[ { "@graph": [ { "@id": "https://idpregistry.org/#sequence-range.359_367", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 367 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 359 } ] }, { "@id": "https://idpregistry.org/#sequence-range.1_12", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 12 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 1 } ] }, { "@id": "https://disprot.org/assets/data/IDPO_v0.3.0.owl", "@type": [ "http://schema.org/DefinedTermSet" ], "http://schema.org/name": [ { "@value": "IDP ontology" } ] }, { "@id": "https://disprot.org/DP00086r077", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: The N-terminal region is dynamically disordered in the full-length p53 tetramer, fluctuating between states in which it is free and fully exposed to solvent and states in which it makes transient contacts with the DNA-binding domain (DBD). Results: The cross-peaks in the spectrum of uniformly labeled p53 (black in Fig. 1C) are from residues in the disordered regions: The resonances of the folded DBD and TET domains are severely broadened in HSQC spectra of the 180-kDa tetramer, and their resonances are not visible. " } ], "http://schema.org/name": [ { "@value": "disorder" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_61" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:30420502" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000002" } ] }, { "@id": "https://disprot.org/DP00086r039", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: Here, we reveal the recognition mechanism of the phosphorylated TAD2 bound to a pleckstrin homology (PH) domain from human TFIIH subunit p62 in an extended string-like conformation. Results: Although the isolated phosphorylated TAD2 seems to be intrinsically disordered, an extended and ordered structure was induced between residues 47\u201358 upon binding to the PH domain " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.47_58" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:25216154" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://disprot.org/DP00086r066", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: Figure 5a shows that residues 39\u201359 have the largest resonance intensity changes in the presence of hRPA701\u2013168 with residues 42\u201356 having intensity ratios that are >10. " } ], "http://schema.org/name": [ { "@value": "disorder to order" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.42_56" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder to order" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:15824059" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000011" } ] }, { "@id": "https://disprot.org/DP00086r034", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: Here, we report that the conserved bromo-domain of the transcriptional coactivator CBP (CREB binding protein) binds specifically to p53 at the C-terminal acetylated lysine 382. This bromodomain/acetyl-lysine binding is responsible for p53 acetylation-dependent coactivator recruitment after DNA damage, a step essential for p53-induced transcriptional activation of the cyclin-dependent kinase inhibitor p21 in G1 cell cycle arrest. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.367_386" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:14759370" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://disprot.org/DP00086r031", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: Here we report the crystal structure of RPA residues 1-120 (RPA70N) bound to the N-terminal transactivation domain of p53 (residues 37-57; p53N) and, by using NMR spectroscopy, characterize two mechanisms by which the RPA/p53 interaction can be modulated. Abstract: In contrast, the N-terminal p53 transactivation domain is largely disordered in solution, but residues 37-57 fold into two amphipathic helices, H1 and H2, upon binding with RPA70N. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.37_57" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:16234232" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://disprot.org/IDPO/IDPO:00499", "@type": [ "http://schema.org/DefinedTerm" ], "http://schema.org/inDefinedTermSet": [ { "@id": "https://disprot.org/assets/data/IDPO_v0.3.0.owl" } ], "http://schema.org/name": [ { "@value": "disorder content" } ], "http://schema.org/termCode": [ { "@value": "IDPO:00499" } ] }, { "@id": "https://identifiers.org/pubmed:14759370", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT", "@type": [ "http://schema.org/CreativeWork" ] }, { "@id": "https://disprot.org/DP00086r042", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: We have determined the crystal structure of the N-terminal domain of human Mdmx bound to a 15-residue transactivation domain peptide of human p53. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.15_29" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:18677113" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://disprot.org/IDPO/IDPO:0000039", "@type": [ "http://schema.org/DefinedTerm" ], "http://schema.org/inDefinedTermSet": [ { "@id": "https://disprot.org/assets/data/IDPO_v0.3.owl" } ], "http://schema.org/name": [ { "@value": "acetylation display site" } ], "http://schema.org/termCode": [ { "@value": "IDPO:0000039" } ] }, { "@id": "https://idpregistry.org/#sequence-range.368_372", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 372 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 368 } ] }, { "@id": "https://identifiers.org/pubmed:10876243", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://identifiers.org/pubmed:25579814", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://identifiers.org/pubmed:15525938", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://identifiers.org/pubmed:16793543", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://identifiers.org/pubmed:8875929", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://bioschemas.org/profiles/Protein/0.12-DRAFT", "@type": [ "http://schema.org/CreativeWork" ] }, { "@id": "https://disprot.org/DP00086r024", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "small-angle X-ray scattering evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: SAXS data were accurately reproduced by intensity curves simulated from the ensemble of p53(1\u201393) conformers that reproduced the RDC data (shown in the form of a semilogarithmic and a Kratky-type plot in Fig. 2), demonstrating that the overall shape of the predicted and measured ensembles was consistent with the model of the unfolded chain described above. The SAXS profile was not consistent with a collapsed structure of the transactivation domain, reported from paramagnetic relaxation enhancement experiments (Fig. S7) (28). " } ], "http://schema.org/name": [ { "@value": "disorder" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_93" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:18391200" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000002" } ] }, { "@id": "https://disprot.org/DP00086r065", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "isothermal titration calorimetry evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Discussion: Our structural and binding studies allow better understanding of the molecular basis for the increased binding affinity between Taz2 and p531-39 upon phosphorylation at Ser15 and Thr18. " } ], "http://schema.org/name": [ { "@value": "phosphorylation display site" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.14_19" } ], "http://schema.org/sequenceValue": [ { "@value": "phosphorylation display site" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:19217391" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000045" } ] }, { "@id": "https://disprot.org/DP00086r057", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: A peptide derived from this region of p53 (residues 367-388) was found to have no regular structure in its native form by NMR spectroscopy, but becomes helical when bound to Ca2+ loaded S100B(betabeta). " } ], "http://schema.org/name": [ { "@value": "disorder to order" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.367_388" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder to order" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:10876243" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000011" } ] }, { "@id": "https://idpregistry.org/#sequence-range.17_27", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 27 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 17 } ] }, { "@id": "https://disprot.org/IDPO/IDPO:0000045", "@type": [ "http://schema.org/DefinedTerm" ], "http://schema.org/inDefinedTermSet": [ { "@id": "https://disprot.org/assets/data/IDPO_v0.3.owl" } ], "http://schema.org/name": [ { "@value": "phosphorylation display site" } ], "http://schema.org/termCode": [ { "@value": "IDPO:0000045" } ] }, { "@id": "https://disprot.org/DP00086r088", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "far-UV circular dichroism evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: Secondary structure content estimated by analysis of CD spectra for each of the thirteen IDRs showed that none contained more than two residues in a helical conformation (Figures 1-3, Table 3-5), which is insufficient for the formation of a stable \u03b1-helix requiring a minimum of six residues. Formation of a minimal beta-structure requires six residues [38], and seven of the thirteen IDRs (Table 3-5) appear to have between six to eight residues in extended or \u03b2-conformation which may be sufficient for forming short stable \u03b2-hairpins (Table 3-5). Thus, while none of the selected IDRs had stable helical structure, several may have short \u03b2-strands. " } ], "http://schema.org/name": [ { "@value": "disorder" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.367_388" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:27179590" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000002" } ] }, { "@id": "https://identifiers.org/pubmed:26134520", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://disprot.org/DP00086r087", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Article: The position of the p53 helix allows Phe19, Trp23, and Leu26, which are aligned along its hydrophobic face, to insert deep inside the MDM2 cleft (Fig. 5A), and pack with the cleft in a complementary fashion (Fig. 5B). Abstract: In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. Article: In normal cells, MDM2 and p53 form a negative feedback loop that helps to limit the growth-suppressing activity of p53. Curator statement: The region 19-26 corresponds to a destruction/degron motif that binds to the MDM2 E3 ubiquitin-protein ligase. " } ], "http://schema.org/name": [ { "@value": "ubiquitin protein ligase binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.19_26" } ], "http://schema.org/sequenceValue": [ { "@value": "ubiquitin protein ligase binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:8875929" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0031625" } ] }, { "@id": "https://idpregistry.org/#sequence-range.1_61", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 61 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 1 } ] }, { "@id": "https://disprot.org/DP00086r054", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Curator statement: Crystal structure of Sir2, residues 1-246, bound to the C-terminal domain of p53, residues 372-389. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.372_389" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:16905097" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://idpregistry.org/#sequence-range.375_385", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 385 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 375 } ] }, { "@id": "https://disprot.org/DP00086r064", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: Here, we report the NMR structure of the complex of the Taz2 (C/H3) domain of p300 and the N-terminal transactivation domain of p53. In the complex, p53 forms a short alpha helix and interacts with the Taz2 domain through an extended surface. " } ], "http://schema.org/name": [ { "@value": "disorder to order" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_39" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder to order" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:19217391" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000011" } ] }, { "@id": "https://disprot.org/DP00086r072", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "far-UV circular dichroism evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: The CD spectrum of p53 TAD peptide at neutral pH showed no apparent alpha-helical structure when analyzed byYang\u2019s method (Fig. 4A; Ref. 50). Curator statement: Although the text only mentions the lack of a helical structure, the CD spectrum shows that the peptide is in fact disordered. " } ], "http://schema.org/name": [ { "@value": "disorder" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_73" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:7559631" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000002" } ] }, { "@id": "https://idpregistry.org/#sequence-range.361_393", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 393 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 361 } ] }, { "@id": "https://identifiers.org/pubmed:16905097", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://identifiers.org/pubmed:25216154", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://identifiers.org/pubmed:14534297", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://idpregistry.org/#sequence-range.38_61", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 61 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 38 } ] }, { "@id": "https://disprot.org/DP00086r056", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: A peptide derived from this region of p53 (residues 367-388) was found to have no regular structure in its native form by NMR spectroscopy, but becomes helical when bound to Ca2+ loaded S100B(betabeta). " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.367_388" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:10876243" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://idpregistry.org/#sequence-range.1_73", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 73 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 1 } ] }, { "@id": "https://disprot.org/DP00086r053", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: Here, we report the crystal structure of the extreme C-terminus (residues 385-393, p53pT387) of p53 in complex with 14-3-3sigma at a resolution of 1.28A. " } ], "http://schema.org/name": [ { "@value": "14-3-3 protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.385_393" } ], "http://schema.org/sequenceValue": [ { "@value": "14-3-3 protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:20206173" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0071889" } ] }, { "@id": "https://disprot.org/DP00086", "@type": [ "http://schema.org/Protein" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/Protein/0.12-DRAFT" } ], "http://schema.org/hasBioPolymerSequence": [ { "@value": "MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD" } ], "http://schema.org/hasSequenceAnnotation": [ { "@id": "https://disprot.org/DP00086#disorder-content" }, { "@id": "https://disprot.org/DP00086r092" }, { "@id": "https://disprot.org/DP00086r091" }, { "@id": "https://disprot.org/DP00086r090" }, { "@id": "https://disprot.org/DP00086r089" }, { "@id": "https://disprot.org/DP00086r088" }, { "@id": "https://disprot.org/DP00086r086" }, { "@id": "https://disprot.org/DP00086r085" }, { "@id": "https://disprot.org/DP00086r077" }, { "@id": "https://disprot.org/DP00086r076" }, { "@id": "https://disprot.org/DP00086r075" }, { "@id": "https://disprot.org/DP00086r072" }, { "@id": "https://disprot.org/DP00086r071" }, { "@id": "https://disprot.org/DP00086r024" }, { "@id": "https://disprot.org/DP00086r018" }, { "@id": "https://disprot.org/DP00086r013" }, { "@id": "https://disprot.org/DP00086r008" }, { "@id": "https://disprot.org/DP00086r066" }, { "@id": "https://disprot.org/DP00086r064" }, { "@id": "https://disprot.org/DP00086r057" }, { "@id": "https://disprot.org/DP00086r055" }, { "@id": "https://disprot.org/DP00086r051" }, { "@id": "https://disprot.org/DP00086r047" }, { "@id": "https://disprot.org/DP00086r043" }, { "@id": "https://disprot.org/DP00086r040" }, { "@id": "https://disprot.org/DP00086r038" }, { "@id": "https://disprot.org/DP00086r032" }, { "@id": "https://disprot.org/DP00086r030" }, { "@id": "https://disprot.org/DP00086r087" }, { "@id": "https://disprot.org/DP00086r084" }, { "@id": "https://disprot.org/DP00086r083" }, { "@id": "https://disprot.org/DP00086r082" }, { "@id": "https://disprot.org/DP00086r081" }, { "@id": "https://disprot.org/DP00086r078" }, { "@id": "https://disprot.org/DP00086r074" }, { "@id": "https://disprot.org/DP00086r073" }, { "@id": "https://disprot.org/DP00086r067" }, { "@id": "https://disprot.org/DP00086r065" }, { "@id": "https://disprot.org/DP00086r063" }, { "@id": "https://disprot.org/DP00086r062" }, { "@id": "https://disprot.org/DP00086r061" }, { "@id": "https://disprot.org/DP00086r060" }, { "@id": "https://disprot.org/DP00086r059" }, { "@id": "https://disprot.org/DP00086r058" }, { "@id": "https://disprot.org/DP00086r056" }, { "@id": "https://disprot.org/DP00086r054" }, { "@id": "https://disprot.org/DP00086r053" }, { "@id": "https://disprot.org/DP00086r052" }, { "@id": "https://disprot.org/DP00086r050" }, { "@id": "https://disprot.org/DP00086r049" }, { "@id": "https://disprot.org/DP00086r048" }, { "@id": "https://disprot.org/DP00086r046" }, { "@id": "https://disprot.org/DP00086r045" }, { "@id": "https://disprot.org/DP00086r044" }, { "@id": "https://disprot.org/DP00086r042" }, { "@id": "https://disprot.org/DP00086r039" }, { "@id": "https://disprot.org/DP00086r037" }, { "@id": "https://disprot.org/DP00086r036" }, { "@id": "https://disprot.org/DP00086r035" }, { "@id": "https://disprot.org/DP00086r034" }, { "@id": "https://disprot.org/DP00086r033" }, { "@id": "https://disprot.org/DP00086r031" }, { "@id": "https://disprot.org/DP00086r029" }, { "@id": "https://disprot.org/DP00086r027" } ], "http://schema.org/identifier": [ { "@value": "https://identifiers.org/disprot:DP00086" } ], "http://schema.org/includedInDataset": [ { "@value": "https://disprot.org/#2022-03" } ], "http://schema.org/name": [ { "@value": "Cellular tumor antigen p53" } ], "http://schema.org/sameAs": [ { "@id": "http://purl.uniprot.org/isoforms/P04637-1" } ], "http://schema.org/taxonomicRange": [ { "@id": "_:N9f3b778295414230ba7a00ad043278a6" } ] }, { "@id": "_:N9f3b778295414230ba7a00ad043278a6", "@type": [ "http://schema.org/DefinedTerm" ], "http://schema.org/inDefinedTermSet": [ { "@id": "_:N4a8d79a882b64fbc8710ae3b20d0b406" } ], "http://schema.org/sameAs": [ { "@id": "http://purl.uniprot.org/taxonomy/9606" }, { "@id": "https://identifiers.org/taxonomy:9606" }, { "@id": "http://purl.obolibrary.org/obo/NCBITaxon_9606" } ], "http://schema.org/termCode": [ { "@value": "9606" } ], "http://schema.org/url": [ { "@id": "http://purl.bioontology.org/ontology/NCBITAXON/9606" } ] }, { "@id": "_:N4a8d79a882b64fbc8710ae3b20d0b406", "@type": [ "http://schema.org/DefinedTermSet" ], "http://schema.org/name": [ { "@value": "NCBI taxon" } ], "http://schema.org/url": [ { "@id": "https://bioportal.bioontology.org/ontologies/NCBITAXON" } ] }, { "@id": "https://identifiers.org/pubmed:16474402", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://disprot.org/DP00086r047", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: Residues with resonances undergoing significant chemical-shift changes were located in the region spanning residues 18\u201357, which contains the elements of nascent secondary structure, namely TAD1 (residues 14\u201328) and TAD2 (residues 38\u201361) (Lee et al., 2000), with the largest changes occurring in TAD2. " } ], "http://schema.org/name": [ { "@value": "disorder to order" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.14_60" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder to order" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:23063560" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000011" } ] }, { "@id": "https://disprot.org/IDPO/GO:0031625", "@type": [ "http://schema.org/DefinedTerm" ], "http://schema.org/inDefinedTermSet": [ { "@id": "https://disprot.org/assets/data/IDPO_v0.3.owl" } ], "http://schema.org/name": [ { "@value": "ubiquitin protein ligase binding" } ], "http://schema.org/termCode": [ { "@value": "GO:0031625" } ] }, { "@id": "https://identifiers.org/pubmed:7559631", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://idpregistry.org/#sequence-range.291_312", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 312 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 291 } ] }, { "@id": "https://idpregistry.org/#sequence-range.14_60", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 60 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 14 } ] }, { "@id": "https://disprot.org/DP00086r067", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: The amide 1H and 15N chemical shifts of an uniformly 15N-labeled sample of p53TAD were also monitored before and after the addition of unlabeled hRPA701-168. In the presence of unlabeled hRPA701-168, resonance lineshapes increased and corresponding intensity reductions were observed for specific p53TAD residues. The largest intensity reductions were observed for p53TAD residues 42-56. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.42_56" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:15824059" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://idpregistry.org/#sequence-range.366_386", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 386 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 366 } ] }, { "@id": "https://idpregistry.org/#sequence-range.17_29", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 29 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 17 } ] }, { "@id": "https://idpregistry.org/#sequence-range.15_29", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 29 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 15 } ] }, { "@id": "https://identifiers.org/pubmed:14499615", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://disprot.org/DP00086r051", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: Here we detail the molecular mechanisms for the recognition of p53K370me2 and p53K382me2 by 53BP1. The solution structures of TTD in complex with the p53K370me2 and p53K382me2 peptides show a remarkable plasticity of 53BP1 in accommodating these diverse dimethyllysine-containing sequences. We demonstrate that dimeric TTDs are capable of interacting with the two PTMs on a single p53K370me2K382me2 peptide, greatly strengthening the 53BP1-p53 interaction. " } ], "http://schema.org/name": [ { "@value": "disorder to order" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.366_386" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder to order" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:25579814" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000011" } ] }, { "@id": "https://disprot.org/DP00086r061", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "methylation assay evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: SMYD2 belongs to a subfamily of histone lysine methyltransferase and was recently identified to methylate tumor suppressor p53 and Rb. Here we report that SMYD2 prefers to methylate p53 Lys-370 over histone substrates in vitro. Consistently, the level of endogenous p53 Lys-370 monomethylation is significantly elevated when SMYD2 is overexpressed in vivo. Results: CTD Domain and EDEE Motif Are Important for p53 Lys-370 Methylation by SMYD2 " } ], "http://schema.org/name": [ { "@value": "methylation display site" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.368_372" } ], "http://schema.org/sequenceValue": [ { "@value": "methylation display site" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:21880715" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000042" } ] }, { "@id": "https://idpregistry.org/#sequence-range.1_39", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 39 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 1 } ] }, { "@id": "https://idpregistry.org/#sequence-range.385_393", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 393 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 385 } ] }, { "@id": "https://disprot.org/DP00086r032", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to a 15-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. " } ], "http://schema.org/name": [ { "@value": "disorder to order" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.17_29" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder to order" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:8875929" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000011" } ] }, { "@id": "https://idpregistry.org/#sequence-range.41_62", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 62 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 41 } ] }, { "@id": "https://disprot.org/DP00086r071", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: For instance, the mean values of R1, R2, R1\u03c1 and the NHNOE for free p53TAD are consistent with values expected for an intrinsically unstructured protein (67). " } ], "http://schema.org/name": [ { "@value": "disorder" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_73" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:15824059" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000002" } ] }, { "@id": "https://disprot.org/DP00086r073", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "bait-prey hybrid interaction evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Figure: The p53 TAD and mutant derivatives were assayed for the ability to bind in vitro translated human TBP in a GST pull-down assay as described under\u201cMaterials and Methods.\u201d Results: As shown in Fig.3Band Table I, the levels of TBP precipitated by GST-p53 TAD and mutant derivatives are linearly correlated with the abilityof transactivation in vivo. " } ], "http://schema.org/name": [ { "@value": "molecular function activator activity" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_73" } ], "http://schema.org/sequenceValue": [ { "@value": "molecular function activator activity" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:7559631" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0140677" } ] }, { "@id": "https://disprot.org/DP00086r060", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: We have solved the high resolution crystal structures of the full-length SMYD2 protein in binary complex with its cofactor S-adenosylmethionine and in ternary complex with cofactor product S-adenosylhomocysteine and p53 substrate peptide (residues 368-375), respectively. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.365_375" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:21880715" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://disprot.org/DP00086r076", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: The p53 TAD2 in the complex is unstructured except for a short amphipathic \u03b1 helix involving residues 47\u201355. Results: Chemical shift analysis and the NOE pattern demonstrated that p53 in complex with Tfb1 adopts an a-helical fold that extends from Pro47 to Thr55. Outside this region, p53 is flexible, as also supported by the 15N-1H heteronuclear NOE data. " } ], "http://schema.org/name": [ { "@value": "disorder" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.56_70" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:16793543" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000002" } ] }, { "@id": "https://identifiers.org/pubmed:21880715", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://disprot.org/IDPO/GO:0140677", "@type": [ "http://schema.org/DefinedTerm" ], "http://schema.org/inDefinedTermSet": [ { "@id": "https://disprot.org/assets/data/IDPO_v0.3.owl" } ], "http://schema.org/name": [ { "@value": "molecular function activator activity" } ], "http://schema.org/termCode": [ { "@value": "GO:0140677" } ] }, { "@id": "https://disprot.org/IDPO/IDPO:0000059", "@type": [ "http://schema.org/DefinedTerm" ], "http://schema.org/inDefinedTermSet": [ { "@id": "https://disprot.org/assets/data/IDPO_v0.3.owl" } ], "http://schema.org/name": [ { "@value": "self-inhibition" } ], "http://schema.org/termCode": [ { "@value": "IDPO:0000059" } ] }, { "@id": "https://disprot.org/DP00086r029", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Introduction: The interaction between the p62/Tfb1 subunit of TFIIH and the TAD of p53 has been shown to be important for the recruitment of p53 to the TFIIH complex in both human and yeast. This interaction is directly correlated with the ability of the p53 TAD to stimulate transcriptional elongation (Blau et al., 1996). " } ], "http://schema.org/name": [ { "@value": "molecular function activator activity" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.20_73" } ], "http://schema.org/sequenceValue": [ { "@value": "molecular function activator activity" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:16793543" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0140677" } ] }, { "@id": "https://identifiers.org/pubmed:15342238", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://disprot.org/DP00086r008", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Introduction: We show here that an essential element in the interaction of p53 with HMGB1 is the N-terminal disordered region (Lee et al., 2000; Dawson et al., 2003; Wells et al., 2008), comprising the transactivation domain and the proline-rich region, the major interacting motif being a region of inducible structure in TAD2 (Lee et al., 2000). " } ], "http://schema.org/name": [ { "@value": "disorder" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_12" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:23063560" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000002" } ] }, { "@id": "https://disprot.org/DP00086r084", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: Taken together, the NMR and fluorescence data suggest a model in which the p53 NTAD can inhibit binding to nontarget DNA but does not affect binding to a cognate recognition element. " } ], "http://schema.org/name": [ { "@value": "self-inhibition" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_61" } ], "http://schema.org/sequenceValue": [ { "@value": "self-inhibition" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:30420502" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000059" } ] }, { "@id": "https://disprot.org/DP00086r089", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "near-UV circular dichroism evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: For Np53, signals in the near-UV region are largely missing. Under denaturing conditions (4 M GdmCl), no significant change in the near-UV CD signal of Np53 could be detected (Figure 2(C)). The low ellipticity values of the CD signal, together with the insensitivity to denaturation account for a solvent-exposed, unstructured protein. " } ], "http://schema.org/name": [ { "@value": "disorder" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_93" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:14499615" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000002" } ] }, { "@id": "https://disprot.org/DP00086r052", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "fluorescence evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: Here we detail the molecular mechanisms for the recognition of p53K370me2 and p53K382me2 by 53BP1. The solution structures of TTD in complex with the p53K370me2 and p53K382me2 peptides show a remarkable plasticity of 53BP1 in accommodating these diverse dimethyllysine-containing sequences. We demonstrate that dimeric TTDs are capable of interacting with the two PTMs on a single p53K370me2K382me2 peptide, greatly strengthening the 53BP1-p53 interaction. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.366_386" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:25579814" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://disprot.org/DP00086r046", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "isothermal titration calorimetry evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: The isolated p53(1\u201393) fragment and the A box interact (Figure 2F), and an estimate of the affinity (Kd 346 nM) was obtained by isothermal titration calorimetry (ITC) " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_93" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:23063560" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://disprot.org/IDPO/GO:0071889", "@type": [ "http://schema.org/DefinedTerm" ], "http://schema.org/inDefinedTermSet": [ { "@id": "https://disprot.org/assets/data/IDPO_v0.3.owl" } ], "http://schema.org/name": [ { "@value": "14-3-3 protein binding" } ], "http://schema.org/termCode": [ { "@value": "GO:0071889" } ] }, { "@id": "https://disprot.org/DP00086r040", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: Here, we reveal the recognition mechanism of the phosphorylated TAD2 bound to a pleckstrin homology (PH) domain from human TFIIH subunit p62 in an extended string-like conformation. " } ], "http://schema.org/name": [ { "@value": "disorder to order" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.41_62" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder to order" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:25216154" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000011" } ] }, { "@id": "https://disprot.org/IDPO/IDPO:0000011", "@type": [ "http://schema.org/DefinedTerm" ], "http://schema.org/inDefinedTermSet": [ { "@id": "https://disprot.org/assets/data/IDPO_v0.3.owl" } ], "http://schema.org/name": [ { "@value": "disorder to order" } ], "http://schema.org/termCode": [ { "@value": "IDPO:0000011" } ] }, { "@id": "https://disprot.org/DP00086r092", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: We observed small proton resonance dispersion in a spectral range of 7.5\u20138.7 ppm, characteristic for a highly unfolded protein. In addition, the seven NH2 side-chain signals of asparagine and glutamine residues accumulate in their characteristic random coil region of 7.59 ppm/6.88 ppm. The same was observed for the side-chain signals of the three tryptophan residues of Np53, which appear at 10.2 ppm. Taken together, the spectrum shows, at the level of amino acids, that residues 1\u201393 of p53 are mostly unstructured " } ], "http://schema.org/name": [ { "@value": "disorder" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_93" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:14499615" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000002" } ] }, { "@id": "https://disprot.org/DP00086r036", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: This binding is dependent upon K382 acetylation of the peptide with a KD of \u223c50 \u03bcM, as estimated from NMR titration. " } ], "http://schema.org/name": [ { "@value": "acetylation display site" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.380_384" } ], "http://schema.org/sequenceValue": [ { "@value": "acetylation display site" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:14759370" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000039" } ] }, { "@id": "https://disprot.org/DP00086r055", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Curator statement: Crystal structure of Sir2, residues 1-246, bound to the C-terminal domain of p53, residues 372-389. " } ], "http://schema.org/name": [ { "@value": "disorder to order" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.375_385" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder to order" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:16905097" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000011" } ] }, { "@id": "https://disprot.org/IDPO/GO:0005515", "@type": [ "http://schema.org/DefinedTerm" ], "http://schema.org/inDefinedTermSet": [ { "@id": "https://disprot.org/assets/data/IDPO_v0.3.owl" } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/termCode": [ { "@value": "GO:0005515" } ] }, { "@id": "https://idpregistry.org/#sequence-range.42_56", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 56 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 42 } ] }, { "@id": "https://disprot.org/DP00086r044", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: The A box interacts with residues 38-61 (TAD2) of the p53 transactivation domain. Residues 19-26 (TAD1) bind weakly, but only in the context of p53(1-93) and not as a free TAD1 peptide. We have solved the structure of the A-box/p53(1-93) complex by nuclear magnetic resonance spectroscopy. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_93" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:23063560" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://disprot.org/DP00086r091", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "fluorescence evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: Spectra recorded under native as well as under denaturing conditions (4 M GdmCl) did not show significant changes in the maximum emission wavelength or the emission intensity (Figure 2(D)). The emission maximum of the standard N-acetyl-tryptophan-amide (Sigma) was 360 nm. Under native conditions, the fluorescence emission maximum of Np53 was 357 nm, under denaturing conditions 356 nm, both indicating complete solvent exposure. The existence of a well-defined tertiary structure could therefore be excluded " } ], "http://schema.org/name": [ { "@value": "disorder" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_93" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:14499615" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000002" } ] }, { "@id": "https://identifiers.org/pubmed:23063560", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://idpregistry.org/#sequence-range.372_389", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 389 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 372 } ] }, { "@id": "https://idpregistry.org/#sequence-range.14_28", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 28 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 14 } ] }, { "@id": "https://disprot.org/DP00086r059", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Curator statement: Crystal structure of a C-terminal acetylated (Lys382) peptide of P53 bound to Sir2 homologue from Thermatoga maritima (Sir2Tm). " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.372_389" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:16768447" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://disprot.org/DP00086r035", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: This binding is dependent upon K382 acetylation of the peptide with a KD of \u223c50 \u03bcM, as estimated from NMR titration. Results: These results confirm that the CBP bromodomain can specifically interact with p53 acetylated at K382. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.367_386" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:14759370" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://disprot.org/DP00086r050", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: Here we detail the molecular mechanisms for the recognition of p53K370me2 and p53K382me2 by 53BP1. The solution structures of TTD in complex with the p53K370me2 and p53K382me2 peptides show a remarkable plasticity of 53BP1 in accommodating these diverse dimethyllysine-containing sequences. We demonstrate that dimeric TTDs are capable of interacting with the two PTMs on a single p53K370me2K382me2 peptide, greatly strengthening the 53BP1-p53 interaction. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.366_386" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:25579814" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://idpregistry.org/#sequence-range.376_386", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 386 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 376 } ] }, { "@id": "https://disprot.org/DP00086r081", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: With the spin label at S15C, cross-peaks of residues in both the AD1 and AD2 regions are broadened; similarly, attachment of the spin label at P58C broadens resonances associated with both the AD2 and AD1 motifs, confirming the presence of interactions between these motifs (SI Appendix, Fig. S4). Transient interactions between the AD1 and AD2 regions have been observed previously in isolated NTAD peptides (59). In addition, selective resonance broadening is observed for several DBD cross-peaks (SI Appendix, Fig. S4), indicating intramolecular interactions between the spin labeled NTAD and the DBD. Results: With the spin label at P58C (AD2), the largest PRE is observed for residues located in the DNA-binding site; these include T118 and V122 in the L1 loop, G245 and to a lesser extent N247 in the L3 loop, A276, and G279, R280, and R283 in the C-terminal helix. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.14_28" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:30420502" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://disprot.org/DP00086#disorder-content", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "Automated from annotations" } ], "http://schema.org/description": [ { "@value": "Fraction of disordered residues in the sequence derived from the annotations" } ], "http://schema.org/name": [ { "@value": "disorder content" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_393.disorder_content" } ], "http://schema.org/sequenceValue": [ { "@type": "http://www.w3.org/2001/XMLSchema#double", "@value": 0.37659033078880405 } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:00499" } ] }, { "@id": "https://disprot.org/DP00086r045", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: Residues with resonances undergoing significant chemical-shift changes were located in the region spanning residues 18\u201357, which contains the elements of nascent secondary structure, namely TAD1 (residues 14\u201328) and TAD2 (residues 38\u201361) (Lee et al., 2000), with the largest changes occurring in TAD2. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_93" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:23063560" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://disprot.org/DP00086r085", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: In addition, all of the new resonance peaks observed in the p53 construct containing the C-terminal domain (Fig. 3b) appear at frequencies typical of unstructured amides (-8 p.p.m. in the proton dimension). This suggests that the C-terminal domain is not likely to be folded into regular secondary structure. " } ], "http://schema.org/name": [ { "@value": "disorder" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.361_393" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:11524676" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000002" } ] }, { "@id": "https://idpregistry.org/#sequence-range.56_70", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 70 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 56 } ] }, { "@id": "https://idpregistry.org/#sequence-range.1_393.disorder_content", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 393 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 1 } ] }, { "@id": "https://idpregistry.org/#sequence-range.14_19", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 19 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 14 } ] }, { "@id": "https://idpregistry.org/#sequence-range.367_388", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 388 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 367 } ] }, { "@id": "https://disprot.org/DP00086r027", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: This short helix interacts with the surface of Tfb1 formed by beta strands b5, b6, and b7 and the loop connecting b5 to b6. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.20_73" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:16793543" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://idpregistry.org/#sequence-range.47_58", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 58 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 47 } ] }, { "@id": "https://identifiers.org/pubmed:12501191", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://identifiers.org/pubmed:15824059", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://disprot.org/DP00086r043", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: We have determined the crystal structure of the N-terminal domain of human Mdmx bound to a 15-residue transactivation domain peptide of human p53. Article: The surface area occupied by aminoacids 17\u201327 of the p53 peptide has 440 \u00c52 for human Mdmx and 407 \u00c52 for zebrafish Mdmx. " } ], "http://schema.org/name": [ { "@value": "disorder to order" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.17_27" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder to order" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:18677113" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000011" } ] }, { "@id": "https://disprot.org/DP00086r038", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Curator statement: P53 region 367-386 binds to CBP upon K382 acetylation and undergoes disorder-to-order transition upon binding " } ], "http://schema.org/name": [ { "@value": "disorder to order" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.367_386" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder to order" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:14759370" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000011" } ] }, { "@id": "https://disprot.org/DP00086r083", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "fluorescence anisotropy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: Taken together, the NMR and fluorescence data suggest a model in which the p53 NTAD can inhibit binding to nontarget DNA but does not affect binding to a cognate recognition element. " } ], "http://schema.org/name": [ { "@value": "self-inhibition" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_61" } ], "http://schema.org/sequenceValue": [ { "@value": "self-inhibition" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:30420502" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000059" } ] }, { "@id": "https://idpregistry.org/#sequence-range.380_384", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 384 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 380 } ] }, { "@id": "https://identifiers.org/pubmed:20206173", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://disprot.org/DP00086r090", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "far-UV circular dichroism evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: The spectrum of the isolated NTD of p53 exhibits a minimum at 200 nm. The \u0398MRW values above 200 nm suggest that \u03b1-helices and \u03b2-strands are largely missing. Far-UV CD spectra of Np53 analyzed under denaturing conditions (4 M GdmCl) showed only minor structural differences from spectra recorded under native conditions (Figure 2(A)). Taken together, the CD spectra indicate a remarkably high content of unstructured regions in Np53 " } ], "http://schema.org/name": [ { "@value": "disorder" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_93" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:14499615" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000002" } ] }, { "@id": "https://idpregistry.org/#sequence-range.365_375", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 375 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 365 } ] }, { "@id": "https://disprot.org/DP00086r037", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "enzyme-linked immunoabsorbent assay evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: p53-Induced p21 Activation Requires the CBP Bromodomain/p53 AcK382 Interaction " } ], "http://schema.org/name": [ { "@value": "molecular function activator activity" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.367_386" } ], "http://schema.org/sequenceValue": [ { "@value": "molecular function activator activity" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:14759370" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0140677" } ] }, { "@id": "https://idpregistry.org/#sequence-range.367_386", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 386 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 367 } ] }, { "@id": "https://disprot.org/DP00086r058", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Curator statement: Crystal structure of a C-terminal 11-residue recruitment peptide of P53 in complex with CDK2/CyclinA " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.376_386" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:12501191" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://identifiers.org/pubmed:27179590", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://disprot.org/DP00086r086", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: In contrast, the behavior of the C-terminal domain was best characterized as unstructured and highly mobile, with chemical shift values close to random coil. " } ], "http://schema.org/name": [ { "@value": "disorder" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.361_393" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:15342238" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000002" } ] }, { "@id": "https://disprot.org/DP00086r049", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: We show that the N-terminal domain of USP7 binds two closely spaced 4-residue sites in both p53 and MDM2, falling between p53 residues 359-367 and MDM2 residues 147-159. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.359_367" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:16474402" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://disprot.org/DP00086r078", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: The N-terminal region is dynamically disordered in the full-length p53 tetramer, fluctuating between states in which it is free and fully exposed to solvent and states in which it makes transient contacts with the DNA-binding domain (DBD). Results: In addition to the chemical shift changes, residues in both AD1 and AD2 have decreased cross-peak intensity in the p53 tetramer relative to the peptide (Fig. 2C). While the intensity loss is greater for AD2 than AD1, it is clear that intramolecular interactions within full-length p53 affect the conformational ensemble and dynamics of both motifs. Results: Cross-peaks in spectra of 15N-labeled p53(1\u201361), p53(1\u2013312), and 15NNTAD\u2013p53 fall along a line, suggesting that p53(1\u2013312) and the segmentally labeled full-length p53 experience the same two-site exchange process between states in which the NTAD is free or bound to the DBD. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_61" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:30420502" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://disprot.org/DP00086r063", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: Here, we report the NMR structure of the complex of the Taz2 (C/H3) domain of p300 and the N-terminal transactivation domain of p53. In the complex, p53 forms a short alpha helix and interacts with the Taz2 domain through an extended surface. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_39" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:19217391" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://disprot.org/DP00086r075", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: The p53 TAD2 in the complex is unstructured except for a short amphipathic \u03b1 helix involving residues 47\u201355. Results: Chemical shift analysis and the NOE pattern demonstrated that p53 in complex with Tfb1 adopts an a-helical fold that extends from Pro47 to Thr55. Outside this region, p53 is flexible, as also supported by the 15N-1H heteronuclear NOE data. " } ], "http://schema.org/name": [ { "@value": "disorder" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.20_46" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:16793543" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000002" } ] }, { "@id": "https://disprot.org/assets/data/IDPO_v0.3.owl", "@type": [ "http://schema.org/DefinedTermSet" ], "http://schema.org/name": [ { "@value": "IDP ontology" } ] }, { "@id": "https://idpregistry.org/#sequence-range.20_73", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 73 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 20 } ] }, { "@id": "https://identifiers.org/pubmed:16234232", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://disprot.org/DP00086r033", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to a 15-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.15_29" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:8875929" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://identifiers.org/pubmed:18391200", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://disprot.org/DP00086r082", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: With the spin label at S15C, cross-peaks of residues in both the AD1 and AD2 regions are broadened; similarly, attachment of the spin label at P58C broadens resonances associated with both the AD2 and AD1 motifs, confirming the presence of interactions between these motifs (SI Appendix, Fig. S4). Transient interactions between the AD1 and AD2 regions have been observed previously in isolated NTAD peptides (59). In addition, selective resonance broadening is observed for several DBD cross-peaks (SI Appendix, Fig. S4), indicating intramolecular interactions between the spin labeled NTAD and the DBD. Results: With the spin label at P58C (AD2), the largest PRE is observed for residues located in the DNA-binding site; these include T118 and V122 in the L1 loop, G245 and to a lesser extent N247 in the L3 loop, A276, and G279, R280, and R283 in the C-terminal helix. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.38_61" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:30420502" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://identifiers.org/pubmed:16768447", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://identifiers.org/pubmed:11524676", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://disprot.org/DP00086r013", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "nuclear magnetic resonance spectroscopy evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: RDC analysis showed that the isolated domain p53(1\u201393) was an IDP with two regions of nascent secondary structure. " } ], "http://schema.org/name": [ { "@value": "disorder" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_93" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:18391200" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000002" } ] }, { "@id": "https://idpregistry.org/#sequence-range.379_385", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 385 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 379 } ] }, { "@id": "https://idpregistry.org/#sequence-range.1_93", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 93 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 1 } ] }, { "@id": "https://disprot.org/DP00086r018", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "X-ray crystallography-based structural model with missing residue coordinates used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: Our final model of the quadruple mutant comprises residues 96\u2013290 for both molecules in the asymmetric unit. As in the structure of wild type, the C-terminal residues up to Thr-312 are disordered. " } ], "http://schema.org/name": [ { "@value": "disorder" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.291_312" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:14534297" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000002" } ] }, { "@id": "https://disprot.org/DP00086r048", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: The crystal structure of a ternary complex of Set9 with a p53 peptide and the cofactor product S-adenosyl-l-homocysteine (AdoHcy) provides the molecular basis for recognition of p53 by this lysine methyltransferase. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.369_377" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:15525938" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://idpregistry.org/#sequence-range.20_46", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 46 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 20 } ] }, { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT", "@type": [ "http://schema.org/CreativeWork" ] }, { "@id": "https://idpregistry.org/#sequence-range.369_377", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 377 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 369 } ] }, { "@id": "https://disprot.org/DP00086r030", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Abstract: In contrast, the N-terminal p53 transactivation domain is largely disordered in solution, but residues 37-57 fold into two amphipathic helices, H1 and H2, upon binding with RPA70N. " } ], "http://schema.org/name": [ { "@value": "disorder to order" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.37_57" } ], "http://schema.org/sequenceValue": [ { "@value": "disorder to order" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:16234232" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/IDPO:0000011" } ] }, { "@id": "https://idpregistry.org/#sequence-range.37_57", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 57 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 37 } ] }, { "@id": "https://disprot.org/IDPO/IDPO:0000042", "@type": [ "http://schema.org/DefinedTerm" ], "http://schema.org/inDefinedTermSet": [ { "@id": "https://disprot.org/assets/data/IDPO_v0.3.owl" } ], "http://schema.org/name": [ { "@value": "methylation display site" } ], "http://schema.org/termCode": [ { "@value": "IDPO:0000042" } ] }, { "@id": "https://disprot.org/IDPO/IDPO:0000002", "@type": [ "http://schema.org/DefinedTerm" ], "http://schema.org/inDefinedTermSet": [ { "@id": "https://disprot.org/assets/data/IDPO_v0.3.owl" } ], "http://schema.org/name": [ { "@value": "disorder" } ], "http://schema.org/termCode": [ { "@value": "IDPO:0000002" } ] }, { "@id": "https://idpregistry.org/#sequence-range.19_26", "@type": [ "http://schema.org/SequenceRange" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceRange/0.2-DRAFT" } ], "http://schema.org/rangeEnd": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 26 } ], "http://schema.org/rangeStart": [ { "@type": "http://www.w3.org/2001/XMLSchema#integer", "@value": 19 } ] }, { "@id": "https://identifiers.org/pubmed:18677113", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://identifiers.org/pubmed:30420502", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://disprot.org/DP00086r074", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "bait-prey hybrid interaction evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Results: As shown in Fig.3Band Table I, the levels of TBP precipitated by GST-p53 TAD and mutant derivatives are linearly correlated with the abilityof transactivation in vivo. " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.1_73" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:7559631" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] }, { "@id": "https://identifiers.org/pubmed:19217391", "@type": [ "http://schema.org/ScholarlyArticle" ] }, { "@id": "https://disprot.org/DP00086r062", "@type": [ "http://schema.org/SequenceAnnotation" ], "http://purl.org/dc/terms/conformsTo": [ { "@id": "https://bioschemas.org/profiles/SequenceAnnotation/0.7-DRAFT" } ], "http://schema.org/creationMethod": [ { "@value": "x-ray crystallography evidence used in manual assertion" } ], "http://schema.org/description": [ { "@value": "Curator statement: Crystal structure of a C-terminal peptide of P53 in complex with Sirt1 " } ], "http://schema.org/name": [ { "@value": "protein binding" } ], "http://schema.org/sequenceLocation": [ { "@id": "https://idpregistry.org/#sequence-range.379_385" } ], "http://schema.org/sequenceValue": [ { "@value": "protein binding" } ], "http://schema.org/subjectOf": [ { "@id": "https://identifiers.org/pubmed:26134520" } ], "http://schema.org/valueReference": [ { "@id": "https://disprot.org/IDPO/GO:0005515" } ] } ], "@id": "https://disprot.org/DP00086#html-jsonld" } ]