX5 peptide [Source organism]=Homo sapiens [PDB ID]=3v30 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.57 [Domain]=Ankyrin repeat [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_ANK_PxLPxL_1). [Type chain A]=Ordered [Evidence chain A]=The ankyrin repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF12796). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3twq. [Chain B name]=DNA-binding protein RFX5 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P48382 [Chain B UniProt boundaries]=167-183 [Chain B UniProt coverage]=2.8% [Chain B UniRef90 accession]=UniRef90_P48382 [Chain B UniRef90 boundaries]=167-183 [Chain A name]=DNA-binding protein RFXANK [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O14593 [Chain A UniProt boundaries]=90-260 [Chain A UniProt coverage]=65.8% [Chain A UniRef90 accession]=UniRef90_O14593 [Chain A UniRef90 boundaries]=90-260 [Entry] [Accession]=DI1000250 [Disorder status]=Inferred from motif [Kd]=1.60E-06 [Name]=Human ANKRA2 in complex with a Histone deacetylase 4 peptide [Source organism]=Homo sapiens [PDB ID]=3v31 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.57 [Domain]=Ankyrin repeat [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_ANK_PxLPxL_1). [Type chain A]=Ordered [Evidence chain A]=The ankyrin repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF12796). A solved monomeric structure of the domain is represented by PDB ID 3so8. [Chain B name]=Histone deacetylase 4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P56524 [Chain B UniProt boundaries]=343-359 [Chain B UniProt coverage]=1.6% [Chain B UniRef90 accession]=UniRef90_P56524 [Chain B UniRef90 boundaries]=343-359 [Chain A name]=Ankyrin repeat family A protein 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9H9E1 [Chain A UniProt boundaries]=148-313 [Chain A UniProt coverage]=53% [Chain A UniRef90 accession]=UniRef90_Q9H9E1 [Chain A UniRef90 boundaries]=148-313 [Entry] [Accession]=DI1000251 [Disorder status]=Inferred from motif [Kd]=1.80E-07 [Name]=Human ANKRA2 in complex with a CCDC8 peptide [Source organism]=Homo sapiens [PDB ID]=4lg6 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=Ankyrin repeat [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_ANK_PxLPxL_1). [Type chain A]=Ordered [Evidence chain A]=The ankyrin repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF12796). A solved monomeric structure of the domain is represented by PDB ID 3so8. [Chain B name]=Coiled-coil domain-containing protein 8 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9H0W5 [Chain B UniProt boundaries]=494-510 [Chain B UniProt coverage]=3.2% [Chain B UniRef90 accession]=UniRef90_Q9H0W5 [Chain B UniRef90 boundaries]=494-510 [Chain A name]=Ankyrin repeat family A protein 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9H9E1 [Chain A UniProt boundaries]=142-313 [Chain A UniProt coverage]=55% [Chain A UniRef90 accession]=UniRef90_Q9H9E1 [Chain A UniRef90 boundaries]=142-313 [Entry] [Accession]=DI1000252 [Disorder status]=Inferred from motif [Kd]=3.00E-06 [Name]=Human ANKRA2 in complex with an RFX7 peptide [Source organism]=Homo sapiens [PDB ID]=4qqi [PDB chain IDs]=X:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.03 [Domain]=Ankyrin repeat [Type chain X]=Disordered [Evidence chain X]=The protein region involved in the interaction contains a known functional linear motif (LIG_ANK_PxLPxL_1). [Type chain A]=Ordered [Evidence chain A]=The ankyrin repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF12796). A solved monomeric structure of the domain is represented by PDB ID 3so8. [Chain X name]=DNA-binding protein RFX7 [Chain X source organism]=Homo sapiens [Chain X UniProt accession]=Q2KHR2 [Chain X UniProt boundaries]=85-101 [Chain X UniProt coverage]=1.2% [Chain X UniRef90 accession]=UniRef90_Q2KHR2 [Chain X UniRef90 boundaries]=85-101 [Chain A name]=Ankyrin repeat family A protein 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9H9E1 [Chain A UniProt boundaries]=142-313 [Chain A UniProt coverage]=55% [Chain A UniRef90 accession]=UniRef90_Q9H9E1 [Chain A UniRef90 boundaries]=142-313 [Entry] [Accession]=DI1000253 [Disorder status]=Inferred from motif [Kd]=2.27E-06 [Name]=PP2A B56gamma in complex with an unmodified BubR1 peptide [Source organism]=Homo sapiens [PDB ID]=5jja [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains C and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.35 [Domain]=B56 subunit of PP2A [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (DOC_PP2A_B56_1). [Type chain A]=Ordered [Evidence chain A]=The B56 subunit of PP2A involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01603). A solved monomeric structure of the domain is represented by PDB ID 2jak. [Chain C name]=Mitotic checkpoint serine/threonine-protein kinase BUB1 beta [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=O60566 [Chain C UniProt boundaries]=647-720 [Chain C UniProt coverage]=7% [Chain C UniRef90 accession]=UniRef90_O60566 [Chain C UniRef90 boundaries]=647-720 [Chain A name]=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q13362 [Chain A UniProt boundaries]=30-380 [Chain A UniProt coverage]=67% [Chain A UniRef90 accession]=UniRef90_Q13362 [Chain A UniRef90 boundaries]=30-380 [Entry] [Accession]=DI1000254 [Disorder status]=Inferred from motif [Kd]=6.60E-07 [Name]=C-terminal WD40 domain of PALB2 in complex with BRCA2 [Source organism]=Homo sapiens [PDB ID]=3eu7 [PDB chain IDs]=X:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=WD40 [Type chain X]=Disordered [Evidence chain X]=The protein region involved in the interaction contains a known functional linear motif (LIG_PALB2_WD40_1). [Type chain A]=Ordered [Evidence chain A]=The BRCA2-interacting WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF16756). A solved monomeric structure of the domain is represented by PDB ID 2w18. [Chain X name]=Breast cancer type 2 susceptibility protein [Chain X source organism]=Homo sapiens [Chain X UniProt accession]=P51587 [Chain X UniProt boundaries]=21-39 [Chain X UniProt coverage]=0.6% [Chain X UniRef90 accession]=UniRef90_P51587 [Chain X UniRef90 boundaries]=21-39 [Chain A name]=Partner and localizer of BRCA2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q86YC2 [Chain A UniProt boundaries]=835-1186 [Chain A UniProt coverage]=29.7% [Chain A UniRef90 accession]=UniRef90_Q86YC2 [Chain A UniRef90 boundaries]=835-1186 [Entry] [Accession]=DI1000255 [Disorder status]=Inferred from motif [Kd]=1.60E-07 [Name]=WDR5 in complex with the WDR5-interacting motif of MLL2 [Source organism]=Homo sapiens [PDB ID]=3uvk [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.40 [Domain]=WD40 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_WD40_WDR5_WIN_1). [Type chain A]=Ordered [Evidence chain A]=The WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00400). A solved monomeric structure of the domain is represented by PDB ID 2gnq. [Chain B name]=Histone-lysine N-methyltransferase 2D [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O14686 [Chain B UniProt boundaries]=5337-5347 [Chain B UniProt coverage]=0.2% [Chain B UniRef90 accession]=UniRef90_O14686 [Chain B UniRef90 boundaries]=5337-5347 [Chain A name]=WD repeat-containing protein 5 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P61964 [Chain A UniProt boundaries]=21-334 [Chain A UniProt coverage]=94% [Chain A UniRef90 accession]=UniRef90_P61964 [Chain A UniRef90 boundaries]=21-334 [Related structures]=4erq [Entry] [Accession]=DI1000256 [Disorder status]=Inferred from motif [Kd]=1.40E-07 [Name]=WDR5 in complex with the WDR5-interacting motif of MLL1 [Source organism]=Homo sapiens [PDB ID]=3emh [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.37 [Domain]=WD40 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_WD40_WDR5_WIN_1). [Type chain A]=Ordered [Evidence chain A]=The WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00400). A solved monomeric structure of the domain is represented by PDB ID 2gnq. [Chain B name]=Histone-lysine N-methyltransferase 2A [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q03164 [Chain B UniProt boundaries]=3764-3776 [Chain B UniProt coverage]=0.3% [Chain B UniRef90 accession]=UniRef90_Q03164 [Chain B UniRef90 boundaries]=3764-3776 [Chain A name]=WD repeat-containing protein 5 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P61964 [Chain A UniProt boundaries]=25-334 [Chain A UniProt coverage]=92.8% [Chain A UniRef90 accession]=UniRef90_P61964 [Chain A UniRef90 boundaries]=25-334 [Related structures]=4esg,3eg6 [Entry] [Accession]=DI1000257 [Disorder status]=Inferred from motif [Kd]=2.03E-06 [Name]=WDR5 in complex with the WDR5-interacting motif of MLL3 [Source organism]=Homo sapiens [PDB ID]=3uvl [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=WD40 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_WD40_WDR5_WIN_1). [Type chain A]=Ordered [Evidence chain A]=The WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00400). A solved monomeric structure of the domain is represented by PDB ID 2gnq. [Chain B name]=Histone-lysine N-methyltransferase 2C [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q8NEZ4 [Chain B UniProt boundaries]=4707-4717 [Chain B UniProt coverage]=0.2% [Chain B UniRef90 accession]=UniRef90_Q8NEZ4 [Chain B UniRef90 boundaries]=4707-4717 [Chain A name]=WD repeat-containing protein 5 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P61964 [Chain A UniProt boundaries]=21-334 [Chain A UniProt coverage]=94% [Chain A UniRef90 accession]=UniRef90_P61964 [Chain A UniRef90 boundaries]=21-334 [Related structures]=4ery [Entry] [Accession]=DI1000258 [Disorder status]=Inferred from motif [Kd]=3.00E-08 [Name]=WDR5 in complex with the WDR5-interacting motif of MLL4 [Source organism]=Homo sapiens [PDB ID]=3uvm [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.57 [Domain]=WD40 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_WD40_WDR5_WIN_1). [Type chain A]=Ordered [Evidence chain A]=The WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00400). A solved monomeric structure of the domain is represented by PDB ID 2gnq. [Chain B name]=Histone-lysine N-methyltransferase 2B [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9UMN6 [Chain B UniProt boundaries]=2508-2517 [Chain B UniProt coverage]=0.4% [Chain B UniRef90 accession]=UniRef90_Q9UMN6 [Chain B UniRef90 boundaries]=2508-2517 [Chain A name]=WD repeat-containing protein 5 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P61964 [Chain A UniProt boundaries]=21-334 [Chain A UniProt coverage]=94% [Chain A UniRef90 accession]=UniRef90_P61964 [Chain A UniRef90 boundaries]=21-334 [Related structures]=4erz [Entry] [Accession]=DI1000259 [Disorder status]=Inferred from motif [Kd]=2.60E-07 [Name]=WDR5 in complex with the WDR5-interacting motif of SET1A [Source organism]=Homo sapiens [PDB ID]=3uvn [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains B and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.79 [Domain]=WD40 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_WD40_WDR5_WIN_1). [Type chain A]=Ordered [Evidence chain A]=The WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00400). A solved monomeric structure of the domain is represented by PDB ID 2gnq. [Chain B name]=Histone-lysine N-methyltransferase SETD1A [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O15047 [Chain B UniProt boundaries]=1492-1502 [Chain B UniProt coverage]=0.6% [Chain B UniRef90 accession]=UniRef90_O15047 [Chain B UniRef90 boundaries]=1492-1502 [Chain A name]=WD repeat-containing protein 5 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P61964 [Chain A UniProt boundaries]=21-334 [Chain A UniProt coverage]=94% [Chain A UniRef90 accession]=UniRef90_P61964 [Chain A UniRef90 boundaries]=21-334 [Related structures]=4ewr [Entry] [Accession]=DI1000260 [Disorder status]=Inferred from motif [Kd]=1.00E-07 [Name]=WDR5 in complex with the WDR5-interacting motif of SET1B [Source organism]=Homo sapiens [PDB ID]=3uvo [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=WD40 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_WD40_WDR5_WIN_1). [Type chain A]=Ordered [Evidence chain A]=The WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00400). A solved monomeric structure of the domain is represented by PDB ID 2gnq. [Chain B name]=Histone-lysine N-methyltransferase SETD1B [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9UPS6 [Chain B UniProt boundaries]=1745-1755 [Chain B UniProt coverage]=0.6% [Chain B UniRef90 accession]=UniRef90_Q9UPS6 [Chain B UniRef90 boundaries]=1745-1755 [Chain A name]=WD repeat-containing protein 5 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P61964 [Chain A UniProt boundaries]=21-334 [Chain A UniProt coverage]=94% [Chain A UniRef90 accession]=UniRef90_P61964 [Chain A UniRef90 boundaries]=21-334 [Related structures]=4es0 [Entry] [Accession]=DI1000261 [Disorder status]=Inferred from motif [Kd]=1.81E-07 [Name]=WDR5 in complex with the WDR5-interacting motif of KANSL1 [Source organism]=Homo sapiens [PDB ID]=4cy1 [PDB chain IDs]=C:B [PDB note]=Chains A and D were removed as chains C and B highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.50 [Domain]=WD40 [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_WD40_WDR5_WIN_1). [Type chain B]=Ordered [Evidence chain B]=The WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00400). A solved monomeric structure of the domain is represented by PDB ID 2gnq. [Chain C name]=KAT8 regulatory NSL complex subunit 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q7Z3B3 [Chain C UniProt boundaries]=585-598 [Chain C UniProt coverage]=1.3% [Chain C UniRef90 accession]=UniRef90_Q7Z3B3 [Chain C UniRef90 boundaries]=585-598 [Chain B name]=WD repeat-containing protein 5 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P61964 [Chain B UniProt boundaries]=23-334 [Chain B UniProt coverage]=93.4% [Chain B UniRef90 accession]=UniRef90_P61964 [Chain B UniRef90 boundaries]=23-334 [Related structures]=4cy2 [Entry] [Accession]=DI1100085 [Disorder status]=Inferred from motif [Kd]=1.81E-07 [Name]=NSL1 peptide bound to WDS [Source organism]=Drosophila melanogaster [PDB ID]=4cy3 [PDB chain IDs]=D:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.40 [Domain]=WD40 [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a known functional linear motif (LIG_WD40_WDR5_WIN_2). [Type chain A]=Ordered [Evidence chain A]=The WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00400). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2gnq. [Chain D name]=Non-specific lethal 1, isoform D [Chain D source organism]=Drosophila melanogaster [Chain D UniProt accession]=A4V2Z1 [Chain D UniProt boundaries]=714-729 [Chain D UniProt coverage]=1% [Chain D UniRef90 accession]=UniRef90_A4V2Z1 [Chain D UniRef90 boundaries]=714-729 [Chain A name]=Protein will die slowly [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=Q9V3J8 [Chain A UniProt boundaries]=50-361 [Chain A UniProt coverage]=86.4% [Chain A UniRef90 accession]=UniRef90_Q9V3J8 [Chain A UniRef90 boundaries]=50-361 [Related structures]=4cy5 [Entry] [Accession]=DI1010082 [Disorder status]=Inferred from motif [Kd]=1.81E-07 [Name]=WD40 domain of Arabidopsis thaliana E3 Ubiquitin Ligase COP1 in complex with peptide from Trib1 [Source organism]=Homo sapiens / Arabidopsis thaliana [PDB ID]=5igo [PDB chain IDs]=U:A [PDB note]=Chains B, C, D, V, W and X were removed as chains A and U highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.60 [Domain]=WD40 [Type chain U]=Disordered [Evidence chain U]=The protein region involved in the interaction contains a known functional linear motif (DEG_COP1_1). [Type chain A]=Ordered [Evidence chain A]=The WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00400). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2gnq. [Chain U name]=Tribbles homolog 1 [Chain U source organism]=Homo sapiens [Chain U UniProt accession]=Q96RU8 [Chain U UniProt boundaries]=354-361 [Chain U UniProt coverage]=2.2% [Chain U UniRef90 accession]=UniRef90_Q96RU8 [Chain U UniRef90 boundaries]=354-361 [Chain A name]=E3 ubiquitin-protein ligase COP1 [Chain A source organism]=Arabidopsis thaliana [Chain A UniProt accession]=P43254 [Chain A UniProt boundaries]=349-675 [Chain A UniProt coverage]=48.4% [Chain A UniRef90 accession]=UniRef90_P43254 [Chain A UniRef90 boundaries]=349-675 [Entry] [Accession]=DI1000262 [Disorder status]=Inferred from motif [Kd]=2.50E-07 [Name]=WD40 domain of Human E3 Ubiquitin Ligase COP1 (RFWD2) bound to peptide from Trib1 [Source organism]=Homo sapiens [PDB ID]=5igq [PDB chain IDs]=U:A [PDB note]=Chains B, C, D, E, F, V, W, X, Y and Z were removed as chains A and U highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.90 [Domain]=WD40 [Type chain U]=Disordered [Evidence chain U]=The protein region involved in the interaction contains a known functional linear motif (DEG_COP1_1). [Type chain A]=Ordered [Evidence chain A]=The WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00400). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 5hqg. [Chain U name]=Tribbles homolog 1 [Chain U source organism]=Homo sapiens [Chain U UniProt accession]=Q96RU8 [Chain U UniProt boundaries]=354-364 [Chain U UniProt coverage]=3% [Chain U UniRef90 accession]=UniRef90_Q96RU8 [Chain U UniRef90 boundaries]=354-364 [Chain A name]=E3 ubiquitin-protein ligase RFWD2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q8NHY2 [Chain A UniProt boundaries]=386-731 [Chain A UniProt coverage]=47.3% [Chain A UniRef90 accession]=UniRef90_Q8NHY2 [Chain A UniRef90 boundaries]=386-731 [Entry] [Accession]=DI1000263 [Disorder status]=Inferred from motif [Kd]=5.80E-06 [Name]=Recognition of the FandH motif by the Lowe Syndrome protein OCRL [Source organism]=Homo sapiens [PDB ID]=3qis [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=Rho-GAP [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_OCRL_FandH_1). [Type chain A]=Ordered [Evidence chain A]=The Rho-GAP domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00620). A solved monomeric structure of the domain is represented by PDB ID 2qv2. [Chain B name]=Sesquipedalian-1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q8N4B1 [Chain B UniProt boundaries]=223-235 [Chain B UniProt coverage]=5.2% [Chain B UniRef90 accession]=UniRef90_Q8N4B1 [Chain B UniRef90 boundaries]=223-235 [Chain A name]=Inositol polyphosphate 5-phosphatase OCRL-1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q01968 [Chain A UniProt boundaries]=536-901 [Chain A UniProt coverage]=40.6% [Chain A UniRef90 accession]=UniRef90_Q01968 [Chain A UniRef90 boundaries]=536-901 [Entry] [Accession]=DI1000264 [Disorder status]=Inferred from motif [Kd]=3.86E-06 [Name]=Human SUFU:GLI1p complex [Source organism]=Homo sapiens [PDB ID]=4kmd [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=SUFU N-terminal [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_SUFU_1). [Type chain A]=Ordered [Evidence chain A]=The SUFU N-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF05076). A solved monomeric structure of the domain is represented by PDB ID 1m1l. [Chain B name]=Zinc finger protein GLI1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P08151 [Chain B UniProt boundaries]=112-128 [Chain B UniProt coverage]=1.5% [Chain B UniRef90 accession]=UniRef90_P08151 [Chain B UniRef90 boundaries]=112-128 [Chain A name]=Suppressor of fused homolog [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UMX1 [Chain A UniProt boundaries]=1-484 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q9UMX1 [Chain A UniRef90 boundaries]=1-484 [Related structures]=4blb [Entry] [Accession]=DI1020035 [Disorder status]=Inferred from motif [Kd]=3.86E-06 [Name]=Human SUFU:GLI3p complex [Source organism]=Homo sapiens / Escherichia coli [PDB ID]=4bld [PDB chain IDs]=E:A [PDB note]=Chains B, C, D, F, G and H were removed as chains E and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=SUFU N-terminal [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (LIG_SUFU_1). [Type chain A]=Ordered [Evidence chain A]=The SUFU N-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF05076). A solved monomeric structure of the domain is represented by PDB ID 1m1l. [Chain E name]=Transcriptional activator GLI3 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P10071 [Chain E UniProt boundaries]=328-344 [Chain E UniProt coverage]=1.1% [Chain E UniRef90 accession]=UniRef90_P10071 [Chain E UniRef90 boundaries]=328-344 [Chain A name]=Suppressor of fused homolog [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=Q9UMX1 [Chain A UniProt boundaries]=32-479 [Chain A UniProt coverage]=92.6% [Chain A UniRef90 accession]=UniRef90_Q9UMX1 [Chain A UniRef90 boundaries]=32-479 [Entry] [Accession]=DI2000035 [Disorder status]=Inferred from motif [Kd]=3.10E-07 [Name]=TRF1 TRFH domain in complex with a TIN2 peptide complex [Source organism]=Homo sapiens [PDB ID]=3bqo [PDB chain IDs]=B:AC [PDB note]=Chain C was generated using the biomatrix described in the PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=TRF [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_TRFH_1). [Type chain A]=Ordered component [Evidence chain A]=The TRF domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF08558). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1h6o. [Type chain C]=Ordered component [Evidence chain C]=The TRF domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF08558). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1h6o. [Chain B name]=TERF1-interacting nuclear factor 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9BSI4 [Chain B UniProt boundaries]=257-276 [Chain B UniProt coverage]=4.4% [Chain B UniRef90 accession]=UniRef90_Q9BSI4 [Chain B UniRef90 boundaries]=257-276 [Chain A name]=Telomeric repeat-binding factor 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P54274 [Chain A UniProt boundaries]=58-268 [Chain A UniProt coverage]=48.1% [Chain A UniRef90 accession]=UniRef90_P54274 [Chain A UniRef90 boundaries]=58-268 [Chain C name]=Telomeric repeat-binding factor 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P54274 [Chain C UniProt boundaries]=58-268 [Chain C UniProt coverage]=48.1% [Chain C UniRef90 accession]=UniRef90_P54274 [Chain C UniRef90 boundaries]=58-268 [Entry] [Accession]=DI2000036 [Disorder status]=Inferred from motif [Kd]=1.20E-07 [Name]=TRF2 TRFH domain and APOLLO peptide complex [Source organism]=Homo sapiens [PDB ID]=3bua [PDB chain IDs]=E:AB [PDB note]=Chains C, D, F, G and H were removed as chains A, B and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=TRF [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (LIG_TRFH_1). [Type chain A]=Ordered component [Evidence chain A]=The TRF domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF08558). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1h6p. [Type chain B]=Ordered component [Evidence chain B]=The TRF domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF08558). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1h6p. [Chain E name]=5' exonuclease Apollo [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=Q9H816 [Chain E UniProt boundaries]=495-530 [Chain E UniProt coverage]=6.8% [Chain E UniRef90 accession]=UniRef90_Q9H816 [Chain E UniRef90 boundaries]=495-530 [Chain A name]=Telomeric repeat-binding factor 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q15554 [Chain A UniProt boundaries]=84-287 [Chain A UniProt coverage]=37.6% [Chain A UniRef90 accession]=UniRef90_Q15554 [Chain A UniRef90 boundaries]=84-287 [Chain B name]=Telomeric repeat-binding factor 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q15554 [Chain B UniProt boundaries]=84-287 [Chain B UniProt coverage]=37.6% [Chain B UniRef90 accession]=UniRef90_Q15554 [Chain B UniRef90 boundaries]=84-287 [Entry] [Accession]=DI1010083 [Disorder status]=Inferred from motif [Kd]=2.37E-05 [Name]=TPR domain of kinesin light chain 2 in complex with a tryptophan-acidic cargo peptide [Source organism]=Homo sapiens / Mus musculus [PDB ID]=3zfw [PDB chain IDs]=X:A [PDB note]=Chains B and Y were removed as chains X and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.90 [Domain]=Tetratricopeptide [Type chain X]=Disordered [Evidence chain X]=The protein region involved in the interaction contains a known functional linear motif (LIG_KLC1_WD_1). [Type chain A]=Ordered [Evidence chain A]=The tetratricopeptide domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13424). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1w3b. [Chain X name]=Pleckstrin homology domain-containing family M member 2 [Chain X source organism]=Homo sapiens [Chain X UniProt accession]=Q8IWE5 [Chain X UniProt boundaries]=203-212 [Chain X UniProt coverage]=1% [Chain X UniRef90 accession]=UniRef90_Q8IWE5 [Chain X UniRef90 boundaries]=203-212 [Chain A name]=Kinesin light chain 2 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=O88448 [Chain A UniProt boundaries]=217-430 [Chain A UniProt coverage]=35.7% [Chain A UniRef90 accession]=UniRef90_O88448 [Chain A UniRef90 boundaries]=217-430 [Entry] [Accession]=DI1100086 [Disorder status]=Inferred from motif [Kd]=3.60E-06 [Name]=Bub3 complex with Bub1 GLEBS motif [Source organism]=Saccharomyces cerevisiae [PDB ID]=2i3s [PDB chain IDs]=B:A [PDB note]=Chains C, D, E and F were removed as chains A and B highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=WD40 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_GLEBS_BUB3_1). [Type chain A]=Ordered [Evidence chain A]=The WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00400). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1u4c. [Chain B name]=Checkpoint serine/threonine-protein kinase BUB1 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P41695 [Chain B UniProt boundaries]=315-350 [Chain B UniProt coverage]=3.5% [Chain B UniRef90 accession]=UniRef90_P41695 [Chain B UniRef90 boundaries]=315-350 [Chain A name]=Cell cycle arrest protein BUB3 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P26449 [Chain A UniProt boundaries]=1-341 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P26449 [Chain A UniRef90 boundaries]=1-341 [Related structures]=4bl0 [Entry] [Accession]=DI1100087 [Disorder status]=Inferred from motif [Kd]=2.70E-06 [Name]=Bub3 complex with Mad3 (BubR1) GLEBS motif [Source organism]=Saccharomyces cerevisiae [PDB ID]=2i3t [PDB chain IDs]=B:A [PDB note]=Chains C, D, E, F, G and H were removed as chains A and B highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=WD40 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_GLEBS_BUB3_1). [Type chain A]=Ordered [Evidence chain A]=The WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00400). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1u4c. [Chain B name]=Spindle assembly checkpoint component MAD3 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P47074 [Chain B UniProt boundaries]=353-400 [Chain B UniProt coverage]=9.3% [Chain B UniRef90 accession]=UniRef90_P47074 [Chain B UniRef90 boundaries]=353-400 [Chain A name]=Cell cycle arrest protein BUB3 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P26449 [Chain A UniProt boundaries]=1-341 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P26449 [Chain A UniRef90 boundaries]=1-341 [Entry] [Accession]=DI1100088 [Disorder status]=Inferred from motif [Kd]=2.70E-06 [Name]=TIR1 ubiquitin ligase in complex with Auxin-responsive protein IAA7 [Source organism]=Arabidopsis thaliana [PDB ID]=2p1q [PDB chain IDs]=C:B [PDB note]=Chain A was removed as chains C and B highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.91 [Domain]=TIR1 [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (DEG_SCF_TIR1_1). [Type chain B]=Ordered [Evidence chain B]=The TIR1 domain involved in the interaction is known to adopt a stable structure in isolation. A solved structure of the domain without bound ligand peptides is represented by PDB ID 2p1p. [Chain C name]=Auxin-responsive protein IAA7 [Chain C source organism]=Arabidopsis thaliana [Chain C UniProt accession]=Q38825 [Chain C UniProt boundaries]=82-94 [Chain C UniProt coverage]=5.3% [Chain C UniRef90 accession]=UniRef90_Q38825 [Chain C UniRef90 boundaries]=82-94 [Chain B name]=Protein TRANSPORT INHIBITOR RESPONSE 1 [Chain B source organism]=Arabidopsis thaliana [Chain B UniProt accession]=Q570C0 [Chain B UniProt boundaries]=1-594 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_Q570C0 [Chain B UniRef90 boundaries]=1-594 [Related structures]=2p1n,2p1o [Entry] [Accession]=DI1000265 [Disorder status]=Inferred from motif [Kd]=2.70E-06 [Name]=Zn2+-bound form of des3-23ALG-2 complexed with Alix ABS peptide [Source organism]=Homo sapiens [PDB ID]=2zne [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=EF-hand [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_EF_ALG2_ABM_1). [Type chain A]=Ordered [Evidence chain A]=The EF-hand domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13202/PF13499). A solved monomeric structure of the domain is represented by PDB ID 2zn8. [Chain C name]=Programmed cell death 6-interacting protein [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q8WUM4 [Chain C UniProt boundaries]=799-814 [Chain C UniProt coverage]=1.8% [Chain C UniRef90 accession]=UniRef90_Q8WUM4 [Chain C UniRef90 boundaries]=799-814 [Chain A name]=Programmed cell death protein 6 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O75340 [Chain A UniProt boundaries]=24-191 [Chain A UniProt coverage]=88% [Chain A UniRef90 accession]=UniRef90_O75340 [Chain A UniRef90 boundaries]=24-191 [Entry] [Accession]=DI2000037 [Disorder status]=Inferred from motif [Kd]=2.70E-06 [Name]=EB1 in complex with microtubule Tip localization signal peptide of MACF [Source organism]=Homo sapiens [PDB ID]=3gjo [PDB chain IDs]=E:AB [PDB note]=Chains C, D, F, G and H were removed as chains A, B and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=EB1-like C-terminal [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (LIG_SxIP_EBH_1). [Type chain A]=Ordered [Evidence chain A]=The EB1-like C-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03271). A solved monomeric structure of the domain is represented by PDB ID 1wu9. [Type chain B]=Ordered [Evidence chain B]=The EB1-like C-terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03271). A solved monomeric structure of the domain is represented by PDB ID 1wu9. [Chain E name]=Dystonin [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=Q03001 [Chain E UniProt boundaries]=7541-7570 [Chain E UniProt coverage]=0.4% [Chain E UniRef90 accession]=UniRef90_Q03001 [Chain E UniRef90 boundaries]=7541-7570 [Chain A name]=Microtubule-associated protein RP/EB family member 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q15691 [Chain A UniProt boundaries]=189-260 [Chain A UniProt coverage]=26.9% [Chain A UniRef90 accession]=UniRef90_Q15691 [Chain A UniRef90 boundaries]=189-260 [Chain B name]=Microtubule-associated protein RP/EB family member 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q15691 [Chain B UniProt boundaries]=189-260 [Chain B UniProt coverage]=26.9% [Chain B UniRef90 accession]=UniRef90_Q15691 [Chain B UniRef90 boundaries]=189-260 [Entry] [Accession]=DI1100089 [Disorder status]=Inferred from motif [Kd]=4.70E-06 [Name]=Complex between Dok7 PH-PTB and the MuSK juxtamembrane region [Source organism]=Mus musculus [PDB ID]=3ml4 [PDB chain IDs]=E:A [PDB note]=Chains C, D, F, G and H were removed as chains A and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=IRS-type PTB [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (LIG_PTB_Phospho_1). [Type chain A]=Ordered [Evidence chain A]=The IRS-type PTB domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02174). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2dlw. [Modified residues chain E]=phosphotyrosine#Y#553 [Chain E name]=Muscle, skeletal receptor tyrosine-protein kinase [Chain E source organism]=Mus musculus [Chain E UniProt accession]=Q61006 [Chain E UniProt boundaries]=544-556 [Chain E UniProt coverage]=1.5% [Chain E UniRef90 accession]=UniRef90_Q62838 [Chain E UniRef90 boundaries]=544-556 [Chain A name]=Protein Dok-7 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q18PE0 [Chain A UniProt boundaries]=1-220 [Chain A UniProt coverage]=43.7% [Chain A UniRef90 accession]=UniRef90_Q18PE0 [Chain A UniRef90 boundaries]=1-220 [Entry] [Accession]=DI1000266 [Disorder status]=Inferred from motif [Kd]=2.70E-05 [Name]=First YWTD beta propeller domain of LRP6 in complex with a DKK1 peptide [Source organism]=Homo sapiens [PDB ID]=3soq [PDB chain IDs]=Z:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=YWTD beta propeller [Type chain Z]=Disordered [Evidence chain Z]=The protein region involved in the interaction contains a known functional linear motif (LIG_LRP6_Inhibitor_1). [Type chain A]=Ordered [Evidence chain A]=The YWTD beta propeller domain domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00058/PF14670). A solved monomeric structure of the domain is represented by PDB ID 3s94. [Chain Z name]=Dickkopf-related protein 1 [Chain Z source organism]=Homo sapiens [Chain Z UniProt accession]=O94907 [Chain Z UniProt boundaries]=38-44 [Chain Z UniProt coverage]=2.6% [Chain Z UniRef90 accession]=UniRef90_O94907 [Chain Z UniRef90 boundaries]=38-44 [Chain A name]=Low-density lipoprotein receptor-related protein 6 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O75581 [Chain A UniProt boundaries]=20-326 [Chain A UniProt coverage]=19% [Chain A UniRef90 accession]=UniRef90_O75581 [Chain A UniRef90 boundaries]=20-326 [Entry] [Accession]=DI1000267 [Disorder status]=Confirmed [Kd]=6.10E-05 [Name]=First YWTD beta propeller domain of LRP6 in complex with peptide S [Source organism]=Homo sapiens [PDB ID]=3sov [PDB chain IDs]=Z:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.27 [Domain]=YWTD beta propeller [Type chain Z]=Disordered [Evidence chain Z]=The 110-133 region described in DisProt entry DP00926 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_LRP6_Inhibitor_1). [Type chain A]=Ordered [Evidence chain A]=The YWTD beta propeller domain domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00058/PF14670). A solved monomeric structure of the domain is represented by PDB ID 3s94. [Chain Z name]=Sclerostin [Chain Z source organism]=Homo sapiens [Chain Z UniProt accession]=Q9BQB4 [Chain Z UniProt boundaries]=115-121 [Chain Z UniProt coverage]=3.3% [Chain Z UniRef90 accession]=UniRef90_Q9BQB4 [Chain Z UniRef90 boundaries]=115-121 [Chain A name]=Low-density lipoprotein receptor-related protein 6 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O75581 [Chain A UniProt boundaries]=20-326 [Chain A UniProt coverage]=19% [Chain A UniRef90 accession]=UniRef90_O75581 [Chain A UniRef90 boundaries]=20-326 [Entry] [Accession]=DI1100090 [Disorder status]=Inferred from motif [Kd]=6.10E-05 [Name]=Acm1-Cdh1 complex [Source organism]=Saccharomyces cerevisiae [PDB ID]=4bh6 [PDB chain IDs]=N:E [PDB note]=Chains A, B, C, D, F, G, H, I, J, K, L, M, O and P were removed as chains E and N highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.90 [Domain]=WD40 [Type chain N]=Disordered [Evidence chain N]=The protein region involved in the interaction contains a known functional linear motif (LIG_APCC_ABBA_1). [Type chain E]=Ordered [Evidence chain E]=The WD40-like beta propeller repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF07676). A solved monomeric structure of the domain is represented by PDB ID 1crz. [Modified residues chain E]=phosphotyrosine#Y#553 [Chain N name]=APC/C-CDH1 modulator 1 [Chain N source organism]=Saccharomyces cerevisiae [Chain N UniProt accession]=Q08981 [Chain N UniProt boundaries]=59-128 [Chain N UniProt coverage]=33.5% [Chain N UniRef90 accession]=UniRef90_Q08981 [Chain N UniRef90 boundaries]=59-128 [Chain E name]=APC/C activator protein CDH1 [Chain E source organism]=Saccharomyces cerevisiae [Chain E UniProt accession]=P53197 [Chain E UniProt boundaries]=241-548 [Chain E UniProt coverage]=54.4% [Chain E UniRef90 accession]=UniRef90_P53197 [Chain E UniRef90 boundaries]=241-548 [Entry] [Accession]=DI1000268 [Disorder status]=Inferred from motif [Kd]=6.10E-05 [Name]=BUB1B peptide recognized by CDC20 [Source organism]=Homo sapiens [PDB ID]=4ggd [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains C and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.44 [Domain]=WD40 [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (DEG_APCC_KENBOX_2). [Type chain A]=Ordered [Evidence chain A]=The WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00400). A solved monomeric structure from a homologous protein is represented by PDB ID 4gga. [Chain C name]=Mitotic checkpoint serine/threonine-protein kinase BUB1 beta [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=O60566 [Chain C UniProt boundaries]=20-42 [Chain C UniProt coverage]=2.2% [Chain C UniRef90 accession]=UniRef90_O60566 [Chain C UniRef90 boundaries]=20-42 [Chain A name]=Cell division cycle protein 20 homolog [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q12834 [Chain A UniProt boundaries]=71-499 [Chain A UniProt coverage]=86% [Chain A UniRef90 accession]=UniRef90_Q12834 [Chain A UniRef90 boundaries]=71-499 [Related structures]=5khu,5lcw [Entry] [Accession]=DI2020003 [Disorder status]=Inferred from motif [Kd]=4.00E-09 [Name]=Calcineurin in complex with the calcineurin-inhibiting domain of the African swine fever virus protein A238L [Source organism]=African swine fever virus / Homo sapiens [PDB ID]=4f0z [PDB chain IDs]=C:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=Calcineurin-like phosphoesterase/EF-hand [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (DOC_PP2B_PxIxI_1). [Type chain A]=Ordered component [Evidence chain A]=The calcineurin-like phosphoesterase domain (found in Serine/threonine-protein phosphatase 2B catalytic subunit) and the EF-hands of the Calcineurin subunit B type 1 form a stable heterodimer that serves as an interacting surface. A solved structure of the dimer without bound ligands is represented by PDB ID 1aui. [Type chain B]=Ordered component [Evidence chain B]=The calcineurin-like phosphoesterase domain (found in Serine/threonine-protein phosphatase 2B catalytic subunit) and the EF-hands of the Calcineurin subunit B type 1 form a stable heterodimer that serves as an interacting surface. A solved structure of the dimer without bound ligands is represented by PDB ID 1aui. [Chain C name]=Ankyrin repeat domain-containing protein A238L [Chain C source organism]=African swine fever virus [Chain C UniProt accession]=O36972 [Chain C UniProt boundaries]=200-239 [Chain C UniProt coverage]=16.7% [Chain C UniRef90 accession]=UniRef90_O36972 [Chain C UniRef90 boundaries]=200-239 [Chain A name]=Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q08209 [Chain A UniProt boundaries]=1-370 [Chain A UniProt coverage]=71% [Chain A UniRef90 accession]=UniRef90_P63328 [Chain A UniRef90 boundaries]=1-370 [Chain B name]=Calcineurin subunit B type 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P63098 [Chain B UniProt boundaries]=1-170 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P63098 [Chain B UniRef90 boundaries]=1-170 [Entry] [Accession]=DI2000038 [Disorder status]=Inferred from motif [Kd]=8.10E-06 [Name]=Ufm1 in complex with UBA5 [Source organism]=Homo sapiens [PDB ID]=5hkh [PDB chain IDs]=B:AC [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.55 [Domain]=Ufm1 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_UFM1_UFIM_1). [Type chain A]=Ordered [Evidence chain A]=The Ubiquitin fold modifier 1 (Ufm1) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03671). A solved monomeric structure of the domain is represented by PDB ID 5ia7. [Type chain C]=Ordered [Evidence chain C]=The Ubiquitin fold modifier 1 (Ufm1) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03671). A solved monomeric structure of the domain is represented by PDB ID 5ia7. [Chain B name]=Ubiquitin-like modifier-activating enzyme 5 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9GZZ9 [Chain B UniProt boundaries]=338-346 [Chain B UniProt coverage]=2.2% [Chain B UniRef90 accession]=UniRef90_Q9GZZ9 [Chain B UniRef90 boundaries]=338-346 [Chain A name]=Ubiquitin-fold modifier 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P61960 [Chain A UniProt boundaries]=1-83 [Chain A UniProt coverage]=97.6% [Chain A UniRef90 accession]=UniRef90_P61960 [Chain A UniRef90 boundaries]=2-83 [Chain C name]=Ubiquitin-fold modifier 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P61960 [Chain C UniProt boundaries]=1-83 [Chain C UniProt coverage]=97.6% [Chain C UniRef90 accession]=UniRef90_P61960 [Chain C UniRef90 boundaries]=2-83 [Related structures]=5ia8,5iaa,5l95 [Entry] [Accession]=DI1100091 [Disorder status]=Inferred from homology [Kd]=8.10E-06 [Name]=Bcl-X:Bim BH3 complex (Mus musculus) [Source organism]=Mus musculus [PDB ID]=1pq1 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.65 [Domain]=Bcl-2 homology [Type chain B]=Disordered [Evidence chain B]=The interacting region (Bcl-x interacting BH3 domain, see Pfam domain PF08946) of human Bim has been shown to be intrinsically disordered in an aqueous environment, and undergo localized conformational change, involving helix formation of the contact residues in the BH3 domain, upon binding to its partner protein (PMID:16645638 and PMID:15694340). [Type chain A]=Ordered [Evidence chain A]=Bcl-2 homology (BH) domains, such as the one involved in the interaction, are known to adopt a stable structure in isolation (see Pfam domain PF00452). A solved monomeric structure of the domain is represented by PDB ID 1pq0. [Chain B name]=Bcl-2-like protein 11 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=O54918 [Chain B UniProt boundaries]=139-171 [Chain B UniProt coverage]=16.8% [Chain B UniRef90 accession]=UniRef90_O54918 [Chain B UniRef90 boundaries]=139-171 [Chain A name]=Bcl-2-like protein 1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q64373 [Chain A UniProt boundaries]=1-196 [Chain A UniProt coverage]=84.1% [Chain A UniRef90 accession]=UniRef90_Q07817 [Chain A UniRef90 boundaries]=1-196 [Entry] [Accession]=DI1000269 [Disorder status]=Confirmed [Kd]=4.50E-08 [Name]=Bcl-X:Bim BH3 complex (human) [Source organism]=Homo sapiens [PDB ID]=2yq6 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=Bcl-2 homology [Type chain B]=Disordered [Evidence chain B]=The interacting region (Bcl-x interacting BH3 domain, see Pfam domain PF08946) of Bim has been shown to be intrinsically disordered in an aqueous environment, and undergo localized conformational change, involving helix formation of the contact residues in the BH3 domain, upon binding to its partner protein (PMID:16645638 and PMID:15694340). The protein region involved in the interaction contains a known functional linear motif (LIG_BH_BH3_1). [Type chain A]=Ordered [Evidence chain A]=Bcl-2 homology (BH) domains, such as the one involved in the interaction, are known to adopt a stable structure in isolation (see Pfam domain PF00452). A solved monomeric structure of the domain is represented by PDB ID 1lxl. [Modified residues chain B]=2-methyl-L-norleucine#L#154|2-methyl-L-norleucine#L#158 [Chain B name]=Bcl-2-like protein 11 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O43521 [Chain B UniProt boundaries]=147-164 [Chain B UniProt coverage]=9.1% [Chain B UniRef90 accession]=UniRef90_O43521 [Chain B UniRef90 boundaries]=147-164 [Chain A name]=Bcl-2-like protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q07817 [Chain A UniProt boundaries]=83-209 [Chain A UniProt coverage]=54.5% [Chain A UniRef90 accession]=UniRef90_Q07817 [Chain A UniRef90 boundaries]=83-209 [Related structures]=4qvf,3fdl,2yq7,3io8,4a1u,4a1w,4yj4,5c3g [Entry] [Accession]=DI1000270 [Disorder status]=Confirmed [Kd]=3.10E-05 [Name]=C-domain of human cardiac troponin C in complex with the inhibitory region of human cardiac troponin I [Source organism]=Homo sapiens [PDB ID]=1ozs [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=EF-hand [Type chain B]=Disordered [Evidence chain B]=The C-terminal region of troponin I was shown to be intrinsically disordered (PMID:21322033). [Type chain A]=Ordered [Evidence chain A]=The EF-hand domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13833). A solved monomeric structure of the domain is represented by PDB ID 2mle. [Chain B name]=Troponin I, cardiac muscle [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P19429 [Chain B UniProt boundaries]=129-148 [Chain B UniProt coverage]=9.5% [Chain B UniRef90 accession]=UniRef90_P19429 [Chain B UniRef90 boundaries]=129-148 [Chain A name]=Troponin C, slow skeletal and cardiac muscles [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63316 [Chain A UniProt boundaries]=89-161 [Chain A UniProt coverage]=45.3% [Chain A UniRef90 accession]=UniRef90_P63316 [Chain A UniRef90 boundaries]=90-161 [Entry] [Accession]=DI1000271 [Disorder status]=Confirmed [Kd]=7.60E-07 [Name]=53BP1 tandem Tudor domains in complex with a p53K381acK382me2 peptide [Source organism]=Homo sapiens [PDB ID]=4x34 [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=Tudor-like [Type chain C]=Disordered [Evidence chain C]=The 320-393 region described in DisProt entry DP00086 and the 364-389 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (DOC_CYCLIN_1). [Type chain A]=Ordered [Evidence chain A]=The Tudor-like domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF09038). A solved monomeric structure of the domain is represented by PDB ID 2g3r. [Modified residues chain C]=N(6)-acetyllysine#K#381|N-dimethyl-lysine#K#382 [Chain C name]=Cellular tumor antigen p53 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P04637 [Chain C UniProt boundaries]=377-386 [Chain C UniProt coverage]=2.5% [Chain C UniRef90 accession]=UniRef90_P04637 [Chain C UniRef90 boundaries]=377-386 [Chain A name]=Tumor suppressor p53-binding protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q12888 [Chain A UniProt boundaries]=1484-1603 [Chain A UniProt coverage]=6.1% [Chain A UniRef90 accession]=UniRef90_Q12888 [Chain A UniRef90 boundaries]=1484-1603 [Entry] [Accession]=DI1000272 [Disorder status]=Confirmed [Kd]=4.20E-05 [Name]=53BP1 tandem Tudor domains in complex with a methylated K810 Rb peptide [Source organism]=Homo sapiens [PDB ID]=4cri [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.35 [Domain]=Tudor-like [Type chain C]=Disordered [Evidence chain C]=The 772-874 region described in IDEAL entry IID00017 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Tudor-like domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF09038). A solved monomeric structure of the domain is represented by PDB ID 2g3r. [Modified residues chain C]=N-dimethyl-lysine#K#810 [Chain C name]=Retinoblastoma-associated protein [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P06400 [Chain C UniProt boundaries]=802-817 [Chain C UniProt coverage]=1.7% [Chain C UniRef90 accession]=UniRef90_P06400 [Chain C UniRef90 boundaries]=802-817 [Chain A name]=Tumor suppressor p53-binding protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q12888 [Chain A UniProt boundaries]=1459-1634 [Chain A UniProt coverage]=8.9% [Chain A UniRef90 accession]=UniRef90_Q12888 [Chain A UniRef90 boundaries]=1459-1633 [Entry] [Accession]=DI1000273 [Disorder status]=Confirmed [Kd]=3.80E-06 [Name]=UHRF1 in complex with unmodified H3.1 N-terminal tail [Source organism]=Homo sapiens [PDB ID]=2lgg [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 2lgl. [Chain B name]=Histone H3.1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68431 [Chain B UniProt boundaries]=2-13 [Chain B UniProt coverage]=8.8% [Chain B UniRef90 accession]=UniRef90_P68431 [Chain B UniRef90 boundaries]=2-13 [Chain A name]=E3 ubiquitin-protein ligase UHRF1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96T88 [Chain A UniProt boundaries]=298-366 [Chain A UniProt coverage]=8.7% [Chain A UniRef90 accession]=UniRef90_Q96T88 [Chain A UniRef90 boundaries]=298-366 [Related structures]=3zvy,3sou [Entry] [Accession]=DI1000274 [Disorder status]=Confirmed [Kd]=4.40E-06 [Name]=WW3 domain of Nedd4L in complex with its HECT domain PY motif [Source organism]=Homo sapiens [PDB ID]=2mpt [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=WW [Type chain B]=Disordered [Evidence chain B]=The PY motif is buried inside the HECT domain and only becomes accessible after its unfolding. The unstructured and exposed PY motif is then bound by the WW domain (PMID:25295397). [Type chain A]=Ordered [Evidence chain A]=The WW domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00397). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2n8u. [Chain B name]=E3 ubiquitin-protein ligase NEDD4-like [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q96PU5 [Chain B UniProt boundaries]=945-958 [Chain B UniProt coverage]=1.4% [Chain B UniRef90 accession]=UniRef90_Q96PU5 [Chain B UniRef90 boundaries]=945-957 [Chain A name]=E3 ubiquitin-protein ligase NEDD4-like [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96PU5 [Chain A UniProt boundaries]=492-539 [Chain A UniProt coverage]=4.9% [Chain A UniRef90 accession]=UniRef90_Q96PU5 [Chain A UniRef90 boundaries]=496-539 [Entry] [Accession]=DI1020036 [Disorder status]=Inferred from motif [Kd]=6.00E-08 [Name]=Nck1 SH2-domain in complex with a dodecaphosphopeptide from Tir [Source organism]=Escherichia coli O127:H6 / Homo sapiens [PDB ID]=2ci9 [PDB chain IDs]=L:A [PDB note]=Chains B and M were removed as chains A and L represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.5 [Domain]=SH2 [Type chain L]=Disordered [Evidence chain L]=The protein region involved in the interaction contains a known functional SH2-domain binding linear motif (PMID:16636066). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain is represented by PDB ID 2ci8. [Modified residues chain L]=phosphotyrosine#Y#474 [Chain L name]=Translocated intimin receptor Tir [Chain L source organism]=Escherichia coli O127:H6 [Chain L UniProt accession]=B7UM99 [Chain L UniProt boundaries]=470-481 [Chain L UniProt coverage]=2.2% [Chain L UniRef90 accession]=UniRef90_B7UM99 [Chain L UniRef90 boundaries]=470-481 [Chain A name]=Cytoplasmic protein NCK1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P16333 [Chain A UniProt boundaries]=276-377 [Chain A UniProt coverage]=27.1% [Chain A UniRef90 accession]=UniRef90_P16333 [Chain A UniRef90 boundaries]=279-377 [Entry] [Accession]=DI1100092 [Disorder status]=Inferred from motif [Kd]=2.02E-05 [Name]=SH3-II of Drosophila Rim-binding protein bound to a Cacophony derived peptide [Source organism]=Drosophila melanogaster [PDB ID]=4z89 [PDB chain IDs]=a:A [PDB note]=Chains B, C, D, E, F, G, H, I, J, b, c, d, e, f, g, h, i and j were removed as chains a and A represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.64 [Domain]=SH3 [Type chain a]=Disordered [Evidence chain a]=The protein region involved in the interaction contains a known functional linear motif (SH3-binding motif PxxP, PMID:26274777). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF07653). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1shg. [Chain a name]=Voltage-dependent calcium channel type A subunit alpha-1 [Chain a source organism]=Drosophila melanogaster [Chain a UniProt accession]=P91645 [Chain a UniProt boundaries]=1688-1702 [Chain a UniProt coverage]=0.8% [Chain a UniRef90 accession]=UniRef90_P91645 [Chain a UniRef90 boundaries]=1688-1702 [Chain A name]=RIM-binding protein, isoform F [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=A0A0B4JDC9 [Chain A UniProt boundaries]=1318-1382 [Chain A UniProt coverage]=3.5% [Chain A UniRef90 accession]=UniRef90_A0A0B4JDC9 [Chain A UniRef90 boundaries]=1318-1382 [Entry] [Accession]=DI1000275 [Disorder status]=Confirmed [Kd]=2.02E-05 [Name]=Human TDRD1 extended Tudor domain in complex with a symmetrically dimethylated E2F peptide [Source organism]=Homo sapiens [PDB ID]=5m9n [PDB chain IDs]=C:A [PDB note]=Chain B was removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.95 [Domain]=Tudor [Type chain C]=Disordered [Evidence chain C]=The interacting region of E2F1 has been shown to be intrinsically disordered only adopting a stable structure upon interacting with partner proteins (PMID:16360038). [Type chain A]=Ordered [Evidence chain A]=The Tudor domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00567). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3pmt. [Modified residues chain C]=N3,N4-dimethyl-arginine#R#8|N3,N4-dimethyl-arginine#R#10 [Chain C name]=Transcription factor E2F1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q01094 [Chain C UniProt boundaries]=104-120 [Chain C UniProt coverage]=3.9% [Chain C UniRef90 accession]=UniRef90_Q01094 [Chain C UniRef90 boundaries]=104-120 [Chain A name]=Tudor domain-containing protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9BXT4 [Chain A UniProt boundaries]=460-679 [Chain A UniProt coverage]=18.6% [Chain A UniRef90 accession]=UniRef90_Q9BXT4 [Chain A UniRef90 boundaries]=460-679 [Entry] [Accession]=DI1000276 [Disorder status]=Confirmed [Kd]=4.30E-05 [Name]=Phosphorylated STING in complex with IRF-3 CTD [Source organism]=Homo sapiens [PDB ID]=5jej [PDB chain IDs]=C:B [PDB note]=Chains A, D and E were removed as chains C and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=IRF-3 [Type chain C]=Disordered [Evidence chain C]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 4f5w, PMID:22728660). The protein region involved in the interaction contains a pLxIS motif that mediates the recruitment of IRF-3 (PMID:27302953). [Type chain B]=Ordered [Evidence chain B]=The IRF-3 (Interferon-regulatory factor 3) domain involved in the interaction is known to adopt a stable structure in solution (see Pfam domain PF10401). A solved monomeric structure of the domain is represented by PDB ID 1j2f. [Modified residues chain C]=phosphoserine#S#366 [Chain C name]=Stimulator of interferon genes protein [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q86WV6 [Chain C UniProt boundaries]=342-379 [Chain C UniProt coverage]=10% [Chain C UniRef90 accession]=UniRef90_Q86WV6 [Chain C UniRef90 boundaries]=342-379 [Chain B name]=Interferon regulatory factor 3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q14653 [Chain B UniProt boundaries]=189-427 [Chain B UniProt coverage]=56% [Chain B UniRef90 accession]=UniRef90_Q14653 [Chain B UniRef90 boundaries]=189-427 [Entry] [Accession]=DI1000277 [Disorder status]=Confirmed [Kd]=1.04E-04 [Name]=Phosphorylated MAVS in complex with IRF-3 [Source organism]=Homo sapiens [PDB ID]=5jek [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains C and A represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=IRF-3 [Type chain C]=Disordered [Evidence chain C]=The consensus IRF3 binding motif: pLxIS (p:hydrophilic, x:non-aromatic), involved in the interaction, always located in a disordered region of the protein (PMID:25636800). [Type chain A]=Ordered [Evidence chain A]=The IRF-3 (Interferon-regulatory factor 3) domain involved in the interaction is known to adopt a stable structure in solution (see Pfam domain PF10401). A solved monomeric structure of the domain is represented by PDB ID 1j2f. [Modified residues chain C]=phosphoserine#S#442 [Chain C name]=Mitochondrial antiviral-signaling protein [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q7Z434 [Chain C UniProt boundaries]=433-450 [Chain C UniProt coverage]=3.3% [Chain C UniRef90 accession]=UniRef90_Q7Z434 [Chain C UniRef90 boundaries]=433-450 [Chain A name]=Interferon regulatory factor 3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q14653 [Chain A UniProt boundaries]=189-427 [Chain A UniProt coverage]=56% [Chain A UniRef90 accession]=UniRef90_Q14653 [Chain A UniRef90 boundaries]=189-427 [Entry] [Accession]=DI1000278 [Disorder status]=Confirmed [Kd]=7.20E-05 [Name]=Phosphorylated TRIF in complex with IRF-3 [Source organism]=Homo sapiens [PDB ID]=5jel [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.60 [Domain]=IRF-3 [Type chain B]=Disordered [Evidence chain B]=The consensus IRF3 binding motif: pLxIS (p:hydrophilic, x:non-aromatic), involved in the interaction, always located in a disordered region of the protein (PMID:25636800). [Type chain A]=Ordered [Evidence chain A]=The IRF-3 (Interferon-regulatory factor 3) domain involved in the interaction is known to adopt a stable structure in solution (see Pfam domain PF10401). A solved monomeric structure of the domain is represented by PDB ID 1j2f. [Modified residues chain B]=phosphoserine#S#202|phosphoserine#S#205|phosphoserine#S#210 [Chain B name]=TIR domain-containing adapter molecule 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q8IUC6 [Chain B UniProt boundaries]=199-219 [Chain B UniProt coverage]=2.9% [Chain B UniRef90 accession]=UniRef90_Q8IUC6 [Chain B UniRef90 boundaries]=199-219 [Chain A name]=Interferon regulatory factor 3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q14653 [Chain A UniProt boundaries]=189-427 [Chain A UniProt coverage]=56% [Chain A UniRef90 accession]=UniRef90_Q14653 [Chain A UniRef90 boundaries]=189-427 [Entry] [Accession]=DI1100093 [Disorder status]=Inferred from motif [Kd]=1.02E-05 (PMID:11124038) [Name]=FHA1 domain of Rad53 in complex with a phosphothreonyl peptide from Rad9 (149-161) [Source organism]=Saccharomyces cerevisiae [PDB ID]=1k3n [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=FHA [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_FHA_2). [Type chain A]=Ordered [Evidence chain A]=The FHA domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00498). A solved monomeric structure of the domain is represented by PDB ID 1dmz. [Modified residues chain B]=phosphothreonine#T#171 [Chain B name]=DNA repair protein RAD9 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=P14737 [Chain B UniProt boundaries]=149-161 [Chain B UniProt coverage]=1% [Chain B UniRef90 accession]=UniRef90_P14737 [Chain B UniRef90 boundaries]=149-161 [Chain A name]=Serine/threonine-protein kinase RAD53 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P22216 [Chain A UniProt boundaries]=14-164 [Chain A UniProt coverage]=18.4% [Chain A UniRef90 accession]=UniRef90_P22216 [Chain A UniRef90 boundaries]=14-164 [Related structures]=1j4p [Entry] [Accession]=DI1000279 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=ATRX ADD bound to unmodified histone H3.3 peptide [Source organism]=Homo sapiens [PDB ID]=3qlc [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=ADD [Type chain C]=Disordered [Evidence chain C]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The 1-45 region described in IDEAL entry IID00239 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The ADD domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 2jm1. [Chain C name]=Histone H3.3 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P84243 [Chain C UniProt boundaries]=2-16 [Chain C UniProt coverage]=11% [Chain C UniRef90 accession]=UniRef90_P84243 [Chain C UniRef90 boundaries]=2-16 [Chain A name]=Transcriptional regulator ATRX [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P46100 [Chain A UniProt boundaries]=161-289 [Chain A UniProt coverage]=5.2% [Chain A UniRef90 accession]=UniRef90_P46100 [Chain A UniRef90 boundaries]=161-289 [Entry] [Accession]=DI1000280 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=ATRX ADD bound to histone H3.3 (H3K9me3S10ph) peptide [Source organism]=Homo sapiens [PDB ID]=4w5a [PDB chain IDs]=C:A [PDB note]=Chains B, D, E and F were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=ADD [Type chain C]=Disordered [Evidence chain C]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The 1-45 region described in IDEAL entry IID00239 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The ADD domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 2jm1. [Modified residues chain C]=N-trimethyllysine#K#9|phosphoserine#S#10 [Chain C name]=Histone H3.3 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P84243 [Chain C UniProt boundaries]=2-16 [Chain C UniProt coverage]=11% [Chain C UniRef90 accession]=UniRef90_P84243 [Chain C UniRef90 boundaries]=2-16 [Chain A name]=Transcriptional regulator ATRX [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P46100 [Chain A UniProt boundaries]=161-289 [Chain A UniProt coverage]=5.2% [Chain A UniRef90 accession]=UniRef90_P46100 [Chain A UniRef90 boundaries]=161-289 [Entry] [Accession]=DI2010015 [Disorder status]=Inferred from homology [Kd]=3.70E-06 (PMID:21666679) [Name]=Complex of human alpha-thrombin and unmodified recombinant hirudin [Source organism]=Hirudo medicinalis / Homo sapiens [PDB ID]=4htc [PDB chain IDs]=I:HL [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=Trypsin [Type chain I]=Disordered [Evidence chain I]=The interacting region of a closely homologous variant of hirudin has been shown to be intrinsically disordered (PMID:1335515). [Type chain H]=Ordered component [Evidence chain H]=Thrombin consists of a large and a small subunit. Trypsin domain of the large subunit involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00089). A solved structure of the thrombin dimer is represented by PDB ID 1jou. [Type chain L]=Ordered component [Evidence chain L]=Thrombin consists of a large and a small subunit. Trypsin domain of the large subunit involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00089). A solved structure of the thrombin dimer is represented by PDB ID 1jou. [Modified residues chain L]=phosphotyrosine#Y#474 [Chain I name]=Hirudin variant-2 (Fragment) [Chain I source organism]=Hirudo medicinalis [Chain I UniProt accession]=P09945 [Chain I UniProt boundaries]=8-72 [Chain I UniProt coverage]=90.3% [Chain I UniRef90 accession]=UniRef90_P09945 [Chain I UniRef90 boundaries]=8-72 [Chain H name]=Prothrombin [Chain H source organism]=Homo sapiens [Chain H UniProt accession]=P00734 [Chain H UniProt boundaries]=364-622 [Chain H UniProt coverage]=41.6% [Chain H UniRef90 accession]=UniRef90_P00734 [Chain H UniRef90 boundaries]=364-622 [Chain L name]=Prothrombin [Chain L source organism]=Homo sapiens [Chain L UniProt accession]=P00734 [Chain L UniProt boundaries]=328-363 [Chain L UniProt coverage]=5.8% [Chain L UniRef90 accession]=UniRef90_P00734 [Chain L UniRef90 boundaries]=328-363 [Related structures]=1a3b,1a3e,1ihs,3htc,1oyt,1tmt,2hgt,3vxe,3vxf [Entry] [Accession]=DI2010016 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=Complex of human alpha-thrombin and acetylated recombinant hirudin [Source organism]=Hirudo medicinalis / Homo sapiens [PDB ID]=1c1u [PDB chain IDs]=I:HL [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.75 [Domain]=Trypsin [Type chain I]=Disordered [Evidence chain I]=The interacting region of hirudin has been shown to be intrinsically disordered (PMID:1335515). The 50-65 region described in DisProt entry DP00137 covers 25% of the sequence present in the structure. [Type chain H]=Ordered component [Evidence chain H]=Thrombin consists of a large and a small subunit. Trypsin domain of the large subunit involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00089). A solved structure of the thrombin dimer is represented by PDB ID 1jou. [Type chain L]=Ordered component [Evidence chain L]=Thrombin consists of a large and a small subunit. Trypsin domain of the large subunit involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00089). A solved structure of the thrombin dimer is represented by PDB ID 1jou. [Modified residues chain I]=O-sulfo-L-tyrosine#Y#63 [Modified residues chain L]=phosphotyrosine#Y#474 [Chain I name]=Hirudin-2 [Chain I source organism]=Hirudo medicinalis [Chain I UniProt accession]=P28504 [Chain I UniProt boundaries]=55-65 [Chain I UniProt coverage]=16.9% [Chain I UniRef90 accession]=UniRef90_P09945 [Chain I UniRef90 boundaries]=55-65 [Chain H name]=Prothrombin [Chain H source organism]=Homo sapiens [Chain H UniProt accession]=P00734 [Chain H UniProt boundaries]=364-622 [Chain H UniProt coverage]=41.6% [Chain H UniRef90 accession]=UniRef90_P00734 [Chain H UniRef90 boundaries]=364-622 [Chain L name]=Prothrombin [Chain L source organism]=Homo sapiens [Chain L UniProt accession]=P00734 [Chain L UniProt boundaries]=328-363 [Chain L UniProt coverage]=5.8% [Chain L UniRef90 accession]=UniRef90_P00734 [Chain L UniRef90 boundaries]=328-363 [Related structures]=1c1v,1c1w,1c5l,1c5n,1c5o,1d9i,1fpc,1g30,1g32,1ghv,1ghw,1ghx,1ghy,1gj4,1gj5,1kts,1ktt,1mu6,1mu8,1mue,1nm6,1nt1,1o2g,1qbv,1riw,1sb1,1sl3,1ta2,1ta6,1twx,1vr1,1xm1,1ype,1ypg,1ypj,1ypk,1ypl,1ypm,1zrb,2gde [Entry] [Accession]=DI1000281 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=CBP Bromodomain interacting with a H4 peptide (8-13) [Source organism]=Homo sapiens [PDB ID]=4n4f [PDB chain IDs]=C:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.83 [Domain]=Bromodomain [Type chain C]=Disordered [Evidence chain C]=The 1-28 region described in IDEAL entry IID00058 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 2d82. [Modified residues chain C]=N(6)-acetyllysine#K#12 [Chain C name]=Histone H4 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P62805 [Chain C UniProt boundaries]=6-26 [Chain C UniProt coverage]=20.4% [Chain C UniRef90 accession]=UniRef90_P62805 [Chain C UniRef90 boundaries]=6-26 [Chain A name]=CREB-binding protein [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q92793 [Chain A UniProt boundaries]=1080-1316 [Chain A UniProt coverage]=9.7% [Chain A UniRef90 accession]=UniRef90_Q92793 [Chain A UniRef90 boundaries]=1080-1316 [Entry] [Accession]=DI1000282 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=UHRF1 in complex with H3.1 N-terminal peptide (H3K4me3) [Source organism]=Homo sapiens [PDB ID]=3sow [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.95 [Domain]=PHD zinc finger [Type chain C]=Disordered [Evidence chain C]=The 1-60 region described in IDEAL entry IID00062 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 2lgl. [Modified residues chain C]=N-trimethyllysine#K#4 [Chain C name]=Histone H3.1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P68431 [Chain C UniProt boundaries]=2-10 [Chain C UniProt coverage]=6.6% [Chain C UniRef90 accession]=UniRef90_P68431 [Chain C UniRef90 boundaries]=2-10 [Chain A name]=E3 ubiquitin-protein ligase UHRF1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96T88 [Chain A UniProt boundaries]=298-367 [Chain A UniProt coverage]=8.8% [Chain A UniRef90 accession]=UniRef90_Q96T88 [Chain A UniRef90 boundaries]=298-367 [Entry] [Accession]=DI1000283 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=Nucleosome-remodeling factor subunit BPTF bound to a H4 histone tail peptide (H4K12ac) [Source organism]=Homo sapiens [PDB ID]=3qzv [PDB chain IDs]=C:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Bromodomain [Type chain C]=Disordered [Evidence chain C]=The 1-28 region described in IDEAL entry IID00058 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 3uv2. [Modified residues chain C]=N(6)-acetyllysine#K#12 [Chain C name]=Histone H4 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P62805 [Chain C UniProt boundaries]=8-18 [Chain C UniProt coverage]=10.7% [Chain C UniRef90 accession]=UniRef90_P62805 [Chain C UniRef90 boundaries]=8-18 [Chain A name]=Nucleosome-remodeling factor subunit BPTF [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q12830 [Chain A UniProt boundaries]=2865-3033 [Chain A UniProt coverage]=5.5% [Chain A UniRef90 accession]=UniRef90_Q12830 [Chain A UniRef90 boundaries]=2865-3033 [Entry] [Accession]=DI1000284 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=MOZ double PHD finger interacting with histone H3.1 tail (H3K9ac) [Source organism]=Homo sapiens [PDB ID]=4lka [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.61 [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=The 1-60 region described in IDEAL entry IID0062 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_14-3-3_CanoR_1). [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 4ljn. [Modified residues chain B]=N(6)-acetyllysine#K#9 [Chain B name]=Histone H3.1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68431 [Chain B UniProt boundaries]=2-22 [Chain B UniProt coverage]=15.4% [Chain B UniRef90 accession]=UniRef90_P68431 [Chain B UniRef90 boundaries]=2-22 [Chain A name]=Histone acetyltransferase KAT6A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q92794 [Chain A UniProt boundaries]=188-323 [Chain A UniProt coverage]=6.8% [Chain A UniRef90 accession]=UniRef90_Q92794 [Chain A UniRef90 boundaries]=194-323 [Entry] [Accession]=DI1000285 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=MOZ double PHD finger interacting with histone H3.1 tail (H3K14ac) [Source organism]=Homo sapiens [PDB ID]=4llb [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=PHD zinc finger [Type chain C]=Disordered [Evidence chain C]=The 1-60 region described in IDEAL entry IID0062 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_14-3-3_CanoR_1). [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 4ljn. [Modified residues chain C]=N(6)-acetyllysine#K#14 [Chain C name]=Histone H3.1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P68431 [Chain C UniProt boundaries]=2-22 [Chain C UniProt coverage]=15.4% [Chain C UniRef90 accession]=UniRef90_P68431 [Chain C UniRef90 boundaries]=2-22 [Chain A name]=Histone acetyltransferase KAT6A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q92794 [Chain A UniProt boundaries]=188-323 [Chain A UniProt coverage]=6.8% [Chain A UniRef90 accession]=UniRef90_Q92794 [Chain A UniRef90 boundaries]=194-323 [Entry] [Accession]=DI1010084 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=Beta-catenin in complex with a 4x phosphorylated APC fragment [Source organism]=Homo sapiens / Mus musculus [PDB ID]=1v18 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.1 [Domain]=Armadillo repeat [Type chain B]=Disordered [Evidence chain B]=The interacting region of APC has been shown to be intrinsically disordered (PMID:24130866). [Type chain A]=Ordered [Evidence chain A]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain is represented by PDB ID 2z6h. [Modified residues chain B]=phosphoserine#S#1504|phosphoserine#S#1505|phosphoserine#S#1507|phosphoserine#S#1510 [Chain B name]=Adenomatous polyposis coli protein [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P25054 [Chain B UniProt boundaries]=1482-1528 [Chain B UniProt coverage]=1.7% [Chain B UniRef90 accession]=UniRef90_P25054 [Chain B UniRef90 boundaries]=1482-1528 [Chain A name]=Catenin beta-1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q02248 [Chain A UniProt boundaries]=134-671 [Chain A UniProt coverage]=68.9% [Chain A UniRef90 accession]=UniRef90_Q02248 [Chain A UniRef90 boundaries]=134-671 [Entry] [Accession]=DI1000286 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=UHRF1 in complex with H3.3 histone tail trimethylated at K10 [Source organism]=Homo sapiens [PDB ID]=3ask [PDB chain IDs]=P:A [PDB note]=Chains B, C, D, Q and R were removed as chains A and P represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.90 [Domain]=PHD zinc finger [Type chain P]=Disordered [Evidence chain P]=The 1-45 region described in IDEAL entry IID00239 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 2lgl. [Modified residues chain P]=N-trimethyllysine#K#9 [Chain P name]=Histone H3.3 [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=P84243 [Chain P UniProt boundaries]=2-14 [Chain P UniProt coverage]=9.6% [Chain P UniRef90 accession]=UniRef90_P84243 [Chain P UniRef90 boundaries]=2-14 [Chain A name]=E3 ubiquitin-protein ligase UHRF1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96T88 [Chain A UniProt boundaries]=134-367 [Chain A UniProt coverage]=29.5% [Chain A UniRef90 accession]=UniRef90_Q96T88 [Chain A UniRef90 boundaries]=134-367 [Related structures]=4gy5 [Entry] [Accession]=DI1000287 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=GABARAP-L1 in complex with a phopshprylated ATG4B peptide [Source organism]=Homo sapiens [PDB ID]=5lxi [PDB chain IDs]=C:D [PDB note]=Chains B and E were removed as chains C and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.44 [Domain]=Atg8 [Type chain C]=Disordered [Evidence chain C]=The 374-393 region described in IDEAL entry IID00347 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a LIR motif (PMID:28330855). [Type chain D]=Ordered [Evidence chain D]=The Atg8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02991). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1gnu. [Modified residues chain C]=phosphoserine#S#392 [Chain C name]=Cysteine protease ATG4B [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q9Y4P1 [Chain C UniProt boundaries]=384-393 [Chain C UniProt coverage]=2.5% [Chain C UniRef90 accession]=UniRef90_Q9Y4P1 [Chain C UniRef90 boundaries]=384-393 [Chain D name]=Gamma-aminobutyric acid receptor-associated protein-like 1 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=Q9H0R8 [Chain D UniProt boundaries]=1-117 [Chain D UniProt coverage]=100% [Chain D UniRef90 accession]=UniRef90_Q9H0R8 [Chain D UniRef90 boundaries]=1-117 [Entry] [Accession]=DI1000288 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=NSD3 tandem PHD5-C5HCH domains complexed with K9me3 H3.3 peptide [Source organism]=Homo sapiens [PDB ID]=4gng [PDB chain IDs]=B:A [PDB note]=Chains D and F were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.73 [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The 1-45 region described in IDEAL entry IID00239 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 4gnd. [Modified residues chain B]=N-trimethyllysine#K#9 [Chain B name]=Histone H3.3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P84243 [Chain B UniProt boundaries]=2-16 [Chain B UniProt coverage]=11% [Chain B UniRef90 accession]=UniRef90_P84243 [Chain B UniRef90 boundaries]=2-16 [Chain A name]=Histone-lysine N-methyltransferase NSD3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9BZ95 [Chain A UniProt boundaries]=1307-1413 [Chain A UniProt coverage]=7.4% [Chain A UniRef90 accession]=UniRef90_Q9BZ95 [Chain A UniRef90 boundaries]=1310-1413 [Entry] [Accession]=DI1010085 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=RAG2-PHD finger in complex with H3.1 histone peptide (H3R2me1K4me3) [Source organism]=Homo sapiens / Mus musculus [PDB ID]=2v85 [PDB chain IDs]=D:A [PDB note]=Chains B and E were removed as chains A and D highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.0 [Domain]=RAG2 PHD [Type chain D]=Disordered [Evidence chain D]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The corresponding region of a closely homologous protein has been shown to be disordered in the 1-38 region described in IDEAL entry IID00086 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The RAG2 PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13341). A solved monomeric structure of the domain is represented by PDB ID 2jwo. [Modified residues chain D]=modified arginine ((2S)-2-amino-5-[(N-methylcarbamimidoyl)amino] pentanoic acid)#R#2|N-trimethyllysine#K#4 [Chain D name]=Histone H3.1 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P68431 [Chain D UniProt boundaries]=2-13 [Chain D UniProt coverage]=8.8% [Chain D UniRef90 accession]=UniRef90_P68431 [Chain D UniRef90 boundaries]=2-13 [Chain A name]=V(D)J recombination-activating protein 2 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P21784 [Chain A UniProt boundaries]=406-487 [Chain A UniProt coverage]=15.6% [Chain A UniRef90 accession]=UniRef90_P21784 [Chain A UniRef90 boundaries]=414-487 [Entry] [Accession]=DI1010086 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=RAG2-PHD finger in complex with H3.1 histone peptide (H3R2me2sK4me2) [Source organism]=Homo sapiens / Mus musculus [PDB ID]=2v88 [PDB chain IDs]=D:A [PDB note]=Chains B and F were removed as chains A and D highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.0 [Domain]=RAG2 PHD [Type chain D]=Disordered [Evidence chain D]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The corresponding region of a closely homologous protein has been shown to be disordered in the 1-38 region described in IDEAL entry IID00086 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The RAG2 PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13341). A solved monomeric structure of the domain is represented by PDB ID 2jwo. [Modified residues chain D]=N3,N4-dimethyl-arginine#R#2|N-dimethyl-lysine#K#4 [Chain D name]=Histone H3.1 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P68431 [Chain D UniProt boundaries]=2-9 [Chain D UniProt coverage]=5.9% [Chain D UniRef90 accession]=UniRef90_P68431 [Chain D UniRef90 boundaries]=2-9 [Chain A name]=V(D)J recombination-activating protein 2 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P21784 [Chain A UniProt boundaries]=406-487 [Chain A UniProt coverage]=15.6% [Chain A UniRef90 accession]=UniRef90_P21784 [Chain A UniRef90 boundaries]=414-487 [Entry] [Accession]=DI1100094 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=SHH1 SAWADEE domain in complex with H3.2 peptide (H3K4me1K9me1) [Source organism]=Arabidopsis thaliana [PDB ID]=4iuv [PDB chain IDs]=C:A [PDB note]=Chain B was removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=SAWADEE [Type chain C]=Disordered [Evidence chain C]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The SAWADEE domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF16719). A solved monomeric structure of the domain is represented by PDB ID 4iuq. [Modified residues chain C]=N-methyl-lysine#K#4|N-methyl-lysine#K#9 [Chain C name]=Histone H3.2 [Chain C source organism]=Arabidopsis thaliana [Chain C UniProt accession]=P59226 [Chain C UniProt boundaries]=2-16 [Chain C UniProt coverage]=11% [Chain C UniRef90 accession]=UniRef90_P59226 [Chain C UniRef90 boundaries]=2-16 [Chain A name]=Protein SAWADEE HOMEODOMAIN HOMOLOG 1 [Chain A source organism]=Arabidopsis thaliana [Chain A UniProt accession]=Q9XI47 [Chain A UniProt boundaries]=124-258 [Chain A UniProt coverage]=52.3% [Chain A UniRef90 accession]=UniRef90_Q9XI47 [Chain A UniRef90 boundaries]=125-258 [Entry] [Accession]=DI1010087 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=Double PHD finger of human transcriptional protein DPF3 bound to an unmodified H3.1 histone peptide [Source organism]=Neurospora crassa / Homo sapiens [PDB ID]=2kwk [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1xwh. [Chain B name]=Histone H3 [Chain B source organism]=Neurospora crassa [Chain B UniProt accession]=P07041 [Chain B UniProt boundaries]=2-21 [Chain B UniProt coverage]=14.7% [Chain B UniRef90 accession]=UniRef90_Q6DL03 [Chain B UniRef90 boundaries]=2-21 [Chain A name]=Zinc finger protein DPF3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q92784 [Chain A UniProt boundaries]=259-372 [Chain A UniProt coverage]=30.2% [Chain A UniRef90 accession]=UniRef90_Q92784 [Chain A UniRef90 boundaries]=260-372 [Entry] [Accession]=DI1000289 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=Double PHD finger of human transcriptional protein DPF3 bound to a H4 histone peptide (H4S1ac) [Source organism]=Homo sapiens [PDB ID]=2kwo [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1xwh. [Modified residues chain B]=N-acetyl-serine#S#1 [Chain B name]=Histone H4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P62805 [Chain B UniProt boundaries]=2-21 [Chain B UniProt coverage]=19.4% [Chain B UniRef90 accession]=UniRef90_P62805 [Chain B UniRef90 boundaries]=2-21 [Chain A name]=Zinc finger protein DPF3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q92784 [Chain A UniProt boundaries]=259-372 [Chain A UniProt coverage]=30.2% [Chain A UniRef90 accession]=UniRef90_Q92784 [Chain A UniRef90 boundaries]=260-372 [Entry] [Accession]=DI1000290 [Disorder status]=Inferred from motif [Kd]=3.70E-06 (PMID:21666679) [Name]=Complex of GGA3-VHS domain and CI-MPR C-terminal unmodified peptide [Source organism]=Homo sapiens [PDB ID]=1jpl [PDB chain IDs]=E:A [PDB note]=Chains B, C, D, F, G and H were removed as chains A and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=VHS [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (TRG_LysEnd_GGAAcLL_1). [Type chain A]=Ordered [Evidence chain A]=The VHS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00790). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1jwf. [Chain E name]=Cation-independent mannose-6-phosphate receptor [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P11717 [Chain E UniProt boundaries]=2480-2491 [Chain E UniProt coverage]=0.5% [Chain E UniRef90 accession]=UniRef90_P11717 [Chain E UniRef90 boundaries]=2480-2491 [Chain A name]=ADP-ribosylation factor-binding protein GGA3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9NZ52 [Chain A UniProt boundaries]=1-166 [Chain A UniProt coverage]=23% [Chain A UniRef90 accession]=UniRef90_Q9NZ52 [Chain A UniRef90 boundaries]=1-166 [Entry] [Accession]=DI1100095 [Disorder status]=Inferred from homology [Kd]=3.70E-06 (PMID:21666679) [Name]=cAMP-dependent protein kinase complexed with a phosphorylated PKI-alpha peptide [Source organism]=Mus musculus [PDB ID]=4hpt [PDB chain IDs]=I:E [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.15 [Domain]=Protein kinase [Type chain I]=Disordered [Evidence chain I]=The corresponding region of a closely homologous protein has been shown to be disordered in the 1-76 region described in DisProt entry DP00015 (covers 100% of the sequence present in the structure). [Type chain E]=Ordered [Evidence chain E]=The protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 4nts. [Modified residues chain I]=phosphoserine#S#21 [Chain I name]=cAMP-dependent protein kinase inhibitor alpha [Chain I source organism]=Mus musculus [Chain I UniProt accession]=P63248 [Chain I UniProt boundaries]=6-25 [Chain I UniProt coverage]=26.3% [Chain I UniRef90 accession]=UniRef90_P63248 [Chain I UniRef90 boundaries]=6-25 [Chain E name]=cAMP-dependent protein kinase catalytic subunit alpha [Chain E source organism]=Mus musculus [Chain E UniProt accession]=P05132 [Chain E UniProt boundaries]=2-351 [Chain E UniProt coverage]=99.7% [Chain E UniRef90 accession]=UniRef90_P17612 [Chain E UniRef90 boundaries]=2-351 [Related structures]=4hpu [Entry] [Accession]=DI1100096 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=Beta-catenin:unmodified E-cadherin complex [Source organism]=Mus musculus [PDB ID]=1i7x [PDB chain IDs]=D:C [PDB note]=Chains A and B was removed as chains C and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.00 [Domain]=Armadillo repeat [Type chain D]=Disordered [Evidence chain D]=The 812-884 region described in DisProt entry DP00159 and the 773-884 region described in IDEAL entry IID50003 cover 100% of the sequence present in the structure. [Type chain C]=Ordered [Evidence chain C]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain is represented by PDB ID 2bct. [Modified residues chain C]=N-methyl-lysine#K#4|N-methyl-lysine#K#9 [Chain D name]=Cadherin-1 [Chain D source organism]=Mus musculus [Chain D UniProt accession]=P09803 [Chain D UniProt boundaries]=734-884 [Chain D UniProt coverage]=17.1% [Chain D UniRef90 accession]=UniRef90_P09803 [Chain D UniRef90 boundaries]=734-884 [Chain C name]=Catenin beta-1 [Chain C source organism]=Mus musculus [Chain C UniProt accession]=Q02248 [Chain C UniProt boundaries]=134-671 [Chain C UniProt coverage]=68.9% [Chain C UniRef90 accession]=UniRef90_Q02248 [Chain C UniRef90 boundaries]=134-671 [Entry] [Accession]=DI1000291 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=Human spliceosomal protein complex p14-SF3b155 (with double selenomethionine) [Source organism]=Homo sapiens [PDB ID]=2f9d [PDB chain IDs]=P:A [PDB note]=Chains B and Q were removed as chains A and P represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=RRM [Type chain P]=Disordered [Evidence chain P]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB ID: 5ife). [Type chain A]=Ordered [Evidence chain A]=The RRM domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00076). A solved monomeric structure of a homologue is represented by PDB ID 2m52. [Modified residues chain P]=selenomethionine#M#378|selenomethionine#M#407 [Chain P name]=Splicing factor 3B subunit 1 [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=O75533 [Chain P UniProt boundaries]=373-415 [Chain P UniProt coverage]=3.3% [Chain P UniRef90 accession]=UniRef90_O75533 [Chain P UniRef90 boundaries]=373-415 [Chain A name]=Splicing factor 3B subunit 6 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9Y3B4 [Chain A UniProt boundaries]=1-125 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q9Y3B4 [Chain A UniRef90 boundaries]=1-125 [Entry] [Accession]=DI2000039 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=SDF1 (constitutively dimeric form) in complex with the CXCR4 N-terminus containing no sulfotyrosines [Source organism]=Homo sapiens [PDB ID]=2k04 [PDB chain IDs]=B:AC [PDB note]=Chain D was removed as chains A, B and C highlight the biologically relevant interaction. [PDB experimental technique]=NMR [Domain]=IL8 [Type chain B]=Disordered [Evidence chain B]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 4rws, 3oe0, 3odu, 3oe8, 3oe9, 3oe6). [Type chain A]=Ordered [Evidence chain A]=The IL8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00048). A solved monomeric structure of the domain is represented by PDB ID 1sdf. [Type chain C]=Ordered [Evidence chain C]=The IL8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00048). A solved monomeric structure of the domain is represented by PDB ID 1sdf. [Modified residues chain C]=N-methyl-lysine#K#4|N-methyl-lysine#K#9 [Chain B name]=C-X-C chemokine receptor type 4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P61073 [Chain B UniProt boundaries]=1-38 [Chain B UniProt coverage]=10.8% [Chain B UniRef90 accession]=UniRef90_P61073 [Chain B UniRef90 boundaries]=1-38 [Chain A name]=Stromal cell-derived factor 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P48061 [Chain A UniProt boundaries]=20-89 [Chain A UniProt coverage]=75.3% [Chain A UniRef90 accession]=UniRef90_P48061 [Chain A UniRef90 boundaries]=22-89 [Chain C name]=Stromal cell-derived factor 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P48061 [Chain C UniProt boundaries]=20-89 [Chain C UniProt coverage]=75.3% [Chain C UniRef90 accession]=UniRef90_P48061 [Chain C UniRef90 boundaries]=22-89 [Entry] [Accession]=DI2010017 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=SDF1 (constitutively dimeric form) in complex with the CXCR4 N-terminus containing sulfotyrosines at postitions 7, 12 and 21 [Source organism]=Pan troglodytes / Homo sapiens [PDB ID]=2k05 [PDB chain IDs]=B:AC [PDB note]=Chain D was removed as chains A, B and C highlight the biologically relevant interaction. [PDB experimental technique]=NMR [Domain]=IL8 [Type chain B]=Disordered [Evidence chain B]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 4rws, 3oe0, 3odu, 3oe8, 3oe9, 3oe6). [Type chain A]=Ordered [Evidence chain A]=The IL8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00048). A solved monomeric structure of the domain is represented by PDB ID 1sdf. [Type chain C]=Ordered [Evidence chain C]=The IL8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00048). A solved monomeric structure of the domain is represented by PDB ID 1sdf. [Modified residues chain B]=O-sulfo-L-tyrosine#Y#107|O-sulfo-L-tyrosine#Y#112|O-sulfo-L-tyrosine#Y#121 [Modified residues chain C]=N-methyl-lysine#K#4|N-methyl-lysine#K#9 [Chain B name]=C-X-C chemokine receptor type 4 [Chain B source organism]=Pan troglodytes [Chain B UniProt accession]=P61072 [Chain B UniProt boundaries]=1-38 [Chain B UniProt coverage]=10.8% [Chain B UniRef90 accession]=UniRef90_P61073 [Chain B UniRef90 boundaries]=1-38 [Chain A name]=Stromal cell-derived factor 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P48061 [Chain A UniProt boundaries]=20-89 [Chain A UniProt coverage]=75.3% [Chain A UniRef90 accession]=UniRef90_P48061 [Chain A UniRef90 boundaries]=22-89 [Chain C name]=Stromal cell-derived factor 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P48061 [Chain C UniProt boundaries]=20-89 [Chain C UniProt coverage]=75.3% [Chain C UniRef90 accession]=UniRef90_P48061 [Chain C UniRef90 boundaries]=22-89 [Entry] [Accession]=DI1000292 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=CTD-specific phosphatase Scp1 in complex with a mono-phosporylated CTD peptide of RNA polymerase II [Source organism]=Homo sapiens [PDB ID]=2ght [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=NIF [Type chain C]=Disordered [Evidence chain C]=The 1593-1960 region described in IDEAL entry IID00126 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The NIF (NLI interacting factor-like phosphatase) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03031). A solved monomeric structure of the domain is represented by PDB ID 1t9z. [Modified residues chain C]=phosphoserine#S#174 [Chain C name]=DNA-directed RNA polymerase II subunit RPB1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P24928 [Chain C UniProt boundaries]=1796-1803 [Chain C UniProt coverage]=0.4% [Chain C UniRef90 accession]=UniRef90_P24928 [Chain C UniRef90 boundaries]=1796-1803 [Chain A name]=Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9GZU7 [Chain A UniProt boundaries]=77-256 [Chain A UniProt coverage]=69% [Chain A UniRef90 accession]=UniRef90_Q9GZU7 [Chain A UniRef90 boundaries]=77-256 [Entry] [Accession]=DI1000293 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=RNA processing factor SCAF8 bound to the unmodified CTD peptide of RNA Polymerase II [Source organism]=Homo sapiens [PDB ID]=3d9o [PDB chain IDs]=Z:B [PDB note]=Chain A was removed as chains B and Z represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=CID [Type chain Z]=Disordered [Evidence chain Z]=The C terminal domain of RNA polymerase II subunit RPB1 has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 5iy7). [Type chain B]=Ordered [Evidence chain B]=The CID domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04818). A solved monomeric structure of the domain is represented by PDB ID 2diw. [Modified residues chain B]=O-sulfo-L-tyrosine#Y#107|O-sulfo-L-tyrosine#Y#112|O-sulfo-L-tyrosine#Y#121 [Chain Z name]=DNA-directed RNA polymerase II subunit RPB1 [Chain Z source organism]=Homo sapiens [Chain Z UniProt accession]=P24928 [Chain Z UniProt boundaries]=1790-1803 [Chain Z UniProt coverage]=0.7% [Chain Z UniRef90 accession]=UniRef90_P24928 [Chain Z UniRef90 boundaries]=1790-1803 [Chain B name]=Protein SCAF8 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9UPN6 [Chain B UniProt boundaries]=1-136 [Chain B UniProt coverage]=10.7% [Chain B UniRef90 accession]=UniRef90_Q9UPN6 [Chain B UniRef90 boundaries]=1-136 [Related structures]=3d9m [Entry] [Accession]=DI1000294 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=RNA processing factor SCAF8 bound to the double phosphorylated CTD peptide of RNA Polymerase II [Source organism]=Homo sapiens [PDB ID]=3d9n [PDB chain IDs]=Y:A [PDB note]=Chains Z and B were removed as chains A and Y represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.60 [Domain]=CID [Type chain Y]=Disordered [Evidence chain Y]=The C terminal domain of RNA polymerase II subunit RPB1 has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 5iy7). [Type chain A]=Ordered [Evidence chain A]=The CID domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04818). A solved monomeric structure of the domain is represented by PDB ID 2diw. [Modified residues chain Y]=phosphoserine#S#0|phosphoserine#S#2 [Chain Y name]=DNA-directed RNA polymerase II subunit RPB1 [Chain Y source organism]=Homo sapiens [Chain Y UniProt accession]=P24928 [Chain Y UniProt boundaries]=1790-1803 [Chain Y UniProt coverage]=0.7% [Chain Y UniRef90 accession]=UniRef90_P24928 [Chain Y UniRef90 boundaries]=1790-1803 [Chain A name]=Protein SCAF8 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UPN6 [Chain A UniProt boundaries]=1-145 [Chain A UniProt coverage]=11.4% [Chain A UniRef90 accession]=UniRef90_Q9UPN6 [Chain A UniRef90 boundaries]=1-138 [Entry] [Accession]=DI1000295 [Disorder status]=Inferred from motif [Kd]=3.70E-06 (PMID:21666679) [Name]=SUMO1 in complex with unmodified PML [Source organism]=Homo sapiens [PDB ID]=4wjo [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.46 [Domain]=SUMO [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains two known functional linear motifs (LIG_SUMO_SIM_anti_2, LIG_SUMO_SIM_par_1). [Type chain A]=Ordered [Evidence chain A]=The SUMO domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF11976). A solved monomeric structure of the domain is represented by PDB ID 1a5r. [Chain B name]=Protein PML [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P29590 [Chain B UniProt boundaries]=546-574 [Chain B UniProt coverage]=3.3% [Chain B UniRef90 accession]=UniRef90_P29590 [Chain B UniRef90 boundaries]=546-573 [Chain A name]=Small ubiquitin-related modifier 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63165 [Chain A UniProt boundaries]=15-97 [Chain A UniProt coverage]=82.2% [Chain A UniRef90 accession]=UniRef90_P63165 [Chain A UniRef90 boundaries]=17-97 [Entry] [Accession]=DI1000296 [Disorder status]=Inferred from motif [Kd]=3.70E-06 (PMID:21666679) [Name]=Unmodified FUNDC1 in complex with LC3BLC3B [Source organism]=Homo sapiens [PDB ID]=2n9x [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Atg8 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (YxxL motif: http://www.uniprot.org/uniprot/Q8IVP5#family_and_domains). [Type chain A]=Ordered [Evidence chain A]=The Atg8 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02991). A solved monomeric structure of the domain is represented by PDB ID 1v49. [Chain B name]=FUN14 domain-containing protein 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q8IVP5 [Chain B UniProt boundaries]=10-26 [Chain B UniProt coverage]=11% [Chain B UniRef90 accession]=UniRef90_Q8IVP5 [Chain B UniRef90 boundaries]=10-26 [Chain A name]=Microtubule-associated proteins 1A/1B light chain 3B [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9GZQ8 [Chain A UniProt boundaries]=1-120 [Chain A UniProt coverage]=96% [Chain A UniRef90 accession]=UniRef90_Q9GZQ8 [Chain A UniRef90 boundaries]=1-120 [Entry] [Accession]=DI1000297 [Disorder status]=Inferred from motif [Kd]=3.70E-06 (PMID:21666679) [Name]=T-cell Lymphoma Invasion and Metastasis-1 PDZ in complex with unmodified Syndecan1 peptide [Source organism]=Homo sapiens [PDB ID]=4gvd [PDB chain IDs]=D:A [PDB note]=Chains B and C were removed as chains A and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.85 [Domain]=PDZ [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a known functional linear motif (LIG_PDZ_Class_2). [Type chain A]=Ordered [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved monomeric structure of the domain is represented by PDB ID 3kzd. [Chain D name]=Syndecan-1 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P18827 [Chain D UniProt boundaries]=303-310 [Chain D UniProt coverage]=2.6% [Chain D UniRef90 accession]=UniRef90_P18827 [Chain D UniRef90 boundaries]=303-310 [Chain A name]=T-lymphoma invasion and metastasis-inducing protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q13009 [Chain A UniProt boundaries]=837-930 [Chain A UniProt coverage]=5.9% [Chain A UniRef90 accession]=UniRef90_Q13009 [Chain A UniRef90 boundaries]=841-928 [Entry] [Accession]=DI1000298 [Disorder status]=Inferred from motif [Kd]=3.70E-06 (PMID:21666679) [Name]=XLP protein SAP SH2 domain in complex with a phosphorylated SLAM peptide [Source organism]=Homo sapiens [PDB ID]=1d4w [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=SH2 [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_TYR_ITSM). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ab2. [Modified residues chain C]=phosphotyrosine#Y#281 [Chain C name]=Signaling lymphocytic activation molecule [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q13291 [Chain C UniProt boundaries]=276-286 [Chain C UniProt coverage]=3.3% [Chain C UniRef90 accession]=UniRef90_Q13291 [Chain C UniRef90 boundaries]=276-286 [Chain A name]=SH2 domain-containing protein 1A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O60880 [Chain A UniProt boundaries]=1-104 [Chain A UniProt coverage]=81.3% [Chain A UniRef90 accession]=UniRef90_O60880 [Chain A UniRef90 boundaries]=1-104 [Related structures]=1ka6 [Entry] [Accession]=DI1000299 [Disorder status]=Inferred from motif [Kd]=3.70E-06 (PMID:21666679) [Name]=VHS Domain of human GGA1 complexed with phosphorylated sortilin C-terminal peptide [Source organism]=Homo sapiens [PDB ID]=3g2v [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=VHS [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (TRG_LysEnd_GGAAcLL_1). [Type chain A]=Ordered [Evidence chain A]=The VHS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00790). A solved monomeric structure of the domain is represented by PDB ID 1jwf. [Modified residues chain C]=phosphoserine#S#6 [Chain C name]=Sortilin [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q99523 [Chain C UniProt boundaries]=819-831 [Chain C UniProt coverage]=1.6% [Chain C UniRef90 accession]=UniRef90_Q99523 [Chain C UniRef90 boundaries]=819-831 [Chain A name]=ADP-ribosylation factor-binding protein GGA1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UJY5 [Chain A UniProt boundaries]=1-147 [Chain A UniProt coverage]=23% [Chain A UniRef90 accession]=UniRef90_Q9UJY5 [Chain A UniRef90 boundaries]=1-147 [Entry] [Accession]=DI1000300 [Disorder status]=Inferred from motif [Kd]=3.70E-06 (PMID:21666679) [Name]=VHS Domain of human GGA1 complexed with unmodified beta-secretase C-terminal peptide [Source organism]=Homo sapiens [PDB ID]=1ujj [PDB chain IDs]=C:A [PDB note]=Chain B was removed as chains A and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=VHS [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (TRG_LysEnd_APsAcLL_1). [Type chain A]=Ordered [Evidence chain A]=The VHS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00790). A solved monomeric structure of the domain is represented by PDB ID 1jwf. [Chain C name]=Beta-secretase 1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P56817 [Chain C UniProt boundaries]=490-501 [Chain C UniProt coverage]=2.4% [Chain C UniRef90 accession]=UniRef90_P56817 [Chain C UniRef90 boundaries]=490-501 [Chain A name]=ADP-ribosylation factor-binding protein GGA1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UJY5 [Chain A UniProt boundaries]=1-147 [Chain A UniProt coverage]=23% [Chain A UniRef90 accession]=UniRef90_Q9UJY5 [Chain A UniRef90 boundaries]=1-147 [Entry] [Accession]=DI1010088 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=Vav1 SH2 domain complexed with a Syk-derived singly phosphorylated peptide [Source organism]=Mus musculus / Homo sapiens [PDB ID]=2mc1 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The interacting region of the protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structure (PDB ID: 4wnm). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2crh. [Modified residues chain B]=phosphotyrosine#Y#346 [Chain B name]=Tyrosine-protein kinase SYK [Chain B source organism]=Mus musculus [Chain B UniProt accession]=P48025 [Chain B UniProt boundaries]=338-350 [Chain B UniProt coverage]=2.1% [Chain B UniRef90 accession]=UniRef90_P48025 [Chain B UniRef90 boundaries]=338-350 [Chain A name]=Proto-oncogene vav [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P15498 [Chain A UniProt boundaries]=661-767 [Chain A UniProt coverage]=12.7% [Chain A UniRef90 accession]=UniRef90_P15498 [Chain A UniRef90 boundaries]=661-767 [Entry] [Accession]=DI2000040 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=14-3-3 zeta in complex with phosphorylated histone H3 tail [Source organism]=Homo sapiens [PDB ID]=2c1n [PDB chain IDs]=C:AB [PDB note]=Chain E was removed as chains A, B and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=14-3-3 [Type chain C]=Disordered [Evidence chain C]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered component [Evidence chain A]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 3rdh. [Type chain B]=Ordered component [Evidence chain B]=The 14-3-3 domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF00244). A solved structure of the domain dimer without bound ligands is represented by PDB ID 3rdh. [Modified residues chain C]=phosphoserine#S#10 [Modified residues chain B]=phosphotyrosine#Y#346 [Chain C name]=Histone H3.1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P68431 [Chain C UniProt boundaries]=8-15 [Chain C UniProt coverage]=5.9% [Chain C UniRef90 accession]=UniRef90_P68431 [Chain C UniRef90 boundaries]=8-15 [Chain A name]=14-3-3 protein zeta/delta [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P63104 [Chain A UniProt boundaries]=1-245 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P63104 [Chain A UniRef90 boundaries]=1-245 [Chain B name]=14-3-3 protein zeta/delta [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P63104 [Chain B UniProt boundaries]=1-245 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P63104 [Chain B UniRef90 boundaries]=1-245 [Entry] [Accession]=DI1100097 [Disorder status]=Inferred from motif [Kd]=3.70E-06 (PMID:21666679) [Name]=Keap1 in complex with phosphorylated sequestosome-1/p62 peptide [Source organism]=Mus musculus [PDB ID]=3wdz [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.60 [Domain]=Kelch [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (DEG_Kelch_Keap1_1). [Type chain A]=Ordered [Evidence chain A]=The Kelch domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01344). A solved monomeric structure of the domain is represented by PDB ID 1x2j. [Modified residues chain B]=phosphoserine#S#351 [Chain B name]=Sequestosome-1 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=Q64337 [Chain B UniProt boundaries]=346-359 [Chain B UniProt coverage]=3.2% [Chain B UniRef90 accession]=UniRef90_Q13501 [Chain B UniRef90 boundaries]=346-359 [Chain A name]=Kelch-like ECH-associated protein 1 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q9Z2X8 [Chain A UniProt boundaries]=321-609 [Chain A UniProt coverage]=46.3% [Chain A UniRef90 accession]=UniRef90_Q14145 [Chain A UniRef90 boundaries]=321-609 [Entry] [Accession]=DI1020037 [Disorder status]=Confirmed [Kd]=3.70E-06 (PMID:21666679) [Name]=Sir2 in complex with an acetylated p53 peptide [Source organism]=Homo sapiens / Thermotoga maritima [PDB ID]=2h2d [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=Sirtuin [Type chain B]=Disordered [Evidence chain B]=The 320-393 region described in DisProt entry DP00086 and the 364-389 region described in IDEAL entry IID00015 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The sirtuin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02146). A solved monomeric structure of the domain is represented by PDB ID 2h2i. [Modified residues chain B]=N(6)-acetyllysine#K#11 [Chain B name]=Cellular tumor antigen p53 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P04637 [Chain B UniProt boundaries]=372-389 [Chain B UniProt coverage]=4.6% [Chain B UniRef90 accession]=UniRef90_P04637 [Chain B UniRef90 boundaries]=372-389 [Chain A name]=NAD-dependent protein deacetylase [Chain A source organism]=Thermotoga maritima [Chain A UniProt accession]=Q9WYW0 [Chain A UniProt boundaries]=1-246 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q9WYW0 [Chain A UniRef90 boundaries]=1-246 [Related structures]=2h4h,2h4f,1yc5,4buz,3pdh [Entry] [Accession]=DI1000301 [Disorder status]=Inferred from motif [Kd]=3.70E-06 (PMID:21666679) [Name]=PP2A B56gamma in complex with a phosphorylated BubR1 peptide [Source organism]=Homo sapiens [PDB ID]=5k6s [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.79 [Domain]=B56 subunit of PP2A [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (DOC_PP2A_B56_1). [Type chain A]=Ordered [Evidence chain A]=The B56 subunit of PP2A involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01603). A solved monomeric structure of the domain is represented by PDB ID 2jak. [Modified residues chain B]=phosphoserine#S#670 [Chain B name]=Mitotic checkpoint serine/threonine-protein kinase BUB1 beta [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O60566 [Chain B UniProt boundaries]=663-681 [Chain B UniProt coverage]=1.8% [Chain B UniRef90 accession]=UniRef90_O60566 [Chain B UniRef90 boundaries]=663-681 [Chain A name]=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q13362 [Chain A UniProt boundaries]=31-380 [Chain A UniProt coverage]=66.8% [Chain A UniRef90 accession]=UniRef90_Q13362 [Chain A UniRef90 boundaries]=31-380 [Related structures]=5swf [Entry] [Accession]=DI1000302 [Disorder status]=Confirmed [Kd]=1.94E-05 (PMID:27545619) [Name]=AF9 YEATS domain in complex with histone H3.1 crotonylation at K18 [Source organism]=Homo sapiens [PDB ID]=2ndg [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=YEATS [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The YEATS domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03366). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3rls. [Modified residues chain B]=N-6-crotonyl-L-lysine#K#218 [Chain B name]=Histone H3.1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68431 [Chain B UniProt boundaries]=13-25 [Chain B UniProt coverage]=9.6% [Chain B UniRef90 accession]=UniRef90_P68431 [Chain B UniRef90 boundaries]=13-25 [Chain A name]=Protein AF-9 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P42568 [Chain A UniProt boundaries]=1-138 [Chain A UniProt coverage]=24.3% [Chain A UniRef90 accession]=UniRef90_P42568 [Chain A UniRef90 boundaries]=1-138 [Related structures]=5hjd [Entry] [Accession]=DI1000303 [Disorder status]=Inferred from motif [Kd]=8.60E-06 [Name]=WDR5 in complex with the WDR5-interacting motif of KANSL2 [Source organism]=Homo sapiens [PDB ID]=4cy2 [PDB chain IDs]=C:A [PDB note]=Chain D was removed as chains C and A highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=WD40 [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_WD40_WDR5_WIN_1). [Type chain A]=Ordered [Evidence chain A]=The WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00400). A solved monomeric structure of the domain is represented by PDB ID 2gnq. [Chain C name]=KAT8 regulatory NSL complex subunit 2 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q9H9L4 [Chain C UniProt boundaries]=406-417 [Chain C UniProt coverage]=2.4% [Chain C UniRef90 accession]=UniRef90_Q9H9L4 [Chain C UniRef90 boundaries]=406-417 [Chain A name]=WD repeat-containing protein 5 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P61964 [Chain A UniProt boundaries]=23-334 [Chain A UniProt coverage]=93.4% [Chain A UniRef90 accession]=UniRef90_P61964 [Chain A UniRef90 boundaries]=23-334 [Entry] [Accession]=DI1100098 [Disorder status]=Inferred from motif [Kd]=7.30E-06 [Name]=NSL2 peptide bound to WDS [Source organism]=Drosophila melanogaster [PDB ID]=4cy5 [PDB chain IDs]=C:A [PDB note]=Chain D was removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=WD40 [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_WD40_WDR5_WIN_2). [Type chain A]=Ordered [Evidence chain A]=The WD40 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00400). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2gnq. [Chain C name]=Dim gamma-tubulin 1, isoform A [Chain C source organism]=Drosophila melanogaster [Chain C UniProt accession]=Q9VAF4 [Chain C UniProt boundaries]=155-166 [Chain C UniProt coverage]=2.5% [Chain C UniRef90 accession]=UniRef90_Q9VAF4 [Chain C UniRef90 boundaries]=155-166 [Chain A name]=Protein will die slowly [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=Q9V3J8 [Chain A UniProt boundaries]=50-361 [Chain A UniProt coverage]=86.4% [Chain A UniRef90 accession]=UniRef90_Q9V3J8 [Chain A UniRef90 boundaries]=50-361 [Entry] [Accession]=DI1000304 [Disorder status]=Confirmed [Kd]=9.20E-06 [Name]=Androgen receptor ligand binding domain in complex with its N-terminal FxxLF motif-containing peptide [Source organism]=Homo sapiens [PDB ID]=1xow [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=Nuclear hormone receptor [Type chain B]=Disordered [Evidence chain B]=The FxxLF motif is a specialized, high-affinity motif that binds AR-LBD in the same manner (PMID:15525515), but out-competes consensus LxxLL motifs of coactivators (LIG_NRBOX). The N-terminal AF1 regions of nuclear receptors are usually disordered (PMID:17464357), including the androgen receptor N-terminal that exists in a molten globule-like collapsed disordered conformation (PMID:18284208). [Type chain A]=Ordered [Evidence chain A]=The nuclear hormone receptor domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form. A solved structure of the domain dimer without bound ligands is represented by PDB ID 1g50. [Chain B name]=Androgen receptor [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P10275 [Chain B UniProt boundaries]=20-30 [Chain B UniProt coverage]=1.2% [Chain B UniRef90 accession]=UniRef90_P10275 [Chain B UniRef90 boundaries]=20-30 [Chain A name]=Androgen receptor [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P10275 [Chain A UniProt boundaries]=672-920 [Chain A UniProt coverage]=27.1% [Chain A UniRef90 accession]=UniRef90_P10275 [Chain A UniRef90 boundaries]=672-920 [Related structures]=2q7i,2q7k,3v49,3v4a,5cj6 [Entry] [Accession]=DI2000041 [Disorder status]=Confirmed [Kd]=4.80E-06 [Name]=BIR domain of BIRC5 in complex with T3 phosphorylated H3.1 peptide (residues 1-15) [Source organism]=Homo sapiens [PDB ID]=3uig [PDB chain IDs]=P:AB [PDB note]=Chain Q was removed as chains A, B and P highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=BIR [Type chain P]=Disordered [Evidence chain P]=The 1-60 region described in IDEAL entry IID00062 covers 100% of the sequence present in the structure. [Type chain A]=Ordered component [Evidence chain A]=The BIR domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00653). A solved structure of the BIR dimer of survivin is represented by PDB ID 1e31. [Type chain B]=Ordered component [Evidence chain B]=The BIR domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00653). A solved structure of the BIR dimer of survivin is represented by PDB ID 1e31. [Modified residues chain P]=phosphothreonine#T#3 [Chain P name]=Histone H3.1 [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=P68431 [Chain P UniProt boundaries]=2-16 [Chain P UniProt coverage]=11% [Chain P UniRef90 accession]=UniRef90_P68431 [Chain P UniRef90 boundaries]=2-16 [Chain A name]=Baculoviral IAP repeat-containing protein 5 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O15392 [Chain A UniProt boundaries]=1-142 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_O15392 [Chain A UniRef90 boundaries]=1-142 [Chain B name]=Baculoviral IAP repeat-containing protein 5 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O15392 [Chain B UniProt boundaries]=1-142 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_O15392 [Chain B UniRef90 boundaries]=1-142 [Related structures]=3uec,3ued,4a0j,4a0n [Entry] [Accession]=DI1100099 [Disorder status]=Inferred from motif [Kd]=2.40E-09 [Name]=Mouse importin alpha in complex with Cbp80 cNLS [Source organism]=Mus musculus [PDB ID]=3ukz [PDB chain IDs]=C:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=Armadillo repeat [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (TRG_NLS_Bipartite_1). [Type chain B]=Ordered [Evidence chain B]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ial. [Chain C name]=Nuclear cap-binding protein subunit 1 [Chain C source organism]=Mus musculus [Chain C UniProt accession]=Q3UYV9 [Chain C UniProt boundaries]=1-23 [Chain C UniProt coverage]=2.9% [Chain C UniRef90 accession]=UniRef90_Q09161 [Chain C UniRef90 boundaries]=1-23 [Chain B name]=Importin subunit alpha-1 [Chain B source organism]=Mus musculus [Chain B UniProt accession]=P52293 [Chain B UniProt boundaries]=70-529 [Chain B UniProt coverage]=87% [Chain B UniRef90 accession]=UniRef90_P52293 [Chain B UniRef90 boundaries]=70-529 [Related structures]=3uky,3ul0 [Entry] [Accession]=DI1010089 [Disorder status]=Confirmed [Kd]=2.40E-09 [Name]=Plakoglobin in complex with E-cadherin C-terminal region [Source organism]=Mus musculus / Homo sapiens [PDB ID]=3ifq [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=Armadillo repeat [Type chain C]=Disordered [Evidence chain C]=The 812-884 region described in DisProt entry DP00159 covers 68% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The armadillo repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00514). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ial. [Modified residues chain C]=phosphoserine#S#684|phosphoserine#S#686|phosphoserine#S#692 [Chain C name]=Cadherin-1 [Chain C source organism]=Mus musculus [Chain C UniProt accession]=P09803 [Chain C UniProt boundaries]=778-884 [Chain C UniProt coverage]=12.1% [Chain C UniRef90 accession]=UniRef90_P09803 [Chain C UniRef90 boundaries]=778-884 [Chain A name]=Junction plakoglobin [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P14923 [Chain A UniProt boundaries]=124-676 [Chain A UniProt coverage]=74.2% [Chain A UniRef90 accession]=UniRef90_P14923 [Chain A UniRef90 boundaries]=124-676 [Entry] [Accession]=DI1000305 [Disorder status]=Inferred from motif [Kd]=1.80E-04 [Name]=Autoregulatory interaction between GAE domain of GGA1 and its hinge region WNSF motif [Source organism]=Homo sapiens [PDB ID]=2dwx [PDB chain IDs]=P:A [PDB note]=Chains B, C, D and Q were removed as chains A and P highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.55 [Domain]=Adaptin C-terminal domain [Type chain P]=Disordered [Evidence chain P]=The WNSF motif is a specialized, high-affinity motif of GGA1 that binds in a similar manner (PMID:17506864) and competes with the consensus acidic phenylalanine motifs of endocytic accessory proteins (LIG_AP_GAE_1). These motifs usually reside in the disordered regions of endocytic accessory proteins (PMID:21536832). [Type chain A]=Ordered [Evidence chain A]=The adaptin C-terminal or gamma-adaptin ear (GAE) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02883/PF02296). A solved monomeric structure of the domain is represented by PDB ID 2dwy. [Chain P name]=ADP-ribosylation factor-binding protein GGA1 [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=Q9UJY5 [Chain P UniProt boundaries]=376-388 [Chain P UniProt coverage]=2% [Chain P UniRef90 accession]=UniRef90_Q9UJY5 [Chain P UniRef90 boundaries]=376-388 [Chain A name]=ADP-ribosylation factor-binding protein GGA1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UJY5 [Chain A UniProt boundaries]=507-639 [Chain A UniProt coverage]=20.8% [Chain A UniRef90 accession]=UniRef90_Q9UJY5 [Chain A UniRef90 boundaries]=507-639 [Entry] [Accession]=DI1000306 [Disorder status]=Inferred from homology [Kd]=1.80E-04 [Name]=human RAC3 in complex with the CRIB domain of human p21-activated kinase 4 (PAK4) [Source organism]=Homo sapiens [PDB ID]=2ov2 [PDB chain IDs]=I:A [PDB note]=Chains B, C, D, E, F, G, H, J, K, L, M, N, O and P were removed as chains A and I highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=Ras [Type chain I]=Disordered [Evidence chain I]=The interacting region of PAK4 (CRIB motif - PF00786) has been shown to be intrinsically disordered in homologous proteins (PMID:9660763 and PMID:15821030). The 65-123 region described in IDEAL entry IID50053 covers 100% of the binding sequence in a homologous protein. [Type chain A]=Ordered [Evidence chain A]=The ras domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00071). A solved monomeric structure of the domain is represented by PDB ID 1aje. [Chain I name]=Serine/threonine-protein kinase PAK 4 [Chain I source organism]=Homo sapiens [Chain I UniProt accession]=O96013 [Chain I UniProt boundaries]=10-44 [Chain I UniProt coverage]=5.9% [Chain I UniRef90 accession]=UniRef90_O96013 [Chain I UniRef90 boundaries]=10-44 [Chain A name]=Ras-related C3 botulinum toxin substrate 3 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P60763 [Chain A UniProt boundaries]=1-177 [Chain A UniProt coverage]=92.2% [Chain A UniRef90 accession]=UniRef90_P60763 [Chain A UniRef90 boundaries]=1-177 [Entry] [Accession]=DI1000307 [Disorder status]=Inferred from motif [Kd]=1.80E-04 [Name]=EIF4E in complex with EIF4G1 peptide [Source organism]=Homo sapiens [PDB ID]=2w97 [PDB chain IDs]=E:A [PDB note]=Chains B and F were removed as chains A and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.29 [Domain]=IF4E [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (LIG_eIF4E_1). [Type chain A]=Ordered [Evidence chain A]=The IF4E domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01652). A solved monomeric structure of the domain is represented by PDB ID 1ap8. [Chain E name]=Eukaryotic translation initiation factor 4 gamma 1 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=Q04637 [Chain E UniProt boundaries]=609-622 [Chain E UniProt coverage]=0.9% [Chain E UniRef90 accession]=UniRef90_Q04637 [Chain E UniRef90 boundaries]=609-622 [Chain A name]=Eukaryotic translation initiation factor 4E [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P06730 [Chain A UniProt boundaries]=1-217 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P06730 [Chain A UniRef90 boundaries]=1-217 [Related structures]=4aza,5ehc,5ei3,5eir,5t46 [Entry] [Accession]=DI1000308 [Disorder status]=Inferred from motif [Kd]=2.24E-06 [Name]=VTA1 MIT domain in complex with IST1 MIT-interacting motif [Source organism]=Homo sapiens [PDB ID]=4u7e [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.60 [Domain]=MIT [Type chain A]=Disordered [Evidence chain A]=The protein region involved in the interaction contains a known functional linear motif (MIT-interacting motif - http://www.uniprot.org/uniprot/P53990#family_and_domains). [Type chain B]=Ordered [Evidence chain B]=The MIT domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04212). A solved monomeric structure of the domain is represented by PDB ID 2dl1. [Chain A name]=IST1 homolog [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P53990 [Chain A UniProt boundaries]=341-364 [Chain A UniProt coverage]=6.6% [Chain A UniRef90 accession]=UniRef90_P53990 [Chain A UniRef90 boundaries]=341-364 [Chain B name]=Vacuolar protein sorting-associated protein VTA1 homolog [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9NP79 [Chain B UniProt boundaries]=1-162 [Chain B UniProt coverage]=52.8% [Chain B UniRef90 accession]=UniRef90_Q9NP79 [Chain B UniRef90 boundaries]=1-162 [Entry] [Accession]=DI1020038 [Disorder status]=Confirmed [Kd]=2.24E-06 [Name]=Clostridium botulinum neurotoxin serotype F catalytic domain in complex with VAMP 22-58/Gln58D-cysteine peptide inhibitor [Source organism]=Homo sapiens / Clostridium botulinum [PDB ID]=3fie [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=Peptidase_M27 [Type chain C]=Disordered [Evidence chain C]=The 27-31 and 40-67 regions described in DisProt entry DP00069 cover 66% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=Peptidase_M27 domain of neurotoxin BoNT/A is known to adopt a stable structure in isolation (see Pfam domain PF01742). A solved monomeric structure of the domain is represented by PDB ID 4ej5. [Modified residues chain C]=D-cysteine#C#58 [Chain C name]=Vesicle-associated membrane protein 2 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P63027 [Chain C UniProt boundaries]=22-57 [Chain C UniProt coverage]=31% [Chain C UniRef90 accession]=UniRef90_P63027 [Chain C UniRef90 boundaries]=22-57 [Chain A name]=Botulinum neurotoxin type F [Chain A source organism]=Clostridium botulinum [Chain A UniProt accession]=P30996 [Chain A UniProt boundaries]=1-419 [Chain A UniProt coverage]=32.9% [Chain A UniRef90 accession]=UniRef90_P30996 [Chain A UniRef90 boundaries]=1-419 [Related structures]=3fii [Entry] [Accession]=DI1200008 [Disorder status]=Confirmed [Kd]=2.24E-06 [Name]=E. coli PNPase core bound to RNase E C-terminal peptide [Source organism]=Escherichia coli O139:H28 [PDB ID]=3gme [PDB chain IDs]=D:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=PNPase core [Type chain D]=Disordered [Evidence chain D]=The 498-1061 region described in DisProt entry DP00207 cover 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The polyribonucleotide nucleotidyltransferase core is known to adopt a stable structure in isolation (see Pfam domains PF01138, PF03725 and PF03726). A solved monomeric structure of PNPase core is represented by PDB ID 3gll. [Chain D name]=Ribonuclease E [Chain D source organism]=Escherichia coli O139:H28 [Chain D UniProt accession]=A7ZKI9 [Chain D UniProt boundaries]=1021-1061 [Chain D UniProt coverage]=3.9% [Chain D UniRef90 accession]=UniRef90_P21513 [Chain D UniRef90 boundaries]=1021-1061 [Chain A name]=Polyribonucleotide nucleotidyltransferase [Chain A source organism]=Escherichia coli O139:H28 [Chain A UniProt accession]=A7ZS61 [Chain A UniProt boundaries]=1-549 [Chain A UniProt coverage]=77.2% [Chain A UniRef90 accession]=UniRef90_A9MP39 [Chain A UniRef90 boundaries]=1-549 [Related structures]=3gcm,3h1c [Entry] [Accession]=DI1000309 [Disorder status]=Inferred from motif [Kd]=2.24E-06 [Name]=Androgen receptor ligand binding domain in complex with co-regulator peptide [Source organism]=Homo sapiens [PDB ID]=4oed [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.79 [Domain]=Nuclear hormone receptor [Type chain B]=Disordered [Evidence chain B]=The region of BUD31 homolog involved in the interaction contains a known Fxx(F/H/L/W/Y)Y motif that is a specialized LxxLL-like motif that binds AR-LBD in the same manner (PMID:25091737) as consensus LxxLL motifs of coactivators (LIG_NRBOX). [Type chain A]=Ordered [Evidence chain A]=The nuclear hormone receptor domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form. A solved structure of the domain dimer without bound ligands is represented by PDB ID 1g50. [Chain B name]=Protein BUD31 homolog [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P41223 [Chain B UniProt boundaries]=56-70 [Chain B UniProt coverage]=10.4% [Chain B UniRef90 accession]=UniRef90_P41223 [Chain B UniRef90 boundaries]=56-70 [Chain A name]=Androgen receptor [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P10275 [Chain A UniProt boundaries]=671-920 [Chain A UniProt coverage]=27.2% [Chain A UniRef90 accession]=UniRef90_P10275 [Chain A UniRef90 boundaries]=671-920 [Related structures]=4oh6,4okb [Entry] [Accession]=DI1000310 [Disorder status]=Inferred from motif [Kd]=2.24E-06 [Name]=Androgen receptor ligand binding domain in complex with Uba3 LxxLL motif-containing peptide [Source organism]=Homo sapiens [PDB ID]=5jjm [PDB chain IDs]=G:A [PDB note]=Chains B, C, D, F, H, I, J, K, L and M were removed as chains A and G highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.15 [Domain]=Nuclear hormone receptor [Type chain G]=Disordered [Evidence chain G]=The protein region involved in the interaction contains a known functional linear motif (LIG_NRBOX). [Type chain A]=Ordered [Evidence chain A]=The nuclear hormone receptor domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00104). A solved structure of the monomeric domain is represented by PDB ID 4ql8. [Chain G name]=NEDD8-activating enzyme E1 catalytic subunit [Chain G source organism]=Homo sapiens [Chain G UniProt accession]=Q8TBC4 [Chain G UniProt boundaries]=62-69 [Chain G UniProt coverage]=1.7% [Chain G UniRef90 accession]=UniRef90_Q8TBC4 [Chain G UniRef90 boundaries]=62-69 [Chain A name]=Androgen receptor [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P10275 [Chain A UniProt boundaries]=669-920 [Chain A UniProt coverage]=27.4% [Chain A UniRef90 accession]=UniRef90_P10275 [Chain A UniRef90 boundaries]=669-920 [Entry] [Accession]=DI1000311 [Disorder status]=Inferred from motif [Kd]=3.10E-06 [Name]=Androgen receptor ligand binding domain in complex with the third LxxLL motif of steroid receptor coactivator-2 [Source organism]=Homo sapiens [PDB ID]=2ao6 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.89 [Domain]=Nuclear hormone receptor [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_NRBOX). [Type chain A]=Ordered [Evidence chain A]=The nuclear hormone receptor domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00104). A solved structure of the monomeric domain is represented by PDB ID 4ql8. [Chain B name]=Nuclear receptor coactivator 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q15596 [Chain B UniProt boundaries]=740-753 [Chain B UniProt coverage]=1% [Chain B UniRef90 accession]=UniRef90_Q61026 [Chain B UniRef90 boundaries]=740-753 [Chain A name]=Androgen receptor [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P10275 [Chain A UniProt boundaries]=672-920 [Chain A UniProt coverage]=27.1% [Chain A UniRef90 accession]=UniRef90_P10275 [Chain A UniRef90 boundaries]=672-920 [Related structures]=1t63,2q7j,2q7l [Entry] [Accession]=DI1000312 [Disorder status]=Confirmed [Kd]=3.10E-06 [Name]=PHD2 domain in complex with HIF1-alpha C-terminal oxygen-dependent degradation (CODD) peptide [Source organism]=Homo sapiens [PDB ID]=3hqr [PDB chain IDs]=S:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Prolyl hydroxylase 2 [Type chain S]=Disordered [Evidence chain S]=The 403-698 region described in DisProt entry DP00262 and in IDEAL entry IID00085 cover 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (DEG_ODPH_VHL_1). [Type chain A]=Ordered [Evidence chain A]=The PHD2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13640). A solved structure of the domain is represented by PDB ID 5l9r. [Chain S name]=Hypoxia-inducible factor 1-alpha [Chain S source organism]=Homo sapiens [Chain S UniProt accession]=Q16665 [Chain S UniProt boundaries]=558-574 [Chain S UniProt coverage]=2.1% [Chain S UniRef90 accession]=UniRef90_Q16665 [Chain S UniRef90 boundaries]=558-574 [Chain A name]=Egl nine homolog 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9GZT9 [Chain A UniProt boundaries]=181-426 [Chain A UniProt coverage]=57.7% [Chain A UniRef90 accession]=UniRef90_Q9GZT9 [Chain A UniRef90 boundaries]=181-426 [Related structures]=5l9b,3hqu [Entry] [Accession]=DI1000313 [Disorder status]=Inferred from motif [Kd]=7.10E-07 [Name]=Androgen receptor ligand binding domain in complex with the first LxxLL motif of steroid receptor coactivator-3 [Source organism]=Homo sapiens [PDB ID]=3l3x [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.55 [Domain]=Nuclear hormone receptor [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_NRBOX). [Type chain A]=Ordered [Evidence chain A]=The nuclear hormone receptor domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00104). A solved structure of the monomeric domain is represented by PDB ID 4ql8. [Chain B name]=Nuclear receptor coactivator 3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9Y6Q9 [Chain B UniProt boundaries]=618-629 [Chain B UniProt coverage]=0.8% [Chain B UniRef90 accession]=UniRef90_Q9Y6Q9 [Chain B UniRef90 boundaries]=618-629 [Chain A name]=Androgen receptor [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P10275 [Chain A UniProt boundaries]=671-919 [Chain A UniProt coverage]=27.1% [Chain A UniRef90 accession]=UniRef90_P10275 [Chain A UniRef90 boundaries]=671-919 [Entry] [Accession]=DI1000314 [Disorder status]=Inferred from motif [Kd]=1.36E-05 [Name]=Androgen receptor ligand binding domain in complex with the third LxxLL motif of steroid receptor coactivator-3 [Source organism]=Homo sapiens [PDB ID]=3l3z [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=Nuclear hormone receptor [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_NRBOX). [Type chain A]=Ordered [Evidence chain A]=The nuclear hormone receptor domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00104). A solved structure of the monomeric domain is represented by PDB ID 4ql8. [Chain B name]=Nuclear receptor coactivator 3 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9Y6Q9 [Chain B UniProt boundaries]=735-746 [Chain B UniProt coverage]=0.8% [Chain B UniRef90 accession]=UniRef90_Q9Y6Q9 [Chain B UniRef90 boundaries]=735-746 [Chain A name]=Androgen receptor [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P10275 [Chain A UniProt boundaries]=671-919 [Chain A UniProt coverage]=27.1% [Chain A UniRef90 accession]=UniRef90_P10275 [Chain A UniRef90 boundaries]=671-919 [Entry] [Accession]=DI1000315 [Disorder status]=Inferred from motif [Kd]=1.27E-06 [Name]=Androgen receptor ligand binding domain in complex with an FxxLF motif of ARA70 coactivator [Source organism]=Homo sapiens [PDB ID]=1t5z [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=Nuclear hormone receptor [Type chain B]=Disordered [Evidence chain B]=The FxxLF motif is a specialized, high-affinity motif that binds AR-LBD in the same manner (PMID:15525515), but out-competes consensus LxxLL motifs of other coactivators (LIG_NRBOX). [Type chain A]=Ordered [Evidence chain A]=The nuclear hormone receptor domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00104). A solved structure of the monomeric domain is represented by PDB ID 4ql8. [Chain B name]=Nuclear receptor coactivator 4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q13772 [Chain B UniProt boundaries]=322-336 [Chain B UniProt coverage]=2.4% [Chain B UniRef90 accession]=UniRef90_Q13772 [Chain B UniRef90 boundaries]=322-336 [Chain A name]=Androgen receptor [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P10275 [Chain A UniProt boundaries]=670-920 [Chain A UniProt coverage]=27.3% [Chain A UniRef90 accession]=UniRef90_P10275 [Chain A UniRef90 boundaries]=670-920 [Entry] [Accession]=DI1200009 [Disorder status]=Confirmed [Kd]=2.00E-06 [Name]=OmpF in complex with colicin peptide OBS1 [Source organism]=Escherichia coli [PDB ID]=3o0e [PDB chain IDs]=L:A [PDB note]=Chains B, C, D, F, M, N, O, P and Q were removed as chains A and L highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.01 [Domain]=Porin [Type chain L]=Disordered [Evidence chain L]=The 1-83 region described in DisProt entry DP00342 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The porin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00267). A solved structure of the domain without bound ligands is represented by PDB ID 1pho. [Chain L name]=Colicin-E9 [Chain L source organism]=Escherichia coli [Chain L UniProt accession]=P09883 [Chain L UniProt boundaries]=2-18 [Chain L UniProt coverage]=2.9% [Chain L UniRef90 accession]=UniRef90_P09883 [Chain L UniRef90 boundaries]=2-18 [Chain A name]=Outer membrane protein F [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=P02931 [Chain A UniProt boundaries]=23-362 [Chain A UniProt coverage]=93.9% [Chain A UniRef90 accession]=UniRef90_P02931 [Chain A UniRef90 boundaries]=23-362 [Entry] [Accession]=DI2020004 [Disorder status]=Confirmed [Kd]=2.00E-06 [Name]=human P-TEFb (Cyclin T1:CDK9) in complex with HIV-1 Tat [Source organism]=Human immunodeficiency virus type 1 group M subtype B / Homo sapiens [PDB ID]=3mi9 [PDB chain IDs]=C:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=Cyclin T1:Cdk9 [Type chain C]=Disordered [Evidence chain C]=The 1-101 region described in DisProt entry DP01087 covers 100% of the sequence present in the structure. [Type chain A]=Ordered component [Evidence chain A]=The cyclin T1:Cdk9 complex involved in the interaction is known to form an ordered dimer, represented by PDB ID 3blh. [Type chain B]=Ordered component [Evidence chain B]=The cyclin T1:Cdk9 complex involved in the interaction is known to form an ordered dimer, represented by PDB ID 3blh. [Chain C name]=Protein Tat [Chain C source organism]=Human immunodeficiency virus type 1 group M subtype B [Chain C UniProt accession]=P04608 [Chain C UniProt boundaries]=1-86 [Chain C UniProt coverage]=100% [Chain C UniRef90 accession]=UniRef90_P04608 [Chain C UniRef90 boundaries]=1-86 [Chain A name]=Cyclin-dependent kinase 9 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P50750 [Chain A UniProt boundaries]=1-345 [Chain A UniProt coverage]=92.7% [Chain A UniRef90 accession]=UniRef90_P50750 [Chain A UniRef90 boundaries]=1-345 [Chain B name]=Cyclin-T1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O60563 [Chain B UniProt boundaries]=1-266 [Chain B UniProt coverage]=36.6% [Chain B UniRef90 accession]=UniRef90_O60563 [Chain B UniRef90 boundaries]=1-266 [Related structures]=3mia,4or5 [Entry] [Accession]=DI1020039 [Disorder status]=Inferred from motif [Kd]=2.00E-06 [Name]=AP1 G2 subunit GAE domain in complex with hepatitis B virus PreS1 site1 peptide [Source organism]=Hepatitis B virus / Homo sapiens [PDB ID]=3zhf [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=Adaptin C-terminal domain [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_AP_GAE_1). [Type chain A]=Ordered [Evidence chain A]=The adaptin C-terminal or gamma-adaptin ear (GAE) domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF02883/PF02296). A solved monomeric structure of the domain is represented by PDB ID 4bcx. [Chain B name]=Large envelope protein [Chain B source organism]=Hepatitis B virus [Chain B UniProt accession]=Q67953 [Chain B UniProt boundaries]=85-91 [Chain B UniProt coverage]=1.6% [Chain B UniRef90 accession]=UniRef90_P03141 [Chain B UniRef90 boundaries]=85-91 [Chain A name]=AP-1 complex subunit gamma-like 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O75843 [Chain A UniProt boundaries]=662-785 [Chain A UniProt coverage]=15.8% [Chain A UniRef90 accession]=UniRef90_O75843 [Chain A UniRef90 boundaries]=669-785 [Entry] [Accession]=DI3000012 [Disorder status]=Inferred from motif [Kd]=2.00E-06 [Name]=p15 PIP-box peptide complexed with human PCNA [Source organism]=Homo sapiens [PDB ID]=4d2g [PDB chain IDs]=D:ABC [PDB note]=Chain E was removed as chains A, B, C and D highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.65 [Domain]=PCNA [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a known functional linear motif (LIG_PCNA_PIPBox_1). [Type chain A]=Ordered component [Evidence chain A]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60. [Type chain B]=Ordered component [Evidence chain B]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60. [Type chain C]=Ordered component [Evidence chain C]=PCNA forms an ordered homotrimeric ring-shaped complex which encircles duplex DNA, providing a DNA-bound platform for binding substrate proteins (PMID:8001157). A solved structure of the PCNA homotrimer without bound ligands is represented by PDB ID 1w60. [Chain D name]=PCNA-associated factor [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=Q15004 [Chain D UniProt boundaries]=52-69 [Chain D UniProt coverage]=16.2% [Chain D UniRef90 accession]=UniRef90_Q15004 [Chain D UniRef90 boundaries]=52-69 [Chain A name]=Proliferating cell nuclear antigen [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P12004 [Chain A UniProt boundaries]=1-261 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P12004 [Chain A UniRef90 boundaries]=1-261 [Chain B name]=Proliferating cell nuclear antigen [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P12004 [Chain B UniProt boundaries]=1-261 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_P12004 [Chain B UniRef90 boundaries]=1-261 [Chain C name]=Proliferating cell nuclear antigen [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P12004 [Chain C UniProt boundaries]=1-261 [Chain C UniProt coverage]=100% [Chain C UniRef90 accession]=UniRef90_P12004 [Chain C UniRef90 boundaries]=1-261 [Entry] [Accession]=DI1000316 [Disorder status]=Inferred from homology [Kd]=2.00E-06 [Name]=Autoinhibitory region bound to p21-activated kinase 4 (PAK4) kinase domain [Source organism]=Homo sapiens [PDB ID]=4l67 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=Protein kinase [Type chain B]=Disordered [Evidence chain B]=The interacting region of PAK4 has been shown to be intrinsically disordered in homologous proteins (PMID:9660763 and PMID:15821030). The 65-123 region described in IDEAL entry IID50053 covers 60% of the binding sequence in a homologous protein. [Type chain A]=Ordered [Evidence chain A]=The protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 1i09. [Chain B name]=Serine/threonine-protein kinase PAK 4 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=O96013 [Chain B UniProt boundaries]=36-60 [Chain B UniProt coverage]=4.2% [Chain B UniRef90 accession]=UniRef90_O96013 [Chain B UniRef90 boundaries]=36-60 [Chain A name]=Serine/threonine-protein kinase PAK 4 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O96013 [Chain A UniProt boundaries]=300-591 [Chain A UniProt coverage]=49.4% [Chain A UniRef90 accession]=UniRef90_O96013 [Chain A UniRef90 boundaries]=300-591 [Related structures]=4fie,4fif,4fii [Entry] [Accession]=DI1210004 [Disorder status]=Inferred from homology [Kd]=2.00E-06 [Name]=Exonuclease I bound by SSB C-terminal peptide motif (site 1) [Source organism]=Klebsiella pneumoniae subsp. pneumoniae / Escherichia coli [PDB ID]=3c94 [PDB chain IDs]=B:A [PDB note]=Chain C was removed as chains A and B highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.70 [Domain]=Exodeoxyribonuclease I [Type chain B]=Disordered [Evidence chain B]=The SSB C-terminal tail is intrinsically disordered in homologous proteins (PMID:15169953) and carries a well-known highly conserved linear motif on its very C-terminal end. The 113-178 region described in DisProt entry DP00722 covers 100% of the binding sequence in a homologous protein. [Type chain A]=Ordered [Evidence chain A]=Exodeoxyribonuclease I involved in the interaction is known to adopt a stable structure in isolation represented by PDB ID 3c95. [Chain B name]=Single-stranded DNA-binding protein [Chain B source organism]=Klebsiella pneumoniae subsp. pneumoniae [Chain B UniProt accession]=A0A0H3GL04 [Chain B UniProt boundaries]=166-174 [Chain B UniProt coverage]=5.2% [Chain B UniRef90 accession]=UniRef90_P0A2F7 [Chain B UniRef90 boundaries]=166-174 [Chain A name]=Exodeoxyribonuclease I [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=P04995 [Chain A UniProt boundaries]=1-475 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P04995 [Chain A UniRef90 boundaries]=1-475 [Entry] [Accession]=DI1210005 [Disorder status]=Inferred from homology [Kd]=2.00E-06 [Name]=Exonuclease I bound by SSB C-terminal peptide motif (site 2) [Source organism]=Klebsiella pneumoniae subsp. pneumoniae / Escherichia coli [PDB ID]=3c94 [PDB chain IDs]=C:A [PDB note]=Chain B was removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.70 [Domain]=Exodeoxyribonuclease I [Type chain C]=Disordered [Evidence chain C]=The SSB C-terminal tail is intrinsically disordered in homologous proteins (PMID:15169953) and carries a well-known highly conserved linear motif on its very C-terminal end. The 113-178 region described in DisProt entry DP00722 covers 100% of the binding sequence in a homologous protein. [Type chain A]=Ordered [Evidence chain A]=Exodeoxyribonuclease I involved in the interaction is known to adopt a stable structure in isolation represented by PDB ID 3c95. [Chain C name]=Single-stranded DNA-binding protein [Chain C source organism]=Klebsiella pneumoniae subsp. pneumoniae [Chain C UniProt accession]=A0A0H3GL04 [Chain C UniProt boundaries]=166-174 [Chain C UniProt coverage]=5.2% [Chain C UniRef90 accession]=UniRef90_P0A2F7 [Chain C UniRef90 boundaries]=166-174 [Chain A name]=Exodeoxyribonuclease I [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=P04995 [Chain A UniProt boundaries]=1-475 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_P04995 [Chain A UniRef90 boundaries]=1-475 [Entry] [Accession]=DI1200010 [Disorder status]=Confirmed [Kd]=2.00E-06 [Name]=RecO bound by SSB C-terminal peptide motif [Source organism]=Escherichia coli [PDB ID]=3q8d [PDB chain IDs]=E:A [PDB note]=Chains B and F were removed as chains A and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=RecO [Type chain E]=Disordered [Evidence chain E]=The SSB C-terminal tail is intrinsically disordered (PMID:15169953) and carries a well-known highly conserved linear motif on its very C-terminal end. The 113-178 region described in DisProt entry DP00722 covers 100% of the binding sequence in a homologous protein. [Type chain A]=Ordered [Evidence chain A]=RecO involved in the interaction is known to adopt a stable structure in isolation represented by PDB ID 1w3s. [Chain E name]=Single-stranded DNA-binding protein [Chain E source organism]=Escherichia coli [Chain E UniProt accession]=P0AGE0 [Chain E UniProt boundaries]=170-178 [Chain E UniProt coverage]=5.1% [Chain E UniRef90 accession]=UniRef90_P0AGE2 [Chain E UniRef90 boundaries]=170-178 [Chain A name]=DNA repair protein RecO [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=P0A7H3 [Chain A UniProt boundaries]=1-242 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q83QI6 [Chain A UniRef90 boundaries]=1-242 [Entry] [Accession]=DI1200011 [Disorder status]=Confirmed [Kd]=2.00E-06 [Name]=Uracil DNA glycosylase bound by SSB C-terminal peptide motif (site 1) [Source organism]=Escherichia coli [PDB ID]=3uf7 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.20 [Domain]=UDG [Type chain B]=Disordered [Evidence chain B]=The SSB C-terminal tail is intrinsically disordered (PMID:15169953) and carries a well-known highly conserved linear motif on its very C-terminal end. The 113-178 region described in DisProt entry DP00722 covers 100% of the binding sequence in a homologous protein. [Type chain A]=Ordered [Evidence chain A]=The UDG domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03167). A solved monomeric structure of the domain is represented by PDB ID 1eug. [Chain B name]=Single-stranded DNA-binding protein [Chain B source organism]=Escherichia coli [Chain B UniProt accession]=P0AGE0 [Chain B UniProt boundaries]=170-178 [Chain B UniProt coverage]=5.1% [Chain B UniRef90 accession]=UniRef90_P0AGE2 [Chain B UniRef90 boundaries]=170-178 [Chain A name]=Uracil-DNA glycosylase [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=P12295 [Chain A UniProt boundaries]=1-229 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q8X444 [Chain A UniRef90 boundaries]=1-229 [Entry] [Accession]=DI1200012 [Disorder status]=Confirmed [Kd]=2.00E-06 [Name]=Uracil DNA glycosylase bound by SSB C-terminal peptide motif (site 2) [Source organism]=Escherichia coli [PDB ID]=3uf7 [PDB chain IDs]=C:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.20 [Domain]=UDG [Type chain C]=Disordered [Evidence chain C]=The SSB C-terminal tail is intrinsically disordered (PMID:15169953) and carries a well-known highly conserved linear motif on its very C-terminal end. The 113-178 region described in DisProt entry DP00722 covers 100% of the binding sequence in a homologous protein. [Type chain A]=Ordered [Evidence chain A]=The UDG domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF03167). A solved monomeric structure of the domain is represented by PDB ID 1eug. [Chain C name]=Single-stranded DNA-binding protein [Chain C source organism]=Escherichia coli [Chain C UniProt accession]=P0AGE0 [Chain C UniProt boundaries]=170-178 [Chain C UniProt coverage]=5.1% [Chain C UniRef90 accession]=UniRef90_P0AGE2 [Chain C UniRef90 boundaries]=170-178 [Chain A name]=Uracil-DNA glycosylase [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=P12295 [Chain A UniProt boundaries]=1-229 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q8X444 [Chain A UniRef90 boundaries]=1-229 [Entry] [Accession]=DI1200013 [Disorder status]=Confirmed [Kd]=2.00E-06 [Name]=PriA helicase bound to SSB C-terminal peptide motif [Source organism]=Klebsiella pneumoniae subsp. pneumoniae [PDB ID]=4nl8 [PDB chain IDs]=C:A [PDB note]=Chains B, D, E and F were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=4.08 [Domain]=Dead box helicase [Type chain C]=Disordered [Evidence chain C]=The SSB C-terminal tail is intrinsically disordered (PMID:15169953) and carries a well-known highly conserved linear motif on its very C-terminal end. The 113-178 region described in DisProt entry DP00722 covers 100% of the binding sequence in a homologous protein. [Type chain A]=Ordered [Evidence chain A]=The dead box helicase and helicase C-terminal domains involved in the interaction are known to adopt a stable structure (see Pfam domain PF00270 and PF00271). A solved structure of this dead box helicase is represented by PDB ID 4nl4. [Chain C name]=Single-stranded DNA-binding protein [Chain C source organism]=Klebsiella pneumoniae subsp. pneumoniae [Chain C UniProt accession]=A0A0H3GL04 [Chain C UniProt boundaries]=166-174 [Chain C UniProt coverage]=5.2% [Chain C UniRef90 accession]=UniRef90_P0A2F7 [Chain C UniRef90 boundaries]=166-174 [Chain A name]=Primosomal protein N' [Chain A source organism]=Klebsiella pneumoniae subsp. pneumoniae [Chain A UniProt accession]=A6TGC5 [Chain A UniProt boundaries]=1-731 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_B5XZ33 [Chain A UniRef90 boundaries]=1-731 [Entry] [Accession]=DI1210006 [Disorder status]=Confirmed [Kd]=2.00E-06 [Name]=RNase H bound to SSB C-terminal peptide motif [Source organism]=Escherichia coli / Escherichia coli O139:H28 [PDB ID]=4z0u [PDB chain IDs]=D:A [PDB note]=Chains B and E were removed as chains A and D highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=RNase_H [Type chain D]=Disordered [Evidence chain D]=The SSB C-terminal tail is intrinsically disordered (PMID:15169953) and carries a well-known highly conserved linear motif on its very C-terminal end. The 113-178 region described in DisProt entry DP00722 covers 100% of the binding sequence in a homologous protein. [Type chain A]=Ordered [Evidence chain A]=The RNase_H domain involved in the interaction is known to adopt a stable structure (see Pfam domain PF00075). A solved structure of RNase HI is represented by PDB ID 1rnh. [Chain D name]=Single-stranded DNA-binding protein [Chain D source organism]=Escherichia coli [Chain D UniProt accession]=P0AGE0 [Chain D UniProt boundaries]=170-178 [Chain D UniProt coverage]=5.1% [Chain D UniRef90 accession]=UniRef90_P0AGE2 [Chain D UniRef90 boundaries]=170-178 [Chain A name]=Ribonuclease H [Chain A source organism]=Escherichia coli O139:H28 [Chain A UniProt accession]=A7ZHV1 [Chain A UniProt boundaries]=1-155 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_A8AKR0 [Chain A UniRef90 boundaries]=1-155 [Entry] [Accession]=DI1200014 [Disorder status]=Confirmed [Kd]=2.00E-06 [Name]=RecJ complexed with DNA and SSB C-terminal tail peptide motif [Source organism]=Deinococcus radiodurans [PDB ID]=5f56 [PDB chain IDs]=B:A [PDB note]=Chain C was removed as chains A and B highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=DHH phosphoesterase [Type chain B]=Disordered [Evidence chain B]=The SSB C-terminal tail is intrinsically disordered (PMID:15169953) and carries a well-known highly conserved linear motif on its very C-terminal end. The 113-178 region described in DisProt entry DP00722 covers 100% of the binding sequence in a homologous protein. [Type chain A]=Ordered [Evidence chain A]=DHH phosphatase family proteins are known to adopt a stable structure (see Pfam domain PF01368). Solved recJ structures with or without SS-DNA are represented by PDB IDs: 5f55, 5f54. [Chain B name]=Single-stranded DNA-binding protein [Chain B source organism]=Deinococcus radiodurans [Chain B UniProt accession]=G9I562 [Chain B UniProt boundaries]=298-301 [Chain B UniProt coverage]=1.3% [Chain B UniRef90 accession]=UniRef90_Q9RY51 [Chain B UniRef90 boundaries]=298-301 [Chain A name]=Single-stranded-DNA-specific exonuclease [Chain A source organism]=Deinococcus radiodurans [Chain A UniProt accession]=D0EM60 [Chain A UniProt boundaries]=1-705 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_D0EM60 [Chain A UniRef90 boundaries]=1-705 [Entry] [Accession]=DI2000042 [Disorder status]=Confirmed [Kd]=4.80E-06 [Name]=BIR domain of BIRC5 in complex with unmodified H3.1 peptide (residues 1-15) [Source organism]=Homo sapiens [PDB ID]=3uee [PDB chain IDs]=B:AC [PDB note]=Chain D was removed as chains A, B and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.61 [Domain]=BIR [Type chain B]=Disordered [Evidence chain B]=The 1-60 region described in IDEAL entry IID00062 covers 100% of the sequence present in the structure. [Type chain A]=Ordered component [Evidence chain A]=The BIR domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00653). A solved structure of the BIR dimer of survivin is represented by PDB ID 1e31. [Type chain C]=Ordered component [Evidence chain C]=The BIR domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00653). A solved structure of the BIR dimer of survivin is represented by PDB ID 1e31. [Chain B name]=Histone H3.1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68431 [Chain B UniProt boundaries]=2-13 [Chain B UniProt coverage]=8.8% [Chain B UniRef90 accession]=UniRef90_P68431 [Chain B UniRef90 boundaries]=2-13 [Chain A name]=Baculoviral IAP repeat-containing protein 5 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O15392 [Chain A UniProt boundaries]=1-142 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_O15392 [Chain A UniRef90 boundaries]=1-142 [Chain C name]=Baculoviral IAP repeat-containing protein 5 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=O15392 [Chain C UniProt boundaries]=1-142 [Chain C UniProt coverage]=100% [Chain C UniRef90 accession]=UniRef90_O15392 [Chain C UniRef90 boundaries]=1-142 [Related structures]=3uef,3uii,3uik [Entry] [Accession]=DI1000317 [Disorder status]=Inferred from motif [Kd]=8.00E-07 [Name]=JNK3 in complex with a JIP1 peptide [Source organism]=Homo sapiens [PDB ID]=4h39 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.99 [Domain]=Protein kinase [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (DOC_MAPK_JIP1_4). [Type chain A]=Ordered [Evidence chain A]=The Protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 1jnk. [Chain B name]=C-Jun-amino-terminal kinase-interacting protein 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q9UQF2 [Chain B UniProt boundaries]=158-167 [Chain B UniProt coverage]=1.4% [Chain B UniRef90 accession]=UniRef90_Q9UQF2 [Chain B UniRef90 boundaries]=158-167 [Chain A name]=Mitogen-activated protein kinase 10 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P53779 [Chain A UniProt boundaries]=45-400 [Chain A UniProt coverage]=76.7% [Chain A UniRef90 accession]=UniRef90_P53779 [Chain A UniRef90 boundaries]=45-400 [Related structures]=3oxi,3ptg [Entry] [Accession]=DI1000318 [Disorder status]=Inferred from motif [Kd]=7.50E-06 [Name]=Human p38alpha complexed with a MAPK docking peptide MKK6 [Source organism]=Homo sapiens [PDB ID]=2y8o [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.95 [Domain]=Protein kinase [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (DOC_MAPK_MEF2A_6). [Type chain A]=Ordered [Evidence chain A]=The Protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 1a9u. [Chain B name]=Dual specificity mitogen-activated protein kinase kinase 6 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P52564 [Chain B UniProt boundaries]=4-17 [Chain B UniProt coverage]=4.2% [Chain B UniRef90 accession]=UniRef90_P52564 [Chain B UniRef90 boundaries]=4-17 [Chain A name]=Mitogen-activated protein kinase 14 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q16539 [Chain A UniProt boundaries]=1-360 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q16539 [Chain A UniRef90 boundaries]=1-360 [Related structures]=5etf [Entry] [Accession]=DI1010090 [Disorder status]=Inferred from motif [Kd]=1.47E-07 [Name]=Human splA/ryanodine receptor domain and SOCS box containing 2 (SPSB2) in complex with a 20-residue VASA peptide [Source organism]=Drosophila melanogaster / Homo sapiens [PDB ID]=3emw [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.80 [Domain]=SPRY [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_SPR_1). [Type chain A]=Ordered [Evidence chain A]=The SPRY domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00622). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3ek9. [Chain B name]=ATP-dependent RNA helicase vasa, isoform A [Chain B source organism]=Drosophila melanogaster [Chain B UniProt accession]=P09052 [Chain B UniProt boundaries]=184-203 [Chain B UniProt coverage]=3% [Chain B UniRef90 accession]=UniRef90_P09052 [Chain B UniRef90 boundaries]=184-203 [Chain A name]=SPRY domain-containing SOCS box protein 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q99619 [Chain A UniProt boundaries]=26-219 [Chain A UniProt coverage]=73.8% [Chain A UniRef90 accession]=UniRef90_Q99619 [Chain A UniRef90 boundaries]=26-219 [Entry] [Accession]=DI1000319 [Disorder status]=Inferred from motif [Kd]=6.30E-06 [Name]=ARC4 from human Tankyrase 2 in complex with peptide from human 3BP2 [Source organism]=Homo sapiens [PDB ID]=3twr [PDB chain IDs]=E:A [PDB note]=Chains B, C, D, F, G and H were removed as chains E and A represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.55 [Domain]=Ankyrin repeat [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a known functional linear motif (DOC_ANK_TNKS_1). [Type chain A]=Ordered [Evidence chain A]=The Ankyrin repeat domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF13857/PF12796). A solved monomeric structure of the domain is represented by PDB ID 3twq. [Modified residues chain E]=aminoserine#S#16 [Chain E name]=SH3 domain-binding protein 2 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P78314 [Chain E UniProt boundaries]=410-425 [Chain E UniProt coverage]=2.9% [Chain E UniRef90 accession]=UniRef90_P78314 [Chain E UniRef90 boundaries]=410-425 [Chain A name]=Tankyrase-2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9H2K2 [Chain A UniProt boundaries]=488-649 [Chain A UniProt coverage]=13.9% [Chain A UniRef90 accession]=UniRef90_Q9H2K2 [Chain A UniRef90 boundaries]=488-649 [Entry] [Accession]=DI2000043 [Disorder status]=Inferred from motif [Kd]=6.49E-06 [Name]=TRF2 TRFH domain in complex with a TIN2 peptide [Source organism]=Homo sapiens [PDB ID]=3bu8 [PDB chain IDs]=C:AB [PDB note]=Chain D was removed as chains C, B and A represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.15 [Domain]=TRF [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a known functional linear motif (LIG_TRFH_1). [Type chain A]=Ordered component [Evidence chain A]=The TRF domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF08558). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1h6p. [Type chain B]=Ordered component [Evidence chain B]=The TRF domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF08558). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1h6p. [Chain C name]=TERF1-interacting nuclear factor 2 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=Q9BSI4 [Chain C UniProt boundaries]=258-275 [Chain C UniProt coverage]=4% [Chain C UniRef90 accession]=UniRef90_Q9BSI4 [Chain C UniRef90 boundaries]=258-275 [Chain A name]=Telomeric repeat-binding factor 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q15554 [Chain A UniProt boundaries]=84-318 [Chain A UniProt coverage]=43.4% [Chain A UniRef90 accession]=UniRef90_Q15554 [Chain A UniRef90 boundaries]=84-318 [Chain B name]=Telomeric repeat-binding factor 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q15554 [Chain B UniProt boundaries]=84-318 [Chain B UniProt coverage]=43.4% [Chain B UniRef90 accession]=UniRef90_Q15554 [Chain B UniRef90 boundaries]=84-318 [Entry] [Accession]=DI1000320 [Disorder status]=Confirmed [Kd]=4.10E-06 [Name]=UHRF1 in complex with H3.1 N-terminal peptide (H3K9me3) [Source organism]=Homo sapiens [PDB ID]=2lgk [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 2lgl. [Modified residues chain B]=N-trimethyllysine#K#9 [Chain B name]=Histone H3.1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68431 [Chain B UniProt boundaries]=2-13 [Chain B UniProt coverage]=8.8% [Chain B UniRef90 accession]=UniRef90_P68431 [Chain B UniRef90 boundaries]=2-13 [Chain A name]=E3 ubiquitin-protein ligase UHRF1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q96T88 [Chain A UniProt boundaries]=298-366 [Chain A UniProt coverage]=8.7% [Chain A UniRef90 accession]=UniRef90_Q96T88 [Chain A UniRef90 boundaries]=298-366 [Entry] [Accession]=DI1100100 [Disorder status]=Inferred from motif [Kd]=4.10E-06 [Name]=SH3-II of Drosophila Rim-binding protein bound to an Aplip1 peptide [Source organism]=Drosophila melanogaster [PDB ID]=4z88 [PDB chain IDs]=M:A [PDB note]=Chains B, C, D, E, F, G, H, I, J, K, L, N, O, P, Q, R, S, T, U, V, W and X were removed as chains A and M represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.09 [Domain]=SH3 [Type chain M]=Disordered [Evidence chain M]=The protein region involved in the interaction contains a known functional linear motif (SH3-binding motif PxxP, PMID:26274777). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF07653). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1shg. [Chain M name]=JNK-interacting protein 1 [Chain M source organism]=Drosophila melanogaster [Chain M UniProt accession]=Q9W0K0 [Chain M UniProt boundaries]=149-163 [Chain M UniProt coverage]=3.1% [Chain M UniRef90 accession]=UniRef90_Q9W0K0 [Chain M UniRef90 boundaries]=149-163 [Chain A name]=RIM-binding protein, isoform F [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=A0A0B4JDC9 [Chain A UniProt boundaries]=1318-1382 [Chain A UniProt coverage]=3.5% [Chain A UniRef90 accession]=UniRef90_A0A0B4JDC9 [Chain A UniRef90 boundaries]=1318-1382 [Entry] [Accession]=DI1100101 [Disorder status]=Inferred from motif [Kd]=1.73E-05 [Name]=SH3-III of Drosophila Rim-binding protein bound to a Cacophony derived peptide [Source organism]=Drosophila melanogaster [PDB ID]=4z8a [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.76 [Domain]=SH3 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (SH3-binding motif PxxP, PMID:26274777). [Type chain A]=Ordered [Evidence chain A]=The SH3 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF07653). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1shg. [Chain B name]=Voltage-dependent calcium channel type A subunit alpha-1 [Chain B source organism]=Drosophila melanogaster [Chain B UniProt accession]=P91645 [Chain B UniProt boundaries]=1688-1702 [Chain B UniProt coverage]=0.8% [Chain B UniRef90 accession]=UniRef90_P91645 [Chain B UniRef90 boundaries]=1688-1702 [Chain A name]=RIM-binding protein, isoform F [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=A0A0B4JDC9 [Chain A UniProt boundaries]=1443-1507 [Chain A UniProt coverage]=3.5% [Chain A UniRef90 accession]=UniRef90_A0A0B4JDC9 [Chain A UniRef90 boundaries]=1443-1507 [Entry] [Accession]=DI1000321 [Disorder status]=Confirmed [Kd]=4.70E-07 [Name]=APLF FHA domain complexed with XRCC4 phosphopeptide [Source organism]=Homo sapiens [PDB ID]=5e50 [PDB chain IDs]=D:A [PDB note]=Chains B and C were removed as chains A and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.38 [Domain]=FHA [Type chain D]=Disordered [Evidence chain D]=The 203-265 region described in DisProt entry DP00152 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The FHA domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00498). A solved monomeric structure of the domain is represented by PDB ID 2brf. [Modified residues chain D]=phosphoserine#S#232|phosphothreonine#T#233 [Chain D name]=DNA repair protein XRCC4 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=Q13426 [Chain D UniProt boundaries]=228-236 [Chain D UniProt coverage]=2.7% [Chain D UniRef90 accession]=UniRef90_Q13426 [Chain D UniRef90 boundaries]=228-236 [Chain A name]=Aprataxin and PNK-like factor [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q8IW19 [Chain A UniProt boundaries]=1-106 [Chain A UniProt coverage]=20.7% [Chain A UniRef90 accession]=UniRef90_Q8IW19 [Chain A UniRef90 boundaries]=1-105 [Entry] [Accession]=DI1010091 [Disorder status]=Inferred from motif [Kd]=4.70E-07 [Name]=Mouse PP1G in complex with human PPP1R15B peptide [Source organism]=Homo sapiens / Mus musculus [PDB ID]=4v0v [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.61 [Domain]=Calcineurin-like phosphoesterase [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a functional linear motif (DOC_PP1_RVXF_1). [Type chain A]=Ordered [Evidence chain A]=The calcineurin-like phosphoesterase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00149). A solved monomeric structure of the domain is represented by PDB ID 4mov. [Chain B name]=Protein phosphatase 1 regulatory subunit 15B [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q5SWA1 [Chain B UniProt boundaries]=631-660 [Chain B UniProt coverage]=4.2% [Chain B UniRef90 accession]=UniRef90_Q5SWA1 [Chain B UniRef90 boundaries]=631-660 [Chain A name]=Serine/threonine-protein phosphatase PP1-gamma catalytic subunit [Chain A source organism]=Mus musculus [Chain A UniProt accession]=P63087 [Chain A UniProt boundaries]=7-300 [Chain A UniProt coverage]=91% [Chain A UniRef90 accession]=UniRef90_P63087 [Chain A UniRef90 boundaries]=7-300 [Related structures]=4v0w,4v0x [Entry] [Accession]=DI1000322 [Disorder status]=Confirmed [Kd]=4.70E-07 [Name]=TRIM33 PHD-Bromo in complex with H3(1-28)K9me3K14acK18acK23ac histone peptide [Source organism]=Homo sapiens [PDB ID]=3u5p [PDB chain IDs]=I:A [PDB note]=Chains B, C, D, E, F, G, H, J, K, L, M, N, O and P were removed as chains A and I highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=PHD zinc finger [Type chain I]=Disordered [Evidence chain I]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The PHD zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 3u5m. [Modified residues chain I]=N-trimethyllysine#K#9|N(6)-acetyllysine#K#14|N(6)-acetyllysine#K#18 [Chain I name]=Histone H3.1 [Chain I source organism]=Homo sapiens [Chain I UniProt accession]=P68431 [Chain I UniProt boundaries]=2-29 [Chain I UniProt coverage]=20.6% [Chain I UniRef90 accession]=UniRef90_P68431 [Chain I UniRef90 boundaries]=2-29 [Chain A name]=E3 ubiquitin-protein ligase TRIM33 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UPN9 [Chain A UniProt boundaries]=882-1087 [Chain A UniProt coverage]=18.3% [Chain A UniRef90 accession]=UniRef90_Q9UPN9 [Chain A UniRef90 boundaries]=882-1087 [Entry] [Accession]=DI1000323 [Disorder status]=Confirmed [Kd]=4.70E-07 [Name]=TRIM33 PHD-Bromo in complex with H3(1-22)K9me3K14acK18ac histone peptide [Source organism]=Homo sapiens [PDB ID]=3u5o [PDB chain IDs]=I:A [PDB note]=Chains B, C, D, E, F, G, H, J, K, L, M, N, O and P were removed as chains A and I highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.70 [Domain]=PHD zinc finger [Type chain I]=Disordered [Evidence chain I]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The PHD zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 3u5m. [Modified residues chain I]=N-trimethyllysine#K#9|N(6)-acetyllysine#K#14|N(6)-acetyllysine#K#18 [Chain I name]=Histone H3.1 [Chain I source organism]=Homo sapiens [Chain I UniProt accession]=P68431 [Chain I UniProt boundaries]=2-23 [Chain I UniProt coverage]=16.2% [Chain I UniRef90 accession]=UniRef90_P68431 [Chain I UniRef90 boundaries]=2-23 [Chain A name]=E3 ubiquitin-protein ligase TRIM33 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UPN9 [Chain A UniProt boundaries]=882-1087 [Chain A UniProt coverage]=18.3% [Chain A UniRef90 accession]=UniRef90_Q9UPN9 [Chain A UniRef90 boundaries]=882-1087 [Entry] [Accession]=DI1000324 [Disorder status]=Confirmed [Kd]=4.70E-07 [Name]=TRIM33 PHD-Bromo in complex with H3(1-20)K9me3K14ac histone peptide [Source organism]=Homo sapiens [PDB ID]=3u5n [PDB chain IDs]=C:A [PDB note]=Chains B and D were removed as chains A and C highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.95 [Domain]=PHD zinc finger [Type chain C]=Disordered [Evidence chain C]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The PHD zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 3u5m. [Modified residues chain C]=N-trimethyllysine#K#9 [Chain C name]=Histone H3.1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P68431 [Chain C UniProt boundaries]=2-21 [Chain C UniProt coverage]=14.7% [Chain C UniRef90 accession]=UniRef90_P68431 [Chain C UniRef90 boundaries]=2-21 [Chain A name]=E3 ubiquitin-protein ligase TRIM33 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q9UPN9 [Chain A UniProt boundaries]=882-1087 [Chain A UniProt coverage]=18.3% [Chain A UniRef90 accession]=UniRef90_Q9UPN9 [Chain A UniRef90 boundaries]=882-1087 [Entry] [Accession]=DI1000325 [Disorder status]=Confirmed [Kd]=4.70E-07 [Name]=MZM-REP domains of Mib1 E3 ligase in complex with Jagged1 N-box peptide [Source organism]=Homo sapiens [PDB ID]=4xi7 [PDB chain IDs]=C:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.05 [Domain]=MZM-REP [Type chain C]=Disordered [Evidence chain C]=The 1094-1218 region described in DisProt entry DP00418 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The MZM-REP domains involved in the interaction are known to adopt a stable structure in isolation. A solved structure of the domains is represented by PDB ID 4xi6. [Chain C name]=Protein jagged-1 [Chain C source organism]=Homo sapiens [Chain C UniProt accession]=P78504 [Chain C UniProt boundaries]=1120-1130 [Chain C UniProt coverage]=0.9% [Chain C UniRef90 accession]=UniRef90_P78504 [Chain C UniRef90 boundaries]=1120-1130 [Chain A name]=E3 ubiquitin-protein ligase MIB1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q86YT6 [Chain A UniProt boundaries]=145-402 [Chain A UniProt coverage]=25.6% [Chain A UniRef90 accession]=UniRef90_Q86YT6 [Chain A UniRef90 boundaries]=145-402 [Entry] [Accession]=DI1020040 [Disorder status]=Confirmed [Kd]=1.60E-07 [Name]=p107 pocket domain in complex with HPV E7 peptide [Source organism]=Human papillomavirus type 16 / Homo sapiens [PDB ID]=4yoz [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.25 [Domain]=Rb pocket [Type chain B]=Disordered [Evidence chain B]=The 1-98 region described in DisProt entry DP00024 covers 100% of the sequence present in the structure. The protein region involved in the interaction contains a known functional linear motif (LIG_Rb_LxCxE_1). [Type chain A]=Ordered [Evidence chain A]=The Rb pocket domain (consist of Rb_A and Rb_B) involved in the interaction is known to adopt a stable structure in isolation (see Pfam domains PF01858 and PF01857). A solved monomeric structure of the domain is represented by PDB ID 3pom. [Chain B name]=Protein E7 [Chain B source organism]=Human papillomavirus type 16 [Chain B UniProt accession]=P03129 [Chain B UniProt boundaries]=21-29 [Chain B UniProt coverage]=9.2% [Chain B UniRef90 accession]=UniRef90_P03129 [Chain B UniRef90 boundaries]=21-29 [Chain A name]=Retinoblastoma-like protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P28749 [Chain A UniProt boundaries]=391-593 [Chain A UniProt coverage]=19% [Chain A UniRef90 accession]=UniRef90_P28749 [Chain A UniRef90 boundaries]=391-593 [Entry] [Accession]=DI1010092 [Disorder status]=Inferred from motif [Kd]=1.40E-06 [Name]=p107 pocket domain in complex with LIN52 phosphopeptide [Source organism]=Gallus gallus / Homo sapiens [PDB ID]=4yos [PDB chain IDs]=E:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=Rb pocket [Type chain E]=Disordered [Evidence chain E]=The protein region involved in the interaction contains a suboptimal LxCxE-type motif LxSxExL together with the phosphate at nearby S28 to bind the LxCxE cleft of the pocket domain with high affinity (PMID:25917549). [Type chain A]=Ordered [Evidence chain A]=The Rb pocket domain (consist of Rb_A and Rb_B) involved in the interaction is known to adopt a stable structure in isolation (see Pfam domains PF01858 and PF01857). A solved monomeric structure of the domain is represented by PDB ID 3pom. [Modified residues chain E]=phosphoserine#S#12 [Chain E name]=Protein lin-52 homolog [Chain E source organism]=Gallus gallus [Chain E UniProt accession]=Q5ZJQ3 [Chain E UniProt boundaries]=11-30 [Chain E UniProt coverage]=17.9% [Chain E UniRef90 accession]=UniRef90_Q5ZJQ3 [Chain E UniRef90 boundaries]=11-30 [Chain A name]=Retinoblastoma-like protein 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P28749 [Chain A UniProt boundaries]=391-599 [Chain A UniProt coverage]=19.6% [Chain A UniRef90 accession]=UniRef90_P28749 [Chain A UniRef90 boundaries]=391-599 [Entry] [Accession]=DI2200006 [Disorder status]=Confirmed [Kd]=1.40E-06 [Name]=RseB in complex with RseA periplasmic tail [Source organism]=Escherichia coli [PDB ID]=3m4w [PDB chain IDs]=E:AC [PDB note]=Chains B, D, F, G and H were removed as chains A, C and E represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.30 [Domain]=RseB [Type chain E]=Disordered [Evidence chain E]=The 121-216 region described in DisProt entry DP00552 covers 100% of the sequence present in the structure. [Type chain A]=Ordered component [Evidence chain A]=RseB domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form. A solved dimeric structure of RseB with no bound ligands is represented by PDB ID 2v42. [Type chain C]=Ordered component [Evidence chain C]=RseB domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form. A solved dimeric structure of RseB with no bound ligands is represented by PDB ID 2v42. [Chain E name]=Anti-sigma-E factor RseA [Chain E source organism]=Escherichia coli [Chain E UniProt accession]=P0AFX7 [Chain E UniProt boundaries]=121-216 [Chain E UniProt coverage]=44.4% [Chain E UniRef90 accession]=UniRef90_P0AFX8 [Chain E UniRef90 boundaries]=121-216 [Chain A name]=Sigma-E factor regulatory protein RseB [Chain A source organism]=Escherichia coli [Chain A UniProt accession]=P0AFX9 [Chain A UniProt boundaries]=24-318 [Chain A UniProt coverage]=92.8% [Chain A UniRef90 accession]=UniRef90_P0AFY0 [Chain A UniRef90 boundaries]=24-318 [Chain C name]=Sigma-E factor regulatory protein RseB [Chain C source organism]=Escherichia coli [Chain C UniProt accession]=P0AFX9 [Chain C UniProt boundaries]=24-318 [Chain C UniProt coverage]=92.8% [Chain C UniRef90 accession]=UniRef90_P0AFY0 [Chain C UniRef90 boundaries]=24-318 [Entry] [Accession]=DI2100010 [Disorder status]=Inferred from motif [Kd]=1.40E-06 [Name]=S. pombe Dcp1/Dcp2 in complex with Edc1 [Source organism]=Schizosaccharomyces pombe [PDB ID]=5j3t [PDB chain IDs]=C:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.60 [Domain]=Dcp1/Dcp2 [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a conserved short-linear motif composed of a tandem Dcp2-activating motif ([FY]AGxxF) and Dcp1-binding motif (LPxP). Decapping coactivators that share this motif enhance the catalytic step of decapping (PMID:27694842). [Type chain A]=Ordered component [Evidence chain A]=Dcp1 and Dcp2 form a dynamic heterodimer mRNA decapping complex. Solved structures of the Dcp1/Dcp2 heteromer without bound ligands are represented by PDB ID 5lon. [Type chain B]=Ordered component [Evidence chain B]=Dcp1 and Dcp2 form a dynamic heterodimer mRNA decapping complex. Solved structures of the Dcp1/Dcp2 heteromer without bound ligands are represented by PDB ID 5lon. [Chain C name]=Uncharacterized protein C18G6.09c [Chain C source organism]=Schizosaccharomyces pombe [Chain C UniProt accession]=Q10108 [Chain C UniProt boundaries]=155-180 [Chain C UniProt coverage]=8.3% [Chain C UniRef90 accession]=UniRef90_Q10108 [Chain C UniRef90 boundaries]=156-180 [Chain A name]=mRNA-decapping enzyme subunit 1 [Chain A source organism]=Schizosaccharomyces pombe [Chain A UniProt accession]=Q9P805 [Chain A UniProt boundaries]=1-127 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q9P805 [Chain A UniRef90 boundaries]=1-127 [Chain B name]=mRNA decapping complex subunit 2 [Chain B source organism]=Schizosaccharomyces pombe [Chain B UniProt accession]=O13828 [Chain B UniProt boundaries]=1-242 [Chain B UniProt coverage]=32.7% [Chain B UniRef90 accession]=UniRef90_O13828 [Chain B UniRef90 boundaries]=1-242 [Entry] [Accession]=DI1000326 [Disorder status]=Inferred from motif [Kd]=1.40E-06 [Name]=Grb2 SH2 domain/CD28-derived peptide complex [Source organism]=Homo sapiens [PDB ID]=3wa4 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.35 [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The interacting region of CD28 contains a known functional YMNM motif (PMID:27927989). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 1ab2. [Modified residues chain B]=phosphotyrosine#Y#191 [Chain B name]=T-cell-specific surface glycoprotein CD28 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P10747 [Chain B UniProt boundaries]=189-196 [Chain B UniProt coverage]=3.6% [Chain B UniRef90 accession]=UniRef90_P10747 [Chain B UniRef90 boundaries]=189-196 [Chain A name]=Growth factor receptor-bound protein 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P62993 [Chain A UniProt boundaries]=55-152 [Chain A UniProt coverage]=45.2% [Chain A UniRef90 accession]=UniRef90_P62993 [Chain A UniRef90 boundaries]=57-152 [Entry] [Accession]=DI1100102 [Disorder status]=Inferred from motif [Kd]=1.40E-06 [Name]=Tom71 TRP domain in complex with HSP90 C-terminal peptide [Source organism]=Saccharomyces cerevisiae [PDB ID]=3fp2 [PDB chain IDs]=Q:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.98 [Domain]=Tetratricopeptide [Type chain Q]=Disordered [Evidence chain Q]=The protein region involved in the interaction contains a known functional linear motif (TPR repeat-binding motif - LIG_TRP). [Type chain A]=Ordered [Evidence chain A]=The TPR domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain involved in the interaction is represented by PDB ID 2lsu. [Chain Q name]=ATP-dependent molecular chaperone HSP82 [Chain Q source organism]=Saccharomyces cerevisiae [Chain Q UniProt accession]=P02829 [Chain Q UniProt boundaries]=698-709 [Chain Q UniProt coverage]=1.7% [Chain Q UniRef90 accession]=UniRef90_P02829 [Chain Q UniRef90 boundaries]=698-709 [Chain A name]=Protein TOM71 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P38825 [Chain A UniProt boundaries]=107-639 [Chain A UniProt coverage]=83.4% [Chain A UniRef90 accession]=UniRef90_P38825 [Chain A UniRef90 boundaries]=107-639 [Entry] [Accession]=DI1010093 [Disorder status]=Inferred from motif [Kd]=6.45E-05 [Name]=FKBP38 in complex with the MEEVD tetratricopeptide binding-motif of Hsp90 [Source organism]=Saccharomyces cerevisiae / Homo sapiens [PDB ID]=5mgx [PDB chain IDs]=A:F [PDB note]=Chains B, C, D, E, G and H were removed as chains A and F represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.18 [Domain]=Tetratricopeptide [Type chain A]=Disordered [Evidence chain A]=The protein region involved in the interaction contains a known functional linear motif (TPR repeat-binding motif - LIG_TRP). [Type chain F]=rdered [Evidence chain F]=The TPR domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain involved in the interaction is represented by PDB ID 2lsu. [Chain A name]=ATP-dependent molecular chaperone HSP82 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P02829 [Chain A UniProt boundaries]=702-709 [Chain A UniProt coverage]=1.1% [Chain A UniRef90 accession]=UniRef90_P02829 [Chain A UniRef90 boundaries]=702-709 [Chain F name]=Peptidyl-prolyl cis-trans isomerase FKBP8 [Chain F source organism]=Homo sapiens [Chain F UniProt accession]=Q14318 [Chain F UniProt boundaries]=91-380 [Chain F UniProt coverage]=70.4% [Chain F UniRef90 accession]=UniRef90_Q14318 [Chain F UniRef90 boundaries]=91-380 [Entry] [Accession]=DI2000044 [Disorder status]=Inferred from motif [Kd]=6.45E-05 [Name]=TRF2 TRFH in complex with an NBS1 peptide [Source organism]=Homo sapiens [PDB ID]=5wqd [PDB chain IDs]=H:AB [PDB note]=Chains C, D, E, F, G, I, J, K, L, M and N were removed as chains A, B and H represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.00 [Domain]=TRF [Type chain H]=Disordered [Evidence chain H]=The protein region involved in the interaction contains a known functional linear motif (LIG_TRFH_1). [Type chain A]=Ordered component [Evidence chain A]=The TRF domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF08558). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1h6p. [Type chain B]=Ordered component [Evidence chain B]=The TRF domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF08558). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1h6p. [Modified residues chain B]=phosphotyrosine#Y#191 [Chain H name]=Nibrin [Chain H source organism]=Homo sapiens [Chain H UniProt accession]=O60934 [Chain H UniProt boundaries]=423-438 [Chain H UniProt coverage]=2.1% [Chain H UniRef90 accession]=UniRef90_O60934 [Chain H UniRef90 boundaries]=423-438 [Chain A name]=Telomeric repeat-binding factor 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q15554 [Chain A UniProt boundaries]=84-287 [Chain A UniProt coverage]=37.6% [Chain A UniRef90 accession]=UniRef90_Q15554 [Chain A UniRef90 boundaries]=84-287 [Chain B name]=Telomeric repeat-binding factor 2 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q15554 [Chain B UniProt boundaries]=84-287 [Chain B UniProt coverage]=37.6% [Chain B UniRef90 accession]=UniRef90_Q15554 [Chain B UniRef90 boundaries]=84-287 [Entry] [Accession]=DI1000327 [Disorder status]=Inferred from motif [Kd]=6.45E-05 [Name]=SH2 domain of Gads complexed with a CD28-derived phosphotyrosine-containing peptide [Source organism]=Homo sapiens [PDB ID]=5gjh [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.20 [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_SH2_GRB2). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain is represented by PDB ID 1fhs. [Modified residues chain B]=phosphotyrosine#Y#191 [Chain B name]=T-cell-specific surface glycoprotein CD28 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P10747 [Chain B UniProt boundaries]=189-196 [Chain B UniProt coverage]=3.6% [Chain B UniRef90 accession]=UniRef90_P10747 [Chain B UniRef90 boundaries]=189-196 [Chain A name]=GRB2-related adapter protein 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O75791 [Chain A UniProt boundaries]=56-155 [Chain A UniProt coverage]=30.3% [Chain A UniRef90 accession]=UniRef90_O75791 [Chain A UniRef90 boundaries]=58-155 [Entry] [Accession]=DI1000328 [Disorder status]=Inferred from motif [Kd]=6.45E-05 [Name]=PI3K p85 N-terminal SH2 domain complexed with a CD28-derived phosphotyrosine-containing peptide [Source organism]=Homo sapiens [PDB ID]=5gji [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=0.90 [Domain]=SH2 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_SH2_GRB2). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain is represented by PDB ID 1fhs. [Modified residues chain B]=phosphotyrosine#Y#191 [Chain B name]=T-cell-specific surface glycoprotein CD28 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P10747 [Chain B UniProt boundaries]=189-196 [Chain B UniProt coverage]=3.6% [Chain B UniRef90 accession]=UniRef90_P10747 [Chain B UniRef90 boundaries]=189-196 [Chain A name]=Phosphatidylinositol 3-kinase regulatory subunit alpha [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P27986 [Chain A UniProt boundaries]=323-430 [Chain A UniProt coverage]=14.9% [Chain A UniRef90 accession]=UniRef90_P27986 [Chain A UniRef90 boundaries]=324-430 [Entry] [Accession]=DI1000329 [Disorder status]=Confirmed [Kd]=6.45E-05 [Name]=Grb2-SH2 domain complexed with AICD peptide [Source organism]=Homo sapiens [PDB ID]=3mxc [PDB chain IDs]=L:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=SH2 [Type chain L]=Disordered [Evidence chain L]=The AICD peptide region of the human Abeta A4 protein has been shown to be intrinsically disordered in isolation (PMID:22001015). [Type chain A]=Ordered [Evidence chain A]=The SH2 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00017). A solved monomeric structure of the domain is represented by PDB ID 1fhs. [Modified residues chain L]=phosphotyrosine#Y#682 [Chain L name]=Amyloid beta A4 protein [Chain L source organism]=Homo sapiens [Chain L UniProt accession]=P05067 [Chain L UniProt boundaries]=754-762 [Chain L UniProt coverage]=1.2% [Chain L UniRef90 accession]=UniRef90_P05067 [Chain L UniRef90 boundaries]=754-762 [Chain A name]=Growth factor receptor-bound protein 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P62993 [Chain A UniProt boundaries]=52-152 [Chain A UniProt coverage]=46.5% [Chain A UniRef90 accession]=UniRef90_P62993 [Chain A UniRef90 boundaries]=55-152 [Related structures]=3mxy [Entry] [Accession]=DI1000330 [Disorder status]=Confirmed [Kd]=6.45E-05 [Name]=TRIM24 PHD-Bromo complexed with H3(1-10)K4 peptide [Source organism]=Homo sapiens [PDB ID]=3o37 [PDB chain IDs]=E:A [PDB note]=Chains B, C, D, F, G and H were removed as chains A and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=PHD zinc finger [Type chain E]=Disordered [Evidence chain E]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The PHD zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 3o33. [Chain E name]=Histone H3.1 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P68431 [Chain E UniProt boundaries]=2-11 [Chain E UniProt coverage]=7.4% [Chain E UniRef90 accession]=UniRef90_P68431 [Chain E UniRef90 boundaries]=2-11 [Chain A name]=Transcription intermediary factor 1-alpha [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O15164 [Chain A UniProt boundaries]=824-1006 [Chain A UniProt coverage]=17.4% [Chain A UniRef90 accession]=UniRef90_Q64127 [Chain A UniRef90 boundaries]=824-1006 [Entry] [Accession]=DI1000331 [Disorder status]=Confirmed [Kd]=6.45E-05 [Name]=CBX1 chromo shadow domain in complex with a histone peptide [Source organism]=Homo sapiens [PDB ID]=5t1g [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=Chromo shadow domain [Type chain B]=Disordered [Evidence chain B]=The 1-60 region described in IDEAL entry IID00062 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The chromo shadow domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01393). A solved monomeric structure of the domain represented by PDB ID 3kup. [Chain B name]=Histone H3.1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68431 [Chain B UniProt boundaries]=39-53 [Chain B UniProt coverage]=11% [Chain B UniRef90 accession]=UniRef90_P68431 [Chain B UniRef90 boundaries]=39-53 [Chain A name]=Chromobox protein homolog 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P83916 [Chain A UniProt boundaries]=107-185 [Chain A UniProt coverage]=42.7% [Chain A UniRef90 accession]=UniRef90_P83916 [Chain A UniRef90 boundaries]=111-176 [Entry] [Accession]=DI1010094 [Disorder status]=Confirmed [Kd]=6.45E-05 [Name]=Mixed Lineage Leukaemia (MLL1) SET Domain with the cofactor product S-Adenosylhomocysteine and histone peptide [Source organism]=Mus musculus / Homo sapiens [PDB ID]=2w5z [PDB chain IDs]=C:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.20 [Domain]=SET [Type chain C]=Disordered [Evidence chain C]=The 1-60 region described in IDEAL entry IID00062 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The SET domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00856). A solved structure of the domain without bound ligands is represented by PDB ID 2w5y. [Modified residues chain C]=N-dimethyl-lysine#K#4 [Chain C name]=Histone H3.1 [Chain C source organism]=Mus musculus [Chain C UniProt accession]=P68433 [Chain C UniProt boundaries]=2-9 [Chain C UniProt coverage]=5.9% [Chain C UniRef90 accession]=UniRef90_P68431 [Chain C UniRef90 boundaries]=2-9 [Chain A name]=Histone-lysine N-methyltransferase 2A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q03164 [Chain A UniProt boundaries]=3785-3969 [Chain A UniProt coverage]=4.7% [Chain A UniRef90 accession]=UniRef90_Q03164 [Chain A UniRef90 boundaries]=3785-3969 [Entry] [Accession]=DI1200015 [Disorder status]=Inferred from motif [Kd]=6.45E-05 [Name]=Type III secretion chaperone SycD in complex with a peptide of the translocator YopD [Source organism]=Yersinia enterocolitica [PDB ID]=4am9 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=Tetratricopeptide [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a short-linear motif [PV]xLxxP that is common in translocator proteins YopD, PopD and IpaB for the binding of their TPR domain-containing secretion chaperones (PMID:22708907). [Type chain A]=Ordered [Evidence chain A]=The TPR domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain TPR_3; PF07720). A solved structure of the domain without bound ligands is represented by PDB ID 2vgy. [Chain B name]=Translocator protein [Chain B source organism]=Yersinia enterocolitica [Chain B UniProt accession]=Q9R2G2 [Chain B UniProt boundaries]=55-65 [Chain B UniProt coverage]=3.6% [Chain B UniRef90 accession]=UniRef90_Q06131 [Chain B UniRef90 boundaries]=56-65 [Chain A name]=Chaperone SycD [Chain A source organism]=Yersinia enterocolitica [Chain A UniProt accession]=O87496 [Chain A UniProt boundaries]=16-163 [Chain A UniProt coverage]=88.1% [Chain A UniRef90 accession]=UniRef90_P21207 [Chain A UniRef90 boundaries]=21-163 [Entry] [Accession]=DI2200007 [Disorder status]=Inferred from motif [Kd]=6.45E-05 [Name]=Type III secretion chaperone PcrH in complex with a peptide of the translocator PopD [Source organism]=Pseudomonas aeruginosa [PDB ID]=2xcb [PDB chain IDs]=C:AB [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.85 [Domain]=Tetratricopeptide [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a short-linear motif [PV]xLxxP that is common in translocator proteins YopD, PopD and IpaB for the binding of their TPR domain-containing secretion chaperones (PMID:22708907). [Type chain A]=Ordered component [Evidence chain A]=The TPR domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain TPR_3; PF07720). A solved structure of the domain dimer without bound ligands is represented by PDB ID 2xcc. [Type chain B]=Ordered component [Evidence chain B]=The TPR domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain TPR_3; PF07720). A solved structure of the domain dimer without bound ligands is represented by PDB ID 2xcc. [Chain C name]=PepD [Chain C source organism]=Pseudomonas aeruginosa [Chain C UniProt accession]=O50280 [Chain C UniProt boundaries]=47-56 [Chain C UniProt coverage]=3.4% [Chain C UniRef90 accession]=UniRef90_A0A0A8RQ28 [Chain C UniRef90 boundaries]=47-56 [Chain A name]=Regulatory protein PcrH [Chain A source organism]=Pseudomonas aeruginosa [Chain A UniProt accession]=Q9I325 [Chain A UniProt boundaries]=19-160 [Chain A UniProt coverage]=85% [Chain A UniRef90 accession]=UniRef90_Q9I325 [Chain A UniRef90 boundaries]=21-160 [Chain B name]=Regulatory protein PcrH [Chain B source organism]=Pseudomonas aeruginosa [Chain B UniProt accession]=Q9I325 [Chain B UniProt boundaries]=19-160 [Chain B UniProt coverage]=85% [Chain B UniRef90 accession]=UniRef90_Q9I325 [Chain B UniRef90 boundaries]=21-160 [Entry] [Accession]=DI2200008 [Disorder status]=Inferred from motif [Kd]=7.20E-05 [Name]=Type III secretion chaperone IpgC in complex with a peptide of the translocator IpaB [Source organism]=Shigella flexneri [PDB ID]=3gz1 [PDB chain IDs]=Q:AB [PDB note]=Chain P was removed as chains A, B and Q represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.15 [Domain]=Tetratricopeptide [Type chain Q]=Disordered [Evidence chain Q]=The protein region involved in the interaction contains a short linear motif [PV]xLxxP that is common in translocator proteins YopD, PopD and IpaB for the binding of their TPR domain-containing secretion chaperones (PMID:22708907). [Type chain A]=Ordered component [Evidence chain A]=The TPR domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain TPR_3; PF07720). A solved structure of the domain dimer without bound ligands is represented by PDB ID 2xcc. [Type chain B]=Ordered component [Evidence chain B]=The TPR domain involved in the interaction is known to adopt a stable structure in isolation in dimeric form (see Pfam domain TPR_3; PF07720). A solved structure of the domain dimer without bound ligands is represented by PDB ID 2xcc. [Chain Q name]=Invasin IpaB [Chain Q source organism]=Shigella flexneri [Chain Q UniProt accession]=P18011 [Chain Q UniProt boundaries]=51-72 [Chain Q UniProt coverage]=3.8% [Chain Q UniRef90 accession]=UniRef90_P18011 [Chain Q UniRef90 boundaries]=51-72 [Chain A name]=Chaperone protein IpgC [Chain A source organism]=Shigella flexneri [Chain A UniProt accession]=P0A2U4 [Chain A UniProt boundaries]=1-151 [Chain A UniProt coverage]=97.4% [Chain A UniRef90 accession]=UniRef90_P0A2U4 [Chain A UniRef90 boundaries]=1-151 [Chain B name]=Chaperone protein IpgC [Chain B source organism]=Shigella flexneri [Chain B UniProt accession]=P0A2U4 [Chain B UniProt boundaries]=1-151 [Chain B UniProt coverage]=97.4% [Chain B UniRef90 accession]=UniRef90_P0A2U4 [Chain B UniRef90 boundaries]=1-151 [Related structures]=3gz2 [Entry] [Accession]=DI1000332 [Disorder status]=Inferred from motif [Kd]=7.20E-05 [Name]=CNOT1 superfamily homology domain in complex with a Nanos1 peptide [Source organism]=Homo sapiens [PDB ID]=4cqo [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=Not1 [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a short CNOT1-interacting motif (NIM) that is conserved in the Nanos proteins of all vertebrates and some invertebrate species [PMID:24736845]. [Type chain A]=Ordered [Evidence chain A]=The Not1 domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF04054). A solved structure of the domain dimer without bound ligands is represented by PDB ID 4c0d. [Chain B name]=Nanos homolog 1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q8WY41 [Chain B UniProt boundaries]=40-56 [Chain B UniProt coverage]=5.8% [Chain B UniRef90 accession]=UniRef90_Q8WY41 [Chain B UniRef90 boundaries]=40-56 [Chain A name]=CCR4-NOT transcription complex subunit 1 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=A5YKK6 [Chain A UniProt boundaries]=1833-2361 [Chain A UniProt coverage]=22.3% [Chain A UniRef90 accession]=UniRef90_A5YKK6 [Chain A UniRef90 boundaries]=1833-2361 [Entry] [Accession]=DI1100103 [Disorder status]=Inferred from homology [Kd]=7.20E-05 [Name]=D. melanogaster eIF4E with the 4E-binding protein 4E-T [Source organism]=Drosophila melanogaster [PDB ID]=4ue9 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.15 [Domain]=IF4E [Type chain B]=Disordered [Evidence chain B]=The interacting region of 4E-T has been shown to be intrinsically disordered in other organisms (PMID:9684899 and PMID:10394359). The protein region involved in the interaction contains a known functional linear motif (LIG_eIF4E_1). [Type chain A]=Ordered [Evidence chain A]=The IF4E domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01652). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3tf2. [Chain B name]=LD07709p [Chain B source organism]=Drosophila melanogaster [Chain B UniProt accession]=Q8IH18 [Chain B UniProt boundaries]=9-44 [Chain B UniProt coverage]=3.6% [Chain B UniRef90 accession]=UniRef90_Q8IH18 [Chain B UniRef90 boundaries]=9-44 [Chain A name]=Eukaryotic translation initiation factor 4E [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=P48598 [Chain A UniProt boundaries]=80-259 [Chain A UniProt coverage]=69.5% [Chain A UniRef90 accession]=UniRef90_P48598 [Chain A UniRef90 boundaries]=80-259 [Entry] [Accession]=DI1100104 [Disorder status]=Inferred from motif [Kd]=7.20E-05 [Name]=D. melanogaster eIF4E with the 4E-binding protein Thor [Source organism]=Drosophila melanogaster [PDB ID]=4ue8 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.10 [Domain]=IF4E [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_eIF4E_1). [Type chain A]=Ordered [Evidence chain A]=The IF4E domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01652). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3tf2. [Chain B name]=4E-binding protein THOR [Chain B source organism]=Drosophila melanogaster [Chain B UniProt accession]=Q9XZ56 [Chain B UniProt boundaries]=50-83 [Chain B UniProt coverage]=29.1% [Chain B UniRef90 accession]=UniRef90_Q9XZ56 [Chain B UniRef90 boundaries]=50-83 [Chain A name]=Eukaryotic translation initiation factor 4E [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=P48598 [Chain A UniProt boundaries]=80-259 [Chain A UniProt coverage]=69.5% [Chain A UniRef90 accession]=UniRef90_P48598 [Chain A UniRef90 boundaries]=80-259 [Entry] [Accession]=DI2100011 [Disorder status]=Inferred from motif [Kd]=7.20E-05 [Name]=Complex of D. melanogaster eIF4E with eIF4G and cap analog [Source organism]=Drosophila melanogaster [PDB ID]=4uec [PDB chain IDs]=B:AC [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=IF4E [Type chain B]=Disordered [Evidence chain B]=The protein region involved in the interaction contains a known functional linear motif (LIG_eIF4E_1). [Type chain A]=Ordered [Evidence chain A]=The IF4E domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01652). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3tf2. [Type chain C]=Ordered [Evidence chain C]=The IF4E domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF01652). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 3tf2. [Chain B name]=Eukaryotic translation initiation factor 4G, isoform A [Chain B source organism]=Drosophila melanogaster [Chain B UniProt accession]=O61380 [Chain B UniProt boundaries]=578-650 [Chain B UniProt coverage]=4.4% [Chain B UniRef90 accession]=UniRef90_O61380 [Chain B UniRef90 boundaries]=578-650 [Chain A name]=Eukaryotic translation initiation factor 4E [Chain A source organism]=Drosophila melanogaster [Chain A UniProt accession]=P48598 [Chain A UniProt boundaries]=80-259 [Chain A UniProt coverage]=69.5% [Chain A UniRef90 accession]=UniRef90_P48598 [Chain A UniRef90 boundaries]=80-259 [Chain C name]=Eukaryotic translation initiation factor 4E [Chain C source organism]=Drosophila melanogaster [Chain C UniProt accession]=P48598 [Chain C UniProt boundaries]=80-259 [Chain C UniProt coverage]=69.5% [Chain C UniRef90 accession]=UniRef90_P48598 [Chain C UniRef90 boundaries]=80-259 [Related structures]=5t47,5t48 [Entry] [Accession]=DI1010095 [Disorder status]=Inferred from motif [Kd]=6.70E-07 [Name]=Paxillin NES Peptide in complex with CRM1-Ran-RanBP1 [Source organism]=Homo sapiens / Saccharomyces cerevisiae [PDB ID]=5uwh [PDB chain IDs]=D:C [PDB note]=Chains A and B were removed as chains C and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.26 [Domain]=CRM1 [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a linear motif termed nuclear export signal, TRG_NES_CRM1_1 (PMID:28282025). [Type chain C]=Ordered [Evidence chain C]=The CRM1 domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 4bsm. [Chain D name]=Paxillin [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=P49023 [Chain D UniProt boundaries]=264-277 [Chain D UniProt coverage]=2.4% [Chain D UniRef90 accession]=UniRef90_P49023 [Chain D UniRef90 boundaries]=264-277 [Chain C name]=Exportin-1 [Chain C source organism]=Saccharomyces cerevisiae [Chain C UniProt accession]=P30822 [Chain C UniProt boundaries]=253-1058 [Chain C UniProt coverage]=74.4% [Chain C UniRef90 accession]=UniRef90_P30822 [Chain C UniRef90 boundaries]=253-1058 [Entry] [Accession]=DI1010096 [Disorder status]=Inferred from motif [Kd]=1.60E-06 [Name]=HDAC5 NES Peptide in complex with CRM1-Ran-RanBP1 [Source organism]=Homo sapiens / Saccharomyces cerevisiae [PDB ID]=5uwi [PDB chain IDs]=D:C [PDB note]=Chains A and B were removed as chains C and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.14 [Domain]=CRM1 [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a linear motif termed nuclear export signal, TRG_NES_CRM1_1 (PMID:28282025). [Type chain C]=Ordered [Evidence chain C]=The CRM1 domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 4bsm. [Chain D name]=Histone deacetylase 5 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=Q9UQL6 [Chain D UniProt boundaries]=1078-1095 [Chain D UniProt coverage]=1.6% [Chain D UniRef90 accession]=UniRef90_Q9UQL6 [Chain D UniRef90 boundaries]=1078-1095 [Chain C name]=Exportin-1 [Chain C source organism]=Saccharomyces cerevisiae [Chain C UniProt accession]=P30822 [Chain C UniProt boundaries]=253-1058 [Chain C UniProt coverage]=74.4% [Chain C UniRef90 accession]=UniRef90_P30822 [Chain C UniRef90 boundaries]=253-1058 [Entry] [Accession]=DI1010097 [Disorder status]=Inferred from motif [Kd]=2.00E-06 [Name]=FMRP NES Peptide in complex with CRM1-Ran-RanBP1 [Source organism]=Homo sapiens / Saccharomyces cerevisiae [PDB ID]=5uwj [PDB chain IDs]=D:C [PDB note]=Chains A and B were removed as chains C and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.22 [Domain]=CRM1 [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a linear motif termed nuclear export signal, TRG_NES_CRM1_1 (PMID:28282025). [Type chain C]=Ordered [Evidence chain C]=The CRM1 domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 4bsm. [Chain D name]=Synaptic functional regulator FMR1 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=Q06787 [Chain D UniProt boundaries]=423-437 [Chain D UniProt coverage]=2.4% [Chain D UniRef90 accession]=UniRef90_Q06787 [Chain D UniRef90 boundaries]=423-437 [Chain C name]=Exportin-1 [Chain C source organism]=Saccharomyces cerevisiae [Chain C UniProt accession]=P30822 [Chain C UniProt boundaries]=253-1058 [Chain C UniProt coverage]=74.4% [Chain C UniRef90 accession]=UniRef90_P30822 [Chain C UniRef90 boundaries]=253-1058 [Related structures]=5uwo [Entry] [Accession]=DI1010098 [Disorder status]=Inferred from motif [Kd]=1.60E-06 [Name]=mDia2 NES Peptide in complex with CRM1-Ran-RanBP1 [Source organism]=Homo sapiens / Saccharomyces cerevisiae [PDB ID]=5uwp [PDB chain IDs]=D:C [PDB note]=Chains A and B were removed as chains C and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.05 [Domain]=CRM1 [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a linear motif termed nuclear export signal, TRG_NES_CRM1_1 (PMID:28282025). [Type chain C]=Ordered [Evidence chain C]=The CRM1 domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 4bsm. [Chain D name]=Protein diaphanous homolog 3 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=Q9NSV4 [Chain D UniProt boundaries]=1179-1193 [Chain D UniProt coverage]=1.3% [Chain D UniRef90 accession]=UniRef90_Q9NSV4 [Chain D UniRef90 boundaries]=1179-1193 [Chain C name]=Exportin-1 [Chain C source organism]=Saccharomyces cerevisiae [Chain C UniProt accession]=P30822 [Chain C UniProt boundaries]=253-1058 [Chain C UniProt coverage]=74.4% [Chain C UniRef90 accession]=UniRef90_P30822 [Chain C UniRef90 boundaries]=253-1058 [Entry] [Accession]=DI1010099 [Disorder status]=Inferred from motif [Kd]=2.00E-05 [Name]=CDC7 NES Peptide in complex with CRM1-Ran-RanBP1 [Source organism]=Homo sapiens / Saccharomyces cerevisiae [PDB ID]=5uwq [PDB chain IDs]=D:C [PDB note]=Chains A and B were removed as chains C and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.28 [Domain]=CRM1 [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a linear motif termed nuclear export signal, TRG_NES_CRM1_1 (PMID:28282025). [Type chain C]=Ordered [Evidence chain C]=The CRM1 domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 4bsm. [Chain D name]=Cell division cycle 7-related protein kinase [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=O00311 [Chain D UniProt boundaries]=456-473 [Chain D UniProt coverage]=3.1% [Chain D UniRef90 accession]=UniRef90_O00311 [Chain D UniRef90 boundaries]=456-473 [Chain C name]=Exportin-1 [Chain C source organism]=Saccharomyces cerevisiae [Chain C UniProt accession]=P30822 [Chain C UniProt boundaries]=253-1058 [Chain C UniProt coverage]=74.4% [Chain C UniRef90 accession]=UniRef90_P30822 [Chain C UniRef90 boundaries]=253-1058 [Related structures]=5uwr [Entry] [Accession]=DI1010100 [Disorder status]=Inferred from motif [Kd]=1.50E-06 [Name]=X11LS NES Peptide in complex with CRM1-Ran-RanBP1 [Source organism]=Homo sapiens / Saccharomyces cerevisiae [PDB ID]=5uws [PDB chain IDs]=D:C [PDB note]=Chains A and B were removed as chains C and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.40 [Domain]=CRM1 [Type chain D]=Disordered [Evidence chain D]=The protein region involved in the interaction contains a linear motif termed nuclear export signal, TRG_NES_CRM1_1 (PMID:28282025). [Type chain C]=Ordered [Evidence chain C]=The CRM1 domain involved in the interaction is known to adopt a stable structure in isolation. A solved monomeric structure of the domain is represented by PDB ID 4bsm. [Chain D name]=Amyloid beta A4 precursor protein-binding family A member 3 [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=O96018 [Chain D UniProt boundaries]=55-72 [Chain D UniProt coverage]=3.1% [Chain D UniRef90 accession]=UniRef90_O96018 [Chain D UniRef90 boundaries]=55-72 [Chain C name]=Exportin-1 [Chain C source organism]=Saccharomyces cerevisiae [Chain C UniProt accession]=P30822 [Chain C UniProt boundaries]=253-1058 [Chain C UniProt coverage]=74.4% [Chain C UniRef90 accession]=UniRef90_P30822 [Chain C UniRef90 boundaries]=253-1058 [Entry] [Accession]=DI1100105 [Disorder status]=Inferred from motif [Kd]=1.50E-06 [Name]=Sky1p in complex with docking motif-containing Npl3p-derived peptide [Source organism]=Saccharomyces cerevisiae [PDB ID]=2jd5 [PDB chain IDs]=C:B [PDB note]=Chain A was were removed as chains B and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.5 [Domain]=protein kinase [Type chain C]=Disordered [Evidence chain C]=The protein region involved in the interaction contains a SR protein kinase-docking motif (PMID:10952997, PMID:17239901). [Type chain B]=Ordered [Evidence chain B]=The protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 1how. [Chain C name]=Nucleolar protein 3 [Chain C source organism]=Saccharomyces cerevisiae [Chain C UniProt accession]=Q01560 [Chain C UniProt boundaries]=408-414 [Chain C UniProt coverage]=1.7% [Chain C UniRef90 accession]=UniRef90_Q01560 [Chain C UniRef90 boundaries]=408-414 [Chain B name]=Serine/threonine-protein kinase SKY1 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=Q03656 [Chain B UniProt boundaries]=138-742 [Chain B UniProt coverage]=81.5% [Chain B UniRef90 accession]=UniRef90_Q03656 [Chain B UniRef90 boundaries]=138-742 [Entry] [Accession]=DI2210003 [Disorder status]=Confirmed [Kd]=3.00E-10 [Name]=Yersinia virulence effector YopE chaperone-binding domain in complex with its secretion chaperone, SycE [Source organism]=Yersinia pseudotuberculosis serotype I / Yersinia pestis [PDB ID]=1l2w [PDB chain IDs]=I:AB [PDB note]=Chains C, D, E, F, G, H, K and L were removed as chains A, B and I represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.00 [Domain]=CesT [Type chain I]=Disordered [Evidence chain I]=The chaperone-binding domain (CBDs) of YopE is disordered in isolation. SycE binding causes a pronounced disorder-to-order transition in the CBD of YopE (PMID:18502763, PMID:19877667). The protein region involved in the interaction contains the so-called beta-motif that can be found in the N-terminal CBDs of a widespread group of T3SS-dependent virulence factors in Yersinia, Salmonella, Shigella, E. coli, and Pseudomonas for binding of their cognate CesT family secretion chaperones (PMID:16507363, PMID:23204470). [Type chain A]=Ordered component [Evidence chain A]=Tir chaperone proteins (CesT family) are known to adopt a stable structure in isolation as dimers (see Pfam domain PF05932). A solved dimerric structure of the domain is represented by PDB ID 1jya. [Type chain B]=Ordered component [Evidence chain B]=Tir chaperone proteins (CesT family) are known to adopt a stable structure in isolation as dimers (see Pfam domain PF05932). A solved dimerric structure of the domain is represented by PDB ID 1jya. [Chain I name]=Outer membrane virulence protein YopE [Chain I source organism]=Yersinia pseudotuberculosis serotype I [Chain I UniProt accession]=P08008 [Chain I UniProt boundaries]=17-85 [Chain I UniProt coverage]=31.5% [Chain I UniRef90 accession]=UniRef90_P31493 [Chain I UniRef90 boundaries]=17-85 [Chain A name]=YopE regulator [Chain A source organism]=Yersinia pestis [Chain A UniProt accession]=P31491 [Chain A UniProt boundaries]=2-122 [Chain A UniProt coverage]=93.1% [Chain A UniRef90 accession]=UniRef90_P31491 [Chain A UniRef90 boundaries]=2-122 [Chain B name]=YopE regulator [Chain B source organism]=Yersinia pestis [Chain B UniProt accession]=P31491 [Chain B UniProt boundaries]=2-122 [Chain B UniProt coverage]=93.1% [Chain B UniRef90 accession]=UniRef90_P31491 [Chain B UniRef90 boundaries]=2-122 [Entry] [Accession]=DI2200009 [Disorder status]=Confirmed [Kd]=3.00E-10 [Name]=Salmonella Virulence Effector SptP in Complex with its Secretion Chaperone SicP [Source organism]=Salmonella typhimurium [PDB ID]=1jyo [PDB chain IDs]=E:BD [PDB note]=Chains A, C and F were removed as chains B, D and E represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=CesT [Type chain E]=Disordered [Evidence chain E]=The chaperone-binding domains (CBDs) of bacterial virulence effectors are disordered in isolation (PMID:18502763, PMID:19877667, PMID:11689946, PMID:24075929) and undergo a pronounced disorder-to-order transition upon binding to their cognate chaperones. The protein region involved in the interaction contains the so-called beta-motif that can be found in the N-terminal CBDs of a widespread group of T3SS-dependent virulence factors in Yersinia, Salmonella, Shigella, E. coli, and Pseudomonas for binding of their cognate CesT family secretion chaperones (PMID:16507363, PMID:23204470). [Type chain B]=Ordered component [Evidence chain B]=Tir chaperone proteins (CesT family) are known to adopt a stable structure in isolation as dimers (see Pfam domain PF05932). A solved dimerric structure of the domain is represented by PDB ID 1jya. [Type chain D]=Ordered component [Evidence chain D]=Tir chaperone proteins (CesT family) are known to adopt a stable structure in isolation as dimers (see Pfam domain PF05932). A solved dimerric structure of the domain is represented by PDB ID 1jya. [Chain E name]=Secreted effector protein SptP [Chain E source organism]=Salmonella typhimurium [Chain E UniProt accession]=P74873 [Chain E UniProt boundaries]=35-139 [Chain E UniProt coverage]=19.3% [Chain E UniRef90 accession]=UniRef90_P74873 [Chain E UniRef90 boundaries]=35-139 [Chain B name]=Chaperone protein sicP [Chain B source organism]=Salmonella typhimurium [Chain B UniProt accession]=P0CL16 [Chain B UniProt boundaries]=1-116 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_E1WAC4 [Chain B UniRef90 boundaries]=1-116 [Chain D name]=Chaperone protein sicP [Chain D source organism]=Salmonella typhimurium [Chain D UniProt accession]=P0CL16 [Chain D UniProt boundaries]=1-116 [Chain D UniProt coverage]=100% [Chain D UniRef90 accession]=UniRef90_E1WAC4 [Chain D UniRef90 boundaries]=1-116 [Entry] [Accession]=DI1210007 [Disorder status]=Confirmed [Kd]=3.00E-10 [Name]=PaaA2-ParE2 antitoxin-toxin complex [Source organism]=Escherichia coli O157:H7 str. SS52 / Escherichia coli O157:H7 [PDB ID]=5czf [PDB chain IDs]=A:D [PDB note]=Chains B and C were removed as chains A and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.67 [Domain]=ParE toxin [Type chain A]=Disordered [Evidence chain A]=The antitoxin PaaA2 is disordered in isolation (PMID:24768114, see solution structure PDB ID 3zbe) and undergoes a pronounced disorder-to-order transition upon binding to its cognate toxin. [Type chain D]=Ordered [Evidence chain D]=The ParE toxin domain is known to adopt a stable structure in isolation (see Pfam domain PF05016). A solved monomeric structure of a ParE-type toxin is represented by PDB ID 4nrn. [Chain A name]=Uncharacterized protein [Chain A source organism]=Escherichia coli O157:H7 str. SS52 [Chain A UniProt accession]=A0A0F6F6Q9 [Chain A UniProt boundaries]=24-75 [Chain A UniProt coverage]=69.3% [Chain A UniRef90 accession]=UniRef90_A0A0B0Z142 [Chain A UniRef90 boundaries]=12-63 [Chain D name]=Uncharacterized protein [Chain D source organism]=Escherichia coli O157:H7 [Chain D UniProt accession]=A0A0H3JHG3 [Chain D UniProt boundaries]=2-92 [Chain D UniProt coverage]=98.9% [Chain D UniRef90 accession]=UniRef90_A0A0D7C2L1 [Chain D UniRef90 boundaries]=2-92 [Entry] [Accession]=DI2200010 [Disorder status]=Confirmed [Kd]=4.60E-10 [Name]=SpoIISA and SpoIISB, a toxin-antitoxin system of B. subtilis [Source organism]=Bacillus subtilis [PDB ID]=3o6q [PDB chain IDs]=B:AC [PDB note]=Chain D was removed as chains A, B and C represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=SpoIISA toxin [Type chain B]=Disordered [Evidence chain B]=The antitoxin SpoIISB is disordered in isolation (PMID:21147767). [Type chain A]=Ordered component [Evidence chain A]=The SpoIISA toxin domain is known to adopt a stable structure as a dimer (see Pfam domain PF14171). A solved dimeric structure of a similar GAF-like domain is represented by PDB ID 2gx5. [Type chain C]=Ordered component [Evidence chain C]=The SpoIISA toxin domain is known to adopt a stable structure as a dimer (see Pfam domain PF14171). A solved dimeric structure of a similar GAF-like domain is represented by PDB ID 2gx5. [Chain B name]=Stage II sporulation protein SB [Chain B source organism]=Bacillus subtilis [Chain B UniProt accession]=O34800 [Chain B UniProt boundaries]=1-56 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_O34800 [Chain B UniRef90 boundaries]=1-56 [Chain A name]=Stage II sporulation protein SA [Chain A source organism]=Bacillus subtilis [Chain A UniProt accession]=O34853 [Chain A UniProt boundaries]=92-248 [Chain A UniProt coverage]=63.3% [Chain A UniRef90 accession]=UniRef90_O34853 [Chain A UniRef90 boundaries]=92-248 [Chain C name]=Stage II sporulation protein SA [Chain C source organism]=Bacillus subtilis [Chain C UniProt accession]=O34853 [Chain C UniProt boundaries]=92-248 [Chain C UniProt coverage]=63.3% [Chain C UniRef90 accession]=UniRef90_O34853 [Chain C UniRef90 boundaries]=92-248 [Entry] [Accession]=DI2200011 [Disorder status]=Confirmed [Kd]=4.60E-10 [Name]=P. aeruginosa type III secretion chaperone ExsC in complex with effector ExsE [Source organism]=Pseudomonas aeruginosa [PDB ID]=3kxy [PDB chain IDs]=T:AB [PDB note]=Chains C, D, E, F, G, H, I, J, K, L, U, V, W, X and Y were removed as chains A, B and T represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.80 [Domain]=CesT [Type chain T]=Disordered [Evidence chain T]=Exse is intrinsically disordered in isolation sapling transiently ordered elements related to the secondary structures involved in ExsC binding (PMID:22138394). [Type chain A]=Ordered component [Evidence chain A]=Tir chaperone proteins (CesT family) are known to adopt a stable structure in isolation as dimers (see Pfam domain PF05932). A solved dimeric structure of the domain is represented by PDB ID 1jya. [Type chain B]=Ordered component [Evidence chain B]=Tir chaperone proteins (CesT family) are known to adopt a stable structure in isolation as dimers (see Pfam domain PF05932). A solved dimeric structure of the domain is represented by PDB ID 1jya. [Chain T name]=ExsE [Chain T source organism]=Pseudomonas aeruginosa [Chain T UniProt accession]=Q9I322 [Chain T UniProt boundaries]=16-81 [Chain T UniProt coverage]=81.5% [Chain T UniRef90 accession]=UniRef90_A0A1L4G2T7 [Chain T UniRef90 boundaries]=16-81 [Chain A name]=Exoenzyme S synthesis protein C [Chain A source organism]=Pseudomonas aeruginosa [Chain A UniProt accession]=P26995 [Chain A UniProt boundaries]=1-133 [Chain A UniProt coverage]=91.7% [Chain A UniRef90 accession]=UniRef90_P26995 [Chain A UniRef90 boundaries]=1-133 [Chain B name]=Exoenzyme S synthesis protein C [Chain B source organism]=Pseudomonas aeruginosa [Chain B UniProt accession]=P26995 [Chain B UniProt boundaries]=1-133 [Chain B UniProt coverage]=91.7% [Chain B UniRef90 accession]=UniRef90_P26995 [Chain B UniRef90 boundaries]=1-133 [Entry] [Accession]=DI2200012 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=P. aeruginosa type III secretion chaperone SpcS in complex with effector toxin ExoT [Source organism]=Pseudomonas aeruginosa [PDB ID]=4jmf [PDB chain IDs]=A:BC [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.10 [Domain]=CesT [Type chain A]=Disordered [Evidence chain A]=The chaperone-binding domains (CBDs) of bacterial virulence effectors are disordered in isolation (PMID:18502763, PMID:19877667, PMID:11689946, PMID:24075929) and undergo a pronounced disorder-to-order transition upon binding to their cognate chaperones. The protein region involved in the interaction contains the so-called beta-motif that can be found in the N-terminal CBDs of a widespread group of T3SS-dependent virulence factors in Yersinia, Salmonella, Shigella, E. coli, and Pseudomonas for binding of their cognate CesT family secretion chaperones (PMID:16507363, PMID:23204470). [Type chain B]=Ordered component [Evidence chain B]=Tir chaperone proteins (CesT family) are known to adopt a stable structure in isolation as dimers (see Pfam domain PF05932). A solved dimeric structure of the domain is represented by PDB ID 1jya. [Type chain C]=Ordered component [Evidence chain C]=Tir chaperone proteins (CesT family) are known to adopt a stable structure in isolation as dimers (see Pfam domain PF05932). A solved dimeric structure of the domain is represented by PDB ID 1jya. [Chain A name]=Exoenzyme T [Chain A source organism]=Pseudomonas aeruginosa [Chain A UniProt accession]=Q9I788 [Chain A UniProt boundaries]=28-77 [Chain A UniProt coverage]=10.9% [Chain A UniRef90 accession]=UniRef90_A0A0A8RAP1 [Chain A UniRef90 boundaries]=28-77 [Chain B name]=Probable chaperone [Chain B source organism]=Pseudomonas aeruginosa [Chain B UniProt accession]=G3XD93 [Chain B UniProt boundaries]=1-116 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_A0A077JM80 [Chain B UniRef90 boundaries]=1-116 [Chain C name]=Probable chaperone [Chain C source organism]=Pseudomonas aeruginosa [Chain C UniProt accession]=G3XD93 [Chain C UniProt boundaries]=1-116 [Chain C UniProt coverage]=100% [Chain C UniRef90 accession]=UniRef90_A0A077JM80 [Chain C UniRef90 boundaries]=1-116 [Entry] [Accession]=DI1200016 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=P. syringae type III secretion chaperone SchA in complex with effector HopA1 [Source organism]=Pseudomonas syringae pv. tomato [PDB ID]=4g6t [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.56 [Domain]=CesT [Type chain B]=Disordered [Evidence chain B]=The chaperone-binding domains (CBDs) of bacterial virulence effectors are disordered in isolation (PMID:18502763, PMID:19877667, PMID:11689946, PMID:24075929) and undergo a pronounced disorder-to-order transition upon binding to their cognate chaperones. The protein region involved in the interaction contains the so-called beta-motif that can be found in the N-terminal CBDs of a widespread group of T3SS-dependent virulence factors in Yersinia, Salmonella, Shigella, E. coli, and Pseudomonas for binding of their cognate CesT family secretion chaperones (PMID:16507363, PMID:23204470). [Type chain A]=Ordered [Evidence chain A]=Tir chaperone proteins (CesT family) are known to adopt a stable structure in isolation as dimers (see Pfam domain PF05932). A solved dimeric structure of the domain is represented by PDB ID 1jya. [Chain B name]=Type III effector HopA1 [Chain B source organism]=Pseudomonas syringae pv. tomato [Chain B UniProt accession]=Q87UE5 [Chain B UniProt boundaries]=21-102 [Chain B UniProt coverage]=21.6% [Chain B UniRef90 accession]=UniRef90_Q87UE5 [Chain B UniRef90 boundaries]=21-102 [Chain A name]=Type III chaperone protein ShcA [Chain A source organism]=Pseudomonas syringae pv. tomato [Chain A UniProt accession]=Q87UE6 [Chain A UniProt boundaries]=1-125 [Chain A UniProt coverage]=98.4% [Chain A UniRef90 accession]=UniRef90_A0A0K8M405 [Chain A UniRef90 boundaries]=1-125 [Entry] [Accession]=DI1210008 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=Y. pestis type III secretion chaperone SycH in complex with effector YopH [Source organism]=Yersinia enterocolitica / Yersinia pestis [PDB ID]=4gf3 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=CesT [Type chain B]=Disordered [Evidence chain B]=The chaperone-binding domains (CBDs) of bacterial virulence effectors are disordered in isolation (PMID:18502763, PMID:19877667, PMID:11689946, PMID:24075929) and undergo a pronounced disorder-to-order transition upon binding to their cognate chaperones. The protein region involved in the interaction contains the so-called beta-motif that can be found in the N-terminal CBDs of a widespread group of T3SS-dependent virulence factors in Yersinia, Salmonella, Shigella, E. coli, and Pseudomonas for binding of their cognate CesT family secretion chaperones (PMID:16507363, PMID:23204470). [Type chain A]=Ordered [Evidence chain A]=Tir chaperone proteins (CesT family) are known to adopt a stable structure in isolation as dimers (see Pfam domain PF05932). A solved dimeric structure of the domain is represented by PDB ID 1jya. [Chain B name]=Tyrosine-protein phosphatase YopH [Chain B source organism]=Yersinia enterocolitica [Chain B UniProt accession]=P15273 [Chain B UniProt boundaries]=21-63 [Chain B UniProt coverage]=9.2% [Chain B UniRef90 accession]=UniRef90_P15273 [Chain B UniRef90 boundaries]=21-63 [Chain A name]=Putative yopH targeting protein [Chain A source organism]=Yersinia pestis [Chain A UniProt accession]=Q7BTX0 [Chain A UniProt boundaries]=1-141 [Chain A UniProt coverage]=100% [Chain A UniRef90 accession]=UniRef90_Q56934 [Chain A UniRef90 boundaries]=1-141 [Entry] [Accession]=DI1210009 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=Y. pestis type III secretion chaperone SycH in complex with effector YscM2 [Source organism]=Yersinia enterocolitica / Yersinia pestis [PDB ID]=1ttw [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.38 [Domain]=CesT [Type chain B]=Disordered [Evidence chain B]=The chaperone-binding domains (CBDs) of bacterial virulence effectors are disordered in isolation (PMID:18502763, PMID:19877667, PMID:11689946, PMID:24075929) and undergo a pronounced disorder-to-order transition upon binding to their cognate chaperones. The protein region involved in the interaction contains the so-called beta-motif that can be found in the N-terminal CBDs of a widespread group of T3SS-dependent virulence factors in Yersinia, Salmonella, Shigella, E. coli, and Pseudomonas for binding of their cognate CesT family secretion chaperones (PMID:16507363, PMID:23204470). [Type chain A]=Ordered [Evidence chain A]=Tir chaperone proteins (CesT family) are known to adopt a stable structure in isolation as dimers (see Pfam domain PF05932). A solved dimeric structure of the domain is represented by PDB ID 1jya. [Chain B name]=Regulatory protein YscM2 [Chain B source organism]=Yersinia enterocolitica [Chain B UniProt accession]=Q93KQ4 [Chain B UniProt boundaries]=33-81 [Chain B UniProt coverage]=42.2% [Chain B UniRef90 accession]=UniRef90_Q93KQ4 [Chain B UniRef90 boundaries]=33-81 [Chain A name]=Putative yopH targeting protein [Chain A source organism]=Yersinia pestis [Chain A UniProt accession]=Q7BTX0 [Chain A UniProt boundaries]=1-138 [Chain A UniProt coverage]=97.9% [Chain A UniRef90 accession]=UniRef90_Q56934 [Chain A UniRef90 boundaries]=1-138 [Entry] [Accession]=DI1100106 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=Snu17p-Pml1p structure intermediate during RES complex assembly [Source organism]=Saccharomyces cerevisiae [PDB ID]=2my3 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=RRM [Type chain B]=Disordered [Evidence chain B]=The interacting region of Pml1p has been shown to be intrinsically disordered in isolation (PMID:26212312). [Type chain A]=Ordered [Evidence chain A]=The RRM domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00076). The solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2m52. [Chain B name]=Pre-mRNA leakage protein 1 [Chain B source organism]=Saccharomyces cerevisiae [Chain B UniProt accession]=Q07930 [Chain B UniProt boundaries]=20-42 [Chain B UniProt coverage]=11.3% [Chain B UniRef90 accession]=UniRef90_Q07930 [Chain B UniRef90 boundaries]=22-42 [Chain A name]=U2 snRNP component IST3 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P40565 [Chain A UniProt boundaries]=21-138 [Chain A UniProt coverage]=79.7% [Chain A UniRef90 accession]=UniRef90_P40565 [Chain A UniRef90 boundaries]=22-138 [Related structures]=2mkc,5gm6 [Entry] [Accession]=DI1100107 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=Rap1 C-terminal domain (Rap1-RCT) in complex with the Rap1 binding module of Rif1 (Rif1-RBM) [Source organism]=Saccharomyces cerevisiae [PDB ID]=4bjt [PDB chain IDs]=D:A [PDB note]=Chains B, C, E and F were removed as chains A and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.61 [Domain]=Rap1 C terminal [Type chain D]=Disordered [Evidence chain D]=Rif1-RBM has been shown to be intrinsically disordered in isolation (PMID:23746845). [Type chain A]=Ordered [Evidence chain A]=The Rap1 C terminal domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF11626). A solved structure of the domain without bound ligands is represented by PDB ID 3cz6. [Chain D name]=Telomere length regulator protein RIF1 [Chain D source organism]=Saccharomyces cerevisiae [Chain D UniProt accession]=P29539 [Chain D UniProt boundaries]=1752-1771 [Chain D UniProt coverage]=1% [Chain D UniRef90 accession]=UniRef90_P29539 [Chain D UniRef90 boundaries]=1752-1771 [Chain A name]=DNA-binding protein RAP1 [Chain A source organism]=Saccharomyces cerevisiae [Chain A UniProt accession]=P11938 [Chain A UniProt boundaries]=627-827 [Chain A UniProt coverage]=24.3% [Chain A UniRef90 accession]=UniRef90_P11938 [Chain A UniRef90 boundaries]=627-827 [Entry] [Accession]=DI2100012 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=Syntenin-1 PDZ domain in complex with Syndecan-4 cytoplasmic tail [Source organism]=Rattus norvegicus [PDB ID]=5a2p [PDB chain IDs]=E:AB [PDB note]=Chains D, E, F, G and H were removed as chains A and B highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.50 [Domain]=PDZ [Type chain E]=Disordered [Evidence chain E]=The cytoplasmic domain of Syndecan-4 has been shown to adopt a stable structure upon binding to a partner protein (either through binding to an ordered domain PMID:16533050 or through dimerization PMID:11456484). [Type chain A]=Ordered component [Evidence chain A]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved structure of the domain dimer without bound ligands is represented by PDB ID 5g1e. [Type chain B]=Ordered component [Evidence chain B]=The PDZ domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00595). A solved structure of the domain dimer without bound ligands is represented by PDB ID 5g1e. [Chain E name]=Syndecan-4 [Chain E source organism]=Rattus norvegicus [Chain E UniProt accession]=P34901 [Chain E UniProt boundaries]=195-202 [Chain E UniProt coverage]=4% [Chain E UniRef90 accession]=UniRef90_P34901 [Chain E UniRef90 boundaries]=195-202 [Chain A name]=Syntenin-1 [Chain A source organism]=Rattus norvegicus [Chain A UniProt accession]=Q9JI92 [Chain A UniProt boundaries]=112-274 [Chain A UniProt coverage]=54.3% [Chain A UniRef90 accession]=UniRef90_O08992 [Chain A UniRef90 boundaries]=112-274 [Chain B name]=Syntenin-1 [Chain B source organism]=Rattus norvegicus [Chain B UniProt accession]=Q9JI92 [Chain B UniProt boundaries]=112-274 [Chain B UniProt coverage]=54.3% [Chain B UniRef90 accession]=UniRef90_O08992 [Chain B UniRef90 boundaries]=112-274 [Related structures]=5g1d [Entry] [Accession]=DI1010101 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=N-Wasp VC domain in complex with skeletal actin [Source organism]=Homo sapiens / Oryctolagus cuniculus [PDB ID]=2vcp [PDB chain IDs]=D:A [PDB note]=Chains B and E were removed as chains A and D represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=3.2 [Domain]=Actin [Type chain D]=Disordered [Evidence chain D]=The corresponding region of N-WASP (WH2 domain or motif) was shown to be intrinsically disordered (PMID:21875562). [Type chain A]=Ordered [Evidence chain A]=Actin domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00022). A solved monomeric structure of the domain is represented by PDB ID 1j6z. [Chain D name]=Neural Wiskott-Aldrich syndrome protein [Chain D source organism]=Homo sapiens [Chain D UniProt accession]=O00401 [Chain D UniProt boundaries]=392-484 [Chain D UniProt coverage]=18.4% [Chain D UniRef90 accession]=UniRef90_O00401 [Chain D UniRef90 boundaries]=392-484 [Chain A name]=Actin, alpha skeletal muscle [Chain A source organism]=Oryctolagus cuniculus [Chain A UniProt accession]=P68135 [Chain A UniProt boundaries]=3-377 [Chain A UniProt coverage]=99.5% [Chain A UniRef90 accession]=UniRef90_P68133 [Chain A UniRef90 boundaries]=3-377 [Related structures]=2ff3,3m3n [Entry] [Accession]=DI1010102 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=NG5 PHD finger in complex with H3K4me3 peptide [Source organism]=Homo sapiens / Mus musculus [PDB ID]=3c6w [PDB chain IDs]=B:A [PDB note]=Chains C and D were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.75 [Domain]=PHD zinc finger [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). The corresponding region of a closely homologous protein has been shown to be disordered in the 1-38 region described in IDEAL entry IID00086 (covers 100% of the sequence present in the structure). [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 1xwh. [Modified residues chain B]=N-trimethyllysine#K#4 [Chain B name]=Histone H3.1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68431 [Chain B UniProt boundaries]=2-13 [Chain B UniProt coverage]=8.8% [Chain B UniRef90 accession]=UniRef90_P68431 [Chain B UniRef90 boundaries]=2-13 [Chain A name]=Inhibitor of growth protein 5 [Chain A source organism]=Mus musculus [Chain A UniProt accession]=Q9D8Y8 [Chain A UniProt boundaries]=184-236 [Chain A UniProt coverage]=22.1% [Chain A UniRef90 accession]=UniRef90_Q9D8Y8 [Chain A UniRef90 boundaries]=184-236 [Entry] [Accession]=DI1010103 [Disorder status]=Inferred from homology [Kd]=2.98E-07 [Name]=cAMP-dependent protein kinase catalytic subunit in complex with cAMP-dependent protein kinase inhibitor [Source organism]=Homo sapiens / Sus scrofa [PDB ID]=1cmk [PDB chain IDs]=I:E [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.90 [Domain]=Protein kinase [Type chain I]=Disordered [Evidence chain I]=The 1-76 region described in DisProt entry DP00015 and the 1-32 region describen in IDEAL entry IID00349 cover 100% of the binding sequence in a homologous protein. [Type chain E]=Ordered [Evidence chain E]=The protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 1i09. [Chain I name]=cAMP-dependent protein kinase inhibitor alpha [Chain I source organism]=Homo sapiens [Chain I UniProt accession]=P61925 [Chain I UniProt boundaries]=6-27 [Chain I UniProt coverage]=28.9% [Chain I UniRef90 accession]=UniRef90_P61925 [Chain I UniRef90 boundaries]=6-27 [Chain E name]=cAMP-dependent protein kinase catalytic subunit alpha [Chain E source organism]=Sus scrofa [Chain E UniProt accession]=P36887 [Chain E UniProt boundaries]=2-351 [Chain E UniProt coverage]=99.7% [Chain E UniRef90 accession]=UniRef90_P17612 [Chain E UniRef90 boundaries]=2-351 [Related structures]=1cdk,1ctp,1q24,1q61,1q62,1q8t,1q8w,1smh,1stc,1sve,1svg,1veb,1xh4,1xh5,1xh6,1xh7,1xh8,1xh9,1xha,1ydr,2c1a,2c1b,2f7e,2f7x,2f7z,2gfc,2gnh,2gni,2gnl,2jds,2jdt,2jdv,2uvx,2uvy,2uvz,2uw0,2uw3,2uw4,2uw5,2uw6,2uw7,2uw8,2vnw,2vny,2vo0,2vo3,2vo6,2vo7,3dnd,3dne,4axa,4ie9,4ij9,4yxs,4z83,4z84,3ama,3amb,3l9l,3l9m,3l9n,3mvj,3nx8,3oog,3ovv,3owp,3oxt,3p0m,3poo,3vqh,4uj1,4uj2,4uj9,4uja,4ujb,4wb5,4wb6,4wb7,4wb8,5bx6,5bx7,1fmo,1jbp,2erz,3x2u,3x2v,3x2w,4iac,4o21,4o22,4xw4,4xw5,4xw6 [Entry] [Accession]=DI1000333 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=PHD domain from the human BPTF in complex with H3(1-15)K4me2 peptide [Source organism]=Homo sapiens [PDB ID]=2fsa [PDB chain IDs]=P:A [PDB note]=Chains B and C were removed as chains A and P represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=PHD zinc finger [Type chain P]=Disordered [Evidence chain P]=The 1-39 region described in IDEAL entry IID50143 covers 100% of the sequence present in the structure. [Type chain A]=Ordered [Evidence chain A]=The PHD domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain from a homologous protein is represented by PDB ID 2e6s. [Modified residues chain P]=N-dimethyl-lysine#K#4 [Chain P name]=Histone H3.1 [Chain P source organism]=Homo sapiens [Chain P UniProt accession]=P68431 [Chain P UniProt boundaries]=2-16 [Chain P UniProt coverage]=11% [Chain P UniRef90 accession]=UniRef90_P68431 [Chain P UniRef90 boundaries]=2-16 [Chain A name]=Nucleosome-remodeling factor subunit BPTF [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q12830 [Chain A UniProt boundaries]=2865-3033 [Chain A UniProt coverage]=5.5% [Chain A UniRef90 accession]=UniRef90_Q12830 [Chain A UniRef90 boundaries]=2865-3033 [Related structures]=2ri7 [Entry] [Accession]=DI1010104 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=BRD2 first bromodomain in complex with acetylated histone H4 peptide [Source organism]=Saccharomyces cerevisiae / Homo sapiens [PDB ID]=2dvq [PDB chain IDs]=P:A [PDB note]=Chains B, C and Q were removed as chains A and P highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.04 [Domain]=Bromodomain [Type chain P]=Disordered [Evidence chain P]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 1x0j. [Modified residues chain P]=N(6)-acetyllysine#K#12 [Chain P name]=Histone H4 [Chain P source organism]=Saccharomyces cerevisiae [Chain P UniProt accession]=P02309 [Chain P UniProt boundaries]=2-16 [Chain P UniProt coverage]=14.6% [Chain P UniRef90 accession]=UniRef90_P02309 [Chain P UniRef90 boundaries]=2-16 [Chain A name]=Bromodomain-containing protein 2 [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=P25440 [Chain A UniProt boundaries]=73-194 [Chain A UniProt coverage]=15.2% [Chain A UniRef90 accession]=UniRef90_P25440 [Chain A UniRef90 boundaries]=73-194 [Related structures]=2dvr [Entry] [Accession]=DI1000334 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=MLL1 PHD3-Bromo complexed with H3(1-9)K4me2 peptide [Source organism]=Homo sapiens [PDB ID]=3lqi [PDB chain IDs]=R:A [PDB note]=Chains B, C, S and T were removed as chains A and R highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.92 [Domain]=PHD zinc finger [Type chain R]=Disordered [Evidence chain R]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The PHD zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 2kyu. [Modified residues chain R]=N-dimethyl-lysine#K#4 [Chain R name]=Histone H3.1 [Chain R source organism]=Homo sapiens [Chain R UniProt accession]=P68431 [Chain R UniProt boundaries]=2-10 [Chain R UniProt coverage]=6.6% [Chain R UniRef90 accession]=UniRef90_P68431 [Chain R UniRef90 boundaries]=2-10 [Chain A name]=Histone-lysine N-methyltransferase 2A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q03164 [Chain A UniProt boundaries]=1566-1784 [Chain A UniProt coverage]=5.5% [Chain A UniRef90 accession]=UniRef90_Q03164 [Chain A UniRef90 boundaries]=1566-1784 [Entry] [Accession]=DI1000335 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=MLL1 PHD3-Bromo complexed with H3(1-9)K4me3 peptide [Source organism]=Homo sapiens [PDB ID]=3lqj [PDB chain IDs]=Q:A [PDB note]=Chains B and T were removed as chains A and Q highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=PHD zinc finger [Type chain Q]=Disordered [Evidence chain Q]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The PHD zinc finger domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00628). A solved monomeric structure of the domain is represented by PDB ID 2kyu. [Modified residues chain Q]=N-trimethyllysine#K#4 [Chain Q name]=Histone H3.1 [Chain Q source organism]=Homo sapiens [Chain Q UniProt accession]=P68431 [Chain Q UniProt boundaries]=2-10 [Chain Q UniProt coverage]=6.6% [Chain Q UniRef90 accession]=UniRef90_P68431 [Chain Q UniRef90 boundaries]=2-10 [Chain A name]=Histone-lysine N-methyltransferase 2A [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=Q03164 [Chain A UniProt boundaries]=1566-1784 [Chain A UniProt coverage]=5.5% [Chain A UniRef90 accession]=UniRef90_Q03164 [Chain A UniRef90 boundaries]=1566-1784 [Entry] [Accession]=DI1020041 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=P/CAF Bromodomain in Complex with HIV-1 Tat Peptide [Source organism]=Human immunodeficiency virus type 1 group M subtype B / Homo sapiens [PDB ID]=1jm4 [PDB chain IDs]=A:B [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=NMR [Domain]=Bromodomain [Type chain A]=Disordered [Evidence chain A]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain B]=Ordered [Evidence chain B]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 1n72. [Modified residues chain A]=N(6)-acetyllysine#K#50 [Modified residues chain B]=N-trimethyllysine#K#4 [Chain A name]=Protein Tat [Chain A source organism]=Human immunodeficiency virus type 1 group M subtype B [Chain A UniProt accession]=P04610 [Chain A UniProt boundaries]=46-55 [Chain A UniProt coverage]=11.6% [Chain A UniRef90 accession]=UniRef90_P04610 [Chain A UniRef90 boundaries]=46-55 [Chain B name]=Histone acetyltransferase KAT2B [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=Q92831 [Chain B UniProt boundaries]=715-832 [Chain B UniProt coverage]=14.2% [Chain B UniRef90 accession]=UniRef90_Q92831 [Chain B UniRef90 boundaries]=715-832 [Entry] [Accession]=DI1000336 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=TRIM24 PHD-Bromo complexed with H3(13-32)K23ac peptide [Source organism]=Homo sapiens [PDB ID]=3o34 [PDB chain IDs]=B:A [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=1.90 [Domain]=Bromodomain [Type chain B]=Disordered [Evidence chain B]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 3o33. [Modified residues chain B]=N(6)-acetyllysine#K#23 [Modified residues chain A]=N(6)-acetyllysine#K#50 [Chain B name]=Histone H3.1 [Chain B source organism]=Homo sapiens [Chain B UniProt accession]=P68431 [Chain B UniProt boundaries]=14-33 [Chain B UniProt coverage]=14.7% [Chain B UniRef90 accession]=UniRef90_P68431 [Chain B UniRef90 boundaries]=14-33 [Chain A name]=Transcription intermediary factor 1-alpha [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O15164 [Chain A UniProt boundaries]=824-1006 [Chain A UniProt coverage]=17.4% [Chain A UniRef90 accession]=UniRef90_Q64127 [Chain A UniRef90 boundaries]=824-1006 [Entry] [Accession]=DI1000337 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=TRIM24 PHD-Bromo complexed with H3(23-31)K27ac peptide [Source organism]=Homo sapiens [PDB ID]=3o35 [PDB chain IDs]=E:A [PDB note]=Chains B and D were removed as chains A and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.76 [Domain]=Bromodomain [Type chain E]=Disordered [Evidence chain E]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 3o33. [Modified residues chain E]=N(6)-acetyllysine#K#27 [Modified residues chain A]=N(6)-acetyllysine#K#50 [Chain E name]=Histone H3.1 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P68431 [Chain E UniProt boundaries]=24-32 [Chain E UniProt coverage]=6.6% [Chain E UniRef90 accession]=UniRef90_P68431 [Chain E UniRef90 boundaries]=24-32 [Chain A name]=Transcription intermediary factor 1-alpha [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O15164 [Chain A UniProt boundaries]=824-1006 [Chain A UniProt coverage]=17.4% [Chain A UniRef90 accession]=UniRef90_Q64127 [Chain A UniRef90 boundaries]=824-1006 [Entry] [Accession]=DI1000338 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=TRIM24 PHD-Bromo complexed with H4(14-19)K16ac peptide [Source organism]=Homo sapiens [PDB ID]=3o36 [PDB chain IDs]=E:A [PDB note]=Chains B and D were removed as chains A and E highlight the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=1.70 [Domain]=Bromodomain [Type chain E]=Disordered [Evidence chain E]=All core histone N-terminal tails are shown to be intrinsically disordered (PMID:16301309). [Type chain A]=Ordered [Evidence chain A]=The Bromodomain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00439). A solved monomeric structure of the domain is represented by PDB ID 3o33. [Modified residues chain E]=N(6)-acetyllysine#K#16 [Modified residues chain A]=N(6)-acetyllysine#K#50 [Chain E name]=Histone H4 [Chain E source organism]=Homo sapiens [Chain E UniProt accession]=P62805 [Chain E UniProt boundaries]=15-20 [Chain E UniProt coverage]=5.8% [Chain E UniRef90 accession]=UniRef90_P62805 [Chain E UniRef90 boundaries]=15-20 [Chain A name]=Transcription intermediary factor 1-alpha [Chain A source organism]=Homo sapiens [Chain A UniProt accession]=O15164 [Chain A UniProt boundaries]=824-1006 [Chain A UniProt coverage]=17.4% [Chain A UniRef90 accession]=UniRef90_Q64127 [Chain A UniRef90 boundaries]=824-1006 [Entry] [Accession]=DI1210010 [Disorder status]=Confirmed [Kd]=2.98E-07 [Name]=PaaA2-ParE2 antitoxin-toxin complex (with PaaA2 containing two selenomethinonines) [Source organism]=Escherichia coli O157:H7 str. SS52 / Escherichia coli O157:H7 [PDB ID]=5cw7 [PDB chain IDs]=A:B [PDB note]=Chains C, D, E, F, G, H, I, J, K, L, M, N, O and P were removed as chains A and B represent the biologically relevant interaction. [PDB experimental technique]=X-ray [PDB resolution]=2.83 [Domain]=ParE toxin [Type chain A]=Disordered [Evidence chain A]=The antitoxin PaaA2 is disordered in isolation (PMID:24768114, see solution structure PDB ID 3zbe) and undergoes a pronounced disorder-to-order transition upon binding to its cognate toxin. [Type chain B]=Ordered [Evidence chain B]=The ParE toxin domain is known to adopt a stable structure in isolation (see Pfam domain PF05016). A solved monomeric structure of a ParE-type toxin is represented by PDB ID 4nrn. [Modified residues chain A]=selenomethionine#M#8|selenomethionine#M#49|selenomethionine#M#56 [Modified residues chain B]=N(6)-acetyllysine#K#23 [Chain A name]=Uncharacterized protein [Chain A source organism]=Escherichia coli O157:H7 str. SS52 [Chain A UniProt accession]=A0A0F6F6Q9 [Chain A UniProt boundaries]=14-75 [Chain A UniProt coverage]=82.7% [Chain A UniRef90 accession]=UniRef90_A0A0B0Z142 [Chain A UniRef90 boundaries]=2-63 [Chain B name]=Uncharacterized protein [Chain B source organism]=Escherichia coli O157:H7 [Chain B UniProt accession]=A0A0H3JHG3 [Chain B UniProt boundaries]=1-92 [Chain B UniProt coverage]=100% [Chain B UniRef90 accession]=UniRef90_A0A0D7C2L1 [Chain B UniRef90 boundaries]=1-92 [Related structures]=5cze [Entry] [Accession]=DI1010105 [Disorder status]=Inferred from homology [Kd]=2.98E-07 [Name]=cAMP-dependent protein kinase catalytic subunit in complex with phosphorylated cAMP-dependent protein kinase inhibitor [Source organism]=Homo sapiens / Mus musculus [PDB ID]=1jlu [PDB chain IDs]=S:E [PDB note]=No modifications of the original PDB file. [PDB experimental technique]=X-ray [PDB resolution]=2.25 [Domain]=Protein kinase [Type chain S]=Disordered [Evidence chain S]=The 1-76 region described in DisProt entry DP00015 and the 1-32 region describen in IDEAL entry IID00349 cover 100% of the binding sequence in a homologous protein. [Type chain E]=Ordered [Evidence chain E]=The protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 1i09. [Modified residues chain S]=phosphoserine#S#377 [Modified residues chain E]=N(6)-acetyllysine#K#16 [Chain S name]=cAMP-dependent protein kinase inhibitor alpha [Chain S source organism]=Homo sapiens [Chain S UniProt accession]=P61925 [Chain S UniProt boundaries]=6-25 [Chain S UniProt coverage]=26.3% [Chain S UniRef90 accession]=UniRef90_P61925 [Chain S UniRef90 boundaries]=6-25 [Chain E name]=cAMP-dependent protein kinase catalytic subunit alpha [Chain E source organism]=Mus musculus [Chain E UniProt accession]=P05132 [Chain E UniProt boundaries]=2-351 [Chain E UniProt coverage]=99.7% [Chain E UniRef90 accession]=UniRef90_P17612 [Chain E UniRef90 boundaries]=2-351 [Related structures]=4iad,4iaf,4iai,4iak,4iay,4iaz,4ib0,4ib1,4ib3