EP300

Summary

EP300 (EP300 lysine acetyltransferase, HGNC:3373) is a protein-coding gene on chromosome 22q13.2, encoding Histone acetyltransferase p300 (Q09472). Functions as a histone acetyltransferase and regulates transcription via chromatin remodeling. It is a selective cancer dependency (DepMap: 33.3% of cell lines) and haploinsufficient (ClinGen: sufficient evidence).

This gene encodes the adenovirus E1A-associated cellular p300 transcriptional co-activator protein. It functions as histone acetyltransferase that regulates transcription via chromatin remodeling and is important in the processes of cell proliferation and differentiation. It mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. This gene has also been identified as a co-activator of HIF1A (hypoxia-inducible factor 1 alpha), and thus plays a role in the stimulation of hypoxia-induced genes such as VEGF. Defects in this gene are a cause of Rubinstein-Taybi syndrome and may also play a role in epithelial cancer.

Source: NCBI Gene 2033 — RefSeq curated summary.

At a glance

• Gene–disease (curated): Rubinstein-Taybi syndrome due to EP300 haploinsufficiency (Definitive, ClinGen) — +2 more curated relationships
• GWAS associations: 10
• Clinical variants (ClinVar): 2,395 total — 163 pathogenic, 101 likely-pathogenic
• Phenotypes (HPO): 247
• Druggable target: yes — 9 molecules with ChEMBL bioactivity
• Cancer driver (intOGen): loss-of-function (tumor-suppressor-like) across 19 cancer types
• Cancer dependency (DepMap): dependent in 33.3% of screened cell lines
• Dosage sensitivity (ClinGen): haploinsufficiency sufficient evidence, triplosensitivity no evidence
• Transcription factor: yes — 74 downstream targets (CollecTRI)
• MANE Select transcript: NM_001429

Identifiers

Gene identifiers

Field	Value
HGNC ID	HGNC:3373
Approved symbol	EP300
Name	EP300 lysine acetyltransferase
Location	22q13.2
Locus type	gene with protein product
Status	Approved
Aliases	p300, KAT3B
Ensembl gene	ENSG00000100393
Ensembl biotype	protein_coding
OMIM	602700
Entrez	2033

Gene structure

Transcript identifiers

Ensembl transcripts: 18 — 8 retained_intron, 7 protein_coding, 2 nonsense_mediated_decay, 1 protein_coding_CDS_not_defined

ENST00000263253, ENST00000634422, ENST00000634690, ENST00000634787, ENST00000634860, ENST00000635083, ENST00000635538, ENST00000635552, ENST00000635584, ENST00000635691, ENST00000637592, ENST00000674155, ENST00000703544, ENST00000703545, ENST00000715703, ENST00000916082, ENST00000916083, ENST00000916084

RefSeq mRNA: 2 — MANE Select: NM_001429 NM_001362843, NM_001429

CCDS: CCDS14010, CCDS93173

Canonical transcript exons

ENST00000263253 — 31 exons

Exon	Start	End
ENSE00000654991	41117187	41117821
ENSE00000655017	41125864	41126040
ENSE00000655023	41127487	41127748
ENSE00000655024	41129890	41130003
ENSE00000655043	41135813	41135906
ENSE00000655048	41137653	41137790
ENSE00000655049	41140140	41140257
ENSE00000655078	41141048	41141222
ENSE00000655093	41146739	41146816
ENSE00000655110	41147837	41147946
ENSE00000655148	41149761	41150198
ENSE00000655228	41157169	41157408
ENSE00000655266	41158412	41158500
ENSE00000655295	41162723	41162779
ENSE00000655323	41166599	41166666
ENSE00000655331	41168449	41168599
ENSE00000655352	41168721	41168867
ENSE00000655374	41170406	41170571
ENSE00000655406	41172499	41172663
ENSE00000655428	41173623	41173784
ENSE00000655442	41176247	41176528
ENSE00000880436	41151833	41152012
ENSE00000880437	41152206	41152350
ENSE00000880438	41154995	41155113
ENSE00001302097	41160642	41160722
ENSE00001307142	41164053	41164130
ENSE00001336303	41149038	41149175
ENSE00001336414	41131388	41131633
ENSE00001730907	41169503	41169616
ENSE00004027638	41092592	41093098
ENSE00004027639	41176773	41180077

Expression profiles

Bgee: expression breadth ubiquitous, 292 present calls, max score 96.50.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 21.4020 / max 580.1176, expressed in 1809 samples.

FANTOM5 promoters (7 alternative TSS)

Promoter ID	TPM avg	Samples expressed
192442	12.3756	1796
192445	7.2128	1535
192449	0.9817	583
192443	0.2931	123
192444	0.2682	116
192447	0.1410	40
192446	0.1296	49

Top tissues by expression

299 total, by Bgee expression score (0-100, higher = more expressed):

Tissue	Anatomy ID	Expression score	Quality
colonic epithelium	UBERON:0000397	96.50	gold quality
adrenal tissue	UBERON:0018303	94.41	gold quality
bone marrow cell	CL:0002092	93.58	gold quality
lower lobe of lung	UBERON:0008949	93.37	gold quality
tonsil	UBERON:0002372	92.93	gold quality
cortical plate	UBERON:0005343	92.66	gold quality
male germ line stem cell (sensu Vertebrata) in testis	CL:0000089 ∩ UBERON:0000473	92.63	gold quality
visceral pleura	UBERON:0002401	92.49	gold quality
ventricular zone	UBERON:0003053	92.46	gold quality
parietal pleura	UBERON:0002400	92.33	gold quality
pleura	UBERON:0000977	91.81	gold quality
corpus callosum	UBERON:0002336	91.71	gold quality
monocyte	CL:0000576	91.70	gold quality
mononuclear cell	CL:0000842	91.50	gold quality
leukocyte	CL:0000738	91.47	gold quality
buccal mucosa cell	CL:0002336	91.37	silver quality
sural nerve	UBERON:0015488	90.79	gold quality
calcaneal tendon	UBERON:0003701	90.77	gold quality
testis	UBERON:0000473	90.65	gold quality
right testis	UBERON:0004534	90.51	gold quality
bone marrow	UBERON:0002371	90.50	gold quality
stromal cell of endometrium	CL:0002255	90.46	gold quality
ganglionic eminence	UBERON:0004023	90.45	gold quality
left testis	UBERON:0004533	90.28	gold quality
secondary oocyte	CL:0000655	90.16	gold quality
right hemisphere of cerebellum	UBERON:0014890	89.92	gold quality
mucosa of stomach	UBERON:0001199	89.80	gold quality
ovary	UBERON:0000992	89.69	gold quality
synovial joint	UBERON:0002217	89.46	gold quality
renal medulla	UBERON:0000362	89.41	gold quality

Single-cell (SCXA)

Detected in 1 experiment(s), a significant marker in 1.

Experiment	Marker?	Max mean expression
E-ANND-3	yes	10.18

Regulation

Is transcription factor: yes

Downstream targets (CollecTRI)

74 targets.

Target	Regulation
ABCB1	Unknown
ALB	Activation
ALDH3A1	Repression
ALOX15	Activation
BIRC5	Activation
BRCA1	Activation
CA9	Activation
CAV3	Activation
CCNB2	Unknown
CCND1	Unknown
CCNE1	Activation
CDKN1A	Activation
CDKN2B	Unknown
COL1A2	Unknown
CPT1B	Activation
CRABP1	Activation
CREBBP	Unknown
CXCL8	Unknown
CYBB	Repression
CYP1B1	Unknown
DNMT1	Activation
EIF2AK1	Activation
EPO	Activation
ERBB2	Unknown
EZH2	Unknown
GFAP	Activation
GREB1
HINFP	Activation
IFNG	Activation
IGF1	Unknown

Upstream regulators (CollecTRI, top): AR, ATF2, BMAL1, BRCA1, CEBPE, CLOCK, CREBBP, DBP, EGR1, EPAS1, ESR1, ETV4, FLI1, FOXA2, GATA4, MBD2, MEF2C, MEF2D, MYC, NCOA1, NCOA2, NCOA3, NFKB1, NFKB, NKX2-5, NR0B2, NUPR1, PML, STAT6, YY1, ZKSCAN4

miRNA regulators (miRDB)

161 targeting EP300, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNA	Max score	Avg score	miRNA target_count
HSA-MIR-190A-3P	100.00	80.35	5520
HSA-MIR-5011-5P	100.00	83.46	5820
HSA-MIR-6867-5P	100.00	82.21	3464
HSA-MIR-1277-5P	100.00	73.95	5056
HSA-MIR-8485	100.00	77.57	4731
HSA-MIR-5692A	100.00	74.40	6850
HSA-MIR-6873-3P	100.00	71.42	2626
HSA-MIR-3613-3P	100.00	76.36	7965
HSA-MIR-6833-3P	100.00	70.63	3197
HSA-MIR-3689D	100.00	66.14	1181
HSA-MIR-6851-5P	100.00	65.63	1294
HSA-MIR-4768-5P	100.00	69.49	2861
HSA-MIR-200B-3P	100.00	73.31	2693
HSA-MIR-200C-3P	100.00	73.35	2685
HSA-MIR-429	100.00	73.44	2698
HSA-MIR-12118	100.00	65.88	1270
HSA-MIR-5193	100.00	67.26	1744
HSA-MIR-4481	100.00	66.42	1669
HSA-MIR-150-5P	99.99	66.69	1976
HSA-MIR-186-5P	99.99	70.83	3707
HSA-MIR-4775	99.98	75.00	6394
HSA-MIR-6891-5P	99.98	66.53	1372
HSA-MIR-3173-3P	99.98	66.49	1217
HSA-MIR-12136	99.98	72.81	5713
HSA-MIR-302C-5P	99.97	72.56	3642
HSA-MIR-590-3P	99.96	74.34	6478
HSA-MIR-6780B-5P	99.96	69.60	2562
HSA-MIR-4725-3P	99.96	69.53	2520
HSA-MIR-551B-5P	99.96	71.28	3493
HSA-MIR-548AA	99.96	70.64	3753

Functional genomics

ClinGen dosage: haploinsufficiency 3 (sufficient evidence), triplosensitivity 0 (no evidence). ClinGen Gene Dosage Map DepMap (CRISPR cell-line fitness): dependent in 33.3% of screened cell lines.

Literature-anchored findings (GeneRIF, showing 40)

• p300 stimulates Type I collagen synthesis in skin fibroblasts (PMID:10918613)
• p300 is involved in the antagonistic regulation of Type I collagen gene expression by Transforming Growth Factor-b and Interferon-g (PMID:11134049)
• substrate specificity; structure activity relationship (PMID:11691934)
• CBP/p300 and NcoA/SRC1a may function in a common pathway to regulate STAT3 transcriptional activity. (PMID:11773079)
• p300 Modulates the BRCA1 inhibition of estrogen receptor activity (PMID:11782371)
• Scaffold/matrix attachment region elements interact with a p300-scaffold attachment factor A complex and are bound by acetylated nucleosomes. (PMID:11909954)
• Results demonstrate that phosphorylation of p65 determines whether it associates with either CBP or HDAC-1, ensuring that only p65 entering the nucleus from cytoplasmic NF-kappa B:Ikappa B complexes can activate transcription. (PMID:11931769)
• The HMG-I/Y-related protein p8 binds to p300 and Pax2 trans-activation domain-interacting protein to regulate the trans-activation activity of the Pax2A and Pax2B transcription factors on the glucagon gene promoter. (PMID:11940591)
• Dual roles of p300 in chromatin assembly and transcriptional activation in cooperation with nucleosome assembly protein 1 in vitro. (PMID:11940655)
• Carboxyl-terminal transactivation activity of hypoxia-inducible factor 1 alpha is governed by a von Hippel-Lindau protein-independent, hydroxylation-regulated association with p300/CBP. (PMID:11940656)
• In vitro assays show an indispensable role for H3 and H4 tails, especially major lysine substrates, in p300-dependent transcriptional activation, as well as activator-targeted acetylation of promoter-proximal histone tails by p300. (PMID:11983172)
• CBP-p300 plays a role in regulating p450scc expression with TReP-132 and steroidogenic factor-1 (PMID:12101186)
• p300 and TATA-binding protein-free TAF-containing complex cooperate during transcriptional activation (PMID:12107188)
• p300 plays an important role in epithelial carcinogenesis by mediating transcription that negatively regulates cell proliferation.(P300-CBP coactivator) (PMID:12136661)
• MDMX dramatically inhibits the acetylation of p53 induced by both endogenous and ectopically expressed p300/CBP. (PMID:12162806)
• p300 coactivator has a role in suppressing tumor cell growth (PMID:12237408)
• results suggest that all-trans-retinoic acid and retinoic acid receptors regulate growth arrest of human mammary epithelial cells and modulate CBP/p300 protein expression (PMID:12242694)
• suggest an important role of p300 in regulation of HPV8 gene expression and reveal a new mechanism by which E2 may be recruited to a promoter to activate transcription without sequence specific DNA binding (PMID:12368347)
• PKC delta inhibits p300/CBP-associated factor activity after phosphorylation at serine 89 (PMID:12379484)
• p300 plays a critical regulatory role in base excision repair (PMID:12453427)
• p300/CBP binds to IRF3, enabling it to act as a transcription factor (PMID:12473110)
• our results indicate an important role for Mediator, as well as its functional interplay with p300/CBP-SRC, in the enhancement of ERalpha-dependent transcription with chromatin templates (PMID:12482985)
• synergism with p68 RNA helicase (PMID:12527917)
• MAPK signaling facilitates HIF1a and HIF2a activation through p300/CBP (PMID:12588875)
• Interferon regulatory factor-7 synergizes with other transcription factors through multiple interactions with p300/CBP coactivators. (PMID:12604599)
• in human mammary epithelial cells, CBP/p300 were both modulated by an all-trans-retinoic acid (ATRA) signaling pathway and were required for a normal response to ATRA (PMID:12646247)
• generation of the polyubiquitinated forms of p53 that are targeted for proteasome degradation requires the intrinsic ubiquitin ligase activities of MDM2 and p300 (PMID:12690203)
• Loss of EP300 was not statistically significant selection in cancer cells stratified by various criteria for the concordant loss of EP300 and CREBBP. (PMID:12696060)
• p300 may further regulate the transcriptional activity of p53 through a novel acetylation site, Lys-305 (PMID:12724314)
• CBP and p300 function as co-activators of Sox9 for cartilage tissue-specific gene expression and chondrocyte differentiation. (PMID:12732631)
• We investigated occupancy of ER-alpha promoter by pRb2/p130-E2F4/5-HDAC1-SUV39 H1-p300 and pRb2/p130-E2F4/5-HDAC1-SUV39H1-DNMT1 complexes, and provided a link between pRb2/p130 and chromatin-modifying enzymes in the regulation of ER-alpha transcription (PMID:12789259)
• S-nitrosation of Cys-800 stimulates the recruitment of p300 co-activator protein to the HIF-1alpha C-terminal domain (PMID:12914934)
• ER81 is acetylated by two coactivators/acetyltransferases, p300 and p300- and CBP-associated factor (P/CAF) . Whereas p300 acetylates two lysine residues (K33 and K116) within the ER81 N-terminal transactivation domain, P/CAF targets only K116. (PMID:12917345)
• p300 plays a role in formation of the TBP-TFIIA-containing basal transcription complex, TAC. (PMID:12941701)
• p300 has a role in NF-kappaB-dependent gene expression along with PARP-1 (PMID:12960163)
• we show that E7 can abolish the p300-mediated E2 transactivation function, suggesting that complex formation between E7 and p300 may contribute to the regulation of E2 transcriptional activity. (PMID:12970734)
• p300 has a role in the trans-repression of beta-catenin signaling by nuclear receptors and their ligands (PMID:12972427)
• EWS-ER81 and EWS-Fli-1 interact with and thereby activate the MMP-1 promoter, which is potentiated by the cofactor p300 and the proto-oncoprotein c-Jun. (PMID:14550555)
• forms complex with SATB1 which binds to the 5’ upstream AT-rich region in the bp -115 to bp -106 segment represses the gp91(phox) promoter activity (PMID:14605447)
• p300-mediated acetylation can be highly constrained by substrate conformation in vivo (PMID:14612423)

Cross-species orthologs

10 orthologs

Organism	Symbol	Gene ID
danio_rerio	ep300b	ENSDARG00000061108
danio_rerio	ep300a	ENSDARG00000100666
mus_musculus	Ep300	ENSMUSG00000055024
rattus_norvegicus	Ep300	ENSRNOG00000065659
drosophila_melanogaster	nej	FBGN0261617
caenorhabditis_elegans		WBGENE00000366
caenorhabditis_elegans		WBGENE00009595
caenorhabditis_elegans		WBGENE00010545
caenorhabditis_elegans		WBGENE00016220
caenorhabditis_elegans		WBGENE00016221

Paralogs (1): CREBBP (ENSG00000005339)

Protein

Protein identifiers

Histone acetyltransferase p300 — Q09472 (reviewed: Q09472)

Alternative names: E1A-associated protein p300, Histone butyryltransferase p300, Histone crotonyltransferase p300, Protein 2-hydroxyisobutyryltransferase p300, Protein isonicotinyltransferase p300, Protein lactyltransferas p300, Protein propionyltransferase p300

All UniProt accessions (5): Q09472, A0A0U1RR87, A0A669KB12, A0A994J3N7, A0A994J6T4

UniProt curated annotations — full annotation on UniProt →

Function. Functions as a histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Mediates acetylation of histone H3 at ‘Lys-122’ (H3K122ac), a modification that localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability. Mediates acetylation of histone H3 at ‘Lys-18’ and ‘Lys-27’ (H3K18ac and H3K27ac, respectively). Also able to acetylate histone lysine residues that are already monomethylated on the same side chain to form N6-acetyl-N6-methyllysine (Kacme), an epigenetic mark of active chromatin associated with increased transcriptional initiation. Catalyzes formation of histone H4 acetyl-methylated at ‘Lys-5’ and ‘Lys-12’ (H4K5acme and H4K12acme, respectively). In response to DNA damage, catalyzes acetylation of histone H1 at ‘Lys-75’ (H1K75ac) following histone H1 deamidation by CTPS1, increasing chromatin accessibility to facilitate the recruitment of DNA repair proteins. Also functions as acetyltransferase for non-histone targets, such as ALX1, HDAC1, PRDM16, PRMT1, SIRT2, STAT3, ZNF76 or GLUL. Acetylates ‘Lys-131’ of ALX1 and acts as its coactivator. Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of p53/TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function. Following DNA damage, forms a stress-responsive p53/TP53 coactivator complex with JMY which mediates p53/TP53 acetylation, thereby increasing p53/TP53-dependent transcription and apoptosis. Promotes chromatin acetylation in heat shock responsive HSP genes during the heat shock response (HSR), thereby stimulating HSR transcription. Acetylates HDAC1 leading to its inactivation and modulation of transcription. Acetylates ‘Lys-247’ of EGR2. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2. Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement. Can also mediate transcriptional repression. Acetylates FOXO1 and enhances its transcriptional activity. Acetylates STAT3 at different sites, promoting both STAT3 dimerization and activation and recruitment to chromatin. Acetylates BCL6 which disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity. Participates in CLOCK or NPAS2-regulated rhythmic gene transcription; exhibits a circadian association with CLOCK or NPAS2, correlating with increase in PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter. Acetylates MTA1 at ‘Lys-626’ which is essential for its transcriptional coactivator activity. Acetylates XBP1 isoform 2; acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity. Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER). Acetylates MEF2D. Acetylates and stabilizes ZBTB7B protein by antagonizing ubiquitin conjugation and degradation, this mechanism may be involved in CD4/CD8 lineage differentiation. Acetylates GABPB1, impairing GABPB1 heterotetramerization and activity. Acetylates PCK1 and promotes PCK1 anaplerotic activity. Acetylates RXRA and RXRG. Acetylates isoform M2 of PKM (PKM2), promoting its homodimerization and conversion into a protein kinase. Acetylates RPTOR in response to leucine, leading to activation of the mTORC1 complex. Acetylates RICTOR, leading to activation of the mTORC2 complex. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREBBP. In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA), butanoyl-CoA (butyryl-CoA), 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), lactoyl-CoA, propanoyl-CoA (propionyl-CoA) or isonicotinyl-CoA, and is able to mediate protein crotonylation, butyrylation, 2-hydroxyisobutyrylation, lactylation, propionylation or isonicotinylation, respectively. Acts as a histone crotonyltransferase; crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. Histone crotonyltransferase activity is dependent on the concentration of (2E)-butenoyl-CoA (crotonyl-CoA) substrate and such activity is weak when (2E)-butenoyl-CoA (crotonyl-CoA) concentration is low. Also acts as a histone butyryltransferase; butyrylation marks active promoters. Catalyzes histone lactylation in macrophages by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription. Acts as a protein-lysine 2-hydroxyisobutyryltransferase; regulates glycolysis by mediating 2-hydroxyisobutyrylation of glycolytic enzymes. Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway. (Microbial infection) In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat’s transactivating activity and may help inducing chromatin remodeling of proviral genes. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein.

Subunit / interactions. Interacts with HIF1A; the interaction is stimulated in response to hypoxia and inhibited by CITED2. Probably part of a complex with HIF1A and CREBBP. Interacts (via N-terminus) with TFAP2A (via N-terminus); the interaction requires CITED2. Interacts (via CH1 domain) with CITED2 (via C-terminus). Interacts with CITED1 (unphosphorylated form preferentially and via C-terminus). Interacts with ESR1; the interaction is estrogen-dependent and enhanced by CITED1. Interacts with HIPK2. Interacts with DTX1, EID1, ELF3, FEN1, LEF1, NCOA1, NCOA6, NR3C1, PCAF, PELP1, PRDM6, SP1, SP3, SPIB, SRY, TCF7L2, DDX5, DDX17, SATB1, SRCAP and TRERF1. Interacts with JMY, the complex activates p53/TP53 transcriptional activity. Interacts with TTC5/STRAP; the interaction facilitates the association between JMY and p300/EP300 cofactors. Interacts with p53/TP53; the interaction is facilitated by TTC5/STRAP. Forms a complex with TTC5/STRAP and HSF1; these interactions augment chromatin-bound HSF1 and p300/EP300 histone acetyltransferase activity. Part of a complex containing CARM1 and NCOA2/GRIP1. Interacts with ING4 and this interaction may be indirect. Interacts with ING5. Interacts with the C-terminal region of CITED4. Non-sumoylated EP300 preferentially interacts with SENP3. Interacts with SS18L1/CREST. Interacts with ALX1 (via homeobox domain). Interacts with NEUROD1; the interaction is inhibited by NR0B2. Interacts with TCF3. Interacts (via CREB-binding domain) with MYOCD (via C-terminus). Interacts with ROCK2 and PPARG. Forms a complex made of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy in cardiomyocytes. Interacts with IRF1 and this interaction enhances acetylation of p53/TP53 and stimulation of its activity. Interacts with ALKBH4 and DDIT3/CHOP. Interacts with KLF15. Interacts with CEBPB and RORA. Interacts with NPAS2, BMAL1 and CLOCK. Interacts with SIRT2 isoform 1, isoform 2 and isoform 5. Interacts with MTA1. Interacts with HDAC4 and HDAC5 in the presence of TFAP2C. Interacts with TRIP4. Directly interacts with ZBTB49; this interaction leads to synergistic transactivation of CDKN1A. Interacts with NR4A3. Interacts with ZNF451. Interacts with ATF5; EP300 is required for ATF5 and CEBPB interaction and DNA binding. Interacts with HSF1. Interacts with ZBTB48/TZAP. Interacts with STAT1; the interaction is enhanced upon IFN-gamma stimulation. Interacts with HNRNPU (via C-terminus); this interaction enhances DNA-binding of HNRNPU to nuclear scaffold/matrix attachment region (S/MAR) elements. Interacts with BCL11B. Interacts with SMAD4; negatively regulated by ZBTB7A. Interacts with DUX4 (via C-terminus). Interacts with NUPR1; this interaction enhances the effect of EP300 on PAX2 transcription factor activity. Interacts with RXRA; the interaction is decreased by 9-cis retinoic acid. NR4A1 competes with EP300 for interaction with RXRA and thereby attenuates EP300 mediated acetylation of RXRA. Interacts with RB1. Interacts with DDX3X; this interaction may facilitate HNF4A acetylation. Interacts with SOX9. Interacts with ATF4; EP300/p300 stabilizes ATF4 and increases its transcriptional activity independently of its catalytic activity by preventing its ubiquitination. Interacts with KAT5; promoting KAT5 autoacetylation. Interacts (via bromo domain) with (acetylated) STAT3; interaction takes place following STAT3 acetylation by EP300 and promotes enhanceosome assembly. (Microbial infection) Interacts with human adenovirus 5 E1A protein; this interaction stimulates the acetylation of RB1 by recruiting EP300 and RB1 into a multimeric-protein complex. (Microbial infection) Interacts with and acetylates HIV-1 Tat. (Microbial infection) Interacts with HTLV-1 proteins Tax, p30II and HBZ.

Subcellular location. Cytoplasm. Nucleus. Chromosome.

Post-translational modifications. Acetylated on Lys at up to 17 positions by intermolecular autocatalysis. Deacetylated in the transcriptional repression domain (CRD1) by SIRT1, preferentially at Lys-1020. Deacetylated by SIRT2, preferentially at Lys-418, Lys-423, Lys-1542, Lys-1546, Lys-1549, Lys-1699, Lys-1704 and Lys-1707. Citrullinated at Arg-2142 by PADI4, which impairs methylation by CARM1 and promotes interaction with NCOA2/GRIP1. Methylated at Arg-580 and Arg-604 in the KIX domain by CARM1, which blocks association with CREB, inhibits CREB signaling and activates apoptotic response. Also methylated at Arg-2142 by CARM1, which impairs interaction with NCOA2/GRIP1. Sumoylated; sumoylation in the transcriptional repression domain (CRD1) mediates transcriptional repression. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3. Probable target of ubiquitination by FBXO3, leading to rapid proteasome-dependent degradation. Phosphorylated by HIPK2 in a RUNX1-dependent manner. This phosphorylation that activates EP300 happens when RUNX1 is associated with DNA and CBFB. Phosphorylated by ROCK2 and this enhances its activity. Phosphorylation at Ser-89 by AMPK reduces interaction with nuclear receptors, such as PPARG.

Disease relevance. Defects in EP300 may play a role in epithelial cancer. Chromosomal aberrations involving EP300 may be a cause of acute myeloid leukemias. Translocation t(8;22)(p11;q13) with KAT6A. Rubinstein-Taybi syndrome 2 (RSTS2) [MIM:613684] A disorder characterized by craniofacial abnormalities, postnatal growth deficiency, broad thumbs, broad big toes, intellectual disability and a propensity for development of malignancies. Some individuals with RSTS2 have less severe mental impairment, more severe microcephaly, and a greater degree of changes in facial bone structure than RSTS1 patients. The disease is caused by variants affecting the gene represented in this entry. Menke-Hennekam syndrome 2 (MKHK2) [MIM:618333] A form of Menke-Hennekam syndrome, a congenital autosomal dominant disease characterized by developmental delay, growth retardation, and craniofacial dysmorphism. Patients have intellectual disability of variable severity, speech delay, autistic behavior, short stature and microcephaly. Main facial characteristics include short palpebral fissures, telecanthi, depressed nasal ridge, short nose, anteverted nares, short columella and long philtrum. The disease is caused by variants affecting the gene represented in this entry.

Domain organisation. The CRD1 domain (cell cycle regulatory domain 1) mediates transcriptional repression of a subset of p300 responsive genes; it can be de-repressed by CDKN1A/p21WAF1 at least at some promoters. It contains sumoylation and acetylation sites and the same lysine residues may be targeted for the respective modifications. It is proposed that deacetylation by SIRT1 allows sumoylation leading to suppressed activity.

RefSeq proteins (2): NP_001349772, NP_001420* (*=MANE)

Domains & families (InterPro)

ID	Name	Type
IPR000197	Znf_TAZ	Domain
IPR000433	Znf_ZZ	Domain
IPR001487	Bromodomain	Domain
IPR003101	KIX_dom	Domain
IPR009110	Nuc_rcpt_coact	Homologous_superfamily
IPR010303	RING_CBP-p300	Domain
IPR013083	Znf_RING/FYVE/PHD	Homologous_superfamily
IPR013178	Histone_AcTrfase_Rtt109/CBP	Family
IPR014744	Nuc_rcpt_coact_CREBbp	Domain
IPR018359	Bromodomain_CS	Conserved_site
IPR031162	CBP_P300_HAT	Domain
IPR035898	TAZ_dom_sf	Homologous_superfamily
IPR036427	Bromodomain-like_sf	Homologous_superfamily
IPR036529	KIX_dom_sf	Homologous_superfamily
IPR037073	Nuc_rcpt_coact_CREBbp_sf	Homologous_superfamily
IPR038547	RING_CBP-p300_sf	Homologous_superfamily
IPR043145	Znf_ZZ_sf	Homologous_superfamily
IPR056484	PHD_P300	Domain

Pfam: PF00439, PF00569, PF02135, PF02172, PF06001, PF08214, PF09030, PF23570

Enzyme classification (BRENDA):

• EC 2.3.1.48 — histone acetyltransferase (BRENDA: 41 organisms, 681 substrates, 1134 inhibitors, 140 Km, 96 kcat entries)

Substrate kinetics (BRENDA)

27 substrates with measured Km, best-characterized 15. Km ranges are aggregated across organisms/conditions.

Substrate	Km (mM)	Measurements
ACETYL-COA	0.0002–0.046	51
HISTONE H3	0.007–2.09	23
HISTONE H4	—	11
HISTONE H4 PEPTIDE	0.0208–0.197	7
HISTONE	0.075–1.4	6
HISTONE H3 TAIL PEPTIDE	0.044–0.112	4
PICCOLONUA4 PEPTIDE	0.135–0.372	4
3-AZIDOPROPIONYL-COA	0.0002–0.0086	3
4-PENTYNOYL-COA	0.0009–0.0859	3
SPERMIDINE	0.18–0.27	3
5-HEXYNOYL-COA	0.0006–0.0117	2
6-HEPTYNOYL-COA	0.0003–0.0237	2
HISTONE H3-PEPTIDE	0.05–0.49	2
PROTEIN P53	1.28–4.63	2
3-AZIDOPROPANOYL-COA	0.0103	1

Catalyzed reactions (Rhea), 9 shown:

• L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+) (RHEA:21992)
• 2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein] + CoA + H(+) (RHEA:24180)
• L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+) (RHEA:45948)
• (2E)-butenoyl-CoA + L-lysyl-[protein] = N(6)-(2E)-butenoyl-L-lysyl-[protein] + CoA + H(+) (RHEA:53908)
• butanoyl-CoA + L-lysyl-[protein] = N(6)-butanoyl-L-lysyl-[protein] + CoA + H(+) (RHEA:53912)
• propanoyl-CoA + L-lysyl-[protein] = N(6)-propanoyl-L-lysyl-[protein] + CoA + H(+) (RHEA:54020)
• (S)-lactoyl-CoA + L-lysyl-[protein] = N(6)-[(S)-lactoyl]-L-lysyl-[protein] + CoA + H(+) (RHEA:61996)
• N(6)-methyl-L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-N(6)-methyl-L-lysyl-[histone] + CoA + H(+) (RHEA:77775)
• isonicotinyl-CoA + L-lysyl-[protein] = N(6)-isonicotinyl-L-lysyl-[protein] + CoA + H(+) (RHEA:83539)

UniProt features (233 total): helix 35, modified residue 30, mutagenesis site 29, compositionally biased region 28, strand 27, binding site 25, region of interest 18, sequence variant 12, turn 11, sequence conflict 4, domain 3, zinc finger region 3, site 3, cross-link 2, initiator methionine 1, chain 1, short sequence motif 1

Structure

Experimental structures (PDB)

60 structures, top 30 by resolution.

PDB	Method	Resolution (Å)
5BT3	X-RAY DIFFRACTION	1.05
3T92	X-RAY DIFFRACTION	1.5
5LPM	X-RAY DIFFRACTION	1.5
5NU5	X-RAY DIFFRACTION	1.6
3BIY	X-RAY DIFFRACTION	1.7
6PGU	X-RAY DIFFRACTION	1.72
6V8K	X-RAY DIFFRACTION	1.84
4PZS	X-RAY DIFFRACTION	1.94
5KJ2	X-RAY DIFFRACTION	1.95
6DS6	X-RAY DIFFRACTION	1.95
7QGS	X-RAY DIFFRACTION	2
7UGI	X-RAY DIFFRACTION	2
7VHZ	X-RAY DIFFRACTION	2
8GZC	X-RAY DIFFRACTION	2
9IT5	X-RAY DIFFRACTION	2
5LKT	X-RAY DIFFRACTION	2.04
6V90	X-RAY DIFFRACTION	2.04
4PZR	X-RAY DIFFRACTION	2.1
5LPK	X-RAY DIFFRACTION	2.1
7VI0	X-RAY DIFFRACTION	2.1
8FVF	X-RAY DIFFRACTION	2.1
9MZA	X-RAY DIFFRACTION	2.1
9JUT	X-RAY DIFFRACTION	2.13
7SS8	X-RAY DIFFRACTION	2.15
3P57	X-RAY DIFFRACTION	2.19
6V8N	X-RAY DIFFRACTION	2.3
7VHY	X-RAY DIFFRACTION	2.3
6PF1	X-RAY DIFFRACTION	2.32
3I3J	X-RAY DIFFRACTION	2.33
7SSK	X-RAY DIFFRACTION	2.36

Predicted structure (AlphaFold)

Model	pLDDT	Fraction very-high
AF-Q09472-F1	54.88	0.22

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Catalytic / active sites (3): 31–32 (breakpoint for translocation to form kat6a-ep300 and ep300-kat6a); 2088 (interaction with ncoa2); 2142 (interaction with ncoa2)

Ligand- & substrate-binding residues (25): 347; 351; 364; 369; 378; 382; 388; 393; 402; 406; 411; 414 …

Post-translational modifications (32): 1546, 1549, 1554, 1555, 1558, 1560, 1583, 1699, 1704, 1707, 1726, 2142, 2142, 1020, 1024, 2, 89, 418, 423, 499 …

Mutagenesis-validated functional residues (29):

Position	Phenotype
89	abolishes ampk-mediated phosphorylation.
89	phosphomimetic mutant that leads to descreased interaction with nuclear receptors.
344	inhibits interaction with hif1a and transcription activation; when associated with a-345.
345	inhibits interaction with hif1a and transcription activation; when associated with a-344.
371–376	inhibits interaction with hif1a. reduces interaction with cited2.
413–418	inhibits interaction with hif1a. does not inhibit interaction with cited2.
1020	abolishes sumoylation and transcriptional repression when associated with a-1024.
1020	abolishes sumoylation and transcriptional repression; when associated with r-1024.
1024	abolishes sumoylation and transcriptional repression; when associated with a-1020.
1024	abolishes sumoylation and transcriptional repression; when associated with r-1020.
1170	increased acetyltransferase activity.
1204	increased acetyltransferase activity.
1242	increased acetyltransferase activity.
1357	40% decrease in activity.
1357	40% decrease in activity. 90% decrease in activity; when associated with r-1505; r-1625 and r-1628.
1396	loss of activity; when associated with r-1397.
1396	loss of activity; when associated with w-1396.
1397	loss of activity; when associated with r-1396.
1397	loss of activity; when associated with w-1397.
1399	abolished acetyltransferase and acyltransferase activities. abolishes autoacetylation. does not interact with tfap2a and
1467	abolishes autoacetylation. loss of acetyltransferase activity.
1504	abolished acetyltransferase activity.
1505	90% decrease in activity; when associated with r-1625 and r-1628. 90% decrease in activity; when associated with r-1357;
1625	70% decrease in activity; when associated with r-1628. 90% decrease in activity; when associated with r-1505 and r-1628.
1628	70% decrease in activity; when associated with r-1625. 90% decrease in activity; when associated with e-1505 and r-1625.

Function

Pathways and Gene Ontology

Reactome pathways

62 pathways

ID	Pathway
R-HSA-1234158	Regulation of gene expression by Hypoxia-inducible Factor
R-HSA-156711	Polo-like kinase mediated events
R-HSA-1912408	Pre-NOTCH Transcription and Translation
R-HSA-1989781	PPARA activates gene expression
R-HSA-201722	Formation of the beta-catenin:TCF transactivating complex
R-HSA-210744	Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells
R-HSA-2122947	NOTCH1 Intracellular Domain Regulates Transcription
R-HSA-2173796	SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-HSA-2197563	NOTCH2 intracellular domain regulates transcription
R-HSA-2644606	Constitutive Signaling by NOTCH1 PEST Domain Mutants
R-HSA-2894862	Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants
R-HSA-3134973	LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production
R-HSA-3214847	HATs acetylate histones
R-HSA-3371568	Attenuation phase
R-HSA-381340	Transcriptional regulation of white adipocyte differentiation
R-HSA-3899300	SUMOylation of transcription cofactors
R-HSA-5250924	B-WICH complex positively regulates rRNA expression
R-HSA-5617472	Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-5621575	CD209 (DC-SIGN) signaling
R-HSA-5689901	Metalloprotease DUBs
R-HSA-6804114	TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest
R-HSA-6804758	Regulation of TP53 Activity through Acetylation
R-HSA-6804760	Regulation of TP53 Activity through Methylation
R-HSA-6811555	PI5P Regulates TP53 Acetylation
R-HSA-8866907	Activation of the TFAP2 (AP-2) family of transcription factors
R-HSA-8936459	RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939243	RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known
R-HSA-8941856	RUNX3 regulates NOTCH signaling
R-HSA-8941858	Regulation of RUNX3 expression and activity
R-HSA-8951936	RUNX3 regulates p14-ARF

MSigDB gene sets: 0 (showing top):

GO Biological Process (83): negative regulation of transcription by RNA polymerase II (GO:0000122), response to hypoxia (GO:0001666), somitogenesis (GO:0001756), thigmotaxis (GO:0001966), behavioral defense response (GO:0002209), stimulatory C-type lectin receptor signaling pathway (GO:0002223), regulation of glycolytic process (GO:0006110), protein acetylation (GO:0006473), internal protein amino acid acetylation (GO:0006475), apoptotic process (GO:0006915), canonical NF-kappaB signal transduction (GO:0007249), nervous system development (GO:0007399), heart development (GO:0007507), skeletal muscle tissue development (GO:0007519), learning or memory (GO:0007611), circadian rhythm (GO:0007623), animal organ morphogenesis (GO:0009887), regulation of autophagy (GO:0010506), negative regulation of autophagy (GO:0010507), regulation of mitochondrion organization (GO:0010821), positive regulation of neuron projection development (GO:0010976), N-terminal peptidyl-lysine acetylation (GO:0018076), internal peptidyl-lysine acetylation (GO:0018393), B cell differentiation (GO:0030183), platelet formation (GO:0030220), lung development (GO:0030324), positive regulation of transforming growth factor beta receptor signaling pathway (GO:0030511), negative regulation of protein-containing complex assembly (GO:0031333), protein destabilization (GO:0031648), cellular response to nutrient levels (GO:0031669), negative regulation of protein oligomerization (GO:0032460), cellular response to UV (GO:0034644), multicellular organism growth (GO:0035264), megakaryocyte development (GO:0035855), swimming (GO:0036268), positive regulation of protein import into nucleus (GO:0042307), intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator (GO:0042771), response to estrogen (GO:0043627), host-mediated activation of viral transcription (GO:0043923), fat cell differentiation (GO:0045444)

GO Molecular Function (45): transcription coregulator binding (GO:0001221), transcription coactivator binding (GO:0001223), p53 binding (GO:0002039), DNA binding (GO:0003677), chromatin binding (GO:0003682), damaged DNA binding (GO:0003684), transcription coactivator activity (GO:0003713), histone acetyltransferase activity (GO:0004402), L-lysine N6-acetyltransferase activity, acting on acetyl phosphate as donor (GO:0004468), beta-catenin binding (GO:0008013), zinc ion binding (GO:0008270), histone H3 acetyltransferase activity (GO:0010484), histone H4 acetyltransferase activity (GO:0010485), acetyltransferase activity (GO:0016407), acyltransferase activity (GO:0016746), nuclear receptor binding (GO:0016922), chromatin DNA binding (GO:0031490), histone H3K18 acetyltransferase activity (GO:0043993), histone H2B acetyltransferase activity (GO:0044013), histone H3K27 acetyltransferase activity (GO:0044017), tau protein binding (GO:0048156), nuclear androgen receptor binding (GO:0050681), NF-kappaB binding (GO:0051059), RNA polymerase II-specific DNA-binding transcription factor binding (GO:0061629), protein-lysine-acetyltransferase activity (GO:0061733), protein propionyltransferase activity (GO:0061920), pre-mRNA intronic binding (GO:0097157), STAT family protein binding (GO:0097677), peptide 2-hydroxyisobutyryltransferase activity (GO:0106226), histone lactyltransferase (CoA-dependent) activity (GO:0120301), acetylation-dependent protein binding (GO:0140033), peptide butyryltransferase activity (GO:0140065), histone crotonyltransferase activity (GO:0140068), histone butyryltransferase activity (GO:0140069), histone isonicotinyltransferase activity (GO:0140230), DNA-binding transcription factor binding (GO:0140297), histone H3K122 acetyltransferase activity (GO:0140908), histone H1K75 acetyltransferase activity (GO:0160263), transcription coregulator activity (GO:0003712), protein binding (GO:0005515)

GO Cellular Component (10): histone acetyltransferase complex (GO:0000123), chromatin (GO:0000785), nucleus (GO:0005634), nucleoplasm (GO:0005654), transcription regulator complex (GO:0005667), cytoplasm (GO:0005737), cytosol (GO:0005829), protein-DNA complex (GO:0032993), chromosome (GO:0005694), protein-containing complex (GO:0032991)

Reactome top-level categories

Rollup of top-20 pathways:

Category	Pathways
Cellular response to hypoxia	1
G2/M Transition	1
Pre-NOTCH Expression and Processing	1
Regulation of lipid metabolism by PPARalpha	1
TCF dependent signaling in response to WNT	1
Regulation of beta-cell development	1
Signaling by NOTCH1	1
Transcriptional activity of SMAD2/SMAD3:SMAD4 heterotrimer	1
Signaling by NOTCH2	1
Signaling by NOTCH1 PEST Domain Mutants in Cancer	1
Signaling by NOTCH1 HD+PEST Domain Mutants in Cancer	1
Cytosolic sensors of pathogen-associated DNA	1
Chromatin modifying enzymes	1
HSF1-dependent transactivation	1
Adipogenesis	1

GO top-level categories

Rollup of top GO terms by namespace:

Category	Terms
cellular anatomical structure	4
behavior	3
histone acetyltransferase activity	3
animal organ development	2
autophagy	2
protein binding	2
DNA binding	2
histone H3 acetyltransferase activity	2
protein-containing complex	2
regulation of transcription by RNA polymerase II	1
transcription by RNA polymerase II	1
negative regulation of DNA-templated transcription	1
response to stress	1
response to decreased oxygen levels	1
anterior/posterior pattern specification	1
segmentation	1
chordate embryonic development	1
anatomical structure formation involved in morphogenesis	1
somite development	1
defense response	1
innate immune response activating cell surface receptor signaling pathway	1
cellular response to lectin	1
glycolytic process	1
regulation of purine nucleotide catabolic process	1
regulation of generation of precursor metabolites and energy	1
regulation of carbohydrate catabolic process	1
regulation of ATP metabolic process	1
protein acylation	1
protein acetylation	1
programmed cell death	1
apoptotic signaling pathway	1
execution phase of apoptosis	1
intracellular signaling cassette	1
system development	1
circulatory system development	1
striated muscle tissue development	1
skeletal muscle organ development	1
cognition	1
rhythmic process	1
anatomical structure morphogenesis	1

Protein interactions and networks

STRING

6450 interactions, top by confidence (×1000):

Protein A	Protein B	Partner UniProt	Score
EP300	TP53	P04637	998
EP300	KAT2B	Q92831	998
EP300	CREB1	P16220	997
EP300	HIF1A	Q16665	996
EP300	HDAC1	Q13547	995
EP300	MDM2	Q00987	994
EP300	MYC	P01106	994
EP300	RELA	Q04206	994
EP300	CITED2	Q99967	993
EP300	NCOA3	Q9Y6Q9	993
EP300	JUN	P05412	992
EP300	ARNT	P27540	992
EP300	CTNNB1	P35222	992
EP300	STAT3	P40763	992
EP300	SMAD3	P84022	992
EP300	IRF3	Q14653	992

IntAct

513 interactions, top by confidence:

A	B	Type	Score
TP53	EP300	psi-mi:“MI:0407”(direct interaction)	0.980
EP300	TP53	psi-mi:“MI:0915”(physical association)	0.980
EP300	TP53	psi-mi:“MI:0407”(direct interaction)	0.980
EP300	TP53	psi-mi:“MI:0192”(acetylation reaction)	0.980
EP300	HIF1A	psi-mi:“MI:0915”(physical association)	0.960
HIF1A	EP300	psi-mi:“MI:0915”(physical association)	0.960
HIF1A	EP300	psi-mi:“MI:0914”(association)	0.960
RELA	NFKB1	psi-mi:“MI:0914”(association)	0.920
CDK2	CCNB2	psi-mi:“MI:0914”(association)	0.860
MED23	MED19	psi-mi:“MI:2364”(proximity)	0.770
HSPA8	GAK	psi-mi:“MI:0914”(association)	0.760
EP300	APEX1	psi-mi:“MI:0915”(physical association)	0.720
EP300	APEX1	psi-mi:“MI:0192”(acetylation reaction)	0.720
AUTS2	EP300	psi-mi:“MI:0915”(physical association)	0.680

BioGRID (3159): EP300 (Affinity Capture-Western), EP300 (Affinity Capture-MS), FOXO1 (Biochemical Activity), EP300 (Affinity Capture-Western), RELA (Affinity Capture-Western), KLF2 (Co-localization), KLF4 (Co-localization), KLF2 (Reconstituted Complex), KLF2 (Affinity Capture-Western), SIRT1 (Affinity Capture-Western), EP300 (Affinity Capture-Western), HSPA5 (Affinity Capture-Western), EP300 (Affinity Capture-Western), EP300 (Affinity Capture-Western), EP300 (Affinity Capture-Western)

ESM2 similar proteins: A1YFU7, A2AJK6, A2BH40, B2RWS6, D3YWE6, E9Q4N7, M9NEY8, O00512, O14497, O35126, O42368, O43365, O57401, P02831, P02833, P22810, P23441, P23512, P25822, P32182, P34545, P35582, P35583, P43698, P43699, P50220, P50901, P54258, P54259, P54269, P55317, Q06A37, Q08DG7, Q08E31, Q09472, Q0VCT9, Q10571, Q1KKX7, Q24248, Q24645

Diamond homologs: A0A0R4IXF6, A0A7U2QYM2, A2AUY4, A2BIL7, A8DZJ1, B2KF05, B2RRD7, B2RWS6, B7ZS37, D4A7T3, E9Q2Z1, F1QW93, F1R5H6, F7DRV9, G5E8P1, G5EGM3, O15164, O60885, O74350, O88379, O95696, P13709, P21675, P25440, P35177, P45481, P51123, P55201, Q03330, Q07442, Q08D75, Q09472, Q12830, Q15059, Q1LUC3, Q23590, Q32S26, Q338B9, Q4R8Y1, Q54BA2

SIGNOR signaling

91 interactions.

A	Effect	B	Mechanism
EP300	“form complex”	CBP/p300	binding
DTX1	up-regulates	EP300	binding
EP300	up-regulates	KPNA2	acetylation
EP300	up-regulates	SMAD7	acetylation
EP300	up-regulates	PLAG1	acetylation
EP300	up-regulates	PLAGL2	acetylation
EP300	up-regulates	RELA	acetylation
MAML1	up-regulates	EP300	binding
AKT1	up-regulates	EP300	phosphorylation
AKT2	up-regulates	EP300	phosphorylation
EP300	up-regulates	MAML1	acetylation
MAPK1	up-regulates	EP300	phosphorylation
ATM	up-regulates	EP300	phosphorylation
EP300	up-regulates	DUSP1	acetylation
EP300	“up-regulates quantity”	RUNX2	acetylation
EP300	“down-regulates activity”	H3-3A	acetylation
EP300	“form complex”	P300/PCAF	binding
PRKAA1	down-regulates	EP300	phosphorylation
SIRT1	down-regulates	EP300	deacetylation
MAML1	up-regulates	EP300	relocalization
EP300	up-regulates	SMAD1	binding
EP300	up-regulates	FLI1	binding
EP300	up-regulates	Differentiation

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 161 IntAct physical interaction partners (hypergeometric vs the genome-wide background, BH-FDR, gene-set size 15–500, ranked by fold). A functional readout of the neighbourhood — distinct from this gene’s own memberships above, and biased toward well-studied / hub proteins, so read it as themes rather than proof.

Reactome pathways:

Pathway	Partners	Fold	FDR
Deactivation of the beta-catenin transactivating complex	7	14.1×	7e-05
Gastrulation	6	13.4×	3e-04
Interleukin-4 and Interleukin-13 signaling	13	11.5×	7e-08
Transcriptional regulation of white adipocyte differentiation	10	11.2×	5e-06
Adipogenesis	8	10.8×	7e-05
MITF-M-dependent gene expression	6	9.4×	1e-03
Epigenetic regulation of adipogenesis genes by MLL3 and MLL4 complexes	5	9.3×	4e-03
Transcriptional and post-translational regulation of MITF-M expression and activity	6	9.2×	1e-03

GO biological processes:

GO term	Partners	Fold	FDR
glial cell proliferation	5	30.2×	7e-05
neuron fate specification	6	28.7×	8e-06
response to muscle stretch	5	26.1×	1e-04
positive regulation of miRNA transcription	13	25.7×	8e-13
negative regulation of miRNA transcription	5	21.2×	3e-04
chromosome organization	5	19.8×	4e-04
positive regulation of transcription initiation by RNA polymerase II	8	14.8×	1e-05
aortic valve morphogenesis	5	14.7×	1e-03

Disease & clinical

Cancer significance

From intOGen — cancer-driver classification: loss-of-function (tumor-suppressor-like) across 19 cancer types — ANGS, BLCA, BRCA, CESC, CHOL, COADREAD, DLBCLNOS, ESCA, HCC, HNSC, LUAD, LUSC…(+7 more).

Clinical variants and AI predictions

ClinVar

2395 variants total. Per-class counts are floors (≥ shown; pagination cap):

Classification	Count (floor)
Pathogenic	163
Likely pathogenic	101
Uncertain significance	879
Likely benign	704
Benign	257

Top pathogenic / likely-pathogenic (30)

Variant ID	HGVS	Classification
1030396	NM_001429.4(EP300):c.2225del (p.Pro742fs)	Pathogenic
1068928	NM_001429.4(EP300):c.4216_4219dup (p.Lys1407delinsThrTer)	Pathogenic
1072487	NM_001429.4(EP300):c.650dup (p.Asn217fs)	Pathogenic
1173071	NM_001429.3:c.4271_4367del	Pathogenic
1194133	NM_001429.4(EP300):c.3740G>A (p.Cys1247Tyr)	Pathogenic
1254455	NM_001429.4(EP300):c.4307G>A (p.Trp1436Ter)	Pathogenic
1320123	NM_001429.4(EP300):c.3826_3827dup (p.Leu1276fs)	Pathogenic
1322823	NM_001429.4(EP300):c.2333dup (p.Asn779fs)	Pathogenic
1326926	NM_001429.4(EP300):c.1423dup (p.Tyr475fs)	Pathogenic
1333868	NM_001429.4(EP300):c.6101del (p.Gly2034fs)	Pathogenic
1335486	NM_001429.4(EP300):c.2305C>T (p.Gln769Ter)	Pathogenic
1341985	NM_001429.4(EP300):c.7081C>T (p.Gln2361Ter)	Pathogenic
1365909	NM_001429.4(EP300):c.4065C>G (p.Tyr1355Ter)	Pathogenic
1370430	NM_001429.4(EP300):c.3684del (p.Glu1229fs)	Pathogenic
1371078	NM_001429.4(EP300):c.4873del (p.Asp1625fs)	Pathogenic
1426847	NM_001429.4(EP300):c.4785del (p.Phe1596fs)	Pathogenic
1427007	NM_001429.4(EP300):c.4826_4833dup (p.Ile1612fs)	Pathogenic
1459685	NC_000022.10:g.(?41553153)(41554524_?)del	Pathogenic
1526737	GRCh37/hg19 22q13.2(chr22:41536475-41540761)	Pathogenic
1685770	NM_001429.4(EP300):c.3875-2A>C	Pathogenic
1685771	NM_001429.4(EP300):c.4783T>A (p.Phe1595Ile)	Pathogenic
1690339	NM_001429.4(EP300):c.1327_1328del (p.Leu443fs)	Pathogenic
1708228	NM_001429.4(EP300):c.6323del (p.Gln2108fs)	Pathogenic
1708232	NM_001429.4(EP300):c.108_111del (p.Phe37fs)	Pathogenic
1708323	NM_001429.4(EP300):c.6840_6841dup (p.Gln2281fs)	Pathogenic
1710191	NM_001429.4(EP300):c.2734C>T (p.Gln912Ter)	Pathogenic
1711553	NM_001429.4(EP300):c.4301A>T (p.His1434Leu)	Pathogenic
1801010	NM_001429.4(EP300):c.1876C>T (p.Arg626Ter)	Pathogenic
183678	NM_001429.4(EP300):c.4933C>T (p.Arg1645Ter)	Pathogenic
2013506	NM_001429.4(EP300):c.4595del (p.Asn1532fs)	Pathogenic

SpliceAI

3880 predictions. Top by Δscore:

Variant	Effect	Δscore
22:41117184:TA:T	acceptor_loss	1.0000
22:41117185:A:AG	acceptor_gain	1.0000
22:41117185:AGATT:A	acceptor_loss	1.0000
22:41117186:G:GA	acceptor_gain	1.0000
22:41117186:GATT:G	acceptor_gain	1.0000
22:41125848:T:A	acceptor_gain	1.0000
22:41125856:A:AG	acceptor_gain	1.0000
22:41125857:C:G	acceptor_gain	1.0000
22:41125858:TCTTA:T	acceptor_loss	1.0000
22:41125859:CTTAG:C	acceptor_loss	1.0000
22:41125860:TTA:T	acceptor_loss	1.0000
22:41125861:TA:T	acceptor_loss	1.0000
22:41125862:A:AG	acceptor_gain	1.0000
22:41125862:A:T	acceptor_loss	1.0000
22:41125862:AGAT:A	acceptor_gain	1.0000
22:41125862:AGATG:A	acceptor_gain	1.0000
22:41125863:G:GT	acceptor_gain	1.0000
22:41125863:GA:G	acceptor_gain	1.0000
22:41125863:GAT:G	acceptor_gain	1.0000
22:41125863:GATG:G	acceptor_gain	1.0000
22:41125863:GATGG:G	acceptor_gain	1.0000
22:41126036:ACATG:A	donor_gain	1.0000
22:41126037:CATG:C	donor_gain	1.0000
22:41126038:ATG:A	donor_gain	1.0000
22:41126039:TG:T	donor_gain	1.0000
22:41126040:GG:G	donor_gain	1.0000
22:41126041:G:GG	donor_gain	1.0000
22:41126041:GTGA:G	donor_loss	1.0000
22:41126042:T:A	donor_loss	1.0000
22:41127482:CTCA:C	acceptor_loss	1.0000

AlphaMissense

15996 scored. Top likely-pathogenic:

Variant	Protein change	am_pathogenicity
22:41127590:T:C	L337P	1.000
22:41127593:T:A	I338N	1.000
22:41127593:T:C	I338T	1.000
22:41127593:T:G	I338S	1.000
22:41127599:A:C	Q340P	1.000
22:41127602:A:C	Q341P	1.000
22:41127603:G:C	Q341H	1.000
22:41127603:G:T	Q341H	1.000
22:41127605:T:A	L342H	1.000
22:41127605:T:C	L342P	1.000
22:41127608:T:A	V343D	1.000
22:41127611:T:A	L344H	1.000
22:41127611:T:C	L344P	1.000
22:41127611:T:G	L344R	1.000
22:41127614:T:A	L345H	1.000
22:41127614:T:C	L345P	1.000
22:41127614:T:G	L345R	1.000
22:41127617:T:C	L346S	1.000
22:41127617:T:G	L346W	1.000
22:41127619:C:A	H347N	1.000
22:41127619:C:G	H347D	1.000
22:41127619:C:T	H347Y	1.000
22:41127620:A:C	H347P	1.000
22:41127620:A:G	H347R	1.000
22:41127620:A:T	H347L	1.000
22:41127621:T:A	H347Q	1.000
22:41127621:T:G	H347Q	1.000
22:41127622:G:C	A348P	1.000
22:41127623:C:A	A348D	1.000
22:41127625:C:G	H349D	1.000

dbSNP variants (sampled 300 via entrez): RS1000009289 (22:41110084 C>T), RS1000019300 (22:41171313 T>G), RS1000025925 (22:41100055 C>A,G), RS1000043588 (22:41116331 A>G), RS1000044098 (22:41134686 C>T), RS1000108822 (22:41121857 G>A,C), RS1000225824 (22:41179419 G>A,T), RS1000249771 (22:41143421 A>C), RS1000255248 (22:41093190 C>G,T), RS1000292624 (22:41121558 G>A,C), RS1000300693 (22:41152743 T>C), RS1000303367 (22:41168132 A>G), RS1000304391 (22:41137889 T>G), RS1000349291 (22:41132665 A>G), RS1000352352 (22:41148075 C>G,T)

Disease associations

OMIM: gene MIM:602700 | disease phenotypes: MIM:613684, MIM:618333, MIM:114500, MIM:180849, MIM:164400, MIM:188100, MIM:160700, MIM:217990, MIM:174200

GenCC curated gene-disease

Disease	Classification	Inheritance
Rubinstein-Taybi syndrome due to EP300 haploinsufficiency	Definitive	Autosomal dominant
Rubinstein-Taybi syndrome	Definitive	Autosomal dominant
retinitis pigmentosa	Limited	Autosomal dominant

ClinGen Gene-Disease Validity (1)

Expert-panel classifications — Definitive > Strong > Moderate > Limited > Disputed > Refuted.

Disease	Classification	Inheritance
Rubinstein-Taybi syndrome due to EP300 haploinsufficiency	Definitive	AD

Mondo (20): Rubinstein-Taybi syndrome due to EP300 haploinsufficiency (MONDO:0013364), Menke-Hennekam syndrome 2 (MONDO:0020769), colorectal cancer (MONDO:0005575), Rubinstein-Taybi syndrome due to CREBBP mutations (MONDO:0008393), neurodevelopmental disorder (MONDO:0700092), autosomal dominant cerebellar ataxia (MONDO:0020380), intellectual disability (MONDO:0001071), hepatoblastoma (MONDO:0018666), colorectal carcinoma (MONDO:0024331), Rubinstein-Taybi syndrome (MONDO:0019188), thumb deformity (MONDO:0008561), myopia (MONDO:0001384), microcephaly (MONDO:0001149), CHARGE syndrome (MONDO:0008965), corpus callosum, agenesis of (MONDO:0009022)

Orphanet (12): Rubinstein-Taybi syndrome due to EP300 haploinsufficiency (Orphanet:353284), Rubinstein-Taybi syndrome (Orphanet:783), Rubinstein-Taybi syndrome due to CREBBP mutations (Orphanet:353277), Autosomal dominant cerebellar ataxia (Orphanet:99), Hepatoblastoma (Orphanet:449), CHARGE syndrome (Orphanet:138), Isolated corpus callosum agenesis (Orphanet:200), Multicystic dysplastic kidney (Orphanet:1851), Rare genetic intellectual disability (Orphanet:183757), Hereditary breast and/or ovarian cancer syndrome (Orphanet:145), NON RARE IN EUROPE: Colorectal cancer (Orphanet:466667), NON RARE IN EUROPE: Unexplained intellectual disability (Orphanet:319658)

HPO phenotypes

247 total (30 of 247 shown, HPO-id order):

HPO	Term
HP:0000006	Autosomal dominant inheritance
HP:0000010	Recurrent urinary tract infections
HP:0000028	Cryptorchidism
HP:0000034	Hydrocele testis
HP:0000047	Hypospadias
HP:0000049	Shawl scrotum
HP:0000076	Vesicoureteral reflux
HP:0000077	Abnormality of the kidney
HP:0000079	Abnormality of the urinary system
HP:0000119	Abnormality of the genitourinary system
HP:0000126	Hydronephrosis
HP:0000160	Narrow mouth
HP:0000175	Cleft palate
HP:0000189	Narrow palate
HP:0000218	High palate
HP:0000219	Thin upper lip vermilion
HP:0000252	Microcephaly
HP:0000260	Wide anterior fontanel
HP:0000270	Delayed cranial suture closure
HP:0000273	Facial grimacing
HP:0000278	Retrognathia
HP:0000286	Epicanthus
HP:0000293	Full cheeks
HP:0000294	Low anterior hairline
HP:0000316	Hypertelorism
HP:0000319	Smooth philtrum
HP:0000321	Square face
HP:0000327	Hypoplasia of the maxilla
HP:0000347	Micrognathia
HP:0000358	Posteriorly rotated ears

GWAS associations

10 associations (top):

Study	Trait	p-value
GCST001652_3	Crohn’s disease	3.000000e-08
GCST002539_94	Schizophrenia	2.000000e-11
GCST004521_55	Autism spectrum disorder or schizophrenia	9.000000e-09
GCST004946_20	Schizophrenia	1.000000e-12
GCST005232_52	Neuroticism	3.000000e-18
GCST006803_24	Schizophrenia	6.000000e-13
GCST007325_263	General risk tolerance (MTAG)	6.000000e-14
GCST009379_305	Type 2 diabetes	4.000000e-08
GCST010002_83	Refractive error	2.000000e-27
GCST90002404_413	Red cell distribution width	2.000000e-16

EFO canonical traits (3, from GWAS)

EFO ID	Trait name
EFO:0007660	neuroticism measurement
EFO:0008579	risk-taking behaviour
EFO:0009188	Red cell distribution width

MeSH disease descriptors (12)

Descriptor	Name	Tree numbers
D061085	Agenesis of Corpus Callosum	C10.500.034; C16.131.666.034; C23.300.008
D058747	CHARGE Syndrome	C09.218.458.341.186.500.250; C10.597.751.418.341.186.500.250; C10.597.751.941.162.625.250; C11.270.147.500; C11.966.075.375.250; C16.131.077.299.250; C16.320.165; C23.888.592.763.393.341.186.500.500; C23.888.592.763.941.162.625.500
D018197	Hepatoblastoma	C04.557.435.380
D061325	Hereditary Breast and Ovarian Cancer Syndrome	C04.588.180.483; C04.588.322.455.431; C04.700.517; C12.050.351.500.056.630.705.431; C12.050.351.937.418.685.431; C12.100.250.056.630.705.431; C12.900.418.685.431; C16.320.700.517; C17.800.090.500.483; C19.344.410.431; C19.391.630.705.431
D008607	Intellectual Disability	C10.597.606.360; C23.888.592.604.646; F01.700.687; F03.625.539
D008831	Microcephaly	C05.660.207.620; C10.500.507.400.500; C16.131.621.207.620; C16.131.666.507.400.500
D021782	Multicystic Dysplastic Kidney	C12.050.351.875.558; C12.050.351.968.419.403.750; C12.200.706.629; C12.200.777.419.403.750; C12.800.629; C12.950.419.403.750; C16.131.939.629
D009216	Myopia	C11.744.636
D065886	Neurodevelopmental Disorders	F03.625
D012174	Retinitis Pigmentosa	C11.270.684; C11.768.585.658.500; C16.320.290.684
D012415	Rubinstein-Taybi Syndrome	C05.116.099.370.797; C05.660.207.850; C10.597.606.360.700; C16.131.077.804; C16.131.260.790; C16.131.621.207.850; C16.320.180.790
C536903	Thumb deformity (supp.)

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (9): CHEMBL3784 (SINGLE PROTEIN), CHEMBL3883300 (PROTEIN FAMILY), CHEMBL3885588 (PROTEIN COMPLEX), CHEMBL4296108 (PROTEIN-PROTEIN INTERACTION), CHEMBL5465214 (PROTEIN-PROTEIN INTERACTION), CHEMBL5483091 (PROTEIN-PROTEIN INTERACTION), CHEMBL6066549 (PROTEIN COMPLEX), CHEMBL6066577 (PROTEIN COMPLEX), CHEMBL6066834 (PROTEIN-PROTEIN INTERACTION)

Molecules with ChEMBL bioactivity

9 molecules (phase ≥1), by development phase (incl. off-target/promiscuous compounds). Patent mentions across the top 20 by phase: 180,672 (via chembl_molecule»patent_compound — counts attach to the compound, not the gene–compound relationship, so off-target/promiscuous molecules can dominate).

Molecule	Name	Phase	Patents
CHEMBL1213327	COENZYME_A	3	10,084
CHEMBL140	CURCUMIN	3	93,882
CHEMBL297453	EPIGALOCATECHIN GALLATE	3	22,804
CHEMBL1232461	MOLIBRESIB	2	1,538
CHEMBL3987016	MIVEBRESIB	2	773
CHEMBL11417	STREPTONIGRIN	2	43,337
CHEMBL12089	BERBERINE CHLORIDE	1	1,860
CHEMBL295316	PLUMBAGIN	1	6,294
CHEMBL4785363	INOBRODIB	1	100

PharmGKB: 1 entry (VIP=true, CPIC=false)

GtoPdb / IUPHAR curated pharmacology

(IUPHAR/BPS Guide to Pharmacology — expert-curated)

Target class: other protein — Non-enzymatic BRD containing proteins

Most potent curated ligand interactions (12 total), top 12:

Ligand	Action	Affinity	Parameter
CBPD-268	Binding	8.02	pIC50
inobrodib	Inhibition	7.72	pIC50
SGC-CBP30	Inhibition	7.42	pIC50
C646	Inhibition	6.4	pKi
Lys-CoA	Inhibition	6.3	pIC50
I-CBP112	Inhibition	6.2	pKd
anacardic acid	Inhibition	5.3	pIC50
garcinol	Inhibition	5.15	pIC50
curcumin	Inhibition	4.6	pIC50
plumbagin	Inhibition	4.6	pIC50
epigallocatechin-3-gallate	Inhibition	4.52	pIC50
H3-CoA-20	Inhibition	3.7	pIC50

Binding affinities (BindingDB)

294 measured of 391 human assays (399 total across all organisms); most potent 50 below. Values come from heterogeneous assays and are not directly comparable.

Ligand	Measure	Value	Patent
2-[(1R,3S)-1-fluoro-2’,5’-dioxo-6-(1-propan-2-ylpyrazol-4-yl)spiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(5-fluoro-2-pyridinyl)methyl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]acetamide	IC50	0.2 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-6-(1-cyclobutylpyrazol-4-yl)-1-fluoro-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(5-fluoro-2-pyridinyl)methyl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]acetamide	IC50	0.2 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-1-fluoro-6-(1-methylpyrazol-4-yl)-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(4-fluorophenyl)methyl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]acetamide	IC50	0.4 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-6-(1-ethylpyrazol-4-yl)-1-fluoro-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(5-fluoro-2-pyridinyl)methyl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]acetamide	IC50	0.4 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
N-[3,3-difluoro-1-(trifluoromethyl)cyclobutyl]-2-[(1R,3S)-1-fluoro-6-[1-[1-(oxetan-3-yl)azetidin-3-yl]pyrazol-4-yl]-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(4-fluorophenyl)methyl]acetamide	IC50	0.5 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-1-fluoro-6-[1-[1-(oxetan-3-yl)azetidin-3-yl]pyrazol-4-yl]-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(4-fluorophenyl)methyl]-N-[3-(trifluoromethyl)oxetan-3-yl]acetamide	IC50	0.6 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
N-[3,3-difluoro-1-(trifluoromethyl)cyclobutyl]-2-[(1R,3S)-1-fluoro-6-[1-[1-(oxetan-3-yl)azetidin-3-yl]pyrazol-4-yl]-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(5-fluoro-2-pyridinyl)methyl]acetamide	IC50	0.6 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-1-fluoro-6-[1-[1-(oxetan-3-yl)azetidin-3-yl]pyrazol-4-yl]-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(5-fluoro-2-pyridinyl)methyl]-N-[3-(trifluoromethyl)oxetan-3-yl]acetamide	IC50	0.9 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-1-fluoro-2’,5’-dioxo-6-(1-propan-2-ylpyrazol-4-yl)spiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(4-fluorophenyl)methyl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]acetamide	IC50	1 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-6-[1-(2-cyanopropan-2-yl)pyrazol-4-yl]-1-fluoro-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(4-fluorophenyl)methyl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]acetamide	IC50	2 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-1-fluoro-6-(3-fluoro-1-methylpyrazol-4-yl)-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(4-fluorophenyl)methyl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]acetamide	IC50	2 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-1-fluoro-6-(1-methylpyrazol-4-yl)-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(5-fluoro-2-pyridinyl)methyl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]acetamide	IC50	2 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-6-(1-ethylpyrazol-4-yl)-1-fluoro-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(4-fluorophenyl)methyl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]acetamide	IC50	2 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-1,5-difluoro-6-(1-methylpyrazol-4-yl)-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(4-fluorophenyl)methyl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]acetamide	IC50	3 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(3S)-6-[1-(2-cyanopropan-2-yl)pyrazol-4-yl]-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(4-fluorophenyl)methyl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]acetamide	IC50	5 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-1-fluoro-6-(1-methylpyrazol-4-yl)-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]-N-[[4-(trifluoromethyl)phenyl]methyl]acetamide	IC50	5 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
N-[3,3-difluoro-1-(trifluoromethyl)cyclobutyl]-N-[(4-fluorophenyl)methyl]-2-[(3S)-6-[1-[1-(oxetan-3-yl)azetidin-3-yl]pyrazol-4-yl]-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]acetamide	IC50	6 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
N-[(4-fluorophenyl)methyl]-2-[(3S)-6-(1-methylpyrazol-4-yl)-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]acetamide	IC50	6 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-1-fluoro-6-(5-fluoro-1-methylpyrazol-4-yl)-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(4-fluorophenyl)methyl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]acetamide	IC50	6 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-1-fluoro-6-[1-(oxetan-3-ylmethyl)pyrazol-4-yl]-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(5-fluoro-2-pyridinyl)methyl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]acetamide	IC50	6 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-1-fluoro-6-[1-(oxan-4-yl)pyrazol-4-yl]-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(4-fluorophenyl)methyl]-N-[3-(trifluoromethyl)oxetan-3-yl]acetamide	IC50	7 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-1-fluoro-6-[1-(1-hydroxy-2-methylpropan-2-yl)pyrazol-4-yl]-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(5-fluoro-2-pyridinyl)methyl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]acetamide	IC50	7 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
3-[(2R)-2-[[(2R)-2-(4-cyanophenyl)propyl]amino]-2-phenylacetyl]-N-ethyl-1H-indole-6-carboxamide	IC50	8.76 nM	US-11414384: P300/CBP hat inhibitors
2-[(1R,3S)-1-fluoro-6-[1-[1-(oxetan-3-yl)piperidin-4-yl]pyrazol-4-yl]-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(5-fluoro-2-pyridinyl)methyl]-N-[3-(trifluoromethyl)oxetan-3-yl]acetamide	IC50	9 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-6-[1-(2-cyanopropan-2-yl)pyrazol-4-yl]-1-fluoro-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(5-fluoro-2-pyridinyl)methyl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]acetamide	IC50	9 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
(2R)-2-[[(2S)-2-(4-cyanophenyl)propyl]amino]-2-phenyl-N-[5-(1H-pyrazol-4-yl)-2-pyridinyl]acetamide	IC50	9.1 nM	US-11274090
2-[(1R,3S)-1-fluoro-6-[1-(oxetan-3-yl)pyrazol-4-yl]-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(5-fluoro-2-pyridinyl)methyl]-N-[1-methyl-3-(trifluoromethyl)azetidin-3-yl]acetamide	IC50	10 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
2-[(1R,3S)-6-[1-[[3-(dimethylamino)oxetan-3-yl]methyl]pyrazol-4-yl]-1-fluoro-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(4-fluorophenyl)methyl]-N-[3-(trifluoromethyl)oxetan-3-yl]acetamide	IC50	11 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
(2R)-2-[[(2S)-2-(4-cyanophenyl)propyl]amino]-N-[5-(3,5-dimethyl-1H-pyrazol-4-yl)-2-pyridinyl]-2-phenylacetamide	IC50	14.4 nM	US-11274090
4-[2-[[(1R)-2-oxo-1-phenyl-2-(6-pyrazolidin-4-ylpyrazolo[1,5-a]pyridin-3-yl)ethyl]amino]ethyl]benzonitrile	IC50	15.6 nM	US-11414384: P300/CBP hat inhibitors
N-[(4-fluorophenyl)methyl]-2-[(1’S)-5’-{1-[1-(oxetan-3-yl)azetidin-3-yl]-1H-pyrazol-4-yl}-2,5-dioxo-2’,3’-dihydrospiro[imidazolidine-4,1’-inden]-1-yl]-N-[3-(trifluoromethyl) oxetan-3-yl]acetamide	IC50	16 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
3-[(2R)-2-[2-(4-cyanophenyl)ethylamino]-2-phenylacetyl]-N-methyl-1H-indole-6-carboxamide	IC50	17 nM	US-11414384: P300/CBP hat inhibitors
N-[3,3-difluoro-1-(trifluoromethyl)cyclobutyl]-N-[(5-fluoro-2-pyridinyl)methyl]-2-[(3S)-6-[1-[1-(oxetan-3-yl)azetidin-3-yl]pyrazol-4-yl]-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]acetamide	IC50	17 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
3-[(2R)-2-[2-(2-chloro-4-cyanophenyl)ethylamino]-2-phenylacetyl]-N-ethyl-1H-indole-6-carboxamide	IC50	17.7 nM	US-11414384: P300/CBP hat inhibitors
4-[2-[[(1S)-2-[6-(1-methyltriazol-4-yl)-1H-indol-3-yl]-2-oxo-1-phenylethyl]amino]ethyl]benzonitrile	IC50	19 nM	US-11414384: P300/CBP hat inhibitors
2-[(3S)-6-[1-[(3-fluoro-1-methylazetidin-3-yl)methyl]pyrazol-4-yl]-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[(4-fluorophenyl)methyl]-N-[3-(trifluoromethyl)oxetan-3-yl]acetamide	IC50	19 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
N-[(5-fluoro-2-pyridinyl)methyl]-2-[(3S)-6-[1-[1-(oxetan-3-yl)azetidin-3-yl]pyrazol-4-yl]-2’,5’-dioxospiro[1,2-dihydroindene-3,4’-imidazolidine]-1’-yl]-N-[3-(trifluoromethyl)oxetan-3-yl]acetamide	IC50	20 nM	US-20250257055: TERTIARY AMIDE DERIVATIVES SUBSTITUTED WITH 4-MEMBERED RING STRUCTURE
3-[(2R)-2-[2-(4-cyanophenyl)ethylamino]-2-phenylacetyl]-N-[(2R)-2-hydroxypropyl]-1H-indole-6-carboxamide	IC50	21.1 nM	US-11414384: P300/CBP hat inhibitors
3-[(2S)-2-[2-(4-cyanophenyl)ethylamino]-2-phenylacetyl]-N-propan-2-yl-1H-indole-6-carboxamide	IC50	23.2 nM	US-11414384: P300/CBP hat inhibitors
(2S)-2-[2-(4-cyanophenyl)ethylamino]-2-phenyl-N-(5-pyrazolidin-4-yl-2-pyridinyl)acetamide	IC50	26 nM	US-11274090
3-[(2R)-2-[2-(4-cyanophenyl)ethylamino]-2-phenylacetyl]-N-ethyl-1H-indole-6-carboxamide	IC50	26 nM	US-11414384: P300/CBP hat inhibitors
4-[2-[[(1S)-2-[6-(1-methylimidazol-4-yl)-1H-indol-3-yl]-2-oxo-1-phenylethyl]amino]ethyl]benzonitrile	IC50	28 nM	US-11414384: P300/CBP hat inhibitors
3-[(2R)-2-[2-(4-cyanophenyl)ethylamino]-2-phenylacetyl]-N-(1,1-dioxothietan-3-yl)-1H-indole-6-carboxamide	IC50	28.8 nM	US-11414384: P300/CBP hat inhibitors
4-[2-[[(1R)-2-[6-(1-methylpiperidin-4-yl)oxy-1H-indol-3-yl]-2-oxo-1-phenylethyl]amino]ethyl]benzonitrile	IC50	36.2 nM	US-11414384: P300/CBP hat inhibitors
3-[(2R)-2-[2-(4-cyanophenyl)ethylamino]-2-phenylacetyl]-N-(oxetan-3-yl)-1H-indole-6-carboxamide	IC50	39 nM	US-11414384: P300/CBP hat inhibitors
4-[2-[[(1R)-2-[6-(1-methylpyrazol-4-yl)-1H-indol-3-yl]-2-oxo-1-phenylethyl]amino]ethyl]benzonitrile	IC50	41 nM	US-11414384: P300/CBP hat inhibitors
3-[(2R)-2-[2-(4-cyanophenyl)ethylamino]-2-phenylacetyl]-N-(1-ethylazetidin-3-yl)-1H-indole-6-carboxamide	IC50	41.9 nM	US-11414384: P300/CBP hat inhibitors
3-chloro-4-[2-[[(1R)-2-[6-(1-methylpyrazol-4-yl)-1H-indol-3-yl]-2-oxo-1-phenylethyl]amino]ethyl]benzonitrile	IC50	42.4 nM	US-11414384: P300/CBP hat inhibitors
3-[(2R)-2-[2-(4-cyanophenyl)ethylamino]-2-phenylacetyl]-N-(3-methylsulfonylpropyl)-1H-indole-6-carboxamide	IC50	44 nM	US-11414384: P300/CBP hat inhibitors
4-[2-[[2-[6-[1-(2-hydroxyethyl)pyrazol-4-yl]-1H-indol-3-yl]-2-oxo-1-phenylethyl]amino]ethyl]benzonitrile	IC50	46 nM	US-11414384: P300/CBP hat inhibitors

ChEMBL bioactivities

1299 potent at pChembl≥5 of 1449 total, top 50 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChembl	Type	Value	Unit	Molecule
10.10	IC50	0.07943	nM	CHEMBL5220994
10.00	IC50	0.1	nM	CHEMBL5221053
9.92	Kd	0.12	nM	CHEMBL4208820
9.90	IC50	0.1259	nM	CHEMBL5219157
9.80	IC50	0.1585	nM	CHEMBL5219693
9.80	IC50	0.1585	nM	CHEMBL5219030
9.70	IC50	0.1995	nM	CHEMBL5219667
9.70	EC50	0.2	nM	CHEMBL5413450
9.60	IC50	0.2512	nM	CHEMBL5220447
9.60	IC50	0.2512	nM	CHEMBL5220732
9.52	EC50	0.3	nM	CHEMBL5438596
9.50	IC50	0.3162	nM	CHEMBL5220956
9.40	IC50	0.3981	nM	CHEMBL5219678
9.31	IC50	0.49	nM	CHEMBL5090239
9.30	IC50	0.5	nM	CHEMBL5090239
9.29	IC50	0.51	nM	CHEMBL5090239
9.25	IC50	0.56	nM	CHEMBL5082755
9.22	EC50	0.6	nM	CHEMBL5439670
9.20	IC50	0.631	nM	CHEMBL5219512
9.20	IC50	0.631	nM	CHEMBL5220956
9.15	EC50	0.7	nM	CHEMBL5412027
9.10	IC50	0.7943	nM	CHEMBL5221030
9.10	IC50	0.7943	nM	CHEMBL5220546
9.10	EC50	0.8	nM	CHEMBL5405240
9.02	IC50	0.95	nM	CHEMBL4475351
9.00	IC50	1	nM	CHEMBL5220332
9.00	IC50	1	nM	CHEMBL5219177
8.96	IC50	1.1	nM	CHEMBL4475351
8.96	EC50	1.1	nM	CHEMBL5402691
8.92	IC50	1.2	nM	CHEMBL4097025
8.92	Kd	1.2	nM	CHEMBL4097025
8.89	IC50	1.3	nM	CHEMBL4076748
8.89	IC50	1.3	nM	CHEMBL4567310
8.89	Kd	1.3	nM	CHEMBL5409153
8.89	Kd	1.3	nM	INOBRODIB
8.89	Kd	1.3	nM	CHEMBL4076748
8.80	EC50	1.6	nM	CHEMBL5406029
8.80	EC50	1.6	nM	CHEMBL5405858
8.77	IC50	1.7	nM	CHEMBL5083020
8.77	Kd	1.7	nM	INOBRODIB
8.74	IC50	1.8	nM	CHEMBL4587968
8.72	IC50	1.9	nM	CHEMBL4457144
8.72	EC50	1.9	nM	CHEMBL5397398
8.70	IC50	1.995	nM	CHEMBL5219466
8.68	IC50	2.1	nM	CHEMBL5620293
8.66	IC50	2.2	nM	CHEMBL5077158
8.64	EC50	2.3	nM	CHEMBL5434991
8.62	IC50	2.4	nM	CHEMBL4464962
8.62	IC50	2.4	nM	CHEMBL4450724
8.60	IC50	2.5	nM	CHEMBL4633516

PubChem BioAssay actives

785 with measured affinity, of 2573 total; 50 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

Compound	Assay	Type	Value	Unit
5-[8-[5-acetyl-1-(oxan-4-yl)-6,7-dihydro-4H-pyrazolo[4,3-c]pyridin-3-yl]isoquinolin-3-yl]-N-methylpyridine-2-carboxamide	1372263: Binding affinity to human partial length EP300 (A1040 to G1161 residues) expressed in bacterial expression system by BROMOscan assay	kd	0.0001	uM
(2R,4R)-1-[1-(4-chlorophenyl)-3,3-difluorocyclobutanecarbonyl]-4-fluoro-N-(1H-pyrazolo[4,5-b]pyridin-5-yl)pyrrolidine-2-carboxamide	1918472: Inhibition of full-length P300 (unknown origin) using ARTKQTARKSTGGKAPRKQLAGG-K(Biotin)-amide as substrate preincubated for 60 mins followed by substrate addition and measured by RapdiFire-MS/MS analysis	ic50	0.0001	uM
(2R)-1-[1-(4-fluorophenyl)cyclobutanecarbonyl]-N-(1H-pyrazolo[4,5-b]pyridin-5-yl)pyrrolidine-2-carboxamide	1918472: Inhibition of full-length P300 (unknown origin) using ARTKQTARKSTGGKAPRKQLAGG-K(Biotin)-amide as substrate preincubated for 60 mins followed by substrate addition and measured by RapdiFire-MS/MS analysis	ic50	0.0001	uM
(2R)-1-[1-(4-chlorophenyl)cyclobutanecarbonyl]-N-(1H-pyrazolo[4,5-b]pyridin-5-yl)pyrrolidine-2-carboxamide	1918472: Inhibition of full-length P300 (unknown origin) using ARTKQTARKSTGGKAPRKQLAGG-K(Biotin)-amide as substrate preincubated for 60 mins followed by substrate addition and measured by RapdiFire-MS/MS analysis	ic50	0.0001	uM
(2R)-1-[1-(3-chlorophenyl)cyclopentanecarbonyl]-N-(1H-pyrrolo[3,2-b]pyridin-5-yl)pyrrolidine-2-carboxamide	1918472: Inhibition of full-length P300 (unknown origin) using ARTKQTARKSTGGKAPRKQLAGG-K(Biotin)-amide as substrate preincubated for 60 mins followed by substrate addition and measured by RapdiFire-MS/MS analysis	ic50	0.0002	uM
(2R,4R)-1-[1-(4-chlorophenyl)cyclobutanecarbonyl]-4-fluoro-N-(1H-pyrazolo[4,5-b]pyridin-5-yl)pyrrolidine-2-carboxamide	1918472: Inhibition of full-length P300 (unknown origin) using ARTKQTARKSTGGKAPRKQLAGG-K(Biotin)-amide as substrate preincubated for 60 mins followed by substrate addition and measured by RapdiFire-MS/MS analysis	ic50	0.0002	uM
(2R)-1-[1-(3-chlorophenyl)cyclopentanecarbonyl]-N-(1H-pyrazolo[4,5-b]pyridin-5-yl)pyrrolidine-2-carboxamide	1918472: Inhibition of full-length P300 (unknown origin) using ARTKQTARKSTGGKAPRKQLAGG-K(Biotin)-amide as substrate preincubated for 60 mins followed by substrate addition and measured by RapdiFire-MS/MS analysis	ic50	0.0002	uM
5-[8-[5-acetyl-1-(oxan-4-yl)-6,7-dihydro-4H-pyrazolo[4,3-c]pyridin-3-yl]isoquinolin-3-yl]-N-[1-[2-(2,6-dioxopiperidin-3-yl)-1-oxo-3H-isoindol-5-yl]piperidin-4-yl]pyridine-2-carboxamide	1990961: Induction of p300 degradation in human RS4-11 cells incubated for 4 hrs by Western blot assay	ec50	0.0002	uM
(2R)-1-[1-(4-cyanophenyl)cyclobutanecarbonyl]-N-(1H-pyrazolo[4,5-b]pyridin-5-yl)pyrrolidine-2-carboxamide	1918472: Inhibition of full-length P300 (unknown origin) using ARTKQTARKSTGGKAPRKQLAGG-K(Biotin)-amide as substrate preincubated for 60 mins followed by substrate addition and measured by RapdiFire-MS/MS analysis	ic50	0.0003	uM
(2R)-1-[1-(4-chlorophenyl)-3,3-difluorocyclobutanecarbonyl]-N-(1H-pyrazolo[4,5-b]pyridin-5-yl)pyrrolidine-2-carboxamide	1918472: Inhibition of full-length P300 (unknown origin) using ARTKQTARKSTGGKAPRKQLAGG-K(Biotin)-amide as substrate preincubated for 60 mins followed by substrate addition and measured by RapdiFire-MS/MS analysis	ic50	0.0003	uM
(2R)-1-[1-(4-methoxyphenyl)cyclobutanecarbonyl]-N-(1H-pyrazolo[4,5-b]pyridin-5-yl)pyrrolidine-2-carboxamide	1918472: Inhibition of full-length P300 (unknown origin) using ARTKQTARKSTGGKAPRKQLAGG-K(Biotin)-amide as substrate preincubated for 60 mins followed by substrate addition and measured by RapdiFire-MS/MS analysis	ic50	0.0003	uM
5-[8-[5-acetyl-1-(oxan-4-yl)-6,7-dihydro-4H-pyrazolo[4,3-c]pyridin-3-yl]isoquinolin-3-yl]-N-[5-[[2-(2,6-dioxopiperidin-3-yl)-1,3-dioxoisoindol-4-yl]amino]pentyl]pyridine-2-carboxamide	1990961: Induction of p300 degradation in human RS4-11 cells incubated for 4 hrs by Western blot assay	ec50	0.0003	uM
(2R)-1-[1-(3-chlorophenyl)cyclopentanecarbonyl]-N-(2-oxo-1,3-dihydrobenzimidazol-5-yl)pyrrolidine-2-carboxamide	1918472: Inhibition of full-length P300 (unknown origin) using ARTKQTARKSTGGKAPRKQLAGG-K(Biotin)-amide as substrate preincubated for 60 mins followed by substrate addition and measured by RapdiFire-MS/MS analysis	ic50	0.0004	uM
(2R)-2-[[(2S)-2-(4-cyanophenyl)propyl]amino]-N-[5-(1-methylpyrazol-4-yl)-2-pyridinyl]-2-phenylacetamide	1658723: Binding affinity to recombinant full length EP300 (unknown origin) incubated for 30 mins followed by H3(1 to 21) addition and measured after 1 hr by scintillation proximity assay	ic50	0.0005	uM
(2R)-2-[2-(4-cyanophenyl)ethylamino]-N-[5-(1-methylpyrazol-4-yl)-2-pyridinyl]-2-phenylacetamide	1658723: Binding affinity to recombinant full length EP300 (unknown origin) incubated for 30 mins followed by H3(1 to 21) addition and measured after 1 hr by scintillation proximity assay	ic50	0.0005	uM
1-[(5R)-3-[2-[(3R)-3-cyclopropyl-7-fluoro-3,5-dihydro-2H-1,4-benzoxazepin-4-yl]-2-oxoethyl]-2,4-dioxospiro[1,3-oxazolidine-5,1’-2,3-dihydroindene]-5’-yl]-3-methylurea	1811548: Inhibition of p300 (unknown origin) preincubated for 15 mins followed by addition of substrate [3H] Ac-CoA and measured after 60 mins by liquid scintillation counting assay	ic50	0.0005	uM
1-[(5R)-3-[2-[(3S)-3-cyclopropyl-7,8-difluoro-1,3,4,5-tetrahydro-2-benzazepin-2-yl]-2-oxoethyl]-2,4-dioxospiro[1,3-oxazolidine-5,1’-2,3-dihydroindene]-5’-yl]-3-methylurea	1811548: Inhibition of p300 (unknown origin) preincubated for 15 mins followed by addition of substrate [3H] Ac-CoA and measured after 60 mins by liquid scintillation counting assay	ic50	0.0006	uM
(2R)-1-[1-(3-chlorophenyl)cyclopentanecarbonyl]-N-(4-hydroxyphenyl)pyrrolidine-2-carboxamide	1918472: Inhibition of full-length P300 (unknown origin) using ARTKQTARKSTGGKAPRKQLAGG-K(Biotin)-amide as substrate preincubated for 60 mins followed by substrate addition and measured by RapdiFire-MS/MS analysis	ic50	0.0006	uM
5-[8-[5-acetyl-1-(oxan-4-yl)-6,7-dihydro-4H-pyrazolo[4,3-c]pyridin-3-yl]isoquinolin-3-yl]-N-[6-[[2-(2,6-dioxopiperidin-3-yl)-1,3-dioxoisoindol-4-yl]amino]hexyl]pyridine-2-carboxamide	1990961: Induction of p300 degradation in human RS4-11 cells incubated for 4 hrs by Western blot assay	ec50	0.0006	uM
5-[8-[5-acetyl-1-(oxan-4-yl)-6,7-dihydro-4H-pyrazolo[4,3-c]pyridin-3-yl]isoquinolin-3-yl]-N-[3-[[2-(2,6-dioxopiperidin-3-yl)-1,3-dioxoisoindol-4-yl]amino]propyl]pyridine-2-carboxamide	1990961: Induction of p300 degradation in human RS4-11 cells incubated for 4 hrs by Western blot assay	ec50	0.0007	uM
(2R)-1-[1-(3-chlorophenyl)cyclopentanecarbonyl]-N-[4-(methylcarbamoyl)phenyl]pyrrolidine-2-carboxamide	1918472: Inhibition of full-length P300 (unknown origin) using ARTKQTARKSTGGKAPRKQLAGG-K(Biotin)-amide as substrate preincubated for 60 mins followed by substrate addition and measured by RapdiFire-MS/MS analysis	ic50	0.0008	uM
(2R)-1-[1-(3-chlorophenyl)cyclopentanecarbonyl]-N-(2-oxo-1,3-dihydroindol-5-yl)pyrrolidine-2-carboxamide	1918472: Inhibition of full-length P300 (unknown origin) using ARTKQTARKSTGGKAPRKQLAGG-K(Biotin)-amide as substrate preincubated for 60 mins followed by substrate addition and measured by RapdiFire-MS/MS analysis	ic50	0.0008	uM
5-[8-[5-acetyl-1-(oxan-4-yl)-6,7-dihydro-4H-pyrazolo[4,3-c]pyridin-3-yl]isoquinolin-3-yl]-N-[4-[[2-(2,6-dioxopiperidin-3-yl)-1,3-dioxoisoindol-4-yl]amino]butyl]pyridine-2-carboxamide	1990961: Induction of p300 degradation in human RS4-11 cells incubated for 4 hrs by Western blot assay	ec50	0.0008	uM
1-[(5R)-3-[2-[(3S)-3-cyclopropyl-7-fluoro-1,3,4,5-tetrahydro-2-benzazepin-2-yl]-2-oxoethyl]-2,4-dioxospiro[1,3-oxazolidine-5,1’-2,3-dihydroindene]-5’-yl]-3-methylurea	1811548: Inhibition of p300 (unknown origin) preincubated for 15 mins followed by addition of substrate [3H] Ac-CoA and measured after 60 mins by liquid scintillation counting assay	ic50	0.0009	uM
(3R)-4-[1-(4-chlorophenyl)-3,3-difluorocyclobutanecarbonyl]-N-(1H-pyrazolo[4,5-b]pyridin-5-yl)morpholine-3-carboxamide	1918473: Inhibition of full-length P300 (1 to 2414 residues) (unknown origin) using ARTKQTARKSTGGKAPRKQLAGG-K(Biotin)-amide as substrate preincubated for 60 mins followed by substrate addition and measured by scintillation proximity assay	ic50	0.0010	uM
(2R)-1-[1-(3-chlorophenyl)cyclopentanecarbonyl]-N-(1H-indazol-5-yl)pyrrolidine-2-carboxamide	1918472: Inhibition of full-length P300 (unknown origin) using ARTKQTARKSTGGKAPRKQLAGG-K(Biotin)-amide as substrate preincubated for 60 mins followed by substrate addition and measured by RapdiFire-MS/MS analysis	ic50	0.0010	uM
4-[[2-[5-[8-[5-acetyl-1-(oxan-4-yl)-6,7-dihydro-4H-pyrazolo[4,3-c]pyridin-3-yl]isoquinolin-3-yl]pyridine-2-carbonyl]-2-azaspiro[3.3]heptan-6-yl]amino]-2-(2,6-dioxopiperidin-3-yl)isoindole-1,3-dione	1990961: Induction of p300 degradation in human RS4-11 cells incubated for 4 hrs by Western blot assay	ec50	0.0011	uM
3-[7-(difluoromethyl)-6-(1-methylpyrazol-4-yl)-3,4-dihydro-2H-quinolin-1-yl]-N-methyl-1-(oxan-4-yl)-6,7-dihydro-4H-pyrazolo[4,3-c]pyridine-5-carboxamide	1489227: Displacement of biotinylated histone H3K14 peptide ligand from human recombinant His-tagged P300 measured after 10 mins by TR-FRET assay	ic50	0.0012	uM
1-[3-[7-(difluoromethyl)-6-(1-methylpyrazol-4-yl)-3,4-dihydro-2H-quinolin-1-yl]-1-(oxan-4-yl)-6,7-dihydro-4H-pyrazolo[4,3-c]pyridin-5-yl]ethanone	1489227: Displacement of biotinylated histone H3K14 peptide ligand from human recombinant His-tagged P300 measured after 10 mins by TR-FRET assay	ic50	0.0013	uM
(6S)-1-(3,4-difluorophenyl)-6-[5-(3,5-dimethyl-1,2-oxazol-4-yl)-1-(4-methoxycyclohexyl)benzimidazol-2-yl]piperidin-2-one	2070661: Binding affinity to p300 (unknown origin) by SPR method	kd	0.0013	uM
(3S)-3’-[2-[(3R)-3-cyclopropyl-7-fluoro-3,5-dihydro-2H-1,4-benzoxazepin-4-yl]-2-oxoethyl]-6-(1-methylpyrazol-4-yl)spiro[1,2-dihydroindene-3,5’-imidazolidine]-2’,4’-dione	1528824: Inhibition of p300 (unknown origin) using histone H3 (1 to 21 residues) as substrate preincubated for 15 mins followed by substrate and [3H]acetyl-CoA addition and measured after 60 mins by scintillation counting analysis	ic50	0.0013	uM
(6R)-1-(3,4-difluorophenyl)-6-[5-(3,5-dimethyl-1,2-oxazol-4-yl)-1-(4-methoxycyclohexyl)benzimidazol-2-yl]piperidin-2-one	2027170: Binding affinity to P300 bromodomain (unknown origin) assessed as dissociation constant	kd	0.0013	uM
4-[4-[5-[8-[5-acetyl-1-(oxan-4-yl)-6,7-dihydro-4H-pyrazolo[4,3-c]pyridin-3-yl]isoquinolin-3-yl]pyridine-2-carbonyl]piperazin-1-yl]-2-(2,6-dioxopiperidin-3-yl)isoindole-1,3-dione	1990961: Induction of p300 degradation in human RS4-11 cells incubated for 4 hrs by Western blot assay	ec50	0.0016	uM
5-[8-[5-acetyl-1-(oxan-4-yl)-6,7-dihydro-4H-pyrazolo[4,3-c]pyridin-3-yl]isoquinolin-3-yl]-N-[8-[[2-(2,6-dioxopiperidin-3-yl)-1,3-dioxoisoindol-4-yl]amino]octyl]pyridine-2-carboxamide	1990961: Induction of p300 degradation in human RS4-11 cells incubated for 4 hrs by Western blot assay	ec50	0.0016	uM
1-[(5R)-3-[2-[(3S)-3-cyclopropyl-7-fluoro-1,3,4,5-tetrahydro-2-benzazepin-2-yl]-2-oxoethyl]-6’-fluoro-2,4-dioxospiro[1,3-oxazolidine-5,1’-2,3-dihydroindene]-5’-yl]-3-methylurea	1811548: Inhibition of p300 (unknown origin) preincubated for 15 mins followed by addition of substrate [3H] Ac-CoA and measured after 60 mins by liquid scintillation counting assay	ic50	0.0017	uM
(3S)-3’-[2-[(3S)-7-fluoro-3-(trifluoromethyl)-3,5-dihydro-2H-1,4-benzoxazepin-4-yl]-2-oxoethyl]-6-(1-methylpyrazol-4-yl)spiro[1,2-dihydroindene-3,5’-imidazolidine]-2’,4’-dione	1528824: Inhibition of p300 (unknown origin) using histone H3 (1 to 21 residues) as substrate preincubated for 15 mins followed by substrate and [3H]acetyl-CoA addition and measured after 60 mins by scintillation counting analysis	ic50	0.0018	uM
1-[(5R)-3-[2-[(3S)-7-fluoro-3-(trifluoromethyl)-1,3,4,5-tetrahydro-2-benzazepin-2-yl]-2-oxoethyl]-2,4-dioxospiro[1,3-oxazolidine-5,1’-2,3-dihydroindene]-5’-yl]-3-methylurea	1528824: Inhibition of p300 (unknown origin) using histone H3 (1 to 21 residues) as substrate preincubated for 15 mins followed by substrate and [3H]acetyl-CoA addition and measured after 60 mins by scintillation counting analysis	ic50	0.0019	uM
5-[8-[5-acetyl-1-(oxan-4-yl)-6,7-dihydro-4H-pyrazolo[4,3-c]pyridin-3-yl]isoquinolin-3-yl]-N-[1-[2-(2,6-dioxopiperidin-3-yl)-1,3-dioxoisoindol-5-yl]piperidin-4-yl]pyridine-2-carboxamide	1990961: Induction of p300 degradation in human RS4-11 cells incubated for 4 hrs by Western blot assay	ec50	0.0019	uM
(2R)-1-[1-(3-chlorophenyl)cyclopentanecarbonyl]-N-(5-methoxy-2-pyridinyl)pyrrolidine-2-carboxamide	1918472: Inhibition of full-length P300 (unknown origin) using ARTKQTARKSTGGKAPRKQLAGG-K(Biotin)-amide as substrate preincubated for 60 mins followed by substrate addition and measured by RapdiFire-MS/MS analysis	ic50	0.0020	uM
(5R)-1-(3,4-difluorophenyl)-5-[5-(3,5-dimethyl-1,2-oxazol-4-yl)-1-(4-methoxycyclohexyl)benzimidazol-2-yl]-5-methylpyrrolidin-2-one	2131136: Inhibition of recombinant p300 bromodomain (unknown origin) using H3(44-60)K56Ac-biotinylated peptide as substrate incubated for 120 mins by AlphaLISA	ic50	0.0021	uM
1-[(5R)-3-[2-[(3S)-3-cyclopropyl-7-fluoro-1,3,4,5-tetrahydro-2-benzazepin-2-yl]-2-oxoethyl]-2,4-dioxospiro[1,3-oxazolidine-5,5’-7,8-dihydro-6H-naphthalene]-2’-yl]-3-methylurea	1811548: Inhibition of p300 (unknown origin) preincubated for 15 mins followed by addition of substrate [3H] Ac-CoA and measured after 60 mins by liquid scintillation counting assay	ic50	0.0022	uM
5-[8-[5-acetyl-1-(oxan-4-yl)-6,7-dihydro-4H-pyrazolo[4,3-c]pyridin-3-yl]isoquinolin-3-yl]-N-[7-[[2-(2,6-dioxopiperidin-3-yl)-1,3-dioxoisoindol-4-yl]amino]heptyl]pyridine-2-carboxamide	1990961: Induction of p300 degradation in human RS4-11 cells incubated for 4 hrs by Western blot assay	ec50	0.0023	uM
1-[(5R)-3-[2-[(3S)-7-fluoro-3-(trifluoromethyl)-3,5-dihydro-2H-1,4-benzoxazepin-4-yl]-2-oxoethyl]-2,4-dioxospiro[1,3-oxazolidine-5,1’-2,3-dihydroindene]-5’-yl]-3-methylurea	1528824: Inhibition of p300 (unknown origin) using histone H3 (1 to 21 residues) as substrate preincubated for 15 mins followed by substrate and [3H]acetyl-CoA addition and measured after 60 mins by scintillation counting analysis	ic50	0.0024	uM
(3R)-3’-[2-[(3S)-7-fluoro-3-(trifluoromethyl)-3,5-dihydro-2H-1,4-benzoxazepin-4-yl]-2-oxoethyl]-6-(1-methylpyrazol-4-yl)spiro[1,2-dihydroindene-3,5’-1,3-oxazolidine]-2’,4’-dione	1528824: Inhibition of p300 (unknown origin) using histone H3 (1 to 21 residues) as substrate preincubated for 15 mins followed by substrate and [3H]acetyl-CoA addition and measured after 60 mins by scintillation counting analysis	ic50	0.0024	uM
1-methyl-3-[(5R)-3-[2-[(3R)-3-methyl-1,3,4,5-tetrahydro-2-benzazepin-2-yl]-2-oxoethyl]-2,4-dioxospiro[1,3-oxazolidine-5,1’-2,3-dihydroindene]-5’-yl]urea	1811548: Inhibition of p300 (unknown origin) preincubated for 15 mins followed by addition of substrate [3H] Ac-CoA and measured after 60 mins by liquid scintillation counting assay	ic50	0.0025	uM
4-[2-[[(1R)-2-[6-(1-methylpyrazol-4-yl)-1H-indol-3-yl]-2-oxo-1-phenylethyl]amino]ethyl]benzonitrile	1658723: Binding affinity to recombinant full length EP300 (unknown origin) incubated for 30 mins followed by H3(1 to 21) addition and measured after 1 hr by scintillation proximity assay	ic50	0.0025	uM
1-[(5R)-2,4-dioxo-3-[2-oxo-2-[(3S)-3-(trifluoromethyl)-1,3,4,5-tetrahydro-2-benzazepin-2-yl]ethyl]spiro[1,3-oxazolidine-5,1’-2,3-dihydroindene]-5’-yl]-3-methylurea	1528824: Inhibition of p300 (unknown origin) using histone H3 (1 to 21 residues) as substrate preincubated for 15 mins followed by substrate and [3H]acetyl-CoA addition and measured after 60 mins by scintillation counting analysis	ic50	0.0026	uM
1-[(5R)-3-[2-[(3R)-7-fluoro-3-methyl-1,3,4,5-tetrahydro-2-benzazepin-2-yl]-2-oxoethyl]-2,4-dioxospiro[1,3-oxazolidine-5,1’-2,3-dihydroindene]-5’-yl]-3-methylurea	1528824: Inhibition of p300 (unknown origin) using histone H3 (1 to 21 residues) as substrate preincubated for 15 mins followed by substrate and [3H]acetyl-CoA addition and measured after 60 mins by scintillation counting analysis	ic50	0.0030	uM
[[(3R)-4-[[3-[2-[2-[[(5S)-5-acetamido-6-amino-6-oxohexyl]amino]-2-oxoethyl]sulfanylethylamino]-3-oxopropyl]amino]-3-hydroxy-2,2-dimethyl-4-oxobutoxy]-hydroxyphosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methyl hydrogen phosphate	1282366: Inhibition of human recombinant C-terminal GST-tagged p300 (1195 to 1673 residues) expressed in competent Escherichia coli DH5alpha cells using histone substrate after 30 mins by scintillation counting method in presence of [3H]acetyl-CoA	ic50	0.0032	uM
(3S,5S)-1-(3,4-difluorophenyl)-5-[5-(3,5-dimethyl-1,2-oxazol-4-yl)-1-[4-(trideuteriomethoxy)cyclohexyl]benzimidazol-2-yl]-3-fluoropyrrolidin-2-one	2131136: Inhibition of recombinant p300 bromodomain (unknown origin) using H3(44-60)K56Ac-biotinylated peptide as substrate incubated for 120 mins by AlphaLISA	ic50	0.0033	uM

CTD chemical–gene interactions

135 total (human), top 30 by PubMed support.

Chemical	Actions (top 5)	PubMed papers
Estradiol	decreases expression, affects binding, decreases reaction, increases reaction	9
Resveratrol	affects binding, increases reaction, decreases response to substance, increases acetylation, increases activity (+5 more)	8
trichostatin A	increases expression, affects localization, affects binding, increases reaction, affects reaction (+3 more)	6
bisphenol A	affects binding, affects folding, increases reaction, decreases reaction	5
Tetrachlorodibenzodioxin	affects binding, decreases reaction, increases reaction, affects reaction, increases expression	5
Quercetin	increases activity, increases reaction, increases expression, decreases expression, affects reaction (+3 more)	4
Cisplatin	increases reaction, increases acetylation, affects cotreatment, decreases expression, affects binding	3
Doxorubicin	increases activity, increases expression, decreases reaction, decreases expression, affects binding (+2 more)	3
Glucose	affects binding, affects cotreatment, increases reaction, affects reaction, increases expression (+1 more)	3
Dihydrotestosterone	affects binding, decreases reaction, increases reaction	3
Tobacco Smoke Pollution	increases expression	3
Valproic Acid	affects expression, decreases methylation	3
arsenite	affects binding, affects reaction, increases degradation, increases phosphorylation, decreases reaction (+5 more)	2
sodium arsenite	affects binding, decreases reaction, increases expression	2
Decitabine	affects methylation, affects binding, increases reaction	2
Arsenic Trioxide	increases activity, increases expression, affects binding, increases acetylation, increases reaction	2
Vorinostat	affects reaction, increases activity, increases reaction, affects cotreatment, increases expression (+1 more)	2
Curcumin	decreases reaction, decreases expression, affects binding, increases reaction, affects localization	2
Diethylstilbestrol	affects binding, increases reaction, decreases reaction	2
Gold	affects binding, decreases reaction, increases expression, increases acetylation, increases stability (+1 more)	2
Oxygen	affects binding, decreases reaction, increases reaction	2
Tretinoin	increases expression, increases reaction, affects binding	2
Cadmium Chloride	decreases expression, increases abundance	2
Genistein	affects binding, decreases reaction, decreases expression, increases expression, increases reaction	2
Particulate Matter	affects binding, increases reaction, affects expression	2
3-((6-(2-methoxyphenyl)pyrimidin-4-yl)amino)phenyl)methane sulfonamide	decreases expression	1
CBP30 compound	affects binding, decreases activity	1
FR900359	increases phosphorylation	1
TAK-243	increases sumoylation	1
crenigacestat	affects expression, affects reaction	1

ChEMBL screening assays

767 unique, capped per target: 763 binding, 3 functional, 1 admet

Representative assays (with source publication via chembl_document):

Assay ID	Type	Description	Source paper
CHEMBL1006960	Binding	Inhibition of recombinant His-tagged HAT p300 expressed in Sf21-Baculovirus system	Synthesis of isothiazol-3-one derivatives as inhibitors of histone acetyltransferases (HATs). — Bioorg Med Chem
CHEMBL4405045	ADMET	Inhibition of MSGRGK(Ac)-GGK(Ac)GLGK(Ac)GGAKRHR-biotin binding to EP300 (1040 to 1160 residues) (unknown origin) expressed in Escherichia coli BL21 (DE3) by Alphascreen assay	Discovery of 8-Methyl-pyrrolo[1,2-a]pyrazin-1(2H)-one Derivatives as Highly Potent and Selective Bromodomain and Extra-Terminal (BET) Bromodomain Inhibitors. — J Med Chem
CHEMBL5723163	Functional	Affinity Biochemical interaction: (FRET) EUB0002298a EP300	Affinity Biochemical Literature for EUbOPEN Chemogenomic Library

Cellosaurus cell lines

2,011 cell lines: 2,008 cancer cell line, 1 embryonic stem cell, 1 transformed cell line, 1 induced pluripotent stem cell

First 10 cell lines (id-ordered, not curated):

Cellosaurus	Name	Category	Sex
CVCL_0248	DLD-1	Cancer cell line	Male
CVCL_0291	HCT 116	Cancer cell line	Male
CVCL_0622	MDA-MB-435S	Cancer cell line	Male
CVCL_1049	647V	Cancer cell line	Male
CVCL_1112	CAL-62	Cancer cell line	Female
CVCL_1140	COR-L279	Cancer cell line	Male
CVCL_1609	NOMO-1	Cancer cell line	Female
CVCL_1648	RCM-1 [Human rectal adenocarcinoma]	Cancer cell line	Female
CVCL_1845	PaTu 8902	Cancer cell line	Female
CVCL_1847	PaTu 8988t	Cancer cell line	Female

Clinical trials (associated diseases)

538 trials via MONDO — disease-level, not drug-specific.

Trial	Phase	Status	Title
NCT00717080	PHASE4	COMPLETED	The Role of Capsular Tension Ring (CTR) in Anterior Capsular Contraction
NCT00114829	PHASE4	UNKNOWN	Preoperative Assessment of Colon Tumor
NCT00114842	PHASE4	COMPLETED	Magnetic Resonance (MR) Colonography With Fecal Tagging
NCT00114946	PHASE4	TERMINATED	A Study to Compare Two Avastin-Based Treatment Regimens for the Treatment of Metastatic Colorectal Cancer
NCT00122720	PHASE4	COMPLETED	The Effect of Darbepoetin Upon Rehabilitation for Colorectal Cancer Surgery
NCT00129870	PHASE4	TERMINATED	CONCEPT: Comparison of Oxaliplatin vs Conventional Methods With Calcium/Magnesium in First-Line Metastatic Colorectal Cancer
NCT00138060	PHASE4	COMPLETED	Toxicity/Benefit Ratio Optimization of Chemotherapy in Colorectal Cancer (CRC) Patients by Determination of Individual Genotypic Determinants
NCT00216424	PHASE4	TERMINATED	Capecitabine (Xeloda) and Radiation for Patients With Rectosigmoid Carcinoma
NCT00327093	PHASE4	TERMINATED	Elaboration of a Model for Predicting Efficacy of Monoclonal Antibodies (Cetuximab and Bevacizumab) in Patients With Colorectal Cancer and Liver Metastases
NCT00332943	PHASE4	COMPLETED	MR Colonography With Fecal Tagging. Barium vs. BariumFerumoxsil
NCT00441311	PHASE4	COMPLETED	Dissemination of Colorectal Cancer Screening to Primary Care Physicians
NCT00460837	PHASE4	WITHDRAWN	Comparison of Bowel Preparation in Virtual Colonoscopy (VC) - Patient Experience
NCT00473980	PHASE4	COMPLETED	Preoperative Non-steroidal Anti-inflammatory Drugs(NSAID) to Colorectal Cancer Patients
NCT00488904	PHASE4	COMPLETED	Omega-3 Fatty Acids and Postoperative Complications After Colorectal Surgery
NCT00496678	PHASE4	COMPLETED	Trial of Patient Navigation-Activation
NCT00502671	PHASE4	COMPLETED	A Study of Xeloda (Capecitabine) as Adjuvant Monotherapy in Patients With Colon Cancer.
NCT00559676	PHASE4	COMPLETED	Study of Biomarkers in Patients Undergoing Chemotherapy for Metastatic Colorectal Cancer
NCT00577031	PHASE4	COMPLETED	OBELIX Study: A Study of Avastin (Bevacizumab) in Combination With XELOX in Patients With Metastatic Cancer of the Colon or Rectum.
NCT00626054	PHASE4	COMPLETED	Comparison of Two Methods of Administration of a PEG Solution
NCT00812864	PHASE4	COMPLETED	Pharmacokinetic Study of Capecitabine in Elderly Cancer Patient (≥ 75 Years)
NCT00868569	PHASE4	UNKNOWN	Transhepatic Arterial Chemotherapy (TAC) Versus Transcatheter Arterial Chemoembolization (TACE) Plus Folfox4 as the Treatment of Unresectable Liver Metastasis of Colorectal Cancer
NCT00868816	PHASE4	COMPLETED	Oxaliplatine Based Adjuvant Chemotherapy for Stage II/III Colorectal Cancer: 8 Cycles Versus 12 Cycles
NCT00874406	PHASE4	UNKNOWN	Preoperative Transhepatic Arterial Chemotherapy (TAC) in the Treatment of Liver Metastasis of Resectable Colorectal Cancer
NCT00928928	PHASE4	COMPLETED	Oxidative Stress Markers in Open and Laparoscopic Colectomy for Cancer
NCT00942461	PHASE4	COMPLETED	Inflammatory Response in Laparoscopic and Open Colectomy
NCT01023633	PHASE4	UNKNOWN	OPTIMOX1 in Chinese mCRC Patients
NCT01271582	PHASE4	UNKNOWN	Investigation of Association Between UGT1A1 Polymorphisms and Irinotecan Toxicity in Korean Patients
NCT01315990	PHASE4	UNKNOWN	FOLFIRI in Combination With Cetuximab in the First-line Treatment of Metastatic Colorectal Cancer Including a Regular Dermal Prophylaxis to Prevent Acneiforme Follicular Exanthema
NCT01493713	PHASE4	COMPLETED	Correlation Between RECIST, Morphologic Response by CT- Histopathologic Response in Hepatic Metastasis Secondary to Colorectal Cancer
NCT01609660	PHASE4	COMPLETED	Impact of Probiotics on the Intestinal Microbiota
NCT01641458	PHASE4	COMPLETED	Pharmacology-driven Dosing of Fluoropyrimidines in Cancer Patients
NCT01689792	PHASE4	COMPLETED	A Multi-centre Study Comparing the Polyp Detection Rate of Two Different Types of Bowel Preparation: a 2-litre Solution (MOVIPREP®) Versus a Hyperosmotic and Stimulant Combined Low Volume Bowel Preparation (Sodium Picosulfate and Magnesium Citrate)
NCT01695772	PHASE4	COMPLETED	A Study of Bevacizumab Plus 5-Flurouracil (5-FU) Based Doublet Chemotherapy as Neoadjuvant Therapy for Participants With Previously Untreated Unresectable Liver-Only Metastases From Colorectal Cancer
NCT01695863	PHASE4	COMPLETED	Efficacy and Patient Satisfaction of Miralax and Gatorade Versus Movi Prep
NCT01706822	PHASE4	TERMINATED	Radial Reload Laparoscopic LAR Case Series
NCT01740947	PHASE4	TERMINATED	Does Administration of Antibiotics in Patients Undergoing Surgery for Colorectal Cancer Result in Less Complications and Better Prognosis?
NCT01831310	PHASE4	COMPLETED	Nutrition for Colorectal Cancer Patients and Neutrophil Functions
NCT01841294	PHASE4	UNKNOWN	NK Activity Modulation Induced by Intravenous Lidocaine During Colorectal Laparoscopic Surgery
NCT01959061	PHASE4	UNKNOWN	Efficacy and Safety of Raltitrexed-based Transarterial Chemoembolisation(TACE)for Colorectal Cancer Liver Metastases
NCT02032953	PHASE4	UNKNOWN	Enhancing the Anabolic Effect of Perioperative Nutrition With Insulin While Maintaining Normoglycemia