CREB-binding protein (CREBBP/CBP) is a transcriptional coregulator and protein lysine acetyltransferase that couples sequence-specific transcription factors to chromatin modification and transcriptional machinery. Its nuclear activities include acetylation of histones and nonhistone regulators and promotion of RNA polymerase II transcription, with repressive effects in particular regulatory contexts. It also modifies cytoplasmic substrates. Substrate-specific studies establish MRE11 lactylation during DNA repair and N-terminal ubiquitin-chain extension activity toward primed p53 in the cytoplasmic fractions studied. Multiple interaction domains support distinct protein assemblies rather than a single invariant complex. Pathogenic CREBBP variation causes RubinsteinβTaybi syndrome; the two protein products differ within the N-terminal recruitment region, and their functional equivalence is not established.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000122 negative regulation of transcription by RNA polymerase II | IDA PMID:21539536 KrΓΌppel-like Factor 4 activates HBG gene expression in prima... | KEEP AS NON CORE | Summary: Contextual repression of an erythroid Pol II reporter. Reason: The original KLF4/HBG experiments show a real CREBBP-dependent repressive effect, including murine CREBBP overexpression in human K562 reporter assays and endogenous human erythroid co-occupancy. This specific negative regulation is compatible with the predominant coactivator role; it is not a universal repressor function. |
| GO:0000123 histone acetyltransferase complex | IBA GO_REF:0000033 | ACCEPT | Summary: Conserved membership in histone acetyltransferase complexes. Reason: The actual PTHR13808 tree places human PTN002492802 below the GO:0000123 IBD at PTN000351795, with the target sequence recovered exactly from the MSA. Native CBPβP/CAF association and direct CBP catalytic evidence support this conserved complex context; neither donor count nor self-source identity is a defect. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000351795 SUPPORTS TRANSFER The actual on-path ancestral IBD and exact target MSA support this conserved assertion. Extant experimental records are preserved separately, including legitimate target evidence. |
| GO:0000123 histone acetyltransferase complex | IEA GO_REF:0000002 | ACCEPT | Summary: The mapped HAT complex context is appropriate. Reason: The literal IPR014744 CBP/p300-family assignment matches the official target record, and biochemical CBPβP/CAF association supports the complex class. This is not a claim of one fixed universal CREBBP complex stoichiometry. |
| GO:0000785 chromatin | IDA PMID:21539536 KrΓΌppel-like Factor 4 activates HBG gene expression in prima... | ACCEPT | Summary: CREBBP associates with chromatin in the erythroid transcription system. Reason: The actual KLF4/CREBBP co-occupancy and chromatin experiments support chromatin localization. The contextual repression measured in the same paper does not negate this positive compartment assertion. |
| GO:0001223 transcription coactivator binding | IEA GO_REF:0000117 | ACCEPT | Summary: Coactivator binding is a supported interaction class. Reason: The current ARBA00089003 rule has a complete matching branch for CREBBP, and positive interactions with established coactivators such as CITED1 and NCOA6 support the biological class. This does not mean every CREBBP partner is itself a coactivator. |
| GO:0001223 transcription coactivator binding | IPI PMID:11349124 A novel zinc finger protein TReP-132 interacts with CBP/p300... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: TRERF1 is an actual promoter-DNA-binding transcriptional regulator in the source abstract, corroborated by the official partner record. GO:0001223 explicitly describes non-DNA-binding coactivators. Preserve the positive interaction and refine its partner class; this is not a wrong-gene rejection. Proposed replacements: DNA-binding transcription factor binding |
| GO:0002039 p53 binding | IPI PMID:9194565 Binding and modulation of p53 by p300/CBP coactivators. | ACCEPT | Summary: The experimentally grounded p53 interaction is retained. Reason: The source supports TP53 binding by CBP. This is more informative than generic protein binding and remains valid independently of the direction of a particular reporter response. |
| GO:0002223 stimulatory C-type lectin receptor signaling pathway | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: A contextual transcriptional contribution to C-type lectin receptor signaling. Reason: CREBBP participates through downstream RelA acetylation/coactivation rather than serving as the carbohydrate receptor. The actual Reactome pathway has a positive typed path to nuclear Q92793 through its RelA event; the pathway-level role is real but one of many signaling contexts. |
| GO:0002223 stimulatory C-type lectin receptor signaling pathway | TAS Reactome:R-HSA-5621481 | KEEP AS NON CORE | Summary: A contextual transcriptional contribution to C-type lectin receptor signaling. Reason: CREBBP participates through downstream RelA acetylation/coactivation rather than serving as the carbohydrate receptor. The actual Reactome pathway has a positive typed path to nuclear Q92793 through its RelA event; the pathway-level role is real but one of many signaling contexts. |
| GO:0003682 chromatin binding | IDA PMID:24939902 CBP and p300 acetylate PCNA to link its degradation with nuc... | ACCEPT | Summary: Chromatin-associated CBPβPCNA interaction is directly supported. Reason: The actual source fractionates soluble and chromatin-bound material and detects CBPβPCNA association in UV-treated chromatin. This supports chromatin binding without requiring a claim that CBP directly recognizes a DNA lesion. |
| GO:0003682 chromatin binding | IEA GO_REF:0000117 | ACCEPT | Summary: The electronic chromatin-binding assertion matches established target biology. Reason: ARBA00027831 has a complete current target match, and the target experiments in PMID:24939902 independently establish chromatin-associated CBP. The positive broad chromatin-binding term is retained. |
| GO:0003684 damaged DNA binding | IDA PMID:24939902 CBP and p300 acetylate PCNA to link its degradation with nuc... | UNDECIDED | Summary: Lesion-specific DNA binding remains unresolved despite positive repair evidence. Reason: The actual Methods/Results establish direct CBP-fragment binding to PCNA, association with UV-damaged chromatin and PCNA acetylation/turnover during nucleotide-excision repair. They do not resolve whether the target molecular interaction is binding to damaged DNA itself or recruitment through chromatin proteins. Retain the original IDA assertion as unresolved, not contradicted; the positive chromatin and repair annotations remain supported. Supporting Evidence: PMID:24939902 CBP interacts with PCNA in vivo, and the interaction increased after DNA damage. |
| GO:0003684 damaged DNA binding | IEA GO_REF:0000117 | UNDECIDED | Summary: The matched rule does not settle the damaged-DNA interaction scope. Reason: ARBA00089041 has a complete current target match, so this is not a missing-rule problem. The available target evidence establishes damaged-chromatin/PCNA association but does not distinguish lesion-DNA binding from protein-mediated recruitment. The specific molecular claim remains unresolved while chromatin binding and repair regulation stay positive. |
| GO:0003712 transcription coregulator activity | IEA GO_REF:0000002 | ACCEPT | Summary: Broad coregulator activity accommodates activation and contextual repression. Reason: The official KIX/domain mappings and extensive coactivation evidence support transcription coregulation. The actual PMID:21539536 erythroid repression results additionally support a negative regulatory context, so narrowing every coregulator assertion to coactivation would lose legitimate biology. |
| GO:0003713 transcription coactivator activity | IBA GO_REF:0000033 | ACCEPT | Summary: Conserved transcriptional coactivation is well grounded. Reason: Human CREBBP lies below the actual GO:0003713 IBD at PTN000351795. The target and extant descendant experimental records are positive grounding for an ancestral judgment, not circularity when the target is named among them. Direct coactivation experiments corroborate retention. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000351795 SUPPORTS TRANSFER The actual on-path ancestral IBD and exact target MSA support this conserved assertion. Extant experimental records are preserved separately, including legitimate target evidence. |
| GO:0003713 transcription coactivator activity | IDA PMID:12169688 The role of Sp1 and AP-2 in basal and protein kinase A--indu... | ACCEPT | Summary: The source-specific transcription-coactivator assertion is retained. Reason: The actual indexed original and abstract report Sp1/AP-2 control of the rat SPT promoter in HepG2 assays, with CBP enhancing Sp1/PKA-driven transcription. This is promoter coactivation, not proof that CBP itself binds the Sp1 recognition sequence. |
| GO:0003713 transcription coactivator activity | IDA PMID:12586840 Physical and functional interactions among AP-2 transcriptio... | ACCEPT | Summary: The source-specific transcription-coactivator assertion is retained. Reason: The abstract reports CBP and p300 coactivation of TFAP2A in the presence of CITED2 and tests CBP-heterozygous mouse fibroblasts. The detailed co-IP, mutant and two-hybrid examples foreground p300; the positive CBP coactivator assertion is retained with that distinction and the full-text access limit. |
| GO:0003713 transcription coactivator activity | IDA PMID:12929931 P300/CBP acts as a coactivator to cartilage homeoprotein-1 (... | ACCEPT | Summary: The source-specific transcription-coactivator assertion is retained. Reason: The structured abstract explicitly reports CBP and p300 enhancement of Cart1-dependent transcription, while several localization and acetylation experiments are described specifically for p300. Retain the positive CBP coactivator assertion at that directly stated transcriptional scope without reassigning p300-specific experiments. |
| GO:0003713 transcription coactivator activity | IDA PMID:14645221 Histone acetyltransferase-dependent chromatin remodeling and... | ACCEPT | Summary: The source-specific transcription-coactivator assertion is retained. Reason: CBP associates with CLOCK and NPAS2 and supports circadian transcriptional activation. Partner binding and coactivation are positive; this does not make CREBBP the sequence-specific clock DNA-binding factor. |
| GO:0003713 transcription coactivator activity | IEA GO_REF:0000120 | ACCEPT | Summary: Independent rule and family mappings support coactivation. Reason: Current ARBA00028308 and IPR014744 match the target and agree with its experimentally established promoter-associated coactivation. These are retained as their original electronic sources, without converting them into direct experiments. |
| GO:0003713 transcription coactivator activity | IPI PMID:8684459 A p300/CBP-associated factor that competes with the adenovir... | ACCEPT | Summary: CBP recruits a histone acetylase as part of coactivation. Reason: The complete original shows CBP fragments and native CBP associated with P/CAF. The acetylase assay in this paper is P/CAF/hGCN5, not intrinsic CBP catalysis. The original self WITH/FROM on the coactivator row is preserved without inventing homodimerization. |
| GO:0003713 transcription coactivator activity | TAS PMID:10362258 Cooperation of Sp1 and p300 in the induction of the CDK inhi... | ACCEPT | Summary: The source-specific transcription-coactivator assertion is retained. Reason: The recovered complete original assays p300 constructs and antibodies in rat PC12 cells. CBP is discussed as related coactivator/HAT background; retain the biologically valid TAS assertions without claiming this paper directly assayed CBP. |
| GO:0003713 transcription coactivator activity | TAS PMID:10893273 CREB-binding protein (CBP)/p300 and RNA polymerase II coloca... | ACCEPT | Summary: The source-specific transcription-coactivator assertion is retained. Reason: The complete selected abstract establishes confocal nuclear localization, Pol II coassociation and transcription-dependent redistribution of CBP. The cache contains full text; the detailed reading boundary here was the abstract, not failed full-text access. The biologically appropriate TAS coactivator assertion is retained without invented construct details. |
| GO:0003713 transcription coactivator activity | TAS PMID:11001584 The sonic hedgehog-patched-gli pathway in human development ... | ACCEPT | Summary: The source-specific transcription-coactivator assertion is retained. Reason: This is a review of HedgehogβPatchedβGLI biology. Its CBP section and Figure 1 caption discuss human GLI3 interaction with mouse CBP and developmental inference from RubinsteinβTaybi syndrome; they are not new human CREBBP developmental experiments. |
| GO:0003714 transcription corepressor activity | IDA PMID:21539536 KrΓΌppel-like Factor 4 activates HBG gene expression in prima... | KEEP AS NON CORE | Summary: A real but contextual corepressor activity is retained. Reason: The KLF4/HBG reporter experiments demonstrate reduced transcription with CREBBP in the assayed erythroid context. The murine expression construct and endogenous human interaction/chromatin evidence are distinguished; this does not replace the predominant coactivator description. Supporting Evidence: PMID:21539536 These data support functional antagonism between KLF4 and CREBBP in HBG gene regulation. |
| GO:0004402 histone acetyltransferase activity | EXP PMID:21131905 Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-med... | ACCEPT | Summary: The histone-acetyltransferase assertion remains supported. Reason: The recovered original uses mouse CBP/p300 deletion experiments to establish H3K18/H3K27 acetylation requirements and transcriptional consequences. These are not purified human CBP-only assays; the conserved catalytic claims remain supported. |
| GO:0004402 histone acetyltransferase activity | EXP PMID:24616510 Binding of the histone chaperone ASF1 to the CBP bromodomain... | ACCEPT | Summary: The histone-acetyltransferase assertion remains supported. Reason: The recovered main source relates ASF1 interaction with the CBP bromodomain to histone acetylation, including H3K56 context. Supplementary material was not recovered; site-specific and construct claims are limited to the actual main text. |
| GO:0004402 histone acetyltransferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: The ancestral histone-acetyltransferase placement is appropriate. Reason: The actual GO:0004402 IBD is on the target path in the PTHR13808 tree. Complete literal donor records, including plant/fly/worm/mammalian products, and direct human CBP experiments support conservation; no target-specific catalytic loss is evident. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000351795 SUPPORTS TRANSFER The actual on-path ancestral IBD and exact target MSA support this conserved assertion. Extant experimental records are preserved separately, including legitimate target evidence. |
| GO:0004402 histone acetyltransferase activity | IDA PMID:11742995 Activation of AML1-mediated transcription by MOZ and inhibit... | ACCEPT | Summary: The histone-acetyltransferase assertion remains supported. Reason: The recovered original distinguishes human CBP from MOZ and the MOZβCBP fusion. CBP acetylates histones and AML1 and stimulates the tested Pol II reporters; fusion-mediated repression must not be attributed to normal CBP. |
| GO:0004402 histone acetyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Conserved catalytic-domain and reaction mappings support histone acetylation. Reason: The official target contains the mapped CBP/p300 catalytic regions and the source retains its RHEA21992 mapping. Actual CBP histone acetylation provides independent target grounding; no inference of all-product equivalence follows. |
| GO:0004402 histone acetyltransferase activity | TAS PMID:10362258 Cooperation of Sp1 and p300 in the induction of the CDK inhi... | ACCEPT | Summary: The histone-acetyltransferase assertion remains supported. Reason: The recovered complete original assays p300 constructs and antibodies in rat PC12 cells. CBP is discussed as related coactivator/HAT background; retain the biologically valid TAS assertions without claiming this paper directly assayed CBP. |
| GO:0005515 protein binding | IPI PMID:10049825 Differences in the interactions of oncogenic adenovirus 12 e... | KEEP AS NON CORE | Summary: Retain the positive source-specific interaction with its assay limits. Reason: The complete available abstract compares Ad12 and Ad2 E1A binding to p300 and CBP. CBP association requires the E1A amino terminus plus CR1, whereas the reported colTRE repression is explicitly p300-dependent and not CBP-dependent. The positive CBPβE1A interaction is retained without inferring a CBP acetyltransferase-modulation assay; full original Methods remain unavailable. No more informative supported partner class is assigned; the positive generic interaction remains non-core. The CLINGEN_MENDELIAN Curation instructions retain supported positive protein-binding annotations as KEEP_AS_NON_CORE when no evidence-backed narrower class is established; the stated source and assay limits still apply. Supporting Evidence: PMID:10049825 the amino-terminus and CR1 are necessary to associate with CBP |
| GO:0005515 protein binding | IPI PMID:10196247 Characterization of an E1A-CBP interaction defines a novel t... | KEEP AS NON CORE | Summary: Retain the positive source-specific interaction with its assay limits. Reason: The abstract and the selected original Discussion characterize E1A binding to the CBP C/H3 TRAM, competition with TRAM-binding transcription factors, and CBP-fragment binding to p53 that competes with MDM2. They do not report E1A acetylation or E1AβCtBP association. The protected main extraction contains the abstract and Discussion, not the complete Methods and Results. No more informative supported partner class is assigned; the positive generic interaction remains non-core. The CLINGEN_MENDELIAN Curation instructions retain supported positive protein-binding annotations as KEEP_AS_NON_CORE when no evidence-backed narrower class is established; the stated source and assay limits still apply. |
| GO:0005515 protein binding | IPI PMID:10196247 Characterization of an E1A-CBP interaction defines a novel t... | MODIFY | Summary: Refine the positive TP53 interaction to p53 binding. Reason: The abstract and the selected original Discussion characterize E1A binding to the CBP C/H3 TRAM, competition with TRAM-binding transcription factors, and CBP-fragment binding to p53 that competes with MDM2. They do not report E1A acetylation or E1AβCtBP association. The protected main extraction contains the abstract and Discussion, not the complete Methods and Results. GO:0002039 preserves the positive interaction while naming the verified TP53 partner. Proposed replacements: p53 binding |
| GO:0005515 protein binding | IPI PMID:10347196 Identification of a novel SNF2/SWI2 protein family member, S... | KEEP AS NON CORE | Summary: Retain the positive source-specific interaction with its assay limits. Reason: The complete available abstract identifies SRCAP as a CBP-interacting ATPase that enhances CBP-dependent transcription; E1A disrupts the SRCAPβCBP interaction. The existing viral E1A pair is retained with curator deference and the full-text access limit, without presenting the abstract as a complete pairwise-assay account. No more informative supported partner class is assigned; the positive generic interaction remains non-core. The CLINGEN_MENDELIAN Curation instructions retain supported positive protein-binding annotations as KEEP_AS_NON_CORE when no evidence-backed narrower class is established; the stated source and assay limits still apply. |
| GO:0005515 protein binding | IPI PMID:10428834 Retinoid-dependent recruitment of a histone H1 displacement ... | KEEP AS NON CORE | Summary: Retain the positive interaction at its source-specific scope. Reason: HMGA1 is an architectural AT-rich DNA-binding protein. A generic coactivator or sequence-specific transcription-factor class is not established by the available material. The positive curated association is retained; the abstract foregrounds RAR and does not resolve the CBP assay details, and the complete original was not recovered. The CLINGEN_MENDELIAN Curation instructions retain supported positive protein-binding annotations as KEEP_AS_NON_CORE when no evidence-backed narrower class is established; the stated source and assay limits still apply. |
| GO:0005515 protein binding | IPI PMID:10722728 The MSG1 non-DNA-binding transactivator binds to the p300/CB... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: CITED1/MSG1 is explicitly a non-DNA-binding coactivator in the source, which also reports CBP/p300 binding and functional coupling to SMADs. Do not turn the interaction into direct DNA binding by CBP. Proposed replacements: transcription coactivator binding |
| GO:0005515 protein binding | IPI PMID:10722738 cAMP-independent activation of the adenovirus type 12 E2 pro... | KEEP AS NON CORE | Summary: Retain the positive source-specific interaction with its assay limits. Reason: Adenoviral E1A interacts with CBP/p300 through distinct regions; the source-specific P03259-2 record is preserved, without a claim of endogenous human partner activity. No more informative supported interaction class is assigned here; the existing positive record is not removed merely for being contextual or generic. The CLINGEN_MENDELIAN Curation instructions retain supported positive protein-binding annotations as KEEP_AS_NON_CORE when no evidence-backed narrower class is established; the stated source and assay limits still apply. |
| GO:0005515 protein binding | IPI PMID:10823891 The Huntington's disease protein interacts with p53 and CREB... | MODIFY | Summary: Refine the positive TP53 interaction to p53 binding. Reason: Polyglutamine-expanded huntingtin associates with CBP and affects CBP-dependent transcription. Preserve both HTT and TP53 interaction records without using disease sequestration as a distinct normal CREBBP core function. GO:0002039 preserves the positive interaction while naming its verified TP53 partner. Proposed replacements: p53 binding |
| GO:0005515 protein binding | IPI PMID:10823891 The Huntington's disease protein interacts with p53 and CREB... | KEEP AS NON CORE | Summary: Retain the positive source-specific interaction with its assay limits. Reason: Polyglutamine-expanded huntingtin associates with CBP and affects CBP-dependent transcription. Preserve both HTT and TP53 interaction records without using disease sequestration as a distinct normal CREBBP core function. No more informative supported interaction class is assigned here; the existing positive record is not removed merely for being contextual or generic. The CLINGEN_MENDELIAN Curation instructions retain supported positive protein-binding annotations as KEEP_AS_NON_CORE when no evidence-backed narrower class is established; the stated source and assay limits still apply. |
| GO:0005515 protein binding | IPI PMID:10866662 A new family of nuclear receptor coregulators that integrate... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: NCOA6/hNRC is a nuclear-receptor coactivator. The recovered Methods and Results show endogenous CBP associated with full-length GST-hNRC in 293T cells, with GST and hNRC(1β852) negative controls; the literal human pair pull-down agrees. This supports transcription coactivator binding at cellular-association scope. It does not establish a purified direct pair, a minimal CBP-binding interface, a universal intact complex or a numbered CREBBP product. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:10866662 CBP was identified bound to GST-hNRC but not to GST-hNRC(1-852) or GST alone |
| GO:0005515 protein binding | IPI PMID:11568182 Interaction of EVI1 with cAMP-responsive element-binding pro... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: EVI1/MECOM interacts with CBP and modulates transcription. Retain the exact MECOM partner identity and distinguish its DNA-binding regulatory role from the effects of an individual reporter assay. The exact partner UniProtKB:Q03112 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:11799127 The interaction of Pax5 (BSAP) with Daxx can result in trans... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: The actual DAXX paper reports both corepression and coactivation with CBP-containing complexes; coregulator binding retains both directions. Literal records include one spoke-expanded complex association. Do not call every record a purified binary interaction or choose a repressor-only class from the official opening sentence. Proposed replacements: transcription coregulator binding |
| GO:0005515 protein binding | IPI PMID:11897665 Prothymosin alpha interacts with the CREB-binding protein an... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: The recovered Results establish endogenous HeLa CBP association and ProTalpha-dependent enhancement of CBP-driven transcription. ProTalpha requires recruitment and is not an autonomous DNA-binding activator. Preserve the rat expression-construct/bovine peptide context separately from endogenous human association. Proposed replacements: transcription coactivator binding |
| GO:0005515 protein binding | IPI PMID:11940655 Dual roles of p300 in chromatin assembly and transcriptional... | KEEP AS NON CORE | Summary: Retain the positive interaction at its source-specific scope. Reason: NAP1L1 is a histone chaperone, not automatically a protein-folding chaperone. The literal CBP pair is positive, including a histone-dependent pull-down and native co-IP. Do not transfer p300 chromatin-assembly catalysis to CBP or claim that binding the chaperone is histone binding. The CLINGEN_MENDELIAN Curation instructions retain supported positive protein-binding annotations as KEEP_AS_NON_CORE when no evidence-backed narrower class is established; the stated source and assay limits still apply. |
| GO:0005515 protein binding | IPI PMID:12435739 Regulation of E2A activities by histone acetyltransferases i... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: CBP interacts with and acetylates E2A/TCF3 and regulates its transcriptional function. The specific P15923-2 source identity is preserved; no isoform-exclusive activity is inferred. The exact partner UniProtKB:P15923-2 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:12482968 Activating signal cointegrator 2 belongs to a novel steady-s... | UNDECIDED | Summary: The positive CBPβASC2 assertion remains unresolved at this paper-specific assay scope. Reason: The available complete main Methods, Results and Discussion describe HeLa ASCOM fractionation and anti-ASC2 immunoprecipitation. A minor CBP peak partly comigrated with ASC2, but CBP was not co-immunoprecipitated from those fractions (Results, Figure 2B experiment). No positive CBPβASC2 assay was identified in this main text; complete figure captions and figure pixels were not inspected. The original IPI source assertion is therefore unresolved rather than replaced by evidence from another paper. Independent PMID:10866662 supports the separate positive NRC interaction row, but cannot authenticate this source-specific assertion. The negative fraction result does not establish absence of CBPβASC2 binding under all conditions. Supporting Evidence: PMID:12482968 both SRC-1 and CBP were not coimmunoprecipitated by anti-ASC-2 antibody in these fractions |
| GO:0005515 protein binding | IPI PMID:14645221 Histone acetyltransferase-dependent chromatin remodeling and... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: CBP associates with CLOCK and NPAS2 and supports circadian transcriptional activation. Partner binding and coactivation are positive; this does not make CREBBP the sequence-specific clock DNA-binding factor. The exact partner UniProtKB:O15516 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:14645221 Histone acetyltransferase-dependent chromatin remodeling and... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: CBP associates with CLOCK and NPAS2 and supports circadian transcriptional activation. Partner binding and coactivation are positive; this does not make CREBBP the sequence-specific clock DNA-binding factor. The exact partner UniProtKB:Q99743 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:14716005 Dendrite development regulated by CREST, a calcium-regulated... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: CREST/SS18L1 is a transcriptional coactivator, with CBP interaction reported in the source abstract. The literal partner accession is RAT Q91XJ0; retain it and do not silently substitute the human ortholog or claim an exclusively human assay. Proposed replacements: transcription coactivator binding |
| GO:0005515 protein binding | IPI PMID:14759370 Structural mechanism of the bromodomain of the coactivator C... | MODIFY | Summary: Refine the positive TP53 interaction to p53 binding. Reason: The abstract directly reports CBP bromodomain recognition of p53 acetylated at K382 and an NMR structure with an acetyl-p53 peptide. This supports p53 binding; it is not a CBP-catalyzed p53 acetylation assay. GO:0002039 preserves the positive interaction while naming its verified TP53 partner. Proposed replacements: p53 binding |
| GO:0005515 protein binding | IPI PMID:15075319 Positive and negative modulation of the transcriptional acti... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: ELF3 interacts with CBP/p300 in transcriptional regulation. The positive association supports the verified DNA-binding transcription-factor partner class. The exact partner UniProtKB:P78545 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:15126506 FOXO4 is acetylated upon peroxide stress and deacetylated by... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: The paper concerns FOXO-family regulation and CBP/p300 interactions. The original FOXO3 source partner is preserved even though other family members are prominent in the abstract; no paralog-misattribution claim is made from incomplete text. The exact partner UniProtKB:O43524 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:15220471 Silent information regulator 2 potentiates Foxo1-mediated tr... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: FOXO1 interacts with CBP and undergoes regulated acetylation. The positive partner and activity context is retained without assuming that every acetylation event activates transcription. The exact partner UniProtKB:Q12778 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:15273251 Site-specific acetylation of the fetal globin activator NF-E... | KEEP AS NON CORE | Summary: Retain the positive interaction at its source-specific scope. Reason: NFE4 participates in the stage-selector complex. The abstract foregrounds PCAF and does not resolve the exact CBP pair assay or autonomous sequence-specific DNA recognition by NFE4. Preserve the positive curated CBP association with its full-text access limit; no more specific partner class is established. The CLINGEN_MENDELIAN Curation instructions retain supported positive protein-binding annotations as KEEP_AS_NON_CORE when no evidence-backed narrower class is established; the stated source and assay limits still apply. |
| GO:0005515 protein binding | IPI PMID:16043483 MEF2-dependent recruitment of the HAND1 transcription factor... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: The abstract establishes MEF2βHAND1 interaction and proposes CBP co-recruitment as a mechanism for synergy. Preserve the positive curated MEF2AβCBP and HAND1βCBP pairs with curator deference and the full-text limit; direct CBP pair assays are not claimed from this abstract. HAND1 DNA binding being dispensable in this context does not abolish its established transcription-factor class. The exact partner UniProtKB:Q02078 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:16154084 Crystal structure of IRF-3 in complex with CBP. | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: IRF3 interacts with CBP in antiviral transcriptional activation. Retain the positive protein association with its transcription-factor partner class. The exact partner UniProtKB:Q14653 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:16291753 A splice variant of stress response gene ATF3 counteracts NF... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: CBP/RelA association contributes to NF-kappaB transcriptional regulation. The interaction is retained without conflating CBP with the upstream signaling kinase. The exact partner UniProtKB:Q04206 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:16611888 Targeting of p300/CREB binding protein coactivators by simia... | KEEP AS NON CORE | Summary: Retain the positive source-specific interaction with its assay limits. Reason: SV40 large T antigen associates with CBP/p300 in a complex whose formation depends on p53. Positive complex association is retained without asserting an unmediated large-TβCBP interface. No more informative supported interaction class is assigned here; the existing positive record is not removed merely for being contextual or generic. The CLINGEN_MENDELIAN Curation instructions retain supported positive protein-binding annotations as KEEP_AS_NON_CORE when no evidence-backed narrower class is established; the stated source and assay limits still apply. |
| GO:0005515 protein binding | IPI PMID:16799563 An ARC/Mediator subunit required for SREBP control of choles... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: The source compares CBP interactions with CREB1 and sterol-regulatory factors. Exact SREBF1 product identities and SREBF2 are retained; partner-class refinements do not imply equivalent affinity among them. The exact partner UniProtKB:P16220 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:16799563 An ARC/Mediator subunit required for SREBP control of choles... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: The source compares CBP interactions with CREB1 and sterol-regulatory factors. Exact SREBF1 product identities and SREBF2 are retained; partner-class refinements do not imply equivalent affinity among them. The exact partner UniProtKB:P36956-1 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:16799563 An ARC/Mediator subunit required for SREBP control of choles... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: The source compares CBP interactions with CREB1 and sterol-regulatory factors. Exact SREBF1 product identities and SREBF2 are retained; partner-class refinements do not imply equivalent affinity among them. The exact partner UniProtKB:P36956-3 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:16799563 An ARC/Mediator subunit required for SREBP control of choles... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: The source compares CBP interactions with CREB1 and sterol-regulatory factors. Exact SREBF1 product identities and SREBF2 are retained; partner-class refinements do not imply equivalent affinity among them. The exact partner UniProtKB:Q12772 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:17075044 Interaction of GATA-3/T-bet transcription factors regulates ... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: T-bet/TBX21 interaction with CBP is positive in the source context. Retain the transcription-factor partner class without making lymphocyte differentiation a separate universal CREBBP core. The exact partner UniProtKB:Q9UL17 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:17362989 Inhibition of NF-kappaB acetylation and its transcriptional ... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: The source investigates RelAβCBP association in NF-kappaB regulation. Binding is retained at the measured context rather than interpreted as a new enzymatic activity. The exact partner UniProtKB:Q04206 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:17382325 Modulation of p300 binding by posttranslational modification... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: HIF1A recruits CBP in hypoxia-responsive transcription. The positive interaction supports the RNA polymerase II transcription-factor partner class. The exact partner UniProtKB:Q16665 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:17500595 Huntingtin interacting proteins are genetic modifiers of neu... | KEEP AS NON CORE | Summary: Retain the positive source-specific interaction with its assay limits. Reason: The source describes huntingtin and CBP interaction in a disease-related context. Positive binding is retained as contextual, without making polyglutamine sequestration a normal core function. No more informative supported interaction class is assigned here; the existing positive record is not removed merely for being contextual or generic. The CLINGEN_MENDELIAN Curation instructions retain supported positive protein-binding annotations as KEEP_AS_NON_CORE when no evidence-backed narrower class is established; the stated source and assay limits still apply. |
| GO:0005515 protein binding | IPI PMID:17761676 Regulation of IRF-3-dependent innate immunity by the papain-... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: The study supports IRF3 association with CBP during antiviral transcription. Preserve the measured protein interaction rather than transferring an entire immune phenotype to the binding annotation. The exact partner UniProtKB:Q14653 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:17923090 Acetylation-dependent signal transduction for type I interfe... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: IFNAR2 is the beta subunit of the type I interferon receptor. Source-specific recruitment and cytoplasmic association support receptor binding through that subunit. State intracellular receptor-tail contact; this term does not make CBP an interferon ligand or receptor agonist. Preserve the mixed host/construct and spoke-expansion limits. The current definition and ancestors do not require ligand or agonist activity, although all 22 current human exact-term annotations are interferons and the checked intracellular comparators lack this exact term. This refinement follows the demonstrated receptor contact and literal definition, not an established intracellular-use precedent. Proposed replacements: type I interferon receptor binding |
| GO:0005515 protein binding | IPI PMID:18250304 Gain-of-function mutation of GATA-2 in acute myeloid transfo... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: GATA2 interaction with CBP contributes to transcriptional control in the studied system. The positive binding claim and exact partner are preserved. The exact partner UniProtKB:P23769 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:18309294 S-glutathionylation of IRF3 regulates IRF3-CBP interaction a... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: The source concerns IRF3βCBP association and its regulation. The curated positive interaction is retained at its actual transcription-factor partner scope. The exact partner UniProtKB:Q14653 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:18316612 Molecular basis of nuclear factor-kappaB activation by astro... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: The source reports AEG-1/MTDHβCBP co-IP, promoter association and a proposed bridging coactivator role in NF-kappaB transcription. This supports the source-specific cofactor class without treating all MTDH functions as transcriptional or co-IP as a purified direct-binding measurement. Proposed replacements: transcription coactivator binding |
| GO:0005515 protein binding | IPI PMID:18836453 Insights into interferon regulatory factor activation from t... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: IRF5 association with CBP supports a positive DNA-binding transcription-factor interaction. The abstract boundary is retained for detailed assay claims. The exact partner UniProtKB:Q13568 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:19234109 Induction of SOX4 by DNA damage is critical for p53 stabiliz... | MODIFY | Summary: Refine the positive TP53 interaction to p53 binding. Reason: The abstract and selected original Discussion report SOX4 association with p300/CBP, formation of p53-containing complexes and increased p53 K373/K382 acetylation. The protected main extraction contains these sections rather than complete Methods and Results. Duplicate raw TP53-source records remain in their one seeded group; multiplicity is not independent experimental replication. GO:0002039 preserves the positive interaction while naming the verified TP53 partner. Proposed replacements: p53 binding |
| GO:0005515 protein binding | IPI PMID:19234109 Induction of SOX4 by DNA damage is critical for p53 stabiliz... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: The abstract and selected original Discussion report SOX4 association with p300/CBP, formation of p53-containing complexes and increased p53 K373/K382 acetylation. The protected main extraction contains these sections rather than complete Methods and Results. Duplicate raw TP53-source records remain in their one seeded group; multiplicity is not independent experimental replication. SOX4 is an RNA polymerase II DNA-binding transcription factor, so GO:0061629 names the partner class without assigning its DNA-recognition activity to CREBBP. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:19805293 CBP and p300 are cytoplasmic E4 polyubiquitin ligases for p5... | MODIFY | Summary: Refine the positive TP53 interaction to p53 binding. Reason: Actual Results/Methods and recovered captions support CBP-dependent ubiquitin-chain extension after MDM2 priming, bacterial N-terminal activity and endogenous human cytoplasmic corroboration. Human cDNA provenance is supported by U47741, but pRSV versus pcDNA vector names and main/caption quantity units differ. No supplementary-material, catalytic-cysteine, linkage-specific or isoform 2 claim is made. GO:0002039 preserves the positive interaction while naming its verified TP53 partner. Proposed replacements: p53 binding |
| GO:0005515 protein binding | IPI PMID:20541699 Regression of castrate-recurrent prostate cancer by a small-... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: CBP interaction with androgen receptor is positive in the source context. The verified DNA-binding receptor class supports a more informative binding term. The exact partner UniProtKB:P10275 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:20541704 GSK-3 promotes conditional association of CREB and its coact... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: CREB1 and CBP interact in transcriptional regulation. This supports the partner-specific binding class, not an inference that CBP itself recognizes CRE DNA motifs. The exact partner UniProtKB:P16220 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:20581830 The transcription factor MafB antagonizes antiviral response... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: IRF3βCBP association is retained in its antiviral transcription context. The source is not used to manufacture an additional immune process annotation. The exact partner UniProtKB:Q14653 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:21483817 LRP16 integrates into NF-ΞΊB transcriptional complex and is r... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: CBPβRelA binding is positive in the source-specific regulatory context. Preserve the exact partner and distinguish association from a claim about all NF-kappaB pathway steps. The exact partner UniProtKB:Q04206 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:21602890 Loss of Mel-18 induces tumor angiogenesis through enhancing ... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: HIF1AβCBP interaction is retained with the detailed assay-access boundary. The positive interaction is not rejected because of a disease or hypoxia-specific setting. The exact partner UniProtKB:Q16665 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:21670263 Structural and functional characterization of an atypical ac... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: The abstract explicitly tests EKLF activation-domain binding to four CBP/p300 domains. Its NMR complex is with Tfb1PH, not CBP. The cache contains full text; the positive transcription-factor partner assertion is retained without an unverified product-specific construct claim. The exact partner UniProtKB:Q13351 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:21751375 Functional analysis of novel phosphorylation sites of CREB-b... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: The partner is beta-catenin and literal human constructs were tested in a mammalian two-hybrid assay. Preserve the CBP Ser92 regulation and mouse host; binding-class refinement does not establish native interaction in every tissue. Proposed replacements: beta-catenin binding |
| GO:0005515 protein binding | IPI PMID:21903422 Mapping a dynamic innate immunity protein interaction networ... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: The source supports IRF3 association with CBP in antiviral transcription. Preserve its positive interaction and reported context. The exact partner UniProtKB:Q14653 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:23273993 Intestinal tumorigenesis initiated by dedifferentiation and ... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: The literal CBP-beta-catenin co-IP supports the exact partner class. Preserve the beta-catenin Ser33 mutant and activated IKKbeta condition; do not relabel the target as a DNA-binding transcription factor. Proposed replacements: beta-catenin binding |
| GO:0005515 protein binding | IPI PMID:23434580 Akt kinase targets the association of CBP with histone H3 to... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: AKT1 is a serine/threonine protein kinase; three literal co-IP records and the source phosphorylation result support the class. CBP is the substrate in this context, not an inferred kinase activator or inhibitor. Proposed replacements: protein serine/threonine kinase binding |
| GO:0005515 protein binding | IPI PMID:23441852 The corepressor activity of Alien is controlled by CREB-bind... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: The source explicitly assays Alien as a transcriptional corepressor interacting with CBP. Retain the Alien-alpha construct scope rather than assuming all COPS2 products or the intact COP9 signalosome have this role. Acetyltransferase-substrate association is not evidence CBP performs deneddylation. Proposed replacements: transcription corepressor binding |
| GO:0005515 protein binding | IPI PMID:23746807 Structural insights into the functions of TBK1 in innate ant... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: IRF3 interaction with CBP is retained as a positive transcription-factor association. No new upstream signaling activity is inferred from it. The exact partner UniProtKB:Q14653 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:24207024 Repression of RNA polymerase I upon stress is caused by inhi... | KEEP AS NON CORE | Summary: Retain the positive interaction at its source-specific scope. Reason: POLR1E/PAF53 is a Pol I subunit and an experimentally supported CBP acetylation substrate. Binding an isolated subunit does not establish binding the assembled multisubunit Pol I core. Retain the positive association without assigning that broader complex-level binding class. The CLINGEN_MENDELIAN Curation instructions retain supported positive protein-binding annotations as KEEP_AS_NON_CORE when no evidence-backed narrower class is established; the stated source and assay limits still apply. |
| GO:0005515 protein binding | IPI PMID:24361270 Structural insights into acetylated-histone H4 recognition b... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: The actual human CBP bromodomain-PHD module binds acetylated H4 peptides in structures; the bromodomain supplies acetyl-lysine recognition and the PHD has a structural role. Histone binding captures this existing IPI result. The additional chromatin-adaptor function in reader terms is not established solely by this isolated binding assay. Proposed replacements: histone binding Supporting Evidence: PMID:24361270 human CBP in complex with a lysine-acetylated histone H4 peptide |
| GO:0005515 protein binding | IPI PMID:24939902 CBP and p300 acetylate PCNA to link its degradation with nuc... | KEEP AS NON CORE | Summary: Retain the positive interaction at its source-specific scope. Reason: Actual Methods/Results and Figure2 caption show CBP-PCNA association in UV-damaged chromatin and CBP C-terminal pull-down of recombinant PCNA. No precise PCNA-binding class was established in the current searches. Do not replace it with DNA-lesion binding, clamp loading/unloading activity, or a generic enzyme class. The CLINGEN_MENDELIAN Curation instructions retain supported positive protein-binding annotations as KEEP_AS_NON_CORE when no evidence-backed narrower class is established; the stated source and assay limits still apply. |
| GO:0005515 protein binding | IPI PMID:25314079 Acetylation of snail modulates the cytokinome of cancer cell... | MODIFY | Summary: Refine the positive TP53 interaction to p53 binding. Reason: The complete cached abstract directly establishes CBPβSNAIL interaction and SNAIL K146/K187 acetylation. The original GOA interaction partner is TP53; that positive curated pair is preserved with explicit full-text-access and source-resolution limits, not portrayed as a TP53 experiment verified from this SNAIL abstract. GO:0002039 preserves the positive interaction while naming its verified TP53 partner. Proposed replacements: p53 binding |
| GO:0005515 protein binding | IPI PMID:25609649 Proteomic analyses reveal distinct chromatin-associated and ... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: The source supports CBP association with FOXO1 and FOXO3. Preserve both exact partner assertions and their transcription-factor class rather than merging paralog-specific rows. The exact partner UniProtKB:O43524 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:25609649 Proteomic analyses reveal distinct chromatin-associated and ... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: The source supports CBP association with FOXO1 and FOXO3. Preserve both exact partner assertions and their transcription-factor class rather than merging paralog-specific rows. The exact partner UniProtKB:Q12778 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:28128295 RNA helicase DDX3 maintains lipid homeostasis through upregu... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: DDX3X is an officially classified DEAD-box helicase. Actual CBP-specific immunoprecipitation from HuH7 nuclear extracts supports association distinct from p300. The experiment does not establish a purified binary complex or direct CBP helicase activity. Proposed replacements: DEAD/H-box RNA helicase binding |
| GO:0005515 protein binding | IPI PMID:28680062 Linking functions: an additional role for an intrinsically d... | KEEP AS NON CORE | Summary: Retain the positive interaction at its source-specific scope. Reason: ZNF106 is an RNA-binding protein, not a DNA-binding transcription factor merely because a figure calls it a transcription factor. The paper tests disordered CBP ID3 and a ZNF106 fragment and identifies substrate association. Retain that direct source-specific interaction without inventing a folded-domain or DNA-binding partner class. The CLINGEN_MENDELIAN Curation instructions retain supported positive protein-binding annotations as KEEP_AS_NON_CORE when no evidence-backed narrower class is established; the stated source and assay limits still apply. |
| GO:0005515 protein binding | IPI PMID:28790157 SIRT7 and the DEAD-box helicase DDX21 cooperate to resolve g... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: DDX21 is a DEAD-box helicase and an experimentally supported CBP acetylation target. The positive curated binding assertion is retained and refined to its verified partner class. The selected Results establish substrate acetylation; they are not described as a newly observed purified binary-binding measurement. Proposed replacements: DEAD/H-box RNA helicase binding |
| GO:0005515 protein binding | IPI PMID:30540930 SIRT7-Dependent Deacetylation of Fibrillarin Controls Histon... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: Fibrillarin is both an RNA methyltransferase and a histone H2A methyltransferase in the actual source. The histone methyltransferase binding class therefore preserves the positive curated interaction more precisely. This neither transfers methyltransferase activity to CBP nor implies that all fibrillarin biology is chromatin-based. Proposed replacements: histone methyltransferase binding |
| GO:0005515 protein binding | IPI PMID:33640491 Proximity-dependent Mapping of the Androgen Receptor Identif... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: The AR proximity-interaction study supports the curated association at proximity-assay resolution. A positive proximity record is not described as a purified direct-binding measurement. The exact partner UniProtKB:P10275 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:33894414 In-vitro acetylation of SARS-CoV and SARS-CoV-2 nucleocapsid... | KEEP AS NON CORE | Summary: Retain the positive source-specific interaction with its assay limits. Reason: Actual Methods use a human CBP catalytic domain with viral nucleocapsid. The abstract emphasizes PCAF/GCN5, whereas Results report faint CBP acetylation and a differing MS pattern; no categorical absence of CBP activity is inferred. No more informative supported interaction class is assigned here; the existing positive record is not removed merely for being contextual or generic. The CLINGEN_MENDELIAN Curation instructions retain supported positive protein-binding annotations as KEEP_AS_NON_CORE when no evidence-backed narrower class is established; the stated source and assay limits still apply. |
| GO:0005515 protein binding | IPI PMID:35140242 Human transcription factor protein interaction networks. | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: GATA2βCBP interaction is retained in the source context, with its DNA-binding transcription-factor class and detailed access limits. The exact partner UniProtKB:P23769 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:A4D2P6. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:O14745. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:O75970. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:O95049. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:O96018. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:P78352. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q02410. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q07157. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q12959. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q14005. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q14160. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q15700. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q5T2W1. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q68DX3. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q86UL8. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q86UT5. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q8N448. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q8NI35. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q8TBB1. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q92796. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q96QZ7. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q99767. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q9C0E4. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q9P202. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: The measured interaction is binding to a PDZ domain. Reason: The literal positive holdup record pairs the CREBBP C-terminal peptide, residues 2433β2442, with an isolated PDZ-domain construct from UniProtKB:Q9Y3R0. Sequence/ROGID reconstruction agrees with the stated products and features. GO:0030165 describes this assay directly; it does not establish native full-length encounter, compartment co-residence or equivalent function of every CREBBP product. The source correction is recorded separately. Proposed replacements: PDZ domain binding |
| GO:0005515 protein binding | IPI PMID:39009827 Proteome-scale characterisation of motif-based interactome r... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: The actual target-bearing Table1 compares wild-type CBP5-19 and K13E with engineered KPNA4 major/minor pockets. Wild-type peptide binds more strongly; the variant weakens binding. The isolated-peptide importin-alpha class is supported. Preserve both mutation feature strings, avoid exact numerical claims from flattened table cells, and do not infer full-length native nuclear import. Proposed replacements: importin-alpha family protein binding |
| GO:0005515 protein binding | IPI PMID:8684459 A p300/CBP-associated factor that competes with the adenovir... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: KAT2B/PCAF is a histone acetyltransferase. Three literal CBP-PCAF records and the independently accepted core peer original reading establish association. Preserve the original source grouping, not a CBP homodimer inference; do not attribute the paper histone enzyme assay to CBP. Proposed replacements: histone acetyltransferase binding |
| GO:0005515 protein binding | IPI PMID:9018065 The adenovirus 12 E1A proteins can bind directly to proteins... | KEEP AS NON CORE | Summary: Retain the positive source-specific interaction with its assay limits. Reason: E1A binds CBP/p300 and perturbs their cellular functions. The two adenoviral accession-specific interactions remain positive contextual associations. No more informative supported interaction class is assigned here; the existing positive record is not removed merely for being contextual or generic. The CLINGEN_MENDELIAN Curation instructions retain supported positive protein-binding annotations as KEEP_AS_NON_CORE when no evidence-backed narrower class is established; the stated source and assay limits still apply. |
| GO:0005515 protein binding | IPI PMID:9018065 The adenovirus 12 E1A proteins can bind directly to proteins... | KEEP AS NON CORE | Summary: Retain the positive source-specific interaction with its assay limits. Reason: E1A binds CBP/p300 and perturbs their cellular functions. The two adenoviral accession-specific interactions remain positive contextual associations. No more informative supported interaction class is assigned here; the existing positive record is not removed merely for being contextual or generic. The CLINGEN_MENDELIAN Curation instructions retain supported positive protein-binding annotations as KEEP_AS_NON_CORE when no evidence-backed narrower class is established; the stated source and assay limits still apply. |
| GO:0005515 protein binding | IPI PMID:9194564 Synergistic activation of transcription by CBP and p53. | MODIFY | Summary: Refine the positive TP53 interaction to p53 binding. Reason: The source reports TP53βCBP interaction in transcriptional activation. Preserve the exact p53 partner and avoid inferring a universal downstream response. GO:0002039 preserves the positive interaction while naming its verified TP53 partner. Proposed replacements: p53 binding |
| GO:0005515 protein binding | IPI PMID:9323138 RNA helicase A mediates association of CBP with RNA polymera... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: DHX9/RHA is officially in the DEAD-box family, DEAH subfamily, and the source reports its role linking CBP to Pol II complexes. This supports the helicase partner class while preserving complex association rather than claiming CBP itself binds Pol II directly. Proposed replacements: DEAD/H-box RNA helicase binding |
| GO:0005515 protein binding | IPI PMID:9687513 E1A directly binds and regulates the P/CAF acetyltransferase... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: The KAT2B/PCAF class and literal CBP pull-down support histone acetyltransferase binding. Preserve the mutation feature on the PCAF construct and distinguish the paper E1A-PCAF direct assay from the target CBP-PCAF interaction. Proposed replacements: histone acetyltransferase binding |
| GO:0005515 protein binding | IPI PMID:9811832 HIV-1 tat transactivator recruits p300 and CREB-binding prot... | KEEP AS NON CORE | Summary: Retain the positive source-specific interaction with its assay limits. Reason: HIV Tat uses CBP/p300 during transcriptional regulation. Tat is RNA targeted; do not call it a sequence-specific DNA-binding transcription factor. No more informative supported interaction class is assigned here; the existing positive record is not removed merely for being contextual or generic. The CLINGEN_MENDELIAN Curation instructions retain supported positive protein-binding annotations as KEEP_AS_NON_CORE when no evidence-backed narrower class is established; the stated source and assay limits still apply. |
| GO:0005515 protein binding | IPI PMID:9887100 Functional role of p35srj, a novel p300/CBP binding protein,... | MODIFY | Summary: Refine the positive interaction to DNA-binding transcription-factor binding. Reason: p35srj/CITED2 binds CBP/p300 and antagonizes HIF-dependent transcription in the investigated context. Preserve both CITED2 and HIF1A interactions, without forcing all coregulatory partners into a single activating direction. The exact partner UniProtKB:Q16665 is an RNA polymerase II transcription factor, so GO:0061629 states the binding class more informatively. This refinement does not assert that a particular assay measured native nuclear encounter or that CREBBP itself binds that factorβs DNA motif. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:9887100 Functional role of p35srj, a novel p300/CBP binding protein,... | MODIFY | Summary: Refine the positive interaction to its experimentally supported partner class. Reason: CITED2/p35srj is a non-DNA-binding transcriptional coregulator. This source examines competitive inhibition of HIF coactivation, not simply positive coactivation. The broader class avoids using the official coactivator label to reverse the specific experimental context; do not infer a promoter-bound repressor complex. Proposed replacements: transcription coregulator binding |
| GO:0005634 nucleus | EXP PMID:15023334 Acetylation of the C terminus of Ku70 by CBP and PCAF contro... | ACCEPT | Summary: Nuclear localization is supported. Reason: The abstract reports CBP/PCAF acetylation of Ku70 K542, association with Ku70 and cytoplasmic CBP accumulation as Ku70βBAX binding is disrupted. The curated nuclear annotation is retained with curator deference; the directly stated positive cytoplasmic observation does not establish exclusive localization. |
| GO:0005634 nucleus | EXP PMID:15488321 The calcium-responsive transactivator recruits CREB binding ... | ACCEPT | Summary: Nuclear localization is supported. Reason: The abstract reports CREST recruitment of CBP to nuclear bodies and explicitly distinguishes them from PML bodies. Rat PC12 and HEK293 assay hosts do not by themselves establish CBP insert species. The positive localization assertions remain at gene-product resolution, without product exclusivity. |
| GO:0005634 nucleus | IC PMID:12169688 The role of Sp1 and AP-2 in basal and protein kinase A--indu... | ACCEPT | Summary: Nuclear localization is supported. Reason: The actual indexed original and abstract report Sp1/AP-2 control of the rat SPT promoter in HepG2 assays, with CBP enhancing Sp1/PKA-driven transcription. This is promoter coactivation, not proof that CBP itself binds the Sp1 recognition sequence. |
| GO:0005634 nucleus | IDA PMID:12929931 P300/CBP acts as a coactivator to cartilage homeoprotein-1 (... | ACCEPT | Summary: Nuclear localization is supported. Reason: The structured abstract explicitly reports CBP and p300 enhancement of Cart1-dependent transcription, while several localization and acetylation experiments are described specifically for p300. Retain curator-grounded CBP localization with that source-resolution limit. |
| GO:0005634 nucleus | IDA PMID:25593309 Screen identifies bromodomain protein ZMYND8 in chromatin re... | ACCEPT | Summary: Nuclear localization is supported. Reason: The complete available abstract describes a human bromodomain-protein DNA-damage localization screen and ZMYND8/NuRD-dependent chromatin repair. It is not a Human Protein Atlas methods paper. The positive curated CREBBP nuclear-localization assertion is retained with curator deference; the exact CREBBP screen panel was not recovered or personally verified from this abstract. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: Nuclear localization is supported. Reason: The official nuclear-location mapping agrees with direct transcriptional and chromatin experiments. It does not exclude cytoplasmic activities. |
| GO:0005634 nucleus | TAS PMID:7913207 Nuclear protein CBP is a coactivator for the transcription f... | ACCEPT | Summary: Nuclear localization is supported. Reason: The original CBPβCREB study supports transcriptional coactivation and complex formation. Historical broad cellular localization and assembly statements are retained without inventing a modern fixed complex stoichiometry. |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | ACCEPT | Summary: The antibody-based nucleoplasm localization is retained. Reason: The original Human Protein Atlas/GO_REF0000052 IDA assertion is consistent with CREBBPβs documented nuclear coactivator and acetyltransferase activities. It is not treated as isoform-resolved detection or as evidence of exclusive localization. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-1028815 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-1028815 record (p-T,4S-IRF3:p-T,4S-IRF3:CREBBP, EP300 binds promoters of Interferon-beta) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-1028817 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-1028817 record (CREBBP, EP300 binds p-T,4S-IRF3:p-T,4S-IRF3) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-1028819 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-1028819 record (VAF/pIRF7:CBP/p300 binds the promoters of type-I IFN genes) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-1028820 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-1028820 record (Formation of VAF (virus-activated factor) complex) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-1234167 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-1234167 record (Formation of HIF:CBP:p300 complex at promoters) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-1912394 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-1912394 record (NICD1 in complex with RBPJ (CSL) recruits MAML) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-212356 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-212356 record (Formation of CSL-NICD coactivator complex) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-2220957 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-2220957 record (NOTCH1 PEST domain mutants coactivator complex binds CDK8:CCNC) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-2220964 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-2220964 record (NICD1 PEST domain mutants in complex with RBPJ (CSL) bind MAML) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-2220971 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-2220971 record (CDK8 phosphorylates NICD1 PEST domain mutants ) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-3134883 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-3134883 record (Beta-catenin enhances association of IRF3 with CBP/p300 ) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-3322427 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-3322427 record (Beta-catenin recruits CBP/p300) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-3371554 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-3371554 record (HSF1 acetylation at Lys80) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-400143 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-400143 record (Fatty acid ligands activate PPARA) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4396371 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-4396371 record (NOTCH1 Coactivator Complex binds MYC promoter) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4396379 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-4396379 record (NOTCH1 Coactivator Complex binds HES5 promoter) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4396392 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-4396392 record (NOTCH1 PEST domain mutants bind HES1 promoter) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4396393 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-4396393 record (NOTCH1 PEST domain mutants bind MYC promoter) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4396401 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-4396401 record (NOTCH1 PEST domain mutants bind HES5 promoter) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4396402 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-4396402 record (NOTCH1 PEST domain mutants bind promoters of HEY genes) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5660660 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-5660660 record (p300 acetylates RELA subunit) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5660666 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-5660666 record (CBP and p300 binds NF-kB complex) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6797993 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-6797993 record (TP53 and CREBBP bind BNIP3L gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8864307 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-8864307 record (TFAP2 homo- and heterodimers bind CITED and EP300/CREBBP) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8878220 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-8878220 record (RUNX3 binds the NOTCH1 coactivator complex) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8878237 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-8878237 record (RUNX3:NOTCH1 coactivator complex binds the HES1 gene promoter) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8938228 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-8938228 record (RUNX1:CBFB:CREBBP binds the CSF2 (GM-CSF) gene promoter) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8938231 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-8938231 record (RUNX1:CBFB binds CREBBP) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9017835 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9017835 record (NOTCH1 coactivator complex binds NOTCH3 gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9021451 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9021451 record (NOTCH1,NOTCH3 coactivator complex binds PLXND1 gene promoter) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9038052 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9038052 record (GREB1 binds ESR1:ESTG and co-activators) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-933536 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-933536 record (p-IRF7 dimer interacts with coactivator CBP/p300) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9626928 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9626928 record (CREBBP binds FOXO1) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9759332 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9759332 record (AcK-NFE2L2 binds the TXNRD1 promoter) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9760081 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9760081 record (CREBBP, EP300 acetylates NFE2L2) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9760082 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9760082 record (NFE2L2 binds CREBBP,EP300) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9760097 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9760097 record (AcK-NFE2L2 and MAFK bind the GSTA1 gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9760099 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9760099 record (AcK-NFE2L2 binds the GCLC gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9760103 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9760103 record (AcK-NFE2L2 binds the GCLM gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9761812 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9761812 record (AcK- NFE2L2, MAFG and CREBBP, EP300 bind the G6PD) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9761815 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9761815 record (AcK-NFE2L2 and ATF4 bind the SLC7A11 gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9761828 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9761828 record (NFE2L2 binds the PGD gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9761836 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9761836 record (p14ARF binds NFE2L2:CREBBP, EP300) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9796039 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9796039 record (AcK-NFE2L2 binds the ABCF2 gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9796048 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9796048 record (AcK-NFE2L2 binds the ABCG2 gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9796049 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9796049 record (AcK-NFE2L2 binds the SOD3 gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9796050 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9796050 record (AcK-NFE2L2 binds the KEAP1 gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9796051 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9796051 record (AcK-NFE2L2 binds the AREG gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9796058 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9796058 record (AcK-NFE2L2 binds the TXN gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9796059 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9796059 record (AcK-NFE2L2 binds the BCL2 gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9796064 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9796064 record (AcK-NFE2L2 binds the NOTCH1 gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9796065 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9796065 record (AcK-NFE2L2 binds the ABCC3 gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9796066 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9796066 record (AcK-NFE2L2 binds the CCL2 gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9796068 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9796068 record (AcK-NFE2L2 binds the ATF4 gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9796077 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9796077 record (AcK-NFE2L2 binds the ABCC1 gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9796082 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9796082 record (AcK-NFE2L2 binds the EGF gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9796084 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9796084 record (AcK-NFE2L2 binds the BCL2L1 gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9825747 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9825747 record (CREBBP acetylates HINT1 dimer) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9833446 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9833446 record (NS1 (1C) binds to CREBBP) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9843120 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9843120 record (Coactivators are recruited to liganded PPARG:RXRA heterodimer) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9909652 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9909652 record (NFE2L2 binding to CD274 gene) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9926478 | ACCEPT | Summary: The event-specific Reactome nucleoplasm annotation is supported. Reason: The actual R-HSA-9926478 record (MITF-M binds CREBBP,EP300) has a positive typed path to the literal Q92793 entity in nucleoplasm. Retain this compartment assertion; the event title is not a claim that CREBBP performs the partnerβs DNA recognition, phosphorylation or enzymatic step. Predicted complex/event contexts remain Reactome provenance, not newly asserted primary assays. |
| GO:0005667 transcription regulator complex | IBA GO_REF:0000033 | ACCEPT | Summary: Conserved transcription-regulator complex association is supported. Reason: The actual GO:0005667 IBD at PTN000351795 lies on the CREBBP path. Native cofactor complexes and promoter-associated CBP biology support the ancestral judgment; no fixed universal complex stoichiometry is inferred. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000351795 SUPPORTS TRANSFER The actual on-path ancestral IBD and exact target MSA support this conserved assertion. Extant experimental records are preserved separately, including legitimate target evidence. |
| GO:0005737 cytoplasm | EXP PMID:15023334 Acetylation of the C terminus of Ku70 by CBP and PCAF contro... | ACCEPT | Summary: Positive cytoplasmic localization is retained. Reason: The complete available abstract reports CBP/PCAF acetylation of Ku70 K542, association with Ku70 and cytoplasmic CBP accumulation as Ku70βBAX binding is disrupted. This directly stated cytoplasmic observation supports the existing positive localization assertion. Cytoplasmic and nuclear localization are nonexclusive; no exclusive compartment or numbered product is inferred. Supporting Evidence: PMID:15023334 coincides with cytoplasmic accumulation of CBP |
| GO:0005737 cytoplasm | IDA PMID:12929931 P300/CBP acts as a coactivator to cartilage homeoprotein-1 (... | ACCEPT | Summary: Positive cytoplasmic localization is retained. Reason: The structured abstract explicitly reports CBP and p300 enhancement of Cart1-dependent transcription, while several localization and acetylation experiments are described specifically for p300. Retain curator-grounded CBP localization with that source-resolution limit. Nuclear localization is not exclusive and does not negate this experimentally curated cytoplasmic scope. |
| GO:0005737 cytoplasm | IDA PMID:35675826 Deubiquitinase OTUD3 regulates metabolism homeostasis in res... | ACCEPT | Summary: Positive cytoplasmic localization is retained. Reason: The recovered original target windows establish CBP-dependent OTUD3 acetylation, nutrient responsiveness and enhanced OTUD3 nuclear localization, with mutant and depletion controls. Human OTUD3 is explicit; CBP insert identity is not inferred from HEK293T host. The G288D metabolic phenotype is not explained simply by altered acetylation or localization. Nuclear localization is not exclusive and does not negate this experimentally curated cytoplasmic scope. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: The broad cytoplasmic mapping is compatible with actual activities. Reason: The source preserves UniProt SL-0086 and agrees with experimentally supported cytoplasmic CBP contexts, including OTUD3 regulation and the E4 study. It is not narrowed to one organelle or product. |
| GO:0005737 cytoplasm | TAS PMID:7913207 Nuclear protein CBP is a coactivator for the transcription f... | ACCEPT | Summary: Positive cytoplasmic localization is retained. Reason: The original CBPβCREB study supports transcriptional coactivation and complex formation. Historical broad cellular localization and assembly statements are retained without inventing a modern fixed complex stoichiometry. Nuclear localization is not exclusive and does not negate this curated cytoplasmic scope. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9756494 | ACCEPT | Summary: Cytosolic CREBBP is explicitly represented in the viral substrate event. Reason: The actual R-HSA-9756494 event leads to Q92793 entity9756493 in cytosol. The recovered PMID:34239064 target experiments support CBP-dependent N acetylation in human cells; the compartment assertion does not make viral immune evasion a core function. |
| GO:0006338 chromatin remodeling | IEA GO_REF:0000002 | ACCEPT | Summary: Catalytic chromatin modification supports chromatin remodeling. Reason: The IPR013178 catalytic-domain mapping is consistent with CREBBP altering histone acetylation and chromatin accessibility. This is a performed chromatin-modification contribution, not a claim that CBP is an ATP-dependent nucleosome motor. |
| GO:0006355 regulation of DNA-templated transcription | IEA GO_REF:0000002 | ACCEPT | Summary: Broad DNA-templated transcription regulation is appropriate. Reason: The original InterPro mappings agree with positive Pol II coactivation and context-dependent repression, including Pol I regulatory effects through acetylated substrates. A blanket refinement to activation alone would discard supported regulatory directions. |
| GO:0006355 regulation of DNA-templated transcription | TAS PMID:15261140 Small molecule blockade of transcriptional coactivation of t... | ACCEPT | Summary: The broad transcription-regulation assertion is retained. Reason: This is primary research on chetomin-mediated disruption of HIF coactivation. The complete available abstract specifically describes disruption of the p300 CH1 domain and HIFβp300 binding, while identifying CBP and p300 as HIF coactivators. The established CBP transcription-regulation assertion is retained at the curated TAS/background scope; no direct CBP chetomin assay is inferred from the p300 experiment. |
| GO:0006355 regulation of DNA-templated transcription | TAS PMID:7913207 Nuclear protein CBP is a coactivator for the transcription f... | ACCEPT | Summary: The broad transcription-regulation assertion is retained. Reason: The original CBPβCREB study supports transcriptional coactivation and complex formation. Historical broad cellular localization and assembly statements are retained without inventing a modern fixed complex stoichiometry. |
| GO:0007249 canonical NF-kappaB signal transduction | IDA PMID:16135789 NF-kappaB RelA phosphorylation regulates RelA acetylation. | KEEP AS NON CORE | Summary: A performed coactivator contribution to NF-kappaB signaling is retained. Reason: The full main passages read here primarily assay p300-dependent RelA acetylation. CBP is named in the broader coactivator context and is independently corroborated by PMID:12456660; no p300-specific panel is described as a direct CBP experiment. Independent CBP substitution experiments in PMID:12456660 preserve the positive pathway contribution; no upstream kinase or receptor function is inferred. |
| GO:0007249 canonical NF-kappaB signal transduction | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: The matched NF-kappaB rule describes a contextual coactivator role. Reason: ARBA00085080 matches the target; CBP-mediated RelA regulation supports this pathway context. The role is downstream catalytic/coactivator work, not every step of NF-kappaB signal transduction. |
| GO:0008270 zinc ion binding | IEA GO_REF:0000002 | ACCEPT | Summary: Zinc binding is consistent with the mapped CBP zinc-binding domain. Reason: The official target carries the IPR000433 zinc-binding region. This is structural domain chemistry, distinct from inferring an unmeasured metal-dependent catalytic mechanism. |
| GO:0008589 regulation of smoothened signaling pathway | TAS PMID:11001584 The sonic hedgehog-patched-gli pathway in human development ... | KEEP AS NON CORE | Summary: Retain the broader Hedgehog transcriptional-regulatory context. Reason: This is a review of HedgehogβPatchedβGLI biology. Its CBP section and Figure 1 caption discuss human GLI3 interaction with mouse CBP and developmental inference from RubinsteinβTaybi syndrome; they are not new human CREBBP developmental experiments. The assertion is retained as a source-qualified developmental signaling context, not a claim that CBP is Smoothened or directly controls its trafficking. |
| GO:0016407 acetyltransferase activity | EXP PMID:12456660 Acetylation of RelA at discrete sites regulates distinct nuc... | MODIFY | Summary: Protein-lysine acetyltransferase is more precise than generic acetyltransferase. Reason: The principal experiments focus on p300/RelA, but the Results explicitly state that substitution with CBP gave similar acetylation and transcriptional effects, reported without displayed data. This is positive CBP corroboration, not a purified CBP claim for every panel. The established reaction modifies protein lysine residues, so GO:0061733 refines the broad source term without changing its source identity. Proposed replacements: protein-lysine-acetyltransferase activity Supporting Evidence: PMID:12456660 Similar findings were obtained when CBP was substituted for p300 (data not shown). |
| GO:0016407 acetyltransferase activity | EXP PMID:16135789 NF-kappaB RelA phosphorylation regulates RelA acetylation. | MODIFY | Summary: Protein-lysine acetyltransferase is more precise than generic acetyltransferase. Reason: The full main passages read here primarily assay p300-dependent RelA acetylation. CBP is named in the broader coactivator context and is independently corroborated by PMID:12456660; no p300-specific panel is described as a direct CBP experiment. The established reaction modifies protein lysine residues, so GO:0061733 refines the broad source term without changing its source identity. Proposed replacements: protein-lysine-acetyltransferase activity |
| GO:0016407 acetyltransferase activity | IDA PMID:11742995 Activation of AML1-mediated transcription by MOZ and inhibit... | MODIFY | Summary: Protein-lysine acetyltransferase is more precise than generic acetyltransferase. Reason: The recovered original distinguishes human CBP from MOZ and the MOZβCBP fusion. CBP acetylates histones and AML1 and stimulates the tested Pol II reporters; fusion-mediated repression must not be attributed to normal CBP. The established reaction modifies protein lysine residues, so GO:0061733 refines the broad source term without changing its source identity. Proposed replacements: protein-lysine-acetyltransferase activity |
| GO:0016407 acetyltransferase activity | IDA PMID:15273251 Site-specific acetylation of the fetal globin activator NF-E... | MODIFY | Summary: Protein-lysine acetyltransferase is more precise than generic acetyltransferase. Reason: The abstract foregrounds PCAF-mediated NFE4 acetylation. Preserve the positive curated CBP interaction and acetyltransferase assertions with explicit curator deference and the full-text access limit; do not describe an unverified CBP panel as personally read. NFE4 partner classification is considered separately. The established reaction modifies protein lysine residues, so GO:0061733 refines the broad source term without changing its source identity. Proposed replacements: protein-lysine-acetyltransferase activity |
| GO:0016479 negative regulation of transcription by RNA polymerase I | IDA PMID:30540930 SIRT7-Dependent Deacetylation of Fibrillarin Controls Histon... | KEEP AS NON CORE | Summary: Fibrillarin acetylation supports contextual negative Pol I regulation. Reason: CBP acetylates fibrillarin and reduces its H2A glutamine methylation/rDNA transcription function. This is an explicit regulatory action on an active enzyme, not merely a secondary expression phenotype. |
| GO:0016604 nuclear body | IDA GO_REF:0000052 | ACCEPT | Summary: The curated nuclear-body localization is retained. Reason: The Human Protein Atlas IDA source is consistent with CBPβs documented subnuclear organization. The assertion is retained at antibody-based gene-product resolution, without an isoform-specific or exclusive-location claim. |
| GO:0016604 nuclear body | IDA PMID:15488321 The calcium-responsive transactivator recruits CREB binding ... | ACCEPT | Summary: Nuclear-body localization is a supported source-specific observation. Reason: The abstract reports CREST recruitment of CBP to nuclear bodies and explicitly distinguishes them from PML bodies. Rat PC12 and HEK293 assay hosts do not by themselves establish CBP insert species. The positive localization assertions remain at gene-product resolution, without product exclusivity. |
| GO:0030511 positive regulation of transforming growth factor beta receptor signaling pathway | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: The matched rule supports a contextual TGF-beta cofactor contribution. Reason: ARBA00086893 matches the current target; the curated target assertion and the PMID:25514493 SMAD4βp300/CBP cofactor context support retention of the positive regulatory role at the available abstract resolution. This does not identify CBP as the ligand receptor. |
| GO:0030511 positive regulation of transforming growth factor beta receptor signaling pathway | IMP PMID:25514493 Pokemon (FBI-1) interacts with Smad4 to repress TGF-Ξ²-induce... | KEEP AS NON CORE | Summary: Retain the curated positive TGF-beta contribution with its source-access limit. Reason: The complete cached abstract reports Pokemon/ZBTB7A interaction with SMAD4, HDAC1 recruitment and reduced SMAD4βp300/CBP association; it explicitly reports unchanged SMAD2/3 activation. It does not report CBP acetylation of SMAD2/3. The curated positive CREBBP contribution is retained at a contextual transcriptional-cofactor scope with the full-text access limit, rather than treating the Pokemon repression phenotype as CREBBP repression. |
| GO:0031490 chromatin DNA binding | IBA GO_REF:0000033 | ACCEPT | Summary: The actual ancestral chromatin-DNA assertion remains supported. Reason: The GO:0031490 IBD is at PTN000351795 on the target path. Complete current mouse and rat donor records include actual p300 chromatin-immunoprecipitation evidence; the read original donor passages resolve chromatin-associated regulatory DNA at that assayβs resolution. These are not purified direct-DNA-affinity measurements, but no target-specific loss or placement error is established. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000351795 SUPPORTS TRANSFER The actual on-path ancestral IBD and exact target MSA support this conserved assertion. Extant experimental records are preserved separately, including legitimate target evidence. |
| GO:0031669 cellular response to nutrient levels | IDA PMID:35675826 Deubiquitinase OTUD3 regulates metabolism homeostasis in res... | KEEP AS NON CORE | Summary: Nutrient-responsive OTUD3 acetylation is a performed contextual role. Reason: The recovered original target windows establish CBP-dependent OTUD3 acetylation, nutrient responsiveness and enhanced OTUD3 nuclear localization, with mutant and depletion controls. Human OTUD3 is explicit; CBP insert identity is not inferred from HEK293T host. The G288D metabolic phenotype is not explained simply by altered acetylation or localization. |
| GO:0031669 cellular response to nutrient levels | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: The nutrient-response rule is biologically corroborated. Reason: ARBA00034580 matches the target, and CBP-dependent OTUD3 acetylation responds to nutritional conditions in PMID:35675826. The activity performs a regulatory step; this is not assigned solely because CREBBP expression changes. |
| GO:0042733 embryonic digit morphogenesis | TAS PMID:11001584 The sonic hedgehog-patched-gli pathway in human development ... | KEEP AS NON CORE | Summary: Retain source-qualified developmental context without a structural digit role. Reason: This is a review of HedgehogβPatchedβGLI biology. Its CBP section and Figure 1 caption discuss human GLI3 interaction with mouse CBP and developmental inference from RubinsteinβTaybi syndrome; they are not new human CREBBP developmental experiments. The positive developmental association is not equated with a direct human embryonic perturbation assay or a separate molecular activity. |
| GO:0043426 MRF binding | IDA PMID:8621548 Human p300 protein is a coactivator for the transcription fa... | ACCEPT | Summary: The positive curated myogenic-regulatory-factor interaction is retained. Reason: The abstract emphasizes p300/MyoD. The positive curated CBP MRF-binding assertion is retained with curator deference and an explicit full-text limit, rather than removed as paralog misattribution. |
| GO:0043993 histone H3K18 acetyltransferase activity | IDA PMID:21131905 Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-med... | ACCEPT | Summary: The specific histone-site acetylation assertion is supported. Reason: The recovered original uses mouse CBP/p300 deletion experiments to establish H3K18/H3K27 acetylation requirements and transcriptional consequences. These are not purified human CBP-only assays; the conserved catalytic claims remain supported. Mouse double-deletion evidence is distinguished from a purified human single-enzyme assay; it agrees with the conserved catalytic function. |
| GO:0043993 histone H3K18 acetyltransferase activity | IEA GO_REF:0000117 | ACCEPT | Summary: The matched rule and experimental histone-site evidence agree. Reason: ARBA00086810 has a complete current target match. Experimental CBP/p300-dependent H3K18/H3K27 acetylation supports the respective site assertion, without implying exclusive specificity for these two residues. |
| GO:0044017 histone H3K27 acetyltransferase activity | IDA PMID:21131905 Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-med... | ACCEPT | Summary: The specific histone-site acetylation assertion is supported. Reason: The recovered original uses mouse CBP/p300 deletion experiments to establish H3K18/H3K27 acetylation requirements and transcriptional consequences. These are not purified human CBP-only assays; the conserved catalytic claims remain supported. Mouse double-deletion evidence is distinguished from a purified human single-enzyme assay; it agrees with the conserved catalytic function. |
| GO:0044017 histone H3K27 acetyltransferase activity | IEA GO_REF:0000117 | ACCEPT | Summary: The matched rule and experimental histone-site evidence agree. Reason: ARBA00092160 has a complete current target match. Experimental CBP/p300-dependent H3K18/H3K27 acetylation supports the respective site assertion, without implying exclusive specificity for these two residues. |
| GO:0045893 positive regulation of DNA-templated transcription | IDA PMID:11742995 Activation of AML1-mediated transcription by MOZ and inhibit... | MODIFY | Summary: Refine the positive transcription claim to RNA polymerase II transcription. Reason: The actual human-CBP reporter experiments in PMID:11742995 test Pol II promoter activation, distinct from MOZβCBP fusion repression. GO:0045944 names that process more precisely. Proposed replacements: positive regulation of transcription by RNA polymerase II |
| GO:0045893 positive regulation of DNA-templated transcription | ISS GO_REF:0000024 | MODIFY | Summary: Refine the conserved positive transcription contribution to Pol II. Reason: The original mouse Crebbp P45481 ISS source is preserved and its literal current annotation joins are documented. Direct target Pol II coactivation provides a more precise term, without declaring the broader mouse source assertion biologically false. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P45481 SUPPORTS TRANSFER Literal mouse Crebbp experimental annotation joins are documented; the broader source process remains valid while direct target evidence permits a Pol II refinement. Proposed replacements: positive regulation of transcription by RNA polymerase II |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IBA GO_REF:0000033 | ACCEPT | Summary: Conserved positive Pol II transcription is a central function. Reason: The actual GO:0045944 IBD lies on the CREBBP path. Target and extant descendant experimental records support an ancestral coactivation role; target self-evidence is legitimate grounding, not circularity. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000351795 SUPPORTS TRANSFER The actual on-path ancestral IBD and exact target MSA support this conserved assertion. Extant experimental records are preserved separately, including legitimate target evidence. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:12169688 The role of Sp1 and AP-2 in basal and protein kinase A--indu... | ACCEPT | Summary: Positive Pol II transcription is retained at the source-specific assay scope. Reason: The actual indexed original and abstract report Sp1/AP-2 control of the rat SPT promoter in HepG2 assays, with CBP enhancing Sp1/PKA-driven transcription. This is promoter coactivation, not proof that CBP itself binds the Sp1 recognition sequence. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:12435739 Regulation of E2A activities by histone acetyltransferases i... | ACCEPT | Summary: Positive Pol II transcription is retained at the source-specific assay scope. Reason: CBP interacts with and acetylates E2A/TCF3 and regulates its transcriptional function. The specific P15923-2 source identity is preserved; no isoform-exclusive activity is inferred. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IEA GO_REF:0000117 | ACCEPT | Summary: Current rule matches support positive Pol II transcription. Reason: ARBA00027996 has complete target matches and agrees with established promoter coactivation. Preserve the electronic source independently of the experimental annotations. |
| GO:0048156 tau protein binding | TAS PMID:28386764 Roles of tau protein in health and disease. | KEEP AS NON CORE | Summary: Tau binding is a supported contextual substrate interaction. Reason: This review discusses tau acetylation by CBP and related enzymes, including site-dependent pathological and protective effects. It supports contextual tau binding and lysine acetylation, not an independent primary assay. |
| GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding | IEA GO_REF:0000117 | ACCEPT | Summary: Transcription-factor binding is a central and supported interaction class. Reason: ARBA00028384 matches the target, and numerous positive partner-specific experiments support binding to RNA polymerase II DNA-binding transcription factors. This is binding-class evidence, not a claim that CBP itself recognizes their DNA sites. |
| GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding | IPI PMID:16043483 MEF2-dependent recruitment of the HAND1 transcription factor... | ACCEPT | Summary: The existing transcription-factor binding term is appropriately specific. Reason: The abstract establishes MEF2βHAND1 interaction and proposes CBP co-recruitment as a mechanism for synergy. Preserve the positive curated MEF2AβCBP and HAND1βCBP pairs with curator deference and the full-text limit; direct CBP pair assays are not claimed from this abstract. HAND1 DNA binding being dispensable in this context does not abolish its established transcription-factor class. |
| GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding | IPI PMID:16043483 MEF2-dependent recruitment of the HAND1 transcription factor... | ACCEPT | Summary: The existing transcription-factor binding term is appropriately specific. Reason: The abstract establishes MEF2βHAND1 interaction and proposes CBP co-recruitment as a mechanism for synergy. Preserve the positive curated MEF2AβCBP and HAND1βCBP pairs with curator deference and the full-text limit; direct CBP pair assays are not claimed from this abstract. HAND1 DNA binding being dispensable in this context does not abolish its established transcription-factor class. |
| GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding | IPI PMID:21539536 KrΓΌppel-like Factor 4 activates HBG gene expression in prima... | ACCEPT | Summary: The existing transcription-factor binding term is appropriately specific. Reason: Actual Methods/Results show CREBBP-dependent repression in a KLF4/HBG reporter context, using a murine CREBBP expression plasmid, together with endogenous human erythroid co-occupancy and interaction. The contextual corepressor effect coexists with extensive coactivation evidence. |
| GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding | TAS PMID:11001584 The sonic hedgehog-patched-gli pathway in human development ... | ACCEPT | Summary: The existing transcription-factor binding term is appropriately specific. Reason: This is a review of HedgehogβPatchedβGLI biology. Its CBP section and Figure 1 caption discuss human GLI3 interaction with mouse CBP and developmental inference from RubinsteinβTaybi syndrome; they are not new human CREBBP developmental experiments. |
| GO:0061733 protein-lysine-acetyltransferase activity | EXP PMID:11154691 Stimulation of NF-E2 DNA binding by CREB-binding protein (CB... | ACCEPT | Summary: Protein-lysine acetylation is directly supported in this substrate context. Reason: The abstract explicitly reports CBP acetylation of MafG, while p45 is not acetylated. This supports the positive protein-lysine acetyltransferase assertion at the named substrate scope; no generic inseparable CBP/p300 assay is claimed. |
| GO:0061733 protein-lysine-acetyltransferase activity | EXP PMID:12738767 Interferon regulatory factor-2 regulates cell growth through... | ACCEPT | Summary: The established protein-lysine acetyltransferase annotation is retained with the source-access limit. Reason: The abstract assays p300/PCAF-dependent IRF2 acetylation and p300 promoter association; CBP appears in the E1A-based interpretation. The biologically established CBP lysine-acetyltransferase assertion is retained with curator deference and the full-text limit, without representing the abstract as a direct CBPβIRF2 assay. |
| GO:0061733 protein-lysine-acetyltransferase activity | EXP PMID:34239064 Targeting liquid-liquid phase separation of SARS-CoV-2 nucle... | ACCEPT | Summary: Protein-lysine acetylation is directly supported in this substrate context. Reason: The authentic publisher main and Extended Data Figure 4 caption show CBP gain/loss effects on viral N K375 acetylation in HEK293T cells. The 2026 correction replaces specified Fig1/Extended Data Figure 5β6 panels and source data; no retraction or correction to the named Extended Data Figure 4 CBP experiment is asserted. CBP insert species is not assigned merely from host cells. |
| GO:0061733 protein-lysine-acetyltransferase activity | IDA PMID:12435739 Regulation of E2A activities by histone acetyltransferases i... | ACCEPT | Summary: Protein-lysine acetylation is directly supported in this substrate context. Reason: CBP interacts with and acetylates E2A/TCF3 and regulates its transcriptional function. The specific P15923-2 source identity is preserved; no isoform-exclusive activity is inferred. |
| GO:0061733 protein-lysine-acetyltransferase activity | IDA PMID:15273251 Site-specific acetylation of the fetal globin activator NF-E... | ACCEPT | Summary: The established protein-lysine acetyltransferase annotation is retained with the source-access limit. Reason: The abstract foregrounds PCAF-mediated NFE4 acetylation. Preserve the positive curated CBP interaction and acetyltransferase assertions with explicit curator deference and the full-text access limit; do not describe an unverified CBP panel as personally read. NFE4 partner classification is considered separately. |
| GO:0061733 protein-lysine-acetyltransferase activity | IDA PMID:24207024 Repression of RNA polymerase I upon stress is caused by inhi... | ACCEPT | Summary: Protein-lysine acetylation is directly supported in this substrate context. Reason: CBP acetylates the Pol I-associated factor PAF53/POLR1E, reducing rDNA transcription. The study supports a performed regulatory step and context-specific negative Pol I regulation, not a universal repressor identity. |
| GO:0061733 protein-lysine-acetyltransferase activity | IDA PMID:24939902 CBP and p300 acetylate PCNA to link its degradation with nuc... | ACCEPT | Summary: Protein-lysine acetylation is directly supported in this substrate context. Reason: Actual Methods/Results/Discussion establish direct CBP-fragmentβPCNA binding, PCNA acetylation, chromatin-associated interaction after UV and PCNA turnover during NER. They do not directly resolve lesion-selective DNA binding; preserve the positive repair mechanism and that narrower uncertainty. |
| GO:0061733 protein-lysine-acetyltransferase activity | IDA PMID:28790157 SIRT7 and the DEAD-box helicase DDX21 cooperate to resolve g... | ACCEPT | Summary: Protein-lysine acetylation is directly supported in this substrate context. Reason: CBP interacts with and acetylates DDX21. The source supports nonhistone lysine acetylation and RNA-helicase partner binding without giving CREBBP helicase activity. |
| GO:0061733 protein-lysine-acetyltransferase activity | IDA PMID:30540930 SIRT7-Dependent Deacetylation of Fibrillarin Controls Histon... | ACCEPT | Summary: Protein-lysine acetylation is directly supported in this substrate context. Reason: CBP acetylates fibrillarin and reduces its H2A glutamine methylation/rDNA transcription function. This is an explicit regulatory action on an active enzyme, not merely a secondary expression phenotype. |
| GO:0061733 protein-lysine-acetyltransferase activity | IDA PMID:35675826 Deubiquitinase OTUD3 regulates metabolism homeostasis in res... | ACCEPT | Summary: Protein-lysine acetylation is directly supported in this substrate context. Reason: The recovered original target windows establish CBP-dependent OTUD3 acetylation, nutrient responsiveness and enhanced OTUD3 nuclear localization, with mutant and depletion controls. Human OTUD3 is explicit; CBP insert identity is not inferred from HEK293T host. The G288D metabolic phenotype is not explained simply by altered acetylation or localization. |
| GO:0061733 protein-lysine-acetyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: The EC and RHEA mappings describe the established catalytic reaction. Reason: RHEA45948 and EC2.3.1.48 support the source protein-lysine acetyltransferase activity and agree with direct target assays. The source chemistry does not establish activity equivalence of the two official products. |
| GO:0061733 protein-lysine-acetyltransferase activity | TAS PMID:28386764 Roles of tau protein in health and disease. | ACCEPT | Summary: The review supports the established lysine-acetyltransferase activity. Reason: This review discusses tau acetylation by CBP and related enzymes, including site-dependent pathological and protective effects. It supports contextual tau binding and lysine acetylation, not an independent primary assay. |
| GO:0061733 protein-lysine-acetyltransferase activity | TAS Reactome:R-HSA-9825747 | ACCEPT | Summary: The actual HINT1 event supports protein-lysine acetylation. Reason: R-HSA-9825747 explicitly represents CREBBP-dependent HINT1 acetylation, with a positive typed path to Q92793. Retain the catalytic assertion without assigning HINT1βs downstream transcription-factor function to CREBBP. |
| GO:0065003 protein-containing complex assembly | TAS PMID:7913207 Nuclear protein CBP is a coactivator for the transcription f... | KEEP AS NON CORE | Summary: Transcriptional complex assembly is retained at its broad source scope. Reason: The original CBPβCREB study supports transcriptional coactivation and complex formation. Historical broad cellular localization and assembly statements are retained without inventing a modern fixed complex stoichiometry. Recruitment/association of transcriptional cofactors supports the contextual assembly statement; no universal fixed complex or independent structural scaffold is inferred. |
| GO:0120300 peptide lactyltransferase (CoA-dependent) activity | IDA PMID:38128537 Metabolic regulation of homologous recombination repair by M... | ACCEPT | Summary: CBP directly catalyzes MRE11 lactylation in the studied repair context. Reason: Actual target Methods/Results support CBP-dependent lactylation of purified MRE11, the K673 site, and DNA-repair effects with mutation/depletion controls. The observed catalytic work supports the existing lactyltransferase and repair-regulation assertions; not every cellular lactylation event is assigned to CBP. |
| GO:0120300 peptide lactyltransferase (CoA-dependent) activity | IEA GO_REF:0000120 | ACCEPT | Summary: The rule and RHEA lactyltransferase mapping have direct target grounding. Reason: ARBA00091530 matches the target and the source RHEA61996 reaction agrees with the actual MRE11/lactyl-CoA experiment. The broad catalytic claim is retained without assigning every cellular lactylation event to CBP. |
| GO:0140297 DNA-binding transcription factor binding | IPI PMID:15509593 HNF1beta/TCF2 mutations impair transactivation potential thr... | ACCEPT | Summary: The existing DNA-binding transcription-factor binding assertion is retained. Reason: HNF1B interaction with CBP is retained as DNA-binding transcription-factor binding. The exact P35680-1 partner identity remains unchanged. The original source partner is preserved; incomplete source access is not evidence of a paralog or target mismatch. |
| GO:0140297 DNA-binding transcription factor binding | IPI PMID:15674325 PARP-10, a novel Myc-interacting protein with poly(ADP-ribos... | ACCEPT | Summary: The existing DNA-binding transcription-factor binding assertion is retained. Reason: The curated MYCβCBP interaction is retained with the abstract access boundary. An abstract foregrounding PARP10 is not evidence that the full paper omitted the curator-assigned CBP experiment. The original source partner is preserved; incomplete source access is not evidence of a paralog or target mismatch. |
| GO:0141156 cAMP/PKA signal transduction | IDA PMID:11522779 Regulation of cAMP-responsive element-binding protein-mediat... | KEEP AS NON CORE | Summary: CBP performs coactivator work in the cAMP/PKA transcriptional response. Reason: SRCAP enhances CBP-dependent transcription in cAMP/PKA signaling. This is a context-specific coactivation mechanism, not evidence that CREBBP itself is a PKA kinase. The cached GO-CAM likewise places CBP as the coactivator, not the kinase or cyclic-nucleotide receptor. |
| GO:1900034 regulation of cellular response to heat | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: The heat-response rule represents a contextual transcriptional role. Reason: ARBA00092510 matches the target. Reactomeβs HSF1 transcription/acetylation context supports a regulatory role, while its source summary emphasizes p300 and does not resolve every CBP-specific assay. |
| GO:1900034 regulation of cellular response to heat | TAS Reactome:R-HSA-3371571 | KEEP AS NON CORE | Summary: Retain the source-qualified HSF1 transcriptional response context. Reason: The actual R-HSA-3371571 graph contains nuclear Q92793 in the HSF1 context. The summary distinguishes DNA binding, phosphorylation and transactivation by HSF1; CREBBP is a cofactor, not HSF1 or its kinase. The paper-specific p300 emphasis is retained in reference assessment. |
| GO:1900182 positive regulation of protein localization to nucleus | IDA PMID:35675826 Deubiquitinase OTUD3 regulates metabolism homeostasis in res... | KEEP AS NON CORE | Summary: Acetylation promotes OTUD3 nuclear localization in the tested context. Reason: The recovered original target windows establish CBP-dependent OTUD3 acetylation, nutrient responsiveness and enhanced OTUD3 nuclear localization, with mutant and depletion controls. Human OTUD3 is explicit; CBP insert identity is not inferred from HEK293T host. The G288D metabolic phenotype is not explained simply by altered acetylation or localization. CBP performs the modifying step; the annotation is not inferred merely because OTUD3 requires a substrate modification. |
| GO:1900182 positive regulation of protein localization to nucleus | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: The localization-regulation rule agrees with the OTUD3 mechanism. Reason: ARBA00092943 has a complete current target match. CBP-dependent substrate acetylation supports positive regulation of OTUD3 nuclear localization, not a claim that CREBBP itself is the nuclear import machinery. |
| GO:1901837 negative regulation of transcription of nucleolar large rRNA by RNA polymerase I | IDA PMID:24207024 Repression of RNA polymerase I upon stress is caused by inhi... | KEEP AS NON CORE | Summary: PAF53 acetylation supports a specific negative rRNA-transcription role. Reason: CBP acetylates the Pol I-associated factor PAF53/POLR1E, reducing rDNA transcription. The study supports a performed regulatory step and context-specific negative Pol I regulation, not a universal repressor identity. Retain the narrower nucleolar-rRNA process without treating it as CREBBPβs universal regulatory direction. |
| GO:1905168 positive regulation of double-strand break repair via homologous recombination | IDA PMID:38128537 Metabolic regulation of homologous recombination repair by M... | ACCEPT | Summary: MRE11 modification provides a performed step in repair regulation. Reason: CBP-mediated MRE11 lactylation at K673 is tested biochemically and functionally with target mutation and depletion controls. Enhanced DNA-end processing and homologous-recombination outcomes are linked to that catalytic event, rather than inferred only from requirement for CBP. |
| GO:2000819 regulation of nucleotide-excision repair | IDA PMID:24939902 CBP and p300 acetylate PCNA to link its degradation with nuc... | KEEP AS NON CORE | Summary: PCNA acetylation directly regulates the NER-associated turnover step. Reason: Actual Methods/Results/Discussion establish direct CBP-fragmentβPCNA binding, PCNA acetylation, chromatin-associated interaction after UV and PCNA turnover during NER. They do not directly resolve lesion-selective DNA binding; preserve the positive repair mechanism and that narrower uncertainty. This is a performed regulatory contribution; CBP is not asserted to recognize or excise the DNA lesion. |
| GO:2000819 regulation of nucleotide-excision repair | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: The current rule matches a mechanistically supported repair context. Reason: ARBA00033899 matches the target and the actual CBPβPCNA acetylation/turnover experiments support NER regulation. Retain the role without confusing it with direct lesion recognition. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:19805293 CBP and p300 are cytoplasmic E4 polyubiquitin ligases for p5... | NEW | Summary: Contextual ubiquitin ligase activity is demonstrated by direct chain-extension assays. Reason: A two-step assay primes p53 with MDM2, removes MDM2, then demonstrates CBP-dependent ubiquitin-chain extension; bacterially expressed N-terminal CBP and endogenous human cytoplasmic fractions provide additional support. This is catalytic work, not merely necessity for p53 turnover. GO:0061630 matches ubiquitin transfer to an amide-linked protein product; the literal thioester-product wording of GO:0034450 does not describe this experiment. The existing 47 term ancestries and five target GO-CAM activities contain no covering ubiquitin MF. Human cDNA provenance is supported by the cited U47741 construct source, while the pRSV/pcDNA vector-name discrepancy, main/caption dose-unit discrepancy and unaccessed supplement remain explicit. No isoform 2 equivalence, linkage specificity, new degradation process or additional compact core is inferred. Supporting Evidence: PMID:19805293 the same region of CBP encodes its E3/E4 activity |
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Download this section (compressed HTML)Q: Does the damaged-DNA binding assertion describe a demonstrated CBPβlesion-DNA interaction, or chromatin recruitment through PCNA and other proteins? The positive PCNA modification and repair contribution are established independently.
Q: Should GO:0034450 ubiquitin-ubiquitin ligase activity be revised to distinguish product isopeptide formation from the thioester-product reaction currently written in its definition? The demonstrated CBP chain-extension assay supports broader GO:0061630.
Q: How does the Q92793-2 replacement within the TAZ1 recruitment region alter partner selection, acetylation or N-terminal ubiquitin ligase activity? Shared catalytic regions do not establish equal function.
Q: Should type I interferon receptor binding include intracellular IFNAR2 contacts such as CREBBP, given the literal receptor-binding definition but predominantly interferon-ligand usage of GO:0005132? The proposed term describes contact, not receptor agonism.
Experiment: Compare sequence-verified full-length Q92793-1 and Q92793-2 with matched expression, localization and recruitment assays, separating changes in TAZ1-mediated binding from catalytic competence.
Experiment: Measure purified CREBBP binding to matched undamaged and lesion-containing DNA, with and without PCNA or nucleosomes, to separate lesion recognition from chromatin-protein recruitment.
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Download this section (compressed HTML)Loading supporting contentβ¦
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