EP300

Summary: Context-dependent transcriptional repression by the CRD1 region is supported.

Reason: The original Methods and Results identify p300 residues 1004–1044 as a repression region in targeted reporter assays. Fig. 8 also tests untethered p300 with p53-responsive reporters. The effect depends on promoter and cell context, and the Discussion cautions that cofactor titration can contribute. Retain this experimentally supported regulatory mode as non-core alongside the predominant coactivator function.

Summary: p300 can repress RNA-polymerase-II transcription in defined contexts.

Reason: The ZNF76-specific experiment in PMID:16337145 remains unavailable beyond its verified abstract, which does not settle the direction of regulation. Independently read PMID:10733570 Methods and Results identify a p300 CRD1 repression region (residues 1004–1044), including targeted reporter assays and untethered p300/p53-responsive reporters in Figure 8. This establishes the general negative-regulation capability represented by the imported term, while leaving the original ZNF76 mechanism unresolved. Retain the context-dependent regulatory mode as non-core; cofactor titration and promoter/cell dependence remain relevant. https://doi.org/10.1128/MCB.20.8.2676-2686.2000.

Summary: EP300 participates in histone-acetyltransferase-containing transcriptional assemblies.

Reason: The official PAINT tree places human EP300 below the GO:0000123 IBD at PTN000351795, without an intervening NOT; the aligned target is identical to canonical Q09472. PMID:9742083 Figure 8 directly tests recombinant GCN5/PCAF association with a p300 fragment, while independent p300 enzymology establishes HAT activity. InterPro IPR014744 supplies a consistent interlocking coactivator-domain mapping for the electronic row. This supports HAT-containing assemblies without claiming that all associated acetyltransferases occupy one permanent complex.

Summary: EP300 participates in histone-acetyltransferase-containing transcriptional assemblies.

Reason: The official PAINT tree places human EP300 below the GO:0000123 IBD at PTN000351795, without an intervening NOT; the aligned target is identical to canonical Q09472. PMID:9742083 Figure 8 directly tests recombinant GCN5/PCAF association with a p300 fragment, while independent p300 enzymology establishes HAT activity. InterPro IPR014744 supplies a consistent interlocking coactivator-domain mapping for the electronic row. This supports HAT-containing assemblies without claiming that all associated acetyltransferases occupy one permanent complex.

Summary: p300 is recruited to active promoter chromatin.

Reason: PMID:21084751 Results on L-PK promoter occupancy/Figure 3 and ChIP Methods show p300 recruitment with ChREBP and polymerase II in glucose-stimulated primary mouse hepatocytes. This supports the conserved chromatin coactivator location; it does not establish sequence-specific DNA binding by p300. HepG2/HEK293T biochemical experiments are distinct. Original: https://doi.org/10.1172/JCI41624.

Summary: p300 engages transcriptional coregulators.

Reason: The PMID:8684459 publisher abstract identifies the p300/CBP-associated acetyltransferase PCAF and competition with E1A; the original main article remains subscription-limited. This coregulator interaction is consistent with independently inspected p300 coactivation complexes, including the human CITED1/ERalpha experiments in PMID:11581164 Figures 1 and 7. The imported PCAF partner is retained without claiming that the inaccessible assay or a purified binary interface was independently inspected. https://doi.org/10.1038/382319a0; https://doi.org/10.1101/gad.906301.

Summary: EP300 binds transcription coactivators, directly demonstrated for AUTS2.

Reason: Independent original PMID:25519132 Figure 4 and Extended Data Figure 3 demonstrate AUTS2–p300 association, recombinant-protein binding and p300-dependent AUTS2 transcriptional activation in human 293-derived cell experiments. This resolves the target coactivator-binding assertion. The matched ARBA rule and mouse orthology sources are genuine; the precise p300 contribution in the older mouse donor source PMID:17641689 remains unresolved because the read experiments chiefly assay CBP/MED25 and its supplement was unavailable. Biological acceptance rests on the independently read target evidence, not an assumed donor experiment.

Summary: The bound TReP-132 protein is a DNA-binding transcription factor.

Reason: The indexed original abstract describes TReP-132/TRERF1 binding the CYP11A1 regulatory DNA and physically interacting with CBP/p300. The coactivator-binding term excludes proteins that directly recognize DNA; the existing RNA-polymerase-II transcription-factor-binding term better describes this interaction. Full experimental details remain inaccessible.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: p300 supports the HIF-dependent hypoxic transcriptional response.

Reason: The verified abstract reports disruption of the p300 CH1–HIF interaction by chetomin and reduced hypoxia-inducible transcription. Independent original PMID:9887100 establishes p300 CH1 interactions and hypoxia-mimetic reporter responses. This is a supported physiological use of coactivation, retained outside the minimal core-function summary.

Summary: p300 participates in the hypoxic response through HIF coactivation.

Reason: Original Results and captions4–7 show CH1 binding to HIF1A, interference by p35srj/CITED2 and altered HIF-responsive transcription after hypoxia or deferoxamine. Retain the context-specific response without treating p300 as the oxygen sensor.

Summary: Reduced mouse Ep300 dosage alters wall-following behavior in a specific maze phase.

Reason: The B2RWS6 mouse donor traces to PMID:19822209. Its actual Methods and Figure 4C compare adult male Ep300 heterozygotes with wild-type littermates and show increased thigmotaxis during the visible-platform task; the effect is absent in later phases. The current GO definition includes wall-following behavior. Retain the ortholog-supported contextual behavioral contribution, with the restricted assay context and without claiming direct human behavioral testing.

Summary: Human EP300 directly binds the p53 transactivation domain.

Reason: The mouse Ep300 donor is correctly mapped, although its PMID:17591690 original was not recovered. Independent target original PMID:19217391 Results/Figures 1–2 and Experimental Procedures directly establish human p300 TAZ2 binding to p53 by intermolecular NMR contacts, fluorescence-anisotropy competition and mutagenesis. The assayed p300 fragment spans1723–1812 with four non-zinc-coordinating cysteines substituted by alanine; p53 is principally the2–39 fragment. This is positive target binding evidence with explicit construct limits, not inference from reporter coactivation or a claim of full-length reconstitution.

Summary: Ep300 dosage contributes to anxiety-related defensive behavior in mice.

Reason: The mouse donor evidence is PMID:19822209, whose Methods and Figure 3E–F document reduced elevated-plus-maze open-arm exploration by Ep300 heterozygotes. This provides a bounded behavioral response to an aversive environment consistent with the GO definition, despite unchanged ordinary open-field center time and largely normal fear conditioning. Retain the contextual ortholog-supported role rather than claiming a general motor or fear-learning failure.

Summary: EP300 contributes to the transcriptional output of lectin-receptor signaling.

Reason: ARBA00087826 matches the actual target domains and lineage. The curated Reactome C-type-lectin-receptor pathway includes nuclear NF-kB regulation, with EP300 recruitment and RELA acetylation represented in reactions R-HSA-5660666 and R-HSA-5660660. Independently read PMID:15616592 Figures 3–4 and7 establishes p300 participation in stimulus-responsive NF-kB coactivation. Retain this specialized pathway context as non-core; the direct original is a TNF/LPS system, not a new p300 experiment stimulating a particular lectin receptor, and EP300 is not a carbohydrate-binding receptor.

Summary: EP300 contributes to the transcriptional output of lectin-receptor signaling.

Reason: ARBA00087826 matches the actual target domains and lineage. The curated Reactome C-type-lectin-receptor pathway includes nuclear NF-kB regulation, with EP300 recruitment and RELA acetylation represented in reactions R-HSA-5660666 and R-HSA-5660660. Independently read PMID:15616592 Figures 3–4 and7 establishes p300 participation in stimulus-responsive NF-kB coactivation. Retain this specialized pathway context as non-core; the direct original is a TNF/LPS system, not a new p300 experiment stimulating a particular lectin receptor, and EP300 is not a carbohydrate-binding receptor.

Summary: A p53–p300 DNA-associated complex does not resolve direct p300 DNA binding.

Reason: The verified abstract reports a stable DNA-binding complex containing p53 and p300. It does not establish which component contacts DNA. Original assay details remain inaccessible; retain the curator annotation undecided. The independent TFIIIC study tests a different template and cannot refute binding in the p53 experiment.

Summary: The supported DNA-associated role is chromatin engagement.

Reason: The mouse ortholog mapping is correct. Actual PMID:18458156 Figure 6 and Methods establish p300 recruitment to promoter chromatin by ChIP, while the official PAINT annotation independently supports chromatin DNA binding. Refine the broad DNA-binding term to that established context; promoter sequence recognition by Pitx2 or other DNA-binding factors is not assigned to EP300.

Proposed replacements: chromatin DNA binding

Summary: p300 associates with chromatin-bound PCNA during the DNA damage response.

Reason: PMID:24939902 Figure 1F and Cell fractionation/immunoprecipitation Methods detect p300-associated PCNA in the chromatin fraction of UV-irradiated human LF-1 fibroblasts. This supports association with the chromatin complex; it does not establish autonomous recognition of a damaged DNA lesion. Original: https://doi.org/10.1093/nar/gku533.

Summary: EP300 binds transcriptionally active chromatin as a histone-modifying coactivator.

Reason: PMID:25818647 Figures 1–2 establish p300 activity on histone octamers and recombinant chromatin, and Figure 4 compares the authors' histone-mark ChIP with previously published mouse macrophage p300 ChIP data. The HeLa nuclear-extract and recombinant-chromatin evidence is distinct from those mouse data. This supports chromatin engagement rather than sequence-specific DNA recognition. PMID:23934153 Figure 4c and Supplementary Table 2 additionally directly measure binding of p300 bromodomain-containing constructs to modified histone peptides.

Summary: EP300 engages chromatin through its histone-modifying and coactivator machinery.

Reason: ARBA00027831 matches EP300 condition set23, and mouse-donor PMID:23752591 main Results identify p300 ChIP enrichment at a myostatin promoter and intronic enhancer. Independent target enzymology and modified-histone binding support the broader chromatin-binding activity. The intronic element here is genomic DNA, not pre-mRNA; chromatin engagement does not imply sequence-specific DNA recognition.

Summary: EP300 chromatin association is independently demonstrated.

Reason: PMID:17641689 operative main experiments chiefly assay CBP/MED25; its unreviewed supplement leaves the precise EP300 source experiment unresolved. Independent human-target PMID:24939902 Figure 1F and cell-fractionation/immunoprecipitation Methods recover p300-associated PCNA in the chromatin fraction of UV-treated LF-1 fibroblasts. This positive evidence resolves chromatin binding without transferring CREBBP experiments or asserting autonomous damaged-DNA recognition. https://doi.org/10.1093/nar/gku533.

Summary: Direct damaged-DNA binding is not resolved by the inspected experiments.

Reason: The current GO:0003684 definition requires binding to damaged DNA. PMID:24939902 Figures 1F,5C and6A establish p300 association with chromatin-bound PCNA and effects of combined CBP/p300 depletion on PCNA retention. Figure 6A describes whole-nuclear CBP/p300 staining and PCNA spots, rather than a purified p300 damaged-DNA binding assay. The main Methods/Results and captions were read, but supplementary original experiments and image pixels were not independently inspected. Retain uncertainty about this IDA assertion instead of equating protein-mediated recruitment with direct DNA binding or claiming the function is disproven. Original: https://doi.org/10.1093/nar/gku533.

Summary: The rule matches EP300, but damaged-DNA binding needs the operative target evidence.

Reason: ARBA00089041 genuinely matches the target FunFam domains and lineage. Actual PMID:24939902 Figure 1F establishes p300 association with chromatin-bound PCNA; Figure 6A describes whole-nuclear CBP/p300 staining and PCNA damage-site spots. These experiments do not by themselves distinguish damaged-DNA binding from protein-mediated chromatin recruitment. The main Methods/Results and captions were inspected, but the supplementary experiments and image pixels were not. Retain uncertainty about the precise binding activity without claiming it is disproven.

Summary: EP300 is specifically a transcription coactivator.

Reason: IPR003101 and IPR036529 map the genuine KIX domain and supply the general transcription-coregulator term. Independent p300-dependent chromatin transcription assays and target interactions establish the more informative coactivator activity. Refine the annotation while preserving the imported domain sources; context-dependent repression elsewhere does not erase the positive activity.

Proposed replacements: transcription coactivator activity

Summary: Transcription coactivation is a defining EP300 activity.

Reason: Human EP300 is below the verified PTN000351795 coactivator IBD in the actual PANTHER tree with no intervening NOT; the self-WITH target is legitimate descendant experimental evidence. ARBA00028308 and IPR014744 independently match its genuine domains. Recovered PMID:25818647 Figure 2 directly couples p300-mediated chromatin modification to transcription, and PMID:20955178 Figure 4B measures p300 enhancement of XBP1s-dependent reporter output with explicit construct limitations.

Summary: p300 acts as a transcriptional coactivator in the JMY–p53 response.

Reason: The verified abstract describes a physiological p300/JMY complex recruited to activated p53, with enhanced p53-dependent transcription. This agrees with independently read p300/p53 coactivation experiments in PMID:10733570. Retain this established core activity while the cited original remains available only as an abstract.

Summary: p300 coactivates TFAP2A in cooperation with CITED2.

Reason: The verified abstract reports p300/CBP-dependent TFAP2A activation, rescue in heterozygous fibroblasts and physical association in transfected U2-OS cells. This is the canonical coactivator function. The D1399Y mutant also loses interaction, so its phenotype alone does not isolate catalytic necessity.

Summary: p300 contributes coactivator activity at the p53-responsive p21 promoter.

Reason: The verified abstract links p300/CBP recruitment and histone acetylation to endogenous p21 induction and reports reduced induction after coactivator knockdown. Independently read PMID:10733570 also directly tests p300-dependent p53 reporter activation. Retain the core function without inventing the inaccessible source-specific assay details.

Summary: p300 coactivates the Cart1/ALX1 transcription factor.

Reason: The verified structured abstract reports physical interaction, p300/CBP-enhanced Cart1 transcription and recombinant p300-HAT acetylation of Cart1. The source binding partner is mouse Alx1, not a human isoform. These experiments support coactivation, while the original full text remains inaccessible.

Summary: HIF-dependent transcription uses the p300 coactivator function.

Reason: The verified abstract reports disruption of HIF binding to the p300 CH1 domain and loss of transcriptional coactivation. Direct CH1 interaction and reporter evidence is independently available in the fully recovered original PMID:9887100. Retain the core coactivator activity.

Summary: p300/CBP recruitment supports STAT1 transcriptional coactivation.

Reason: The verified abstract identifies STAT1 Leu724 and phospho-Ser727 as determinants of CBP/p300 recruitment to target promoters. Retain the well-established coactivator function, with the source-specific construct and p300-versus-CBP assay details unresolved because the original full text was inaccessible.

Summary: p300 functions as a transcriptional coactivator at the HIV promoter.

Reason: The verified abstract reports cooperation between p300 and SWI/SNF in Tat-dependent promoter activation, including dependence on p300 acetyltransferase activity and Tat Lys50/Lys51. Retain this demonstrated use of the core coactivator function; the original Methods and figures remain unread.

Summary: Transcriptional coactivation is a directly established p300 function.

Reason: The accessible MED25 study primarily assays CBP rather than EP300 in its operative Methods and Figs.6–8. It is therefore not treated as independently verified EP300 evidence. Retain the biologically established activity using direct p300 reporter experiments in PMID:10733570 and the reconstituted p300 system in PMID:18644873; preserve the imported reference.

Summary: p300 participates in the activated androgen-receptor coactivator complex.

Reason: The recovered original Fig. 4 and Methods show DHT-dependent p300 occupancy at the PSA promoter and association with AR in LNCaP cells. Antagonist-dependent recruitment of prohibitin accompanies loss of p300. Retain the coactivator function; this study does not make p300 the antagonist-induced repressor.

Summary: Transcription coactivation is a defining EP300 activity.

Reason: Human EP300 is below the verified PTN000351795 coactivator IBD in the actual PANTHER tree with no intervening NOT; the self-WITH target is legitimate descendant experimental evidence. ARBA00028308 and IPR014744 independently match its genuine domains. Recovered PMID:25818647 Figure 2 directly couples p300-mediated chromatin modification to transcription, and PMID:20955178 Figure 4B measures p300 enhancement of XBP1s-dependent reporter output with explicit construct limitations.

Summary: p300 supports TReP-132-dependent transcriptional activation.

Reason: The verified abstract reports physical CBP/p300 association with TReP-132 and increased CYP11A1 reporter activity on coexpression. This is consistent with p300 coactivation. The nuclear localization described there is for TReP-132 and is not reused as a p300 localization experiment.

Summary: p300 contributes coactivation in the p8–Pax2 promoter system.

Reason: The verified abstract reports p8/NUPR1 binding to p300 and enhancement of p300-supported Pax2A/Pax2B transcription in glucagon-producing cells. The study also reports p300 acetylation of recombinant p8, but explicitly leaves the significance of that modification unresolved. Retain coactivation without adding a separate glucagon-process claim.

Summary: p300 coactivates NF-kappaB-dependent nNOS transcription.

Reason: The verified abstract describes enhanced nNOS promoter activity and expression, p300–NF-kappaB interaction and acetylation of p65/p50 in human SK-N-SH cells. This directly supports the annotated coactivator function, although original Methods and figures could not be recovered.

Summary: p300 coactivates Sp1-dependent transcription during the PC12 response.

Reason: The original publisher abstract reports p300 recruitment to promoter-associated complexes, p300/Sp1 interaction and enhanced Sp1-dependent transcription. PC12 is the experimental cellular context. The full article was not recovered; independently read p300 coactivation experiments corroborate the core activity.

Summary: Histone acetyltransferase activity is independently established.

Reason: PMID:21131905 Figure 5/Table II measures histone acetylation after mouse CBP/p300 double deletion. Independent recombinant-p300 histone acetylation in PMID:25818647 Figure 1E–G resolves the catalytic claim without describing the mouse study as a human purified-enzyme assay. Originals: https://doi.org/10.1038/emboj.2010.318; https://doi.org/10.1016/j.molcel.2015.02.029.

Summary: Histone acetyltransferase activity is independently established.

Reason: The PMID:23415232 abstract explicitly identifies p300/CBP-dependent H3K122 acetylation, but the original methods remain inaccessible after the recorded Cell publisher attempt. Independent recombinant p300 histone acetylation in PMID:25818647 Figure 1E–G supports the broad HAT claim without inventing the unavailable H3K122 assay details. Originals: https://doi.org/10.1016/j.cell.2013.01.032; https://doi.org/10.1016/j.molcel.2015.02.029.

Summary: EP300 has intrinsic histone lysine acetyltransferase activity.

Reason: The original PMID:23934153 supplement, Supplementary Figure 1c, directly measures HAT activity on an H3 peptide with an activation-loop-deleted catalytic-core reagent. Supplementary Table 1 and Figure 6 document autoacetylation and substrate-acetylation mutants. The main article remains unavailable; no full-length-protein kinetic constants are inferred from the engineered core. Independently read PMID:25818647 Figures 1F–G and 2 directly establish p300 histone acetylation. The access limit therefore does not make this well-established function uncertain.

Summary: p300 directly acetylates linker histone H1.

Reason: PMID:40240600 Results/Figure 4 and In vitro acetylation Methods use purified GST-p300 HAT, histone substrates and acetyl-CoA. Wild-type catalytic-domain rescue, the inactive E1399A control and substrate K75R distinguish enzymatic activity from recruitment alone. This expands the directly tested histone substrate context without changing p300’s established HAT identity. Original: https://doi.org/10.1038/s41586-025-08835-0.

Summary: EP300 is a histone lysine acetyltransferase, independently established beyond the historical citation.

Reason: PMID:8945521 has independently verified identity and an abstract reporting p300/CBP HAT activity, but its full Methods and Results were not recovered. The function is independently demonstrated in PMID:25818647 Figures 1F–G and 2 using recombinant p300 and histone/chromatin substrates, and in the original PMID:23934153 Supplementary Figure 1c. Retain the established function while preserving the original citation and its explicit access limit.

Summary: EP300 directly catalyzes histone lysine acetylation.

Reason: The verified PAINT root assertion, genuine CBP/p300 HAT-domain matches and RHEA:21992 all specify transfer of an acetyl group from acetyl-CoA to histone lysine. Reactome R-HSA-3662335 explicitly represents EP300 acetylation of core histones. Independently read PMID:25818647 Figures 1–2 supplies direct p300/histone and chromatin evidence, and PMID:27105113 Figure 7 directly compares acetylation with butyrylation. Neither the number of donors nor the presence of the target in WITH/FROM weakens this supported function.

Summary: Independent direct experiments establish p300 histone acetyltransferase activity.

Reason: PMID:12040021 remains abstract-only; its MBF-1-focused abstract does not resolve the supporting p300 assay. That limited view is not evidence of a wrong-target citation. Recombinant p300 histone acetylation in independently inspected PMID:25818647 Figure 1E–G establishes the same broad function. Sources: https://doi.org/10.1210/mend.16.6.0843; https://doi.org/10.1016/j.molcel.2015.02.029.

Summary: NPAS2-associated p300 retains histone acetyltransferase activity.

Reason: PMID:14645221 Experimental Procedures, Histone Acetyltransferase Assays (p7092), and Figure 1E/Results (p7093) test recombinant FLAG-p300 retained on GST-NPAS2 with purified histones and radiolabeled acetyl-CoA. This directly supports HAT activity. The inspected main text does not specify recombinant p300 species or residue boundaries. Original: https://doi.org/10.1074/jbc.M311973200.

Summary: Purified p300 acetylates histones and promotes transcription from modified chromatin.

Reason: PMID:25818647 Figures 1E–G compare purified HATs, include acyl-donor controls and directly detect p300-mediated histone acetylation. Figure 2 couples histone modification to transcription from recombinant chromatin and tests histone lysine substitutions. Human-cell p300/CBP perturbations in Figure 1H corroborate the chromatin acetylation role. This is an intrinsic, characteristic EP300 catalytic function.

Summary: EP300 directly catalyzes histone lysine acetylation.

Reason: The verified PAINT root assertion, genuine CBP/p300 HAT-domain matches and RHEA:21992 all specify transfer of an acetyl group from acetyl-CoA to histone lysine. Reactome R-HSA-3662335 explicitly represents EP300 acetylation of core histones. Independently read PMID:25818647 Figures 1–2 supplies direct p300/histone and chromatin evidence, and PMID:27105113 Figure 7 directly compares acetylation with butyrylation. Neither the number of donors nor the presence of the target in WITH/FROM weakens this supported function.

Summary: Histone acetyltransferase activity is independently demonstrated for p300.

Reason: The cited Oncogene article is available here only as an abstract, which emphasizes neuronal coactivation rather than its HAT assay. Independent original PMID:18644873 Methods and Fig. 2C directly test purified p300-dependent histone acetylation with acetyl-CoA. Retain the established core activity without claiming the source article was fully inspected.

Summary: EP300 directly catalyzes histone lysine acetylation.

Reason: The verified PAINT root assertion, genuine CBP/p300 HAT-domain matches and RHEA:21992 all specify transfer of an acetyl group from acetyl-CoA to histone lysine. Reactome R-HSA-3662335 explicitly represents EP300 acetylation of core histones. Independently read PMID:25818647 Figures 1–2 supplies direct p300/histone and chromatin evidence, and PMID:27105113 Figure 7 directly compares acetylation with butyrylation. Neither the number of donors nor the presence of the target in WITH/FROM weakens this supported function.

Summary: p300 acetylates human Dna2 using acetyl-CoA, with full-length and catalytic-domain preparations tested.

Reason: PMID:20019387 Experimental Procedures and Figure 1 use [14C]acetyl-CoA and a protein substrate. Current GO:0004468 instead specifies acetyl phosphate plus free L-lysine. Replace this chemically mismatched activity with GO:0061733, already present elsewhere in this review; retain the imported source assertion unchanged.

Proposed replacements: protein-lysine-acetyltransferase activity

Summary: The source-specific atrophin interaction remains unresolved.

Reason: PMID:17150957 identity and abstract were verified, but the original interaction experiments were inaccessible. The abstract discusses atrophin transcriptional activities without resolving this EP300 interaction. Preserve the curator assertion and uncertainty; this access limit is not evidence against binding.

Summary: The demonstrated partner is the nuclear receptor PPARalpha.

Reason: PMID:26983400 Results/Figure 3A and Methods show p300–PPARalpha association in human HepG2 cells and loss of association with the p300 LXXAA mutant. Mouse liver adenovirus experiments are separate from this human-cell binding evidence. Nuclear receptor binding captures the established partner class; p300 is not assigned PPARalpha DNA-binding or SIK2 kinase activity. Original: https://doi.org/10.1038/srep23317.

Proposed replacements: nuclear receptor binding

Summary: Adenovirus 12 E1A associates with p300.

Reason: PMID:10049825 explicitly reports p300 binding by adenovirus 12 E1A in its abstract, including distinct p300 interaction regions. The main experimental details remain unread. Retain the supported viral-protein association as non-core without assigning a new transcriptional activity from binding alone.

Summary: Adenovirus E1A associates with the C-terminal region of p300.

Reason: PMID:10330164 Methods and Results/Figures 1–4 test 12S and 13S E1A with p300 fragments. E1A variants alter TFIIB and cyclin E–CDK2 association differently. Preserve the imported partner and isoform context; retain the supported generic interaction as non-core.

Summary: Adenovirus E1A associates with the C-terminal region of p300.

Reason: PMID:10330164 Methods and Results/Figures 1–4 test 12S and 13S E1A with p300 fragments. E1A variants alter TFIIB and cyclin E–CDK2 association differently. Preserve the imported partner and isoform context; retain the supported generic interaction as non-core.

Summary: p300 associates with the protein kinase CDK2 in a cyclin E-containing complex.

Reason: PMID:10330164 Methods and Results show p300–CDK2–cyclin E complexes and recruitment of cellular CDK2 by a p300 fragment. The association requires the cellular context and was not reproduced with in vitro translated CDK2/cyclin E alone. Protein kinase binding describes the partner more specifically; this does not assert an isolated binary interaction or kinase activity of p300.

Proposed replacements: protein kinase binding

Summary: p300 binds the general transcription factor TFIIB.

Reason: PMID:10330164 Methods and Results/Figures 1–3 examine TFIIB association with C-terminal p300 fragments and modulation by E1A. GO:0001093 identifies the general RNA polymerase II factor involved; a sequence-specific DNA-binding transcription factor term would not describe TFIIB.

Proposed replacements: TFIIB-class transcription factor binding

Summary: The named p53 interaction can be represented as transcription-factor binding.

Reason: The source partner P04637 is human TP53. The verified abstract describes recruitment of the p300/JMY complex to activated p53. Replace uninformative protein binding with the existing RNA-polymerase-II-specific DNA-binding transcription-factor-binding term; the interaction does not establish p300 DNA binding.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: p300 binds the JMY transcriptional coactivator.

Reason: The source partner Q9QXM1 is mouse Jmy, and the verified abstract reports a physiological p300/JMY complex that enhances p53 transcription. Coactivator binding captures the demonstrated partner role more precisely than generic binding. The heterologous partner identity is retained, without inventing an EP300 isoform.

Proposed replacements: transcription coactivator binding

Summary: p300 binds the human papillomavirus 18 E2 transcription factor.

Reason: PMID:10702269 is abstract-only here and emphasizes CBP; its EP300 experiments cannot be independently assessed. Independently read PMID:12368347 Figure 1B tests HPV18 E2 binding to p300 fragments, and Figure 2A tests transcriptional cooperation. Refine the binding partner to a RNA polymerase II-specific DNA-binding transcription factor without claiming that the inaccessible original source lacks p300 experiments.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: p300 associates with the non-DNA-binding coactivator CITED1/MSG1.

Reason: PMID:10722728 abstract explicitly describes MSG1 binding to p300/CBP and enhancement of their functional connection with Smad transcription factors. This supports coactivator binding. Preserve the distinct mouse and human source partners; main Methods and species-specific assay details were not accessible and are not inferred.

Proposed replacements: transcription coactivator binding

Summary: p300 associates with the non-DNA-binding coactivator CITED1/MSG1.

Reason: PMID:10722728 abstract explicitly describes MSG1 binding to p300/CBP and enhancement of their functional connection with Smad transcription factors. This supports coactivator binding. Preserve the distinct mouse and human source partners; main Methods and species-specific assay details were not accessible and are not inferred.

Proposed replacements: transcription coactivator binding

Summary: p300 associates with the DNA-binding transcription factor BRN2/POU3F2.

Reason: PMID:11029584 abstract reports GST and two-hybrid evidence for a low-affinity p300 interaction with the POU transcription factor BRN2. The more informative binding term is supported, while exact constructs and main experimental controls remain unread.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: p300 binds the transcriptional coregulator EID1.

Reason: PMID:11073990 operative original Methods and Results/Figures 9–11 show endogenous p300–EID1 association, fragment binding, and EID1 inhibition of MyoD/MEF2-dependent transcription and p300 acetylation activity. GO:0001221 captures the transcriptional coregulator partner without assigning EID1 inhibitory activity to p300. Tethered reporter behavior is not generalized to natural coactivation.

Proposed replacements: transcription coregulator binding

Summary: p300 associates with the DNA repair nuclease FEN1.

Reason: PMID:11430825 abstract explicitly reports a p300–FEN1 complex and FEN1 acetylation. Main assays were inaccessible. Retain the supported substrate-associated interaction as non-core; FEN1 nuclease activity is not an activity of p300.

Summary: p300 associates with the transcriptional cofactor Strap/TTC5.

Reason: PMID:11511361 abstract describes Strap binding to p300 and enhancement of the p300-dependent p53 response. This supports coactivator binding. Preserve the mouse Ttc5 source partner; detailed constructs, species-specific experimental provenance and main controls were not accessible.

Proposed replacements: transcription coactivator binding

Summary: p300 associates with the transcriptional coactivator JMY.

Reason: The main experiments of PMID:11511361 remain inaccessible. Independent PMID:10518217 abstract explicitly supports p300–JMY association and p53 coactivation, as adjudicated for the other JMY source row. Retain the mouse Jmy partner and refine to coactivator binding without representing either inaccessible original as fully read.

Proposed replacements: transcription coactivator binding

Summary: The supported estrogen-receptor interaction has a specific nuclear-receptor binding term.

Reason: PMID:11581164 Results/Figure 7B show endogenous ERalpha–p300 co-immunoprecipitation in human MCF-7 cells after estradiol, enhanced by CITED1; Figure 1E shows cooperative reporter activation. This supports nuclear-receptor binding. The purified Figure 5 binding assay tests CITED1–ERalpha, not a purified p300–ERalpha pair. Original: https://doi.org/10.1101/gad.906301.

Proposed replacements: nuclear receptor binding

Summary: p300 associates with scaffold attachment factor A/HNRNPU.

Reason: PMID:11909954 Methods and Results/Figure 1 show reciprocal endogenous association in U2OS cells and mapping with p300 and SAF-A fragments. Retain the supported interaction as non-core. The RNA-binding properties of HNRNPU do not themselves establish RNA binding by p300.

Summary: The p8/NUPR1 interaction is supported but does not specify an additional core activity.

Reason: The source partner O60356 is NUPR1/p8. The verified abstract reports a pull-down interaction and p300 acetylation of recombinant p8. It does not establish a more specific sequence-selective transcription-factor-binding activity for this interaction. Retain the interaction as non-core.

Summary: p300 associates with the histone chaperone NAP1L1.

Reason: PMID:11940655 original Methods and Results distinguish an initial CBP KIX screen from endogenous p300–NAP1 coimmunoprecipitation and recombinant p300 binding assays. Retain the supported human interaction as non-core. Drosophila chromatin-assembly reagents are separate evidence and do not turn this binding annotation into p300 histone-chaperone activity.

Summary: p300 associates with the E2 transcription factor of bovine papillomavirus 1.

Reason: PMID:12368347 Methods and Results/Figure 1B compare all three E2 proteins with p300 fragments, and Figure 2A examines their transcriptional cooperation with p300. Purified direct binding in Figure 1D specifically uses HPV8 E2 and a p300 HAT fragment; that preparation is not generalized to the other viruses. Refine to the DNA-binding transcription factor partner while preserving its imported identity.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: p300 associates with the E2 transcription factor of human papillomavirus 8.

Reason: PMID:12368347 Methods and Results/Figure 1B compare all three E2 proteins with p300 fragments, and Figure 2A examines their transcriptional cooperation with p300. Purified direct binding in Figure 1D specifically uses HPV8 E2 and a p300 HAT fragment; that preparation is not generalized to the other viruses. Refine to the DNA-binding transcription factor partner while preserving its imported identity.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: p300 associates with the E2 transcription factor of human papillomavirus 18.

Reason: PMID:12368347 Methods and Results/Figure 1B compare all three E2 proteins with p300 fragments, and Figure 2A examines their transcriptional cooperation with p300. Purified direct binding in Figure 1D specifically uses HPV8 E2 and a p300 HAT fragment; that preparation is not generalized to the other viruses. Refine to the DNA-binding transcription factor partner while preserving its imported identity.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: The E2A interaction supports a specific transcription-factor binding term.

Reason: PMID:12435739 reports endogenous E2A co-immunoprecipitation with p300 from human pre-B nuclear extract and HAT-dependent E2A acetylation/coactivation in its abstract. This is a specific transcription-factor interaction rather than an unspecified protein-binding function. The imported P15923-2 partner is preserved; the inaccessible main article prevents independent resolution of construct bounds or isoform exclusivity. https://doi.org/10.1074/jbc.M211464200.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: p300 associates with the transcriptional coactivator p68/DDX5.

Reason: PMID:12527917 abstract/preview distinguishes p68–p300 coimmunoprecipitation from CBP-fragment mapping and reports p68/p300 transcriptional synergy. This supports coactivator binding; complete Methods and figures were inaccessible. No RNA helicase activity is assigned to p300.

Proposed replacements: transcription coactivator binding

Summary: The named AP-2-alpha interaction is transcription-factor binding.

Reason: The source partner P05549 is TFAP2A. The verified abstract describes physical interaction and the role of its activation domain in p300/CITED2-dependent coactivation. Replace the broad binding annotation with the existing specific transcription-factor-binding term; this does not imply every assay measures an isolated binary complex.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: p300 binds the CITED2 transcriptional coactivator.

Reason: The source partner Q99967 is CITED2. The verified abstract places CITED2 in the p300–TFAP2A coactivation complex. Transcription coactivator binding captures the demonstrated partner role more precisely than generic binding.

Proposed replacements: transcription coactivator binding

Summary: The CITED2 product-specific interaction supports coactivator binding.

Reason: This source row names Q99967-1 as the interacting CITED2 product. Preserve that source identity and refine generic binding to coactivator binding, consistent with the p300/CITED2–TFAP2A activation described in the verified abstract. This is not an isoform assignment for p300.

Proposed replacements: transcription coactivator binding

Summary: Adenovirus E1A associates with p300.

Reason: PMID:12743606 abstract/preview describes distinct E1A-containing p300/CBP and TRRAP/GCN5 complexes; the main experiments were inaccessible. Independent PMID:10330164 original Methods and Figures 1–4 establish E1A association with p300. Preserve the source partner/isoform and retain the supported generic viral-protein interaction as non-core.

Summary: Adenovirus E1A associates with p300.

Reason: PMID:12743606 abstract/preview describes distinct E1A-containing p300/CBP and TRRAP/GCN5 complexes; the main experiments were inaccessible. Independent PMID:10330164 original Methods and Figures 1–4 establish E1A association with p300. Preserve the source partner/isoform and retain the supported generic viral-protein interaction as non-core.

Summary: p300 associates with ING5.

Reason: PMID:12750254 abstract reports association of ING4 and ING5 with p300 and p53. Partial indexed publisher text describes immunoprecipitation controls, but the complete original could not be retrieved. Retain supported association as non-core; do not infer a more specific partner activity solely from enhanced p53 acetylation or reporter output.

Summary: p300 associates with ING4.

Reason: PMID:12750254 abstract reports association of ING4 and ING5 with p300 and p53. Partial indexed publisher text describes immunoprecipitation controls, but the complete original could not be retrieved. Retain supported association as non-core; do not infer a more specific partner activity solely from enhanced p53 acetylation or reporter output.

Summary: The Cart1 interaction is binding to a DNA-binding transcription factor.

Reason: The source partner Q8C8B0 is mouse Alx1/Cart1. The verified structured abstract reports physical p300 interaction with the homeodomain protein and enhanced Cart1-dependent transcription. Refine generic binding to the existing RNA-polymerase-II transcription-factor-binding term while retaining the actual partner identity.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: p300 associates with adenovirus E1A in human-cell extract experiments.

Reason: PMID:1331501 original scanned pages 6894–6895 describe E1A immunoprecipitation from mixed 293/HeLa extracts and show the associated p300 band in Figure 1A. The tested E1A region-1/2 peptides do not displace p300, distinguishing this interaction from E1A binding to pRB/p107. Retain the supported generic interaction as non-core; do not assign the viral binding specificity to an endogenous p300 catalytic role.

Summary: The interaction is with the DNA-binding clock transcription factor BMAL1.

Reason: PMID:14645221 In Vitro Interaction Assays (p7092) and Figure 1C–D/Results (p7093) test p300 association with BMAL1. Reticulocyte-labeled factors/recombinant proteins and GST pull-down are distinguished from endogenous human-cell co-immunoprecipitation. RNA polymerase II-specific DNA-binding transcription factor binding specifies the established partner role without inventing a separate adapter activity. Original: https://doi.org/10.1074/jbc.M311973200.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: The interaction is with the DNA-binding clock transcription factor CLOCK.

Reason: PMID:14645221 In Vitro Interaction Assays (p7092) and Figure 1C–D/Results (p7093) test p300 association with CLOCK. Reticulocyte-labeled factors/recombinant proteins and GST pull-down are distinguished from endogenous human-cell co-immunoprecipitation. RNA polymerase II-specific DNA-binding transcription factor binding specifies the established partner role without inventing a separate adapter activity. Original: https://doi.org/10.1074/jbc.M311973200.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: The interaction is with the DNA-binding clock transcription factor NPAS2.

Reason: PMID:14645221 In Vitro Interaction Assays (p7092) and Figure 1C–D/Results (p7093) test p300 association with NPAS2. Reticulocyte-labeled factors/recombinant proteins and GST pull-down are distinguished from endogenous human-cell co-immunoprecipitation. RNA polymerase II-specific DNA-binding transcription factor binding specifies the established partner role without inventing a separate adapter activity. Original: https://doi.org/10.1074/jbc.M311973200.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: The source reports CREST-coactivator interaction, but its p300-specific experiments remain inaccessible.

Reason: PMID:14716005 identity and abstract were verified; the Science main article and PDF were inaccessible. Its abstract foregrounds CBP and mouse phenotypes, while the imported partner Q91XJ0 is rat CREST/SS18L1. None of these metadata facts demonstrates a mistaken p300 attribution. Retain uncertainty until the actual interaction assay and constructs can be checked.

Summary: The specific p300-TCF3/E47 interaction cannot be resolved from the accessible source material.

Reason: PMID:14752053 abstract discusses BETA2/NeuroD, E47 and competition with p300, but the original Methods and interaction figures were inaccessible through the publisher routes. Preserve the experimental annotation and partner P15923 without inferring an error from the paper title or the abstract emphasis.

Summary: BETA2/NeuroD association with p300 is explicitly reported.

Reason: PMID:14752053 describes competition by SHP for the BETA2/NeuroD-p300 interaction. Together with the curated IPI assertion for the imported NEUROD1 partner, that positive, partner-specific account supports retaining the broad association as non-core. The main Methods and figures remain inaccessible, so exact constructs, species and a purified binary mechanism are not newly asserted. The separate E47 source row is not resolved by this BETA2-specific evidence.

Summary: p300 binds p53; the cited CBP structural paper also tests p300 but in a distinct experimental setting.

Reason: PMID:14759370 Results and Figure 3E show weak endogenous p300-p53 association in mouse NIH/3T3 cells, distinct from the acetylation-dependent CBP interaction; its CBP bromodomain structure is not a p300 structure. Independent human p300-domain binding to human p53 is directly established by PMID:17438265 Table 1 and Figures 2–4. Refine generic protein binding to the existing GO:0002039 p53 binding (index 11), which names the verified partner without transferring the CBP reader mechanism.

Proposed replacements: p53 binding

Summary: The reported ESE-1/ELF3-p300 association is supported at the abstract level.

Reason: PMID:15075319 explicitly identifies p300 among ESE-1-interacting proteins and reports p300-enhanced ESE-1 transcription. The imported partner is ELF3/P78545. Defer to the curated IPI annotation for the reported association and retain it as non-core. The inaccessible main Methods/figures still limit assay and construct claims; this acceptance does not certify a purified binary interaction or introduce a narrower mechanistic term.

Summary: HIF1A binding can be described by a specific transcription-factor-binding term.

Reason: The source partner Q16665 is HIF1A. The verified abstract describes the p300 CH1–HIF interaction, independently supported by original PMID:9887100 binding assays. Replace generic binding with the existing RNA-polymerase-II-specific transcription-factor-binding term.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: The reported HCV core-p300 association is retained as non-core.

Reason: PMID:15380363 explicitly reports interaction of HCV core with p300/CBP alongside coactivation effects. This positive source statement and the curated IPI annotation support the generic association with the imported core product. Retain that product identifier unchanged. Main Methods and figures remain unavailable, so the exact viral preparation, host constructs and binary interaction controls are not independently verified.

Summary: Human IRF1 binds p300 and can stimulate p300-dependent p53 acetylation.

Reason: PMID:15509808 Figure 2A shows endogenous IRF1 in p300 immunocomplexes after irradiation of human A375 cells. Figure 2B-C and Methods map human IRF1 peptide binding to human p300, including full-length Sf9-purified protein. IRF1 is the sequence-specific transcription factor in this coactivator interface, even though its DNA-binding activity is dispensable for the separately tested stimulation of p53. Refine to existing GO:0061629 (indices 400–403); this describes p300 binding the transcription factor and does not assign IRF1 DNA-binding activity to p300.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: p300 and p53 form a complex in human H1299 cells, with VRK1 expression increasing their association.

Reason: PMID:15542844 Figure 6B and immunoprecipitation Methods directly detect p53 in p300 immunoprecipitates from human H1299 cells, with input and tagged-p300 controls; Figure 6A separately measures p53 acetylation. Refine to existing GO:0002039 p53 binding (index 11). VRK1 enhances association but its protein kinase activity is not transferred to p300.

Proposed replacements: p53 binding

Summary: The SMAD3 linker associates with p300 in human HEK-293 cells.

Reason: PMID:15588252 Figure 3 and Experimental immunoprecipitation Methods show association of p300-HA with SMAD3 linker and full-length constructs in HEK-293 cells. SMAD3 is a receptor-regulated SMAD, making current GO:0070412 R-SMAD binding a directly supported refinement of protein binding. The linker interaction is constitutive under these conditions, whereas full-length SMAD3 association is TGF-beta dependent; the replacement preserves that tested partner role without inferring a receptor or kinase activity for p300.

Proposed replacements: R-SMAD binding

Summary: SIRT1 association supports histone deacetylase binding.

Reason: Verified PMID:15632193 and PMID:19047049 abstracts explicitly report p300–SIRT1 interaction; their operative main interaction experiments remain unavailable. Independently read PMID:20660480 Results preceding Figure 5 and Discussion explicitly report p300–SIRT1 interaction and cite their Supplementary Figure4, which could not be inspected. That main-text interaction report corroborates the positive source claims; Figure 5B re-ChIP demonstrates shared promoter occupancy only and is not used as proof of physical binding. SIRT1 is a classIII histone deacetylase, so GO:0042826 identifies the supported partner class more informatively. Neither a purified binary interface nor deacetylase catalysis by p300 is asserted. https://doi.org/10.1093/nar/gkq609.

Proposed replacements: histone deacetylase binding

Summary: The source-specific p300-beta-catenin interaction remains unresolved.

Reason: PMID:15843474 accessible material is the abstract, which describes Cited1 effects on Wnt/beta-catenin and Smad4 transcription. The original interaction data and constructs were not accessible from the publisher landing page. Preserve the imported CTNNB1 partner and retain uncertainty; a pathway-level transcriptional effect alone is not an independently verified binding assay.

Summary: CITED1 association supports transcription coactivator binding.

Reason: The operative interaction assay in PMID:15843474 remains inaccessible. Independent PMID:10722728 explicitly reports MSG1/CITED1 association with p300/CBP and its non-DNA-binding coactivator role in the verified abstract. Actual PMID:11581164 Results/Figures 1E and3D separately establish p300-dependent CITED1 coactivation and functional CR2-domain requirements; these reporter assays are not represented as a purified CITED1–p300 interface. Together the positive same-partner evidence supports refining the human Q99966 interaction to coactivator binding, without certifying the unread source-specific phosphorylation or nephrogenesis experiment. https://doi.org/10.1101/gad.906301.

Proposed replacements: transcription coactivator binding

Summary: p300-dependent FOXO1 acetylation is reported, but the binding assertion requires the inaccessible original experiments.

Reason: PMID:15890677 abstract explicitly reports direct p300 acetylation of Foxo1, whereas the publisher main article was inaccessible. The exact interaction assay and species/construct details for the imported human FOXO1 partner were not checked. Retain uncertainty for the binding row; substrate modification alone is not substituted for its particular interaction evidence.

Summary: SV40 large T antigen associates with p300 in a p53-dependent complex.

Reason: PMID:16611888 Figures 1C and 3C show endogenous human p300 association with SV40 large T antigen and loss of that association after p53 depletion; Figure 4 maps a human p300 CH3 construct. The study supports complex association, not p53-independent binary binding. Retain the contextual interaction as non-core with this explicit bridging mechanism.

Summary: Human p300 CH3 binds p53 independently of SV40 large T antigen.

Reason: PMID:16611888 Figure 4B uses a FLAG-tagged human p300 CH3 fragment (1709–1913) and endogenous p53 in U-2 OS cells, with two p53 antibodies and an IgG control. This supports the already-present GO:0002039 p53 binding (index 11), a more precise replacement than generic protein binding. The evidence is a domain association assay, not a structure of full-length p300.

Proposed replacements: p53 binding

Summary: Human FOXP3 associates with p300 in a coimmunoprecipitation assay.

Reason: PMID:16652169 Figure 7D detects human FOXP3 in p300-HA immunoprecipitates from HEK293T cells; the plasmid Methods specify human FOXP3. FOXP3 is the DNA-binding forkhead transcription factor in this interface, and Figure 7C tests its interference with p300-assisted CREB transcription. Refine to existing GO:0061629 (indices 400–403). The interaction is measured by coimmunoprecipitation, not purified binary affinity, and the replacement does not assign FOXP3 repression activity to p300.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: The reported bICP0-p300 association is supported.

Reason: PMID:16760386 explicitly reports bICP0-p300 interaction during productive infection and transient transfection, with a separate comparison to a p300 CH3-deletion mutant. This is affirmative support for the named source association, rather than only a pathway phenotype. Retain generic binding as non-core and defer to the curated IPI assertion. Exact host species, constructs and operative controls remain inaccessible; no assay details are inferred from the viral title.

Summary: CITED1 association supports transcription coactivator binding.

Reason: The operative interaction assay in PMID:16864582 remains inaccessible. Independent PMID:10722728 explicitly reports MSG1/CITED1 association with p300/CBP and its non-DNA-binding coactivator role in the verified abstract. Actual PMID:11581164 Results/Figures 1E and3D separately establish p300-dependent CITED1 coactivation and functional CR2-domain requirements; these reporter assays are not represented as a purified CITED1–p300 interface. Together the positive same-partner evidence supports refining the human Q99966 interaction to coactivator binding, without certifying the unread source-specific phosphorylation or nephrogenesis experiment. https://doi.org/10.1101/gad.906301.

Proposed replacements: transcription coactivator binding

Summary: HIPK2 associates with p300, including its acetyltransferase-region fragment.

Reason: PMID:16917507 Figure 4B-D shows reciprocal HIPK2-p300 coimmunoprecipitation and p300 deletion mapping in 293T cells; Figure 4E tests in vitro-translated HIPK2 with bacterial GST-p300(HAT). Figure 2 and Methods establish HIPK2 as the kinase that phosphorylates p300. Current GO:0019901 protein kinase binding therefore captures the verified partner role more precisely than generic protein binding. This is binding to a kinase, not an assertion that p300 itself phosphorylates proteins.

Proposed replacements: protein kinase binding

Summary: T-bet/TBX21 associates with p300 in transcriptional complexes.

Reason: PMID:17075044 Figures 2B-D and 4C show p300-T-bet association in endogenous Jurkat and tagged COS7 experiments, including p300-specific immunoprecipitation and T-bet detection. The paper identifies T-bet as the sequence-specific factor at the FUT7 regulatory region and tests transcriptional consequences. Refine to existing GO:0061629 (indices 400–403); the protein interaction assay, rather than promoter ChIP alone, grounds the binding claim.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: p300 associates with HIF-1alpha, although the cited peptide-modification experiments remain inaccessible.

Reason: PMID:17382325 abstract describes a fluorescence-polarization binding assay, but its full Methods were not recovered. Independently, PMID:18268343 Figure 6A and IP Methods demonstrate p300-HIF-1alpha association in human U251 nuclear extracts, with IgG control, and connect that interface to HIF-dependent transcription. Refine generic binding to existing GO:0061629 (indices 400–403), using the verified transcription-factor role without claiming verification of the 2007 peptide modifications or affinity measurements.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: BAT3/BAG6 associates with p300 and promotes p300-p53 association in human cells.

Reason: PMID:17403783 Figure 4A,D shows tagged and endogenous BAT3-p300 coimmunoprecipitation in 293T and U2OS cells. This is a supported interaction, retained as non-core under the campaign binding policy. The paper separately tests p53 acetylation and does not establish an additional molecular activity from binding alone.

Summary: Multiple purified human p300 domains bind the human p53 transactivation region.

Reason: PMID:17438265 Table 1, Figures 2–4 and Experimental Procedures directly measure binding by fluorescence anisotropy and NMR using human p300 TAZ1, KIX, TAZ2/CH3 and IBiD domains and human p53 sequences. Refine to existing GO:0002039 p53 binding (index 11). The partner specificity is established, while the measured domain affinities are not assigned to intact p300.

Proposed replacements: p53 binding

Summary: Endogenous human p300 associates with CREB1 constructs in HEK293T cells.

Reason: PMID:17476304 Figure 2D explicitly recovers endogenous human p300 with GAL4-CREB(1–283), comparing wild type, Ser133Ala and Ser142Leu; the Results connect this interface to CREB-dependent transcription. Refine to existing GO:0061629 (indices 400–403), which captures binding to the sequence-specific RNA polymerase II transcription factor CREB1. Figure 2E instead uses CBP KIX; that purified-domain assay is not relabeled as p300. Preserve the imported partner isoform identifier without claiming isoform-exclusive binding.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: The reported CHOP-p300 association is retained as non-core.

Reason: PMID:17872950 explicitly links the CHOP N-terminal region to p300 interaction and describes interference with the association by TRB3. This directly addresses the imported CHOP/P35638 partner, so the verified positive abstract plus curated IPI annotation are sufficient to retain the broad association. Main Methods and figures remain unavailable; the judgment does not assert purified binary binding or uninspected construct details.

Summary: p300-p53 binding is independently established, while the cited Pin1-dependent recruitment experiments were only partially accessible.

Reason: PMID:17906639 main article remained inaccessible; its actual supplement describes p300-dependent p53 acetylation and promoter recruitment, not the complete missing main interaction assays. Independent human p300-p53 binding is directly measured in PMID:17438265 Table 1 and Figures 2–4. Refine to existing GO:0002039 p53 binding (index 11) on that explicit independent evidence, without claiming verification of the full Pin1 mechanism.

Proposed replacements: p53 binding

Summary: p300 recruitment to a LYL1-CREB1 complex supports the reported association.

Reason: PMID:18160048 explicitly reports recruitment of p300 and CBP to LYL1-CREB1 complexes. This supports a complex-associated physical interaction in the imported LYL1/P12980 context and is retained as non-core under the campaign binding policy. It does not establish direct binary p300-LYL1 contact or resolve the inaccessible Methods, species and construct details. The reason for retention is the positive source-specific complex report plus the curated IPI assertion.

Summary: p300 associates with HIF-1alpha in hypoxic human glioma cells.

Reason: PMID:18268343 Figure 6A and IP Methods directly assay p300-HIF-1alpha complexes in human U251 nuclear extracts with an IgG control. The same study tests the p300-dependent HIF transcriptional interface. Refine to existing GO:0061629 (indices 400–403), reflecting the experimentally identified DNA-binding transcription-factor partner. Mouse MEF reporter and promoter experiments are separate evidence and are not substituted for the human interaction assay.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: The p300 TAZ2 domain forms complexes with full-length p53 in solution.

Reason: PMID:18391200 Figure 5 and SAXS Results analyze p53-TAZ2 and p53-TAZ2-DNA complexes, with four TAZ2 domains per p53 tetramer. Main Methods refer protein construction to prior work and supplementary text; independently read PMID:17438265 explicitly documents human p300-domain and human p53 reagents. Refine to existing GO:0002039 p53 binding (index 11), without treating the SAXS model as a structure of full-length p300.

Proposed replacements: p53 binding

Summary: HSF1 associates with p300 in a heat-responsive complex in human U2OS cells.

Reason: PMID:18451878 Results and actual Supplementary Figure 1B show p300 immunoprecipitation followed by HSF1 detection in human U2OS cells, with a control antibody. The study establishes HSF1 as the heat-shock-element-binding transcription factor in this coactivator complex and examines Hsp promoter activation. Refine to existing GO:0061629 (indices 400–403). The evidence supports transcription-factor association in the complex, not an isolated binary affinity or a chaperone activity of p300.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: p300 associates with the transcription coactivator Strap/TTC5.

Reason: PMID:18451878 Figure 3A-B and Supplementary Figure 1B show Strap in p300 immunoprecipitates from U2OS cells, with heat shock and inducible Strap comparisons. The imported partner Q99LG4 denotes mouse Strap; the read Methods refer construction to earlier work, so the human host is not used to relabel the reagent as human. Preserve that partner identifier and the cellular-complex assay boundary. Results/Figures 1–4 also show Hsp-promoter activation, p300-complex HAT enhancement and promoter recruitment, establishing the bound protein as a transcription coactivator. Refine to coactivator binding while retaining the source reagent and co-complex limits; no p300-independent DNA-recognition activity is inferred for Strap.

Proposed replacements: transcription coactivator binding

Summary: p300-p53 binding is clearly supported, while the specific interaction experiments in this acetylation paper remain incompletely accessible.

Reason: PMID:18485870 normal cache exposes introduction/discussion material but not the operative binding Results/Methods; live PMC and XML attempts did not recover them. Human p300-p53 binding is directly established by PMID:17438265 Table 1 and Figures 2–4 and PMID:16611888 Figure 4B. Refine to existing GO:0002039 p53 binding (index 11) using these independent originals rather than claiming the cited 2008 experiment was read.

Proposed replacements: p53 binding

Summary: FUS/TLS associates with p300 in an RNA-dependent manner in the tested preparations.

Reason: PMID:18509338 Results, Figure 1D and actual Supplementary Figure S6A show p300 recovery with GST-TLS and loss after RNase A treatment. The comparison with TIP60 and the HAT-regulation experiments distinguish RNA-sensitive association from an invariant binary interaction. Retain the supported generic binding as non-core; RNA binding itself is performed by TLS and is not inferred for p300 from this complex.

Summary: EWSR1 associates with p300 in an RNA-sensitive interaction assay.

Reason: PMID:18509338 actual Supplementary Figure S6A explicitly shows Flag-p300 recovery with GST-EWS and loss after RNase A treatment, alongside GST and input controls. The main Results also report this RNA dependence. Retain the supported generic interaction as non-core, without transferring the separately mapped CBP-binding domains to p300 or asserting RNA-independent binding.

Summary: The reported NUPR1-p53-p300 complex is retained as non-core.

Reason: PMID:18690848 explicitly reports NUPR1 in a complex with p53 and p300. This addresses both imported partners O60356 and P04637 and therefore resolves the earlier concern that only the independently established p53 partner had support. Retain the reported complex association as non-core, deferring to the curated IPI assertion. Full Methods and figures remain inaccessible, so purified pairwise NUPR1-p300 binding is not asserted.

Summary: The reported p300-SIRT2 interaction is supported.

Reason: PMID:18722353 explicitly reports p300 interaction with SIRT2 as well as SIRT2 acetylation and reduced deacetylase activity. The interaction statement directly matches the imported SIRT2/Q8IXJ6 partner; retain generic binding as non-core with deference to the curated IPI annotation. The original Methods/figures remain unavailable. This does not resolve the separate tubulin-specific process row, which requires a substrate-specific assay absent from the abstract.

Summary: SIRT1 association supports histone deacetylase binding.

Reason: Verified PMID:15632193 and PMID:19047049 abstracts explicitly report p300–SIRT1 interaction; their operative main interaction experiments remain unavailable. Independently read PMID:20660480 Results preceding Figure 5 and Discussion explicitly report p300–SIRT1 interaction and cite their Supplementary Figure4, which could not be inspected. That main-text interaction report corroborates the positive source claims; Figure 5B re-ChIP demonstrates shared promoter occupancy only and is not used as proof of physical binding. SIRT1 is a classIII histone deacetylase, so GO:0042826 identifies the supported partner class more informatively. Neither a purified binary interface nor deacetylase catalysis by p300 is asserted. https://doi.org/10.1093/nar/gkq609.

Proposed replacements: histone deacetylase binding

Summary: The Tcl1–p300 association is supported in human cells.

Reason: PMID:19064921 Results/Figure 1C and DNA Constructs/Immunoprecipitation Methods show reciprocal co-IP after tagged expression in293 cells and endogenous association in Daudi cells, with FHIT as a negative control. The proposed conformational explanation is not directly established, and this source does not resolve a more specific p300 adapter or binding-regulator activity. Keep the supported association as non-core. Original: https://doi.org/10.1073/pnas.0810965105.

Summary: The HIF1A interaction has a specific transcription-factor binding term.

Reason: PMID:19071119 abstract explicitly describes regulated HIF1A–p300 association, while its operative main article was not inspected. Independently read PMID:23746844 Figure 4C and HIF1A-TAD interaction Methods show HIF1A C-TAD/2X-TAD capture of endogenous p300 from human HeLa nuclear extracts. This supports the specific RNA polymerase II transcription-factor interaction; it does not establish a purified binary assay in the inaccessible source. https://doi.org/10.1016/j.cell.2013.04.048.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: The direct interaction is specifically with p53.

Reason: PMID:19217391 Results/Figures 1–2 and Expression/Purification, NMR and fluorescence-binding Methods establish a binary human p300 TAZ2–p53 transactivation-domain complex. The construct is p300 residues 1723–1812 with four non-zinc-coordinating cysteines replaced by alanine; p53(2–39) and shorter peptides are distinct from full-length proteins. Intermolecular NOEs and interface mutations support p53 binding without treating a domain structure as a whole-protein cellular assay. Original: https://doi.org/10.1016/j.str.2008.12.009.

Proposed replacements: p53 binding

Summary: The direct p73 interaction is covered by p53-family binding.

Reason: GO:0002039 explicitly covers binding to any p53-family protein, including p73. PMID:19218448 Results/Figures 1–4 and Protein Expression/NMR/Fluorescence Anisotropy Methods characterize purified p300-domain binding to p73 N-terminal constructs; the p73 L18Q/W19S mutant weakens binding, with distinct H1299 reporter/siRNA tests linking the interaction to transcription. The main Methods defer exact p300-domain production details to an earlier paper, so no full-length purified-complex claim is made. Original: https://doi.org/10.1073/pnas.0900383106.

Proposed replacements: p53 binding

Summary: This interaction is specifically with p53.

Reason: PMID:19234109 actual Results/Figure 5B and plasmid/cell Methods assay p53 association with HA-p300 separately from HA-CBP in human HCT116 cells, enhanced by SOX4. The source is no longer limited to the Discussion-only normal cache: operative original text was independently recovered. The specific p53-family-binding term captures the source partner. Original: https://doi.org/10.1073/pnas.0810147106.

Proposed replacements: p53 binding

Summary: The source partner SOX4 is a DNA-binding RNA-polymerase-II transcription factor.

Reason: PMID:19234109 Results/Figure 5C and plasmid/cell Methods directly test Myc-SOX4 association with HA-p300 in human HCT116 cells; p300 and CBP are assayed separately. Refine generic binding to the supported transcription-factor class without converting the co-IP into a purified binary-binding claim. Original: https://doi.org/10.1073/pnas.0810147106.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Purified-protein experiments directly support p53 binding.

Reason: PMID:19339993 Results/Figure 3D and Solution Interaction Methods incubate purified p53 or SUMO-conjugated p53 with p300 and recover both with anti-p300; the tested SUMO state preserves association. Protein Purification Methods identify recombinant proteins but defer p300 production to an earlier protocol. The specific binding term is justified without inferring the uninspected preparation details. Original: https://doi.org/10.1038/emboj.2009.83.

Proposed replacements: p53 binding

Summary: The annotated partner HIF1A is a DNA-binding RNA-polymerase-II transcription factor.

Reason: PMID:19680224 Results/Figure 6D–G show HIF1A–p300 association and its modulation by p300 SUMO state, with wild-type and CRD1-deletion constructs distinguished. Cell/co-IP Methods identify human HeLa/HEK293T assays but defer detailed constructs and some binding procedures to unread supplementary data. The main positive association supports the specific transcription-factor-binding class without assigning deSUMOylase activity to p300. Original: https://doi.org/10.1038/emboj.2009.210.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Human Dna2 associates with p300 in purified-protein assays and endogenous HeLa complexes.

Reason: PMID:20019387 Figure 1B-C and the binding/immunoprecipitation Methods directly support the interaction. Both full-length p300 and the 965–1810 and 1284–1673 catalytic preparations bind Dna2. Keep the supported generic interaction as non-core; acetyltransferase activity supplies its functional interpretation.

Summary: VDR association supports a specific nuclear-receptor binding term.

Reason: PMID:20089040 abstract describes VDR/EGR1/p300 transcriptional cooperation in HGC-27 cells but its operative physical-interaction assay remains unread. Independent PMID:21988832 deposited record IM-15364-3185/IntAct EBI-3940392 verifies a human EP300–VDR two-hybrid interaction, and the original screen Methods were inspected. Use nuclear-receptor binding without pretending that coactivation synergy alone proves binding or that the independent yeast assay verifies every gastric-cell mechanism. https://doi.org/10.1111/j.1742-4658.2009.07542.x; https://doi.org/10.1038/msb.2011.67.

Proposed replacements: nuclear receptor binding

Summary: BRD7 associates with endogenous p300 in human cells.

Reason: PMID:20228809 Figure 6B and the author-deposited chapter Methods show endogenous BRD7-p300 coimmunoprecipitation in BJ/ET-RasV12ER cells with an antibody control. Supplementary Figure S11 describes p53-independent association in H1299 cells. Retain this supported generic interaction as non-core; no binding-derived activity is invented.

Summary: The HIF1A interaction has a specific transcription-factor binding term.

Reason: PMID:20603618 abstract explicitly describes regulated HIF1A–p300 association, while its operative main article was not inspected. Independently read PMID:23746844 Figure 4C and HIF1A-TAD interaction Methods show HIF1A C-TAD/2X-TAD capture of endogenous p300 from human HeLa nuclear extracts. This supports the specific RNA polymerase II transcription-factor interaction; it does not establish a purified binary assay in the inaccessible source. https://doi.org/10.1016/j.cell.2013.04.048.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: The FoxA2 association is a transcription-factor interaction.

Reason: PMID:20609350 Results/Figure 4E–L show FoxA2-dependent recruitment of p300 and association of p300 with a FoxA2/HIF complex; CH1 deletion disrupts complex association. The imported mouse FoxA2 partner is preserved. These experiments do not isolate a binary p300–FoxA2 contact, so the contextual interaction is retained without inventing a direct interface. Original: https://doi.org/10.1016/j.ccr.2010.05.024. FoxA2 is the DNA-binding transcription-factor partner in this RNAPII coactivation complex, allowing refinement to GO:0061629 while preserving the explicit cellular-complex/interface limitation.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: SIRT1 association supports histone deacetylase binding.

Reason: Verified PMID:15632193 and PMID:19047049 abstracts explicitly report p300–SIRT1 interaction; their operative main interaction experiments remain unavailable. Independently read PMID:20660480 Results preceding Figure 5 and Discussion explicitly report p300–SIRT1 interaction and cite their Supplementary Figure4, which could not be inspected. That main-text interaction report corroborates the positive source claims; Figure 5B re-ChIP demonstrates shared promoter occupancy only and is not used as proof of physical binding. SIRT1 is a classIII histone deacetylase, so GO:0042826 identifies the supported partner class more informatively. Neither a purified binary interface nor deacetylase catalysis by p300 is asserted. https://doi.org/10.1093/nar/gkq609.

Proposed replacements: histone deacetylase binding

Summary: p300 associates with APE1-containing nuclear complexes.

Reason: PMID:20808282 abstract describes a human erythroid multiprotein complex but does not independently resolve its APE1 contact; main text remained inaccessible. Independent human HEK-293T reciprocal p300–APE1 co-immunoprecipitation in PMID:20856196 Figure 1A/B establishes the imported partner association. Retain the context-dependent interaction without attributing APE1 nuclease chemistry or DNA-replication catalysis to p300. https://doi.org/10.1038/emboj.2010.204; https://doi.org/10.1038/onc.2010.435.

Summary: p300 associates with APE1 in a regulated transcriptional complex.

Reason: PMID:20856196 Figure 1A/B provides reciprocal co-immunoprecipitation of p300 and APE1 in human HEK-293T nuclear extracts; APE1 N-terminal deletion disrupts association, and Figure 1D/F shows acetylation-enhanced recruitment. Preserve this substrate/cofactor interaction as non-core without assigning APE1 nuclease activity to p300. Original Methods specify FLAG constructs and a separate recombinant p300 HAT-domain acetylation assay; residue bounds follow an earlier protocol. https://doi.org/10.1038/onc.2010.435.

Summary: The YB-1 interaction is part of RNA polymerase II transcription-factor recruitment.

Reason: PMID:20856196 Figure 2B shows YB-1 associated with p300 in human HEK-293T nuclear extracts, reduced after APE1 depletion; Figure 2E links this complex to MDR1 promoter occupancy and polymerase II loading. A specific RNA polymerase II transcription-factor binding term captures this coactivation context. The assay establishes a cellular complex and APE1 dependence, not a purified binary interface. https://doi.org/10.1038/onc.2010.435.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: The reported NBS1-p300 association is retained as non-core.

Reason: PMID:21108945 explicitly reports reduced NBS1-p300 interaction with a nonphosphorylatable p300 S106A mutant. Thus the abstract addresses the imported NBN/O60934 association, not merely an overall DNA-repair phenotype. Retain the broad association as non-core with the curated IPI annotation. The main interaction assay and reagent details remain inaccessible, so no purified interface, exact construct scope or damaged-DNA binding activity is inferred.

Summary: The p53 interaction has a specific p53-binding term.

Reason: PMID:21471221 does not provide an independently inspected operative p300-binding assay in this assessment. Direct human p300–p53 binding is established independently in PMID:19217391 Results/NMR and anisotropy assays, using p300 TAZ2 residues 1723–1812 with four specified non-zinc-coordinating cysteine substitutions and p53 N-terminal fragments. Use p53 binding while preserving the source reference and partner; the engineered-domain evidence does not establish all full-length conformations. Original source: https://doi.org/10.1074/jbc.M110.209916; independent assay: https://doi.org/10.1016/j.str.2008.12.009.

Proposed replacements: p53 binding

Summary: p300 associates with the p53 coactivator ASPP2.

Reason: PMID:21513714 Results and Figures 1–2 show ASPP2-associated p300 in human cells, including p53-null H1299 cells, and cooperative activation of a p53-dependent PIG3 reporter. Transcription coactivator binding captures the demonstrated partner role. These are cellular complex and reporter assays, not purified binary reconstitution.

Proposed replacements: transcription coactivator binding

Summary: p300 associates with iASPP in human cellular complexes.

Reason: PMID:21513714 Figure 2 recovers endogenous p300 with iASPP in U2OS and p53-null H1299 cells. Figure 1 distinguishes iASPP from the positively cooperating ASPP1/2 proteins. Retain the supported interaction as non-core, without transferring the ASPP1/2 coactivator role or claiming purified binary binding.

Summary: p300 associates with the p53 coactivator ASPP1.

Reason: PMID:21513714 Figures 1–2 show ASPP1-associated p300 in human cells and cooperation on a p53-dependent PIG3 reporter. Refine to transcription coactivator binding. Association persists in p53-null H1299 cells; this excludes an obligatory p53 bridge in that assay but does not establish purified binary binding.

Proposed replacements: transcription coactivator binding

Summary: The deposited VDR interaction supports nuclear-receptor binding.

Reason: PMID:21988832 Results and Y2H Methods describe human liver ORF/fragment screens and deposit IM-15364. The current deposited target record IM-15364-3185 (IntAct EBI-3940392) explicitly pairs human EP300 Q09472 with VDR P11473 by two-hybrid physical association. The specific nuclear-receptor binding term captures the partner identity. This is heterologous interaction-screen evidence; no target-pair mammalian validation, full-length construct equivalence or liver-specific physiological effect is inferred. Original: https://doi.org/10.1038/msb.2011.67; deposited record: https://www.ebi.ac.uk/intact/interaction/EBI-3940392.

Proposed replacements: nuclear receptor binding

Summary: The EWSR1 association is retained as a contextual interaction.

Reason: PMID:21988832 deposits human EP300–EWSR1 physical association by two-hybrid in IM-15364-2111/IntAct EBI-3929037. The original Y2H Methods and the exact deposited pair were inspected. This supports the existing generic interaction while avoiding an unsupported stable binary-interface or dedicated EWSR1-specific functional claim. The independently reviewed PMID:18509338 Figure S6A shows RNA-sensitive GST-EWS recovery of Flag-p300, consistent with contextual rather than invariant association. https://doi.org/10.1038/msb.2011.67; https://www.ebi.ac.uk/intact/interaction/EBI-3929037.

Summary: p300 associates with and acetylates SKP2.

Reason: PMID:22770219 Results, Figure 1A and the accompanying acetylation experiments support the p300–SKP2 interaction and its substrate-regulatory context. Retain the interaction as non-core. The source separately tests human and mouse SKP2; neither substrate binding nor the downstream stability/localization phenotypes make p300 an E3 ubiquitin ligase or a transport factor.

Summary: The p53 interaction has a specific p53-binding term.

Reason: PMID:23010591 does not provide an independently inspected operative p300-binding assay in this assessment. Direct human p300–p53 binding is established independently in PMID:19217391 Results/NMR and anisotropy assays, using p300 TAZ2 residues 1723–1812 with four specified non-zinc-coordinating cysteine substitutions and p53 N-terminal fragments. Use p53 binding while preserving the source reference and partner; the engineered-domain evidence does not establish all full-length conformations. Original source: https://doi.org/10.1016/j.febslet.2012.09.012; independent assay: https://doi.org/10.1016/j.str.2008.12.009.

Proposed replacements: p53 binding

Summary: ALKBH4 interaction with p300 is supported by yeast two-hybrid screens with important validation limits.

Reason: PMID:23145062 Table 1 and Figure 1 identify p300 fragments in two human-library Y2H screens; the mapped region includes the bromodomain/PHD. Results explicitly report failure to robustly confirm the interactions by GST pull-down or co-IP. Figure 2F uses a p300 1039–1285 fragment with an added localization signal. Retain the positive screen evidence as non-core, without describing a verified native full-length complex or ALKBH4 acetylation.

Summary: p300 binds the transcriptional corepressor Alien alpha.

Reason: Recovered PMID:23441852 Results and Figure 3A show a p300 HAT-region GST pull-down of translated Alien alpha, including a catalytically inactive p300 control. The paper explicitly identifies Alien alpha as a COPS2 product and demonstrates its silencing role in Figure 6. Refine to transcription corepressor binding, retaining the short-product and recombinant-fragment scope; the initial mouse-library CBP screen and CBP cellular assays are separate evidence.

Proposed replacements: transcription corepressor binding

Summary: The CDK2-associated complex supports protein kinase binding.

Reason: The detailed EP300–CDK2 edge in the high-throughput source PMID:23455922 was not independently recovered from its supplementary interaction table. Independent original PMID:10330164 Methods and Figures 1C/4 directly recover p300 with human Jurkat cyclin E–CDK2 complexes. Retain the supported association. The same source failed to reconstitute interaction using translated cyclin E and CDK2, so no binary kinase-binding mechanism or kinase activity is inferred. CDK2 is the identified protein kinase partner, so the more informative GO:0019901 describes this association. Failure of purified reconstitution limits the mechanism; it does not erase the positive cellular kinase-partner association or make p300 a kinase.

Proposed replacements: protein kinase binding

Summary: p300 associates with the DNA-binding transcription factor STAT6.

Reason: PMID:23461825 Figure 2F shows p300–STAT6 co-immunoprecipitation in human HEK293 cells; Figure 2G places them together on the ORMDL3 promoter by sequential ChIP. Methods describe the antibodies and cellular IP. Refine to DNA-binding transcription factor binding, without converting promoter occupancy into direct DNA binding by p300 or claiming purified binary association. The demonstrated partner role is STAT6-dependent ORMDL3 gene-promoter activation, placing the interaction in RNA-polymerase-II transcription. Use the corresponding specific transcription-factor-binding term; this does not assign DNA recognition to p300.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: HIF1A binding is a transcription-factor interaction of p300.

Reason: PMID:23746844 Figure 4C and HIF1A-TAD interaction Methods show capture of p300 from human HeLa nuclear extract by GST-HIF1A C-TAD and 2X-TAD baits, with GST and N-TAD controls. Use the specific RNA polymerase II transcription-factor binding term. The assay uses nuclear extract rather than purified p300, and CDK8 kinase/RNAPII elongation mechanisms remain distinct from p300 activity. https://doi.org/10.1016/j.cell.2013.04.048.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: The mature NF-kappaB p50 interaction supports NF-kappaB binding.

Reason: The source explicitly identifies the processed NFKB1 p50 product P19838-PRO_0000030311. The verified abstract describes interaction with NF-kappaB and acetylation of p50. Refine generic binding to the NF-kappaB-binding term already present for this source, without relabeling the partner as the entire p105 precursor.

Proposed replacements: NF-kappaB binding

Summary: The RELA interaction supports NF-kappaB binding.

Reason: The source partner Q04206 is NF-kappaB p65/RELA. The verified abstract directly identifies p300 interaction with NF-kappaB and p65 acetylation. Refine the generic term to the existing NF-kappaB-binding annotation.

Proposed replacements: NF-kappaB binding

Summary: p300 directly associates with ASH2L in the SET1 complex.

Reason: PMID:23870121 Figure 2F–I combines HeLa co-IP, purified SET1C–p300 binding, individual-subunit analysis and purified ASH2L binding to p300 domains. Retain this specific chromatin-cofactor interaction as non-core. SET1C performs H3K4 methylation; p300 supplies acetylation and recruitment. The linked correction concerns the Figure 5A actin image, not these Figure 2 interaction assays.

Summary: p300 associates with the DNA-binding transcription factor KLF15.

Reason: PMID:23999430 Results and Figure 5 demonstrate KLF15–p300 co-IP, competition with p65 and loss of functional competition after deleting the KLF15 transactivation-domain segment. Human aortic smooth-muscle-cell experiments are distinguished from mouse knockout studies. Refine to DNA-binding transcription factor binding; the cellular complexes do not establish a purified binary affinity. The demonstrated partner role is KLF15/p65-dependent inflammatory gene transcription, placing the interaction in RNA-polymerase-II transcription. Use the corresponding specific transcription-factor-binding term; this does not assign DNA recognition to p300.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: The source-specific p300–RUNX3 interaction needs operative original access.

Reason: PMID:24229708 identity and abstract were verified, but its p300 interaction experiment, construct/species details and supporting figures were not recovered. Its RUNX3 and lung-tumor emphasis is not evidence of misattribution. Preserve the source assertion as unresolved rather than extrapolating from pathway summaries.

Summary: The reported HDAC4-p300 complex association is retained as non-core.

Reason: The recovered original Discussion of PMID:24413532 explicitly reports HDAC4-p300 association in MCF-7 cells and loss after TFAP2C silencing, referring to Supplementary Figure S2A-B. This source-specific positive statement plus the curated IPI annotation supports retaining the broad association as non-core. The supplement and complete interaction Methods remain unavailable; no purified binary contact or independent inspection of those panels is claimed.

Summary: The reported HDAC5-p300 complex association is retained as non-core.

Reason: The recovered original Discussion of PMID:24413532 explicitly reports HDAC5-p300 association in MCF-7 but not MDA-MB-231 cells, with TFAP2C dependence, referring to Supplementary Figure S2A-B. Retain this contextual association as non-core on that positive report and the curated IPI assertion. The operative supplementary panels and complete interaction Methods remain inaccessible; the conclusion is complex association, not purified binary binding.

Summary: p300 associates with the DNA-binding transcription factor HIF1A.

Reason: PMID:24421387 Figure 7B–C/E/G measures p300–HIF1A association and its modulation by EAF2, including endogenous co-IP in human RCC4 cells. The human constructs and IP methods are described. Refine the broad binding term to DNA-binding transcription factor binding, distinguishing these human cellular experiments from separate Eaf2-null mouse assays. The demonstrated partner role is HIF1A-dependent hypoxia-response gene transcription, placing the interaction in RNA-polymerase-II transcription. Use the corresponding specific transcription-factor-binding term; this does not assign DNA recognition to p300.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: p300 associates with the DNA-binding transcription factor REL.

Reason: PMID:24529102 Figure 3A includes endogenous wild-type p300 from human A293 cells pulled down by the REL transactivation-domain construct. Figure 2C tests wild-type p300 coactivation. The paper also assays lymphoma-derived p300 truncations; their altered regulatory activity is not equated with the canonical protein. Refine to DNA-binding transcription factor binding, without treating cell-extract pull-down as purified binary reconstitution. The demonstrated partner role is REL-dependent reporter transcription, placing the interaction in RNA-polymerase-II transcription. Use the corresponding specific transcription-factor-binding term; this does not assign DNA recognition to p300.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: The p300–PCNA association is supported in human cells.

Reason: PMID:24939902 Figure 1F immunoprecipitates p300 with chromatin-bound PCNA after UV irradiation; Figure 5C independently detects association with wild-type and acetylation-site mutant PCNA. The direct recombinant domain-binding experiment in Figure 2 is for CBP, not p300. Retain the supported generic association as non-core; this source does not establish a more specific adapter or regulatory binding activity. Original: https://doi.org/10.1093/nar/gku533.

Summary: The p300–ASC1/TRIP4 assertion remains limited by access to its interaction experiment.

Reason: PMID:25219498 and the TRIP4/Q15650 partner identity were verified. The abstract describes ASC1 ufmylation and estrogen-receptor coactivation, but the operative p300 interaction assay was not recovered. Do not infer a direct p300–ASC1 interface or assign an enzymatic UFM1-conjugation role to p300 from this context.

Summary: p300 binds the DNA-binding transcription factor ZNF509L/ZBTB49.

Reason: PMID:25245946 Figure 3F–G shows human-cell co-IP and association of recombinant ZNF509L with p300; Figure 3H–I connects recruitment to promoter acetylation and activation. The GST assay methods separately describe translated p300 fragments. Refine to DNA-binding transcription factor binding while preserving the source's ZNF509L product specificity. The demonstrated partner role is ZNF509L-dependent gene-promoter activation, placing the interaction in RNA-polymerase-II transcription. Use the corresponding specific transcription-factor-binding term; this does not assign DNA recognition to p300.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: The p300–SNAI1 interaction in this source remains unverified.

Reason: PMID:25314079 identity and abstract were verified, but the original p300-specific interaction experiment was not recovered. The abstract emphasizes CBP; that does not establish that p300 was absent from the full study. Retain uncertainty without asserting paralog misattribution or transferring all CBP results to EP300.

Summary: p300 binds AUTS2 in a transcription-activating complex.

Reason: PMID:25519132 Results, Figure 4 and Extended Data Figure 3 show AUTS2–p300 cellular association, an assay with recombinant proteins purified from Sf9 cells, and p300-dependent AUTS2 reporter activation in human 293-derived cells. Refine to transcription coactivator binding. Mouse brain occupancy is corroborating context, not the identity of the human cell assays, and p300 is not assigned the PRC1 ubiquitin-ligase reaction.

Proposed replacements: transcription coactivator binding

Summary: The p300 bromodomain recognizes acetylated p53 peptides.

Reason: Actual PMID:25651062 Results and Figure 2E–F measure NMR perturbations and binding of the p300 bromodomain to p53 K381-acetylated peptides, with or without adjacent K382 dimethylation. Refine to p53 binding. The isolated-domain peptide assay is distinct from the paper's mouse chromatin colocalization and 53BP1 crystal structures; it does not establish a full-length p300–p53 affinity.

Proposed replacements: p53 binding

Summary: p300 associates with p53 in human cellular assays.

Reason: PMID:26302407 Figure 4I and co-IP Methods recover p53 with p300 in human 293T cells and show suppression of this association by increasing CSL. Refine to p53 binding. The purified binary assay in the same paper concerns CSL–p53, not p300. The linked corrigendum corrects an author's name and does not change this experiment.

Proposed replacements: p53 binding

Summary: p300 associates with HIF1A in a phosphorylation-dependent cellular context.

Reason: PMID:26751287 Figure 5A–B and the accompanying Results measure HIF1A–p300 association after LINK-A/LRRK2 perturbation and HIF1A S797A substitution in human-cell experiments. Refine to DNA-binding transcription factor binding. These experiments do not make p300 the kinase, demonstrate direct RNA binding by p300, or establish a purified binary interaction. The demonstrated partner role is HIF1A-dependent hypoxia-response gene transcription, placing the interaction in RNA-polymerase-II transcription. Use the corresponding specific transcription-factor-binding term; this does not assign DNA recognition to p300.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: The specific NleC–p300 screen interaction remains unverified.

Reason: PMID:27018634 is a genuine effector–host quantitative proteomics study, and Q8X834 is the bacterial NleC partner. The p300/NleC experiment or data row was not recovered from the inaccessible original and supplement; the verified abstract foregrounds other effectors. Retain uncertainty without claiming that the narrower abstract disproves the imported interaction.

Summary: p300 associates with DDX3X in human liver-cell nuclear extracts.

Reason: PMID:28128295 Figure 6A and co-IP Methods show HA-DDX3 recovery using a p300-specific antibody in HuH7 nuclear extracts, separately from the CBP immunoprecipitation. Retain this supported association as non-core. The study's HNF4 acetylation and transcriptional effects provide context but do not establish p300 RNA-helicase activity or purified binary DDX3X binding.

Summary: The CDK2-associated complex supports protein kinase binding.

Reason: PMID:28514442 describes human-cell BioPlex affinity-purification mass spectrometry; the exact EP300–CDK2 supplementary edge was not independently re-extracted. Independent PMID:10330164 Figure 4 directly recovers endogenous p300, cyclin E and CDK2 in human Jurkat complexes. Retain the supported interaction, with this independent provenance and without a binary-binding claim. CDK2 is the identified protein kinase partner, so the more informative GO:0019901 describes this association. Failure of purified reconstitution limits the mechanism; it does not erase the positive cellular kinase-partner association or make p300 a kinase.

Proposed replacements: protein kinase binding

Summary: The CDK2-associated complex supports protein kinase binding.

Reason: Recovered PMID:33961781 STAR Methods establish the BioPlex cellular AP-MS framework, but its exact EP300–CDK2 edge was not independently re-extracted. Original PMID:10330164 Methods and Figure 4 independently support the same human protein association in a cyclin E–CDK2 complex. Retain the association without relabeling co-complex detection as purified binary binding or p300 kinase activity. CDK2 is the identified protein kinase partner, so the more informative GO:0019901 describes this association. Failure of purified reconstitution limits the mechanism; it does not erase the positive cellular kinase-partner association or make p300 a kinase.

Proposed replacements: protein kinase binding

Summary: AUTS2 recruits p300 for transcriptional activation.

Reason: PMID:34637754 Figure 3B–E shows reciprocal association in human 293-derived cells and defective p300 recruitment/transcriptional activation with AUTS2 HX-region variants; mouse motor-neuron experiments are separate. Refine to transcription coactivator binding, also independently supported by the directly read PMID:25519132 Figure 4 and Extended Data Figure 3. A linked correction is recorded; its body was not recovered, so no specific correction scope is presumed.

Proposed replacements: transcription coactivator binding

Summary: The PCAF interaction is better described as transcription coregulator binding.

Reason: PMID:8684459 explicitly identifies association of PCAF with p300/CBP in its publisher abstract. PCAF is the associated transcriptional acetyltransferase, so the already imported specific coregulator-binding term at the same source is more informative than protein binding. Main-text assay details remain inaccessible; this does not assert a newly demonstrated interface or transfer PCAF catalysis to p300. https://doi.org/10.1038/382319a0.

Proposed replacements: transcription coregulator binding

Summary: The reported direct Ad12 E1A-p300 interaction is retained as non-core.

Reason: PMID:9018065 explicitly reports direct binding between Ad12 E1A and p300, matching the imported P03259 partner. Together with the curated IPI assertion, this is sufficient affirmative support for retaining generic binding as non-core; lack of full-text access alone does not negate that clearly stated interaction. The main Methods and figures remain unavailable. No Ad5 assay is substituted, and no uninspected construct or species detail is asserted.

Summary: The p53 interaction has a specific p53-binding term.

Reason: PMID:9194564 does not provide an independently inspected operative p300-binding assay in this assessment. Direct human p300–p53 binding is established independently in PMID:19217391 Results/NMR and anisotropy assays, using p300 TAZ2 residues 1723–1812 with four specified non-zinc-coordinating cysteine substitutions and p53 N-terminal fragments. Use p53 binding while preserving the source reference and partner; the engineered-domain evidence does not establish all full-length conformations. Original source: https://doi.org/10.1038/42972; independent assay: https://doi.org/10.1016/j.str.2008.12.009.

Proposed replacements: p53 binding

Summary: The p53 interaction supports specific transcription-factor binding.

Reason: The source partner is human TP53/P04637. The verified original abstract explicitly reports p300/CBP–p53 binding without viral oncoproteins. Replace generic binding with the existing specific transcription-factor-binding term while keeping direct p300 DNA binding undecided.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: HIV Tat recruits p300 in a viral transcriptional context.

Reason: PMID:9811832 abstract explicitly reports human p300 binding to Tat in vitro and in vivo, Tat basic-domain dependence, and recruitment to the integrated viral promoter by an RNA-targeted activator. Preserve this supported viral interaction as non-core. It is not refined to DNA-binding transcription-factor binding because Tat is recruited through viral RNA. The original operative article and exact recombinant construct bounds remained inaccessible through the attempted PMC/EuropePMC routes. https://doi.org/10.1073/pnas.95.23.13519.

Summary: p300 interaction with Ad5 E1A is independently supported.

Reason: The operative PMID:9881977 experiments were not recovered beyond the verified abstract. Independent original PMID:10330164 Methods and Figure 1B directly test translated p300 fragments with both Ad5 12S and 13S E1A proteins. Retain the supported viral interaction as non-core while preserving the imported P03255-2 partner and avoiding extrapolation of the source's STAT1 regulatory mechanism from the independent binding assay.

Summary: Direct p300 CH1 binding to HIF1A is supported.

Reason: Recovered original Results and captions4–5 include GST-CH1 binding and competition assays with HIF1A, plus cellular interaction reporters. The source partner Q16665 is HIF1A. Refine generic binding to the existing RNA-polymerase-II transcription-factor-binding term.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: p300 binds the CITED2 transcription coregulator.

Reason: Recovered original Results and captions2–5 identify p35srj/CITED2 interaction with p300 CH1 and competition with HIF1A. Transcription coregulator binding captures its inhibitory role in this experiment; coactivator binding alone would obscure that context. The source partner Q99967 remains unchanged.

Proposed replacements: transcription coregulator binding

Summary: p300 has a supported nuclear location.

Reason: PMID:16219772 remains abstract-only. The available source abstract describes ATF4 recruitment to nuclear speckles but does not define a constitutive p300 subcompartment. Independently inspected PMID:14645221 Immunofluorescence Methods and Figure 2A/Results show predominantly nuclear p300 in human vascular smooth-muscle cells, supporting the imported broad location without an unsupported finer localization. Sources: https://doi.org/10.1074/jbc.M505294200; https://doi.org/10.1074/jbc.M311973200.

Summary: p300 has a supported nuclear location.

Reason: PMID:16574662 remains abstract-only. The source abstract directly reports p300/ROCK2 colocalization in insoluble nuclear structures. Independently inspected PMID:14645221 Immunofluorescence Methods and Figure 2A/Results show predominantly nuclear p300 in human vascular smooth-muscle cells, supporting the imported broad location without an unsupported finer localization. Sources: https://doi.org/10.1074/jbc.M510954200; https://doi.org/10.1074/jbc.M311973200.

Summary: p300 has a supported nuclear location.

Reason: PMID:17761950 remains abstract-only. The source abstract concerns RXRalpha acetylation and later RXRalpha/TR3 mitochondrial movement; that movement is not assigned to p300. Independently inspected PMID:14645221 Immunofluorescence Methods and Figure 2A/Results show predominantly nuclear p300 in human vascular smooth-muscle cells, supporting the imported broad location without an unsupported finer localization. Sources: https://doi.org/10.1210/me.2007-0107; https://doi.org/10.1074/jbc.M311973200.

Summary: p300 is a nuclear transcriptional coactivator.

Reason: The normal PMID:20940255 extraction supplies Discussion, not an independently inspected localization assay; its PCAF/Rb emphasis is not a wrong-target finding. Independent original human-cell localization evidence includes PMID:14645221 Methods and early Results and PMID:25593309 nuclear damage-recruitment screen/Methods. These support the broad nuclear location while leaving the source-specific keratinocyte image unverified. https://doi.org/10.1242/jcs.068924; https://doi.org/10.1101/gad.252189.114.

Summary: Nuclear p300 localization is directly supported.

Reason: The verified structured abstract reports recruitment of endogenous and overexpressed p300 to a Cart1-specific subnuclear compartment. Independently recovered PMID:9887100 Fig. 2C shows tagged p300 nuclear structures. Retain nuclear localization without equating overexpression-induced dots with a distinct constitutive compartment.

Summary: p300 is predominantly nuclear in human vascular smooth-muscle cells.

Reason: PMID:14645221 Immunofluorescence Methods (p7092) and Results/Figure 2A (p7093) report predominantly nuclear p300 in primary human vascular smooth-muscle cells, with nuclear colocalization with CLOCK/NPAS2. Original caption/body were read; image pixels were not independently inspected. Original: https://doi.org/10.1074/jbc.M311973200.

Summary: p300 is observed in the nuclear DNA damage response screen.

Reason: PMID:25593309 actual Results on BRD dynamics/Figure 1 and Laser microirradiation Methods include p300 among proteins recruited to damaged nuclear chromatin. The main text explicitly distinguishes p300 from CBP, which was not recovered in that screen. Retain nuclear localization; damage recruitment does not by itself establish direct damaged-DNA binding. Original: https://doi.org/10.1101/gad.252189.114.

Summary: p300 nuclear localization is supported.

Reason: The verified source abstract explicitly reports nuclear colocalization of p300 and p53. The independently recovered p300 localization experiment in PMID:9887100 Fig. 2C corroborates the cellular compartment. The source article itself remains available only as a preview.

Summary: The principal nuclear compartment supported for human EP300 is the nucleoplasm.

Reason: IPR014744 and UniProt SL-0191 explain the imported broad nucleus mapping. Actual HPA target records identify supported nucleoplasmic localization with two antibodies in human A431, U251MG and U2OS cells and GFP-tagged EP300 in HeLa. Refine to this more informative compartment; no claim is made that every cellular pool is nuclear. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Proposed replacements: nucleoplasm

Summary: Human EP300 localizes to the nucleoplasm.

Reason: The actual HPA ENSG00000100393 target subcellular record supports the imported IDA assignment: HPA003128 and HPA004112 both detect nucleoplasm in A431, U251MG and U2OS cells, and the tagged HeLa validation also reports nucleoplasm. This is direct target-specific localization evidence, separate from inferred Reactome compartments. Figure pixels were not independently reinterpreted.

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-1028815 represents p-T,4S-IRF3:p-T,4S-IRF3:CREBBP, EP300 binds promoters of Interferon-beta. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-1028817 represents CREBBP, EP300 binds p-T,4S-IRF3:p-T,4S-IRF3. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-1028819 represents VAF/pIRF7:CBP/p300 binds the promoters of type-I IFN genes. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-1028820 represents Formation of VAF (virus-activated factor) complex. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-1234167 represents Formation of HIF:CBP:p300 complex at promoters. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-1912394 represents NICD1 in complex with RBPJ (CSL) recruits MAML. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-2220957 represents NOTCH1 PEST domain mutants coactivator complex binds CDK8:CCNC. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-2220964 represents NICD1 PEST domain mutants in complex with RBPJ (CSL) bind MAML. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-2220971 represents CDK8 phosphorylates NICD1 PEST domain mutants. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-3134883 represents Beta-catenin enhances association of IRF3 with CBP/p300. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-3215152 represents TP53 in complex with EP300, PRMT1 and CARM1 binds the GADD45A promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-3222093 represents BRD7 binds TP53 and EP300. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-3322427 represents Beta-catenin recruits CBP/p300. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-3371554 represents HSF1 acetylation at Lys80. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-3662335 represents EP300 acetylates histone H2A, H2B, H3, H4. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-3899291 represents SUMOylation of EP300 with SUMO1. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-4088162 represents FOXM1 binds CDC25A promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-4396371 represents NOTCH1 Coactivator Complex binds MYC promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-4396379 represents NOTCH1 Coactivator Complex binds HES5 promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-4396392 represents NOTCH1 PEST domain mutants bind HES1 promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-4396393 represents NOTCH1 PEST domain mutants bind MYC promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-4396401 represents NOTCH1 PEST domain mutants bind HES5 promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-4396402 represents NOTCH1 PEST domain mutants bind promoters of HEY genes. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-5250930 represents B-WICH recruits histone acetyltransferases. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-5250938 represents B-WICH:histone acetyltransferase acetylates histone H3 at lysine-9. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-5628871 represents BRD7 promotes EP300-mediated acetylation of TP53. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-5660660 represents p300 acetylates RELA subunit. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-5660666 represents CBP and p300 binds NF-kB complex. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-5691381 represents MYSM1 deubiquitinates Histone H2A. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-6804229 represents JMY, TTC5 and EP300 bind. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-6804242 represents TP53 binds the complex of JMY, EP300 and TTC5. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-6804379 represents PRMT5 binds TTC5. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-6804383 represents PRMT5 methylates TP53. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-6811479 represents ING2 recruits EP300 to TP53. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-6811508 represents ING2-bound EP300 acetylates TP53. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-8864307 represents TFAP2 homo- and heterodimers bind CITED and EP300/CREBBP. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-8878050 represents HIPK2 phosphorylates RUNX1 and EP300. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-8878056 represents RUNX1:CBFB binds EP300. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-8878220 represents RUNX3 binds the NOTCH1 coactivator complex. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-8878237 represents RUNX3:NOTCH1 coactivator complex binds the HES1 gene promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-8935740 represents RUNX1 and GATA1 bind the promoter of the ITGA2B gene. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-8936481 represents Core MLL complex methylates H3K4Me2-Nucleosome at the ITGA2B gene promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-8936616 represents RUNX1 and GATA1 bind the promoter of the GP1BA gene. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-8936621 represents Core MLL complex methylates H3K4Me2-Nucleosome at the GP1BA gene promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-8936979 represents RUNX1 and GATA1 bind the promoter of the THBS1 gene. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-8937016 represents Core MLL complex methylates H3K4Me2-Nucleosome at the THBS1 gene promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-8937037 represents RUNX1 and GATA1 bind the promoter of the MIR27A gene. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-8937050 represents Core MLL complex methylates H3K4Me2-Nucleosome at the MIR27A gene promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-8951951 represents RUNX3 binds EP300. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-8951966 represents EP300 acetylates RUNX3. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-8951977 represents Acetylated RUNX3 binds to BRD2. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-8952058 represents CCND1 binds RUNX3 and displaces EP300. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9008271 represents CITED1 and EP300 bind ESR1:estrogen:TGFA gene promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9008285 represents NCOA3 recruits EP300 to ESR1:estrogen:TFGA gene:NCOA3. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9009371 represents Binding of AP1 transcriptional activator complexes to CCND1 promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9011981 represents EP300 is recruited to MYC and BCL2 genes. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9017835 represents NOTCH1 coactivator complex binds NOTCH3 gene. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9018499 represents ESR1:ESTG and EP300 are recruited to TFF3 promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9021451 represents NOTCH1,NOTCH3 coactivator complex binds PLXND1 gene promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9023840 represents HATs and coactivators are recruited to the CTSD gene. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9023860 represents Histone acetyltransferases are recruited to the TFF1 gene. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9023884 represents NCOA1 recruits EP300 to TGFA promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9029561 represents NCOA1 recruits EP300 to the ABCA1 promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9038052 represents GREB1 binds ESR1:ESTG and co-activators. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9038163 represents ESR1:ESTG:PGR:P4 bind pioneer factors and coactivators. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-933536 represents p-IRF7 dimer interacts with coactivator CBP/p300. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9613451 represents p-S133 CREB1, LYL1 and EP300 bind the ID1 and ID3 genes. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9617064 represents SPI1 (PU.1), PML isoform 4, and EP300 bind the promoter of the CEBPE gene. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The current Reactome event R-HSA-9701531 has a cytosol event-compartment value, but the catalyst activity 9701519 identifies EP300 physical entity R-HSA-381325. The independently retrieved physical-entity record is explicitly nucleoplasm and maps to human UniProt Q09472. Thus the source participant supports the imported nucleoplasm annotation even though the enclosing event has an inconsistent compartment value. Actual HPA target records independently support human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the location; the structured source query concerns the event-level compartment, not an incorrect gene location or reference. The source guide provides the exact event-to-participant chain and official URLs.

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9733207 represents p-2S-SMAD3:p-2S-SMAD3:SMAD4 forms a complex with SP1 and EP300 at the COL1A2 gene promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9737710 represents SARS-CoV-1 N binds SMAD3 and EP300 at the SERPINE1 gene promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9759332 represents AcK-NFE2L2 binds the TXNRD1 promoter. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The cited Reactome object R-HSA-9760081 represents CREBBP, EP300 acetylates NFE2L2. The recovered current object places the modeled event in the nucleoplasm. Actual HPA target records independently establish human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the correct location holistically; this does not assign the reaction performed by another complex member to EP300. Independent HPA support refers specifically to the human EP300 target record: https://www.proteinatlas.org/ENSG00000100393-EP300/subcellular (GO_REF:0000052).

Summary: Nucleoplasmic EP300 localization is independently supported in human cells.

Reason: The current Reactome event R-HSA-9760082 has a cytosol event-compartment value, but input set R-HSA-1027362 contains EP300 physical entity R-HSA-381325. The independently retrieved physical-entity record is explicitly nucleoplasm and maps to human UniProt Q09472. Thus the source participant supports the imported nucleoplasm annotation even though the enclosing event has an inconsistent compartment value. Actual HPA target records independently support human EP300 nucleoplasm with two antibodies and tagged-protein validation. Retain the location; the structured source query concerns the event-level compartment, not an incorrect gene location or reference. The source guide provides the exact event-to-participant chain and official URLs.