Q09472 · EP300_HUMAN
- ProteinHistone acetyltransferase p300
- GeneEP300
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2414 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions as a histone acetyltransferase and regulates transcription via chromatin remodeling (PubMed:23415232, PubMed:23934153, PubMed:8945521).
Acetylates all four core histones in nucleosomes (PubMed:23415232, PubMed:23934153, PubMed:8945521).
Histone acetylation gives an epigenetic tag for transcriptional activation (PubMed:23415232, PubMed:23934153, PubMed:8945521).
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 (PubMed:23415232).
Mediates acetylation of histone H3 at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac, respectively) (PubMed:21131905, PubMed:23911289).
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 (PubMed:37731000).
Catalyzes formation of histone H4 acetyl-methylated at 'Lys-5' and 'Lys-12' (H4K5acme and H4K12acme, respectively) (PubMed:37731000).
Also functions as acetyltransferase for non-histone targets, such as ALX1, HDAC1, PRMT1, SIRT2, STAT3 or GLUL (PubMed:12929931, PubMed:15653507, PubMed:16285960, PubMed:16762839, PubMed:18722353, PubMed:18782771, PubMed:26990986).
Acetylates 'Lys-131' of ALX1 and acts as its coactivator (PubMed:12929931).
Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of p53/TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function (PubMed:18722353).
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 (PubMed:11511361, PubMed:15448695).
Promotes chromatin acetylation in heat shock responsive HSP genes during the heat shock response (HSR), thereby stimulating HSR transcription (PubMed:18451878).
Acetylates HDAC1 leading to its inactivation and modulation of transcription (PubMed:16762839).
Acetylates 'Lys-247' of EGR2 (By similarity).
Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2 (PubMed:12586840).
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 (PubMed:14752053).
Can also mediate transcriptional repression. Acetylates FOXO1 and enhances its transcriptional activity (PubMed:15890677).
Acetylates STAT3 at different sites, promoting both STAT3 dimerization and activation and recruitment to chromatin (PubMed:15653507, PubMed:16285960, PubMed:18782771).
Acetylates BCL6 wich disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity (PubMed:12402037).
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 (PubMed:14645221).
Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity (PubMed:16617102).
Acetylates XBP1 isoform 2; acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity (PubMed:20955178).
Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24939902).
Acetylates MEF2D (PubMed:21030595).
Acetylates and stabilizes ZBTB7B protein by antagonizing ubiquitin conjugation and degradation, this mechanism may be involved in CD4/CD8 lineage differentiation (PubMed:20810990).
Acetylates GABPB1, impairing GABPB1 heterotetramerization and activity (By similarity).
Acetylates PCK1 and promotes PCK1 anaplerotic activity (PubMed:30193097).
Acetylates RXRA and RXRG (PubMed:17761950).
Acetylates isoform M2 of PKM (PKM2), promoting its homodimerization and conversion into a protein kinase (PubMed:24120661).
Acetylates RPTOR in response to leucine, leading to activation of the mTORC1 complex (PubMed:30197302, PubMed:32561715).
Mediates cAMP-gene regulation by binding specifically to phosphorylated CREBBP (PubMed:8917528).
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 or propanoyl-CoA (propionyl-CoA), and is able to mediate protein crotonylation, butyrylation, 2-hydroxyisobutyrylation, lactylation or propionylation, respectively (PubMed:17267393, PubMed:25818647, PubMed:29775581, PubMed:31645732).
Acts as a histone crotonyltransferase; crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors (PubMed:25818647).
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 (PubMed:25818647).
Also acts as a histone butyryltransferase; butyrylation marks active promoters (PubMed:17267393).
Catalyzes histone lactylation in macrophages by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription (PubMed:31645732).
Acts as a protein-lysine 2-hydroxyisobutyryltransferase; regulates glycolysis by mediating 2-hydroxyisobutyrylation of glycolytic enzymes (PubMed:29775581).
Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (PubMed:25514493).
Acetylates all four core histones in nucleosomes (PubMed:23415232, PubMed:23934153, PubMed:8945521).
Histone acetylation gives an epigenetic tag for transcriptional activation (PubMed:23415232, PubMed:23934153, PubMed:8945521).
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 (PubMed:23415232).
Mediates acetylation of histone H3 at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac, respectively) (PubMed:21131905, PubMed:23911289).
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 (PubMed:37731000).
Catalyzes formation of histone H4 acetyl-methylated at 'Lys-5' and 'Lys-12' (H4K5acme and H4K12acme, respectively) (PubMed:37731000).
Also functions as acetyltransferase for non-histone targets, such as ALX1, HDAC1, PRMT1, SIRT2, STAT3 or GLUL (PubMed:12929931, PubMed:15653507, PubMed:16285960, PubMed:16762839, PubMed:18722353, PubMed:18782771, PubMed:26990986).
Acetylates 'Lys-131' of ALX1 and acts as its coactivator (PubMed:12929931).
Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of p53/TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function (PubMed:18722353).
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 (PubMed:11511361, PubMed:15448695).
Promotes chromatin acetylation in heat shock responsive HSP genes during the heat shock response (HSR), thereby stimulating HSR transcription (PubMed:18451878).
Acetylates HDAC1 leading to its inactivation and modulation of transcription (PubMed:16762839).
Acetylates 'Lys-247' of EGR2 (By similarity).
Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2 (PubMed:12586840).
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 (PubMed:14752053).
Can also mediate transcriptional repression. Acetylates FOXO1 and enhances its transcriptional activity (PubMed:15890677).
Acetylates STAT3 at different sites, promoting both STAT3 dimerization and activation and recruitment to chromatin (PubMed:15653507, PubMed:16285960, PubMed:18782771).
Acetylates BCL6 wich disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity (PubMed:12402037).
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 (PubMed:14645221).
Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity (PubMed:16617102).
Acetylates XBP1 isoform 2; acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity (PubMed:20955178).
Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24939902).
Acetylates MEF2D (PubMed:21030595).
Acetylates and stabilizes ZBTB7B protein by antagonizing ubiquitin conjugation and degradation, this mechanism may be involved in CD4/CD8 lineage differentiation (PubMed:20810990).
Acetylates GABPB1, impairing GABPB1 heterotetramerization and activity (By similarity).
Acetylates PCK1 and promotes PCK1 anaplerotic activity (PubMed:30193097).
Acetylates RXRA and RXRG (PubMed:17761950).
Acetylates isoform M2 of PKM (PKM2), promoting its homodimerization and conversion into a protein kinase (PubMed:24120661).
Acetylates RPTOR in response to leucine, leading to activation of the mTORC1 complex (PubMed:30197302, PubMed:32561715).
Mediates cAMP-gene regulation by binding specifically to phosphorylated CREBBP (PubMed:8917528).
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 or propanoyl-CoA (propionyl-CoA), and is able to mediate protein crotonylation, butyrylation, 2-hydroxyisobutyrylation, lactylation or propionylation, respectively (PubMed:17267393, PubMed:25818647, PubMed:29775581, PubMed:31645732).
Acts as a histone crotonyltransferase; crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors (PubMed:25818647).
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 (PubMed:25818647).
Also acts as a histone butyryltransferase; butyrylation marks active promoters (PubMed:17267393).
Catalyzes histone lactylation in macrophages by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription (PubMed:31645732).
Acts as a protein-lysine 2-hydroxyisobutyryltransferase; regulates glycolysis by mediating 2-hydroxyisobutyrylation of glycolytic enzymes (PubMed:29775581).
Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (PubMed:25514493).
(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.
Catalytic activity
- acetyl-CoA + L-lysyl-[histone] = CoA + H+ + N6-acetyl-L-lysyl-[histone]This reaction proceeds in the forward direction.
- acetyl-CoA + L-lysyl-[protein] = CoA + H+ + N6-acetyl-L-lysyl-[protein]This reaction proceeds in the forward direction.
- acetyl-CoA + N6-methyl-L-lysyl-[histone] = CoA + H+ + N6-acetyl-N6-methyl-L-lysyl-[histone]This reaction proceeds in the forward direction.
- (2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H+ + N6-(2E)-butenoyl-L-lysyl-[protein]
- butanoyl-CoA + L-lysyl-[protein] = CoA + H+ + N6-butanoyl-L-lysyl-[protein]
- L-lysyl-[protein] + propanoyl-CoA = CoA + H+ + N6-propanoyl-L-lysyl-[protein]
- 2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H+ + N6-(2-hydroxyisobutanoyl)-L-lysyl-[protein]This reaction proceeds in the forward direction.
- (S)-lactoyl-CoA + L-lysyl-[protein] = CoA + H+ + N6-[(S)-lactoyl]-L-lysyl-[protein]This reaction proceeds in the forward direction.
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 31-32 | Breakpoint for translocation to form KAT6A-EP300 and EP300-KAT6A | ||||
Sequence: TD | ||||||
Binding site | 347 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 351 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 364 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 369 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 378 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 382 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 388 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 393 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 402 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 406 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 411 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 414 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1398-1400 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: LDS | ||||||
Binding site | 1410-1411 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: RT | ||||||
Binding site | 1457 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 1462 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 1466 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 1670 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1673 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1683 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1686 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1692 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1695 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1701 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1703 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 2088 | Interaction with NCOA2 | ||||
Sequence: R | ||||||
Site | 2142 | Interaction with NCOA2 | ||||
Sequence: R |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameHistone acetyltransferase p300
- EC number
- Short namesp300 HAT
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ09472
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to active chromatin: Colocalizes with histone H3 acetylated and/or crotonylated at 'Lys-18' (H3K18ac and H3K18cr, respectively) (PubMed:25818647).
In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Colocalizes with ROCK2 in the nucleus (PubMed:12929931).
Localizes to sites of DNA damage (PubMed:25593309).
In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Colocalizes with ROCK2 in the nucleus (PubMed:12929931).
Localizes to sites of DNA damage (PubMed:25593309).
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Rubinstein-Taybi syndrome 2 (RSTS2)
- Note
- DescriptionA 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.
- See alsoMIM:613684
Menke-Hennekam syndrome 2 (MKHK2)
- Note
- DescriptionA 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.
- See alsoMIM:618333
Natural variants in MKHK2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_081986 | 1824 | Q>P | in MKHK2; dbSNP:rs1569120903 | |
VAR_081987 | 1831 | missing | in MKHK2 |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 89 | Abolishes AMPK-mediated phosphorylation. | ||||
Sequence: S → A | ||||||
Mutagenesis | 89 | Phosphomimetic mutant that leads to descreased interaction with nuclear receptors. | ||||
Sequence: S → D | ||||||
Natural variant | VAR_055554 | 289 | in dbSNP:rs2230111 | |||
Sequence: M → V | ||||||
Mutagenesis | 344 | Inhibits interaction with HIF1A and transcription activation; when associated with A-345. | ||||
Sequence: L → A | ||||||
Mutagenesis | 345 | Inhibits interaction with HIF1A and transcription activation; when associated with A-344. | ||||
Sequence: L → A | ||||||
Mutagenesis | 371-376 | Inhibits interaction with HIF1A. Reduces interaction with CITED2. | ||||
Sequence: TMKNVL → NAAIRS | ||||||
Mutagenesis | 413-418 | Inhibits interaction with HIF1A. Does not inhibit interaction with CITED2. | ||||
Sequence: VCLPLK → NAAIRS | ||||||
Natural variant | VAR_014428 | 827 | in a breast cancer sample | |||
Sequence: L → P | ||||||
Natural variant | VAR_020425 | 997 | in dbSNP:rs20551 | |||
Sequence: I → V | ||||||
Natural variant | VAR_014429 | 1013 | in a breast cancer sample; dbSNP:rs1234168115 | |||
Sequence: E → G | ||||||
Mutagenesis | 1020 | Abolishes sumoylation and transcriptional repression when associated with A-1024. | ||||
Sequence: K → A | ||||||
Mutagenesis | 1020 | Abolishes sumoylation and transcriptional repression; when associated with R-1024. | ||||
Sequence: K → R | ||||||
Mutagenesis | 1024 | Abolishes sumoylation and transcriptional repression; when associated with A-1020. | ||||
Sequence: K → A | ||||||
Mutagenesis | 1024 | Abolishes sumoylation and transcriptional repression; when associated with R-1020. | ||||
Sequence: K → R | ||||||
Mutagenesis | 1170 | Increased acetyltransferase activity. | ||||
Sequence: F → E | ||||||
Mutagenesis | 1204 | Increased acetyltransferase activity. | ||||
Sequence: C → R | ||||||
Mutagenesis | 1242 | Increased acetyltransferase activity. | ||||
Sequence: E → K | ||||||
Mutagenesis | 1357 | 40% decrease in activity. | ||||
Sequence: T → L | ||||||
Mutagenesis | 1357 | 40% decrease in activity. 90% decrease in activity; when associated with R-1505; R-1625 and R-1628. | ||||
Sequence: T → R | ||||||
Mutagenesis | 1396 | Loss of activity; when associated with R-1397. | ||||
Sequence: S → R | ||||||
Mutagenesis | 1396 | Loss of activity; when associated with W-1396. | ||||
Sequence: S → W | ||||||
Mutagenesis | 1397 | Loss of activity; when associated with R-1396. | ||||
Sequence: Y → R | ||||||
Mutagenesis | 1397 | Loss of activity; when associated with W-1397. | ||||
Sequence: Y → W | ||||||
Mutagenesis | 1399 | Abolished acetyltransferase and acyltransferase activities. Abolishes autoacetylation. Does not interact with TFAP2A and inhibits transcriptional coactivation of TFAP2A by CITED2. Does not inhibit interaction with CITED2, DNA-binding of TFAP2A or nuclear localization of TFAP2A or CITED2. No enhancement of FOXO1-mediated transcriptional activity. No inhibition of insulin-mediated translocation to the cytoplasm. No acetylation of RXRA. | ||||
Sequence: D → Y | ||||||
Mutagenesis | 1467 | Abolishes autoacetylation. Loss of acetyltransferase activity. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 1504 | Abolished acetyltransferase activity. | ||||
Sequence: F → A | ||||||
Mutagenesis | 1505 | 90% decrease in activity; when associated with R-1625 and R-1628. 90% decrease in activity; when associated with R-1357; R-1625 and R-1628. | ||||
Sequence: E → R | ||||||
Natural variant | VAR_074021 | 1511 | in dbSNP:rs763860567 | |||
Sequence: N → I | ||||||
Mutagenesis | 1625 | 70% decrease in activity; when associated with R-1628. 90% decrease in activity; when associated with R-1505 and R-1628. 90% decrease in activity; when associated with R-1357; R-1505 and R-1628. | ||||
Sequence: D → R | ||||||
Mutagenesis | 1628 | 70% decrease in activity; when associated with R-1625. 90% decrease in activity; when associated with E-1505 and R-1625. 90% decrease in activity; when associated with R-1357; R-1505 and R-1625. | ||||
Sequence: D → R | ||||||
Mutagenesis | 1645-1646 | Increased acetyltransferase activity. | ||||
Sequence: RR → EE | ||||||
Natural variant | VAR_014430 | 1650 | in a pancreatic cancer sample; dbSNP:rs2145513278 | |||
Sequence: S → Y | ||||||
Natural variant | VAR_081986 | 1824 | in MKHK2; dbSNP:rs1569120903 | |||
Sequence: Q → P | ||||||
Natural variant | VAR_081987 | 1831 | in MKHK2 | |||
Sequence: Missing | ||||||
Natural variant | VAR_080731 | 2007 | found in a patient with spinocerebellar ataxia; uncertain significance; dbSNP:rs763892493 | |||
Sequence: Q → R | ||||||
Mutagenesis | 2056 | No effect on interaction with NCOA2. | ||||
Sequence: R → K | ||||||
Mutagenesis | 2088 | Abolishes interaction with NCOA2. | ||||
Sequence: R → K | ||||||
Mutagenesis | 2142 | Strongly reduces interaction with NCOA2. | ||||
Sequence: R → K | ||||||
Natural variant | VAR_038376 | 2174 | in dbSNP:rs5758252 | |||
Sequence: T → S | ||||||
Natural variant | VAR_014431 | 2221 | in a colorectal cancer sample; dbSNP:rs28937578 | |||
Sequence: P → Q | ||||||
Natural variant | VAR_038377 | 2223 | in dbSNP:rs1046088 | |||
Sequence: Q → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 6,624 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000211193 | 2-2414 | UniProt | Histone acetyltransferase p300 | |||
Sequence: AENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDINQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQSSPGLGLINSMVKSPMTQAGLTSPNMGMGTSGPNQGPTQSTGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQPLKMGMMNNPNPYGSPYTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAMDKKAVPGGGMPNMGQQPAPQVQQPGLVTPVAQGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNAGDKRNQQPILTGAPVGLGNPSSLGVGQQSAPNLSTVSQIDPSSIERAYAALGLPYQVNQMPTQPQVQAKNQQNQQPGQSPQGMRPMSNMSASPMGVNGGVGVQTPSLLSDSMLHSAINSQNPMMSENASVPSLGPMPTAAQPSTTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPNAAGMVPVSMNPGPNMGQPQPGMTSNGPLPDPSMIRGSVPNQMMPRITPQSGLNQFGQMSMAQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNIPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTPTPHHTPPSIGAQQPPATTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQQVQPSLPAAPSADQPQQQPRSQQSTAASVPTPTAPLLPPQPATPLSQPAVSIEGQVSNPPSTSSTEVNSQAIAEKQPSQEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELKTEIKEEEDQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPAGFVCDGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVVGQQQGLPSPTPATPTTPTGQQPTTPQTPQPTSQPQPTPPNSMPPYLPRTQAAGPVSQGKAAGQVTPPTPPQTAQPPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPPMTPMAPMGMNPPPMTRGPSGHLEPGMGPTGMQQQPPWSQGGLPQPQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGISPLKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPIPGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGMANHNQFQQPQGVGYPPQQQQRMQHHMQQMQQGNMGQIGQLPQALGAEAGASLQAYQQRLLQQQMGSPVQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPGLVAAQANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNSDLNSNLSQSTLDIH | |||||||
Modified residue (large scale data) | 12 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 89 | UniProt | Phosphoserine; by AMPK | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 285 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 418 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 423 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 499 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 499 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 580 | UniProt | Asymmetric dimethylarginine; by CARM1 | ||||
Sequence: R | |||||||
Modified residue | 604 | UniProt | Asymmetric dimethylarginine; by CARM1 | ||||
Sequence: R | |||||||
Modified residue | 636 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 885 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 887 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 890 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 977 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 992 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1020 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 1020 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | |||||||
Modified residue | 1024 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 1024 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1037 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1038 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1038 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1180 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 1336 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 1473 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 1499 | UniProt | N6-acetyllysine; by autocatalysis | ||||
Sequence: K | |||||||
Modified residue | 1542 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 1546 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 1549 | UniProt | N6-acetyllysine; by autocatalysis | ||||
Sequence: K | |||||||
Modified residue | 1554 | UniProt | N6-acetyllysine; by autocatalysis | ||||
Sequence: K | |||||||
Modified residue | 1555 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 1558 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 1560 | UniProt | N6-acetyllysine; by autocatalysis | ||||
Sequence: K | |||||||
Modified residue | 1583 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 1699 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 1704 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 1707 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1724 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1726 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1726 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1906 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1909 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1913 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2142 | UniProt | Asymmetric dimethylarginine; by CARM1; alternate | ||||
Sequence: R | |||||||
Modified residue | 2142 | UniProt | Citrulline; by PADI4; alternate | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 2309 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2315 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2320 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2325 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2326 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2328 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
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.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with HIF1A; the interaction is stimulated in response to hypoxia and inhibited by CITED2 (PubMed:11959990, PubMed:9887100).
Probably part of a complex with HIF1A and CREBBP (PubMed:8917528).
Interacts (via N-terminus) with TFAP2A (via N-terminus); the interaction requires CITED2 (PubMed:12586840).
Interacts (via CH1 domain) with CITED2 (via C-terminus) (PubMed:12586840, PubMed:12778114).
Interacts with CITED1 (unphosphorylated form preferentially and via C-terminus) (PubMed:10722728, PubMed:16864582).
Interacts with ESR1; the interaction is estrogen-dependent and enhanced by CITED1 (PubMed:11581164).
Interacts with HIPK2 (By similarity).
Interacts with DTX1, EID1, ELF3, FEN1, LEF1, NCOA1, NCOA6, NR3C1, PCAF, PELP1, PRDM6, SP1, SP3, SPIB, SRY, TCF7L2, DDX5, DDX17, SATB1, SRCAP and TRERF1 (PubMed:10823961, PubMed:11073989, PubMed:11073990, PubMed:11349124, PubMed:11430825, PubMed:11481323, PubMed:11564735, PubMed:11581372, PubMed:11864910, PubMed:12446687, PubMed:12527917, PubMed:12837748, PubMed:14605447, PubMed:15075319, PubMed:15297880, PubMed:16478997, PubMed:17226766, PubMed:8684459, PubMed:9590696).
Interacts with JMY, the complex activates p53/TP53 transcriptional activity (PubMed:10518217, PubMed:11511361).
Interacts with TTC5/STRAP; the interaction facilitates the association between JMY and p300/EP300 cofactors (PubMed:11511361).
Interacts with p53/TP53; the interaction is facilitated by TTC5/STRAP (PubMed:15186775, PubMed:15448695, PubMed:19217391).
Forms a complex with TTC5/STRAP and HSF1; these interactions augment chromatin-bound HSF1 and p300/EP300 histone acetyltransferase activity (PubMed:18451878).
Part of a complex containing CARM1 and NCOA2/GRIP1 (PubMed:11701890, PubMed:11997499, PubMed:15731352).
Interacts with ING4 and this interaction may be indirect (PubMed:12750254).
Interacts with ING5 (PubMed:12750254).
Interacts with the C-terminal region of CITED4 (PubMed:11744733).
Non-sumoylated EP300 preferentially interacts with SENP3 (PubMed:19680224).
Interacts with SS18L1/CREST (PubMed:14716005).
Interacts with ALX1 (via homeobox domain) (PubMed:12929931).
Interacts with NEUROD1; the interaction is inhibited by NR0B2 (PubMed:14752053).
Interacts with TCF3 (PubMed:14752053).
Interacts (via CREB-binding domain) with MYOCD (via C-terminus) (By similarity).
Interacts with ROCK2 and PPARG (PubMed:11518699, PubMed:16574662).
Forms a complex made of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy in cardiomyocytes (PubMed:20081228).
Interacts with IRF1 and this interaction enhances acetylation of p53/TP53 and stimulation of its activity (PubMed:15509808).
Interacts with ALKBH4 and DDIT3/CHOP (PubMed:17872950, PubMed:23145062).
Interacts with KLF15 (PubMed:23999430).
Interacts with CEBPB and RORA (PubMed:9862959).
Interacts with NPAS2, BMAL1 and CLOCK (PubMed:14645221).
Interacts with SIRT2 isoform 1, isoform 2 and isoform 5 (PubMed:24177535).
Interacts with MTA1 (PubMed:16617102).
Interacts with HDAC4 and HDAC5 in the presence of TFAP2C (PubMed:24413532).
Interacts with TRIP4 (PubMed:25219498).
Directly interacts with ZBTB49; this interaction leads to synergistic transactivation of CDKN1A (PubMed:25245946).
Interacts with NR4A3 (By similarity).
Interacts with ZNF451 (PubMed:24324267).
Interacts with ATF5; EP300 is required for ATF5 and CEBPB interaction and DNA binding (By similarity).
Interacts with HSF1 (PubMed:27189267).
Interacts with ZBTB48/TZAP (PubMed:24382891).
Interacts with STAT1; the interaction is enhanced upon IFN-gamma stimulation (PubMed:26479788).
Interacts with HNRNPU (via C-terminus); this interaction enhances DNA-binding of HNRNPU to nuclear scaffold/matrix attachment region (S/MAR) elements (PubMed:11909954).
Interacts with BCL11B (PubMed:16809611, PubMed:27959755).
Interacts with SMAD4; negatively regulated by ZBTB7A (PubMed:25514493).
Interacts with DUX4 (via C-terminus) (PubMed:26951377).
Interacts with NUPR1; this interaction enhances the effect of EP300 on PAX2 transcription factor activity (PubMed:11940591).
Interacts with RXRA; the interaction is decreased by 9-cis retinoic acid (PubMed:17761950).
NR4A1 competes with EP300 for interaction with RXRA and thereby attenuates EP300 mediated acetylation of RXRA (PubMed:17761950).
Interacts with RB1 (By similarity).
Interacts with DDX3X; this interaction may facilitate HNF4A acetylation (PubMed:28128295).
Interacts with SOX9 (PubMed:12732631).
Interacts with ATF4; EP300/p300 stabilizes ATF4 and increases its transcriptional activity independently of its catalytic activity by preventing its ubiquitination (PubMed:16219772).
Interacts with KAT5; promoting KAT5 autoacetylation (PubMed:24835996).
Interacts (via bromo domain) with (acetylated) STAT3; interaction takes place following STAT3 acetylation by EP300 and promotes enhanceosome assembly (PubMed:18782771).
Probably part of a complex with HIF1A and CREBBP (PubMed:8917528).
Interacts (via N-terminus) with TFAP2A (via N-terminus); the interaction requires CITED2 (PubMed:12586840).
Interacts (via CH1 domain) with CITED2 (via C-terminus) (PubMed:12586840, PubMed:12778114).
Interacts with CITED1 (unphosphorylated form preferentially and via C-terminus) (PubMed:10722728, PubMed:16864582).
Interacts with ESR1; the interaction is estrogen-dependent and enhanced by CITED1 (PubMed:11581164).
Interacts with HIPK2 (By similarity).
Interacts with DTX1, EID1, ELF3, FEN1, LEF1, NCOA1, NCOA6, NR3C1, PCAF, PELP1, PRDM6, SP1, SP3, SPIB, SRY, TCF7L2, DDX5, DDX17, SATB1, SRCAP and TRERF1 (PubMed:10823961, PubMed:11073989, PubMed:11073990, PubMed:11349124, PubMed:11430825, PubMed:11481323, PubMed:11564735, PubMed:11581372, PubMed:11864910, PubMed:12446687, PubMed:12527917, PubMed:12837748, PubMed:14605447, PubMed:15075319, PubMed:15297880, PubMed:16478997, PubMed:17226766, PubMed:8684459, PubMed:9590696).
Interacts with JMY, the complex activates p53/TP53 transcriptional activity (PubMed:10518217, PubMed:11511361).
Interacts with TTC5/STRAP; the interaction facilitates the association between JMY and p300/EP300 cofactors (PubMed:11511361).
Interacts with p53/TP53; the interaction is facilitated by TTC5/STRAP (PubMed:15186775, PubMed:15448695, PubMed:19217391).
Forms a complex with TTC5/STRAP and HSF1; these interactions augment chromatin-bound HSF1 and p300/EP300 histone acetyltransferase activity (PubMed:18451878).
Part of a complex containing CARM1 and NCOA2/GRIP1 (PubMed:11701890, PubMed:11997499, PubMed:15731352).
Interacts with ING4 and this interaction may be indirect (PubMed:12750254).
Interacts with ING5 (PubMed:12750254).
Interacts with the C-terminal region of CITED4 (PubMed:11744733).
Non-sumoylated EP300 preferentially interacts with SENP3 (PubMed:19680224).
Interacts with SS18L1/CREST (PubMed:14716005).
Interacts with ALX1 (via homeobox domain) (PubMed:12929931).
Interacts with NEUROD1; the interaction is inhibited by NR0B2 (PubMed:14752053).
Interacts with TCF3 (PubMed:14752053).
Interacts (via CREB-binding domain) with MYOCD (via C-terminus) (By similarity).
Interacts with ROCK2 and PPARG (PubMed:11518699, PubMed:16574662).
Forms a complex made of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy in cardiomyocytes (PubMed:20081228).
Interacts with IRF1 and this interaction enhances acetylation of p53/TP53 and stimulation of its activity (PubMed:15509808).
Interacts with ALKBH4 and DDIT3/CHOP (PubMed:17872950, PubMed:23145062).
Interacts with KLF15 (PubMed:23999430).
Interacts with CEBPB and RORA (PubMed:9862959).
Interacts with NPAS2, BMAL1 and CLOCK (PubMed:14645221).
Interacts with SIRT2 isoform 1, isoform 2 and isoform 5 (PubMed:24177535).
Interacts with MTA1 (PubMed:16617102).
Interacts with HDAC4 and HDAC5 in the presence of TFAP2C (PubMed:24413532).
Interacts with TRIP4 (PubMed:25219498).
Directly interacts with ZBTB49; this interaction leads to synergistic transactivation of CDKN1A (PubMed:25245946).
Interacts with NR4A3 (By similarity).
Interacts with ZNF451 (PubMed:24324267).
Interacts with ATF5; EP300 is required for ATF5 and CEBPB interaction and DNA binding (By similarity).
Interacts with HSF1 (PubMed:27189267).
Interacts with ZBTB48/TZAP (PubMed:24382891).
Interacts with STAT1; the interaction is enhanced upon IFN-gamma stimulation (PubMed:26479788).
Interacts with HNRNPU (via C-terminus); this interaction enhances DNA-binding of HNRNPU to nuclear scaffold/matrix attachment region (S/MAR) elements (PubMed:11909954).
Interacts with BCL11B (PubMed:16809611, PubMed:27959755).
Interacts with SMAD4; negatively regulated by ZBTB7A (PubMed:25514493).
Interacts with DUX4 (via C-terminus) (PubMed:26951377).
Interacts with NUPR1; this interaction enhances the effect of EP300 on PAX2 transcription factor activity (PubMed:11940591).
Interacts with RXRA; the interaction is decreased by 9-cis retinoic acid (PubMed:17761950).
NR4A1 competes with EP300 for interaction with RXRA and thereby attenuates EP300 mediated acetylation of RXRA (PubMed:17761950).
Interacts with RB1 (By similarity).
Interacts with DDX3X; this interaction may facilitate HNF4A acetylation (PubMed:28128295).
Interacts with SOX9 (PubMed:12732631).
Interacts with ATF4; EP300/p300 stabilizes ATF4 and increases its transcriptional activity independently of its catalytic activity by preventing its ubiquitination (PubMed:16219772).
Interacts with KAT5; promoting KAT5 autoacetylation (PubMed:24835996).
Interacts (via bromo domain) with (acetylated) STAT3; interaction takes place following STAT3 acetylation by EP300 and promotes enhanceosome assembly (PubMed:18782771).
(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.
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif, compositional bias, zinc finger, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-29 | Disordered | ||||
Sequence: MAENVVEPGPPSAKRPKLSSPALSASASD | ||||||
Region | 2-139 | Interaction with ALX1 | ||||
Sequence: AENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDINQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQSSPGLGLINSMVKSPMTQAGLTSPNMGMG | ||||||
Region | 2-149 | Interaction with RORA | ||||
Sequence: AENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDINQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQSSPGLGLINSMVKSPMTQAGLTSPNMGMGTSGPNQGPTQ | ||||||
Motif | 11-17 | Nuclear localization signal | ||||
Sequence: PSAKRPK | ||||||
Region | 133-157 | Disordered | ||||
Sequence: SPNMGMGTSGPNQGPTQSTGMMNSP | ||||||
Compositional bias | 196-234 | Polar residues | ||||
Sequence: IGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQT | ||||||
Region | 196-235 | Disordered | ||||
Sequence: IGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTG | ||||||
Zinc finger | 331-417 | TAZ-type 1 | ||||
Sequence: DPEKRKLIQQQLVLLLHAHKCQRREQANGEVRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPL | ||||||
Region | 482-518 | Disordered | ||||
Sequence: TQPQVQAKNQQNQQPGQSPQGMRPMSNMSASPMGVNG | ||||||
Domain | 566-645 | KIX | ||||
Sequence: GIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELE | ||||||
Region | 729-1050 | Disordered | ||||
Sequence: QTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNIPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTPTPHHTPPSIGAQQPPATTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQQVQPSLPAAPSADQPQQQPRSQQSTAASVPTPTAPLLPPQPATPLSQPAVSIEGQVSNPPSTSSTEVNSQAIAEKQPSQEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELKTEIKEEEDQPSTSATQSSPAPGQSKKKIFK | ||||||
Compositional bias | 753-811 | Polar residues | ||||
Sequence: PRMQQPSNQGQFLPQTQFPSQGMNVTNIPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPG | ||||||
Compositional bias | 827-849 | Pro residues | ||||
Sequence: LHQNSPSPVPSRTPTPHHTPPSI | ||||||
Compositional bias | 857-895 | Pro residues | ||||
Sequence: TTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQ | ||||||
Compositional bias | 896-926 | Polar residues | ||||
Sequence: QVQPSLPAAPSADQPQQQPRSQQSTAASVPT | ||||||
Compositional bias | 941-971 | Polar residues | ||||
Sequence: SQPAVSIEGQVSNPPSTSSTEVNSQAIAEKQ | ||||||
Compositional bias | 974-1029 | Basic and acidic residues | ||||
Sequence: QEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELKTEIKEEEDQ | ||||||
Region | 1017-1029 | CRD1; mediates transcriptional repression | ||||
Sequence: TELKTEIKEEEDQ | ||||||
Domain | 1067-1139 | Bromo | ||||
Sequence: RQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVY | ||||||
Domain | 1287-1663 | CBP/p300-type HAT | ||||
Sequence: KFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQ | ||||||
Region | 1397-1399 | Interaction with histone | ||||
Sequence: YLD | ||||||
Compositional bias | 1520-1547 | Basic and acidic residues | ||||
Sequence: LEQEEEERKREENTSNESTDVTKGDSKN | ||||||
Region | 1520-1578 | Disordered | ||||
Sequence: LEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGMPNVSN | ||||||
Compositional bias | 1548-1565 | Basic residues | ||||
Sequence: AKKKNNKKTSKNKSSLSR | ||||||
Region | 1572-1818 | Binding region for E1A adenovirus | ||||
Sequence: GMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCPVPFCLNIKQKLRQQQL | ||||||
Zinc finger | 1665-1713 | ZZ-type | ||||
Sequence: RFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLD | ||||||
Zinc finger | 1728-1809 | TAZ-type 2 | ||||
Sequence: GDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCPVPFCLNI | ||||||
Region | 1833-1924 | Disordered | ||||
Sequence: ASMQRTGVVGQQQGLPSPTPATPTTPTGQQPTTPQTPQPTSQPQPTPPNSMPPYLPRTQAAGPVSQGKAAGQVTPPTPPQTAQPPLPGPPPA | ||||||
Compositional bias | 1851-1886 | Pro residues | ||||
Sequence: TPATPTTPTGQQPTTPQTPQPTSQPQPTPPNSMPPY | ||||||
Compositional bias | 1909-1924 | Pro residues | ||||
Sequence: TPPQTAQPPLPGPPPA | ||||||
Region | 1980-2010 | Disordered | ||||
Sequence: LEPGMGPTGMQQQPPWSQGGLPQPQQLQSGM | ||||||
Compositional bias | 1989-2010 | Polar residues | ||||
Sequence: MQQQPPWSQGGLPQPQQLQSGM | ||||||
Region | 2003-2212 | Interaction with HTLV-1 Tax | ||||
Sequence: PQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGISPLKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPIPGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGMANHNQFQ | ||||||
Region | 2041-2240 | Interaction with NCOA2 | ||||
Sequence: LKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPIPGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGMANHNQFQQPQGVGYPPQQQQRMQHHMQQMQQGNMG | ||||||
Region | 2094-2163 | Disordered | ||||
Sequence: NSNPQPIPGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGGMSP | ||||||
Compositional bias | 2100-2114 | Pro residues | ||||
Sequence: IPGQPGMPQGQPGLQ | ||||||
Compositional bias | 2115-2163 | Polar residues | ||||
Sequence: PPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGGMSP | ||||||
Region | 2186-2237 | Disordered | ||||
Sequence: QQMMQQQQQQGAGPGIGPGMANHNQFQQPQGVGYPPQQQQRMQHHMQQMQQG | ||||||
Compositional bias | 2206-2237 | Polar residues | ||||
Sequence: ANHNQFQQPQGVGYPPQQQQRMQHHMQQMQQG | ||||||
Compositional bias | 2267-2310 | Polar residues | ||||
Sequence: QQMGSPVQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSP | ||||||
Region | 2267-2385 | Disordered | ||||
Sequence: QQMGSPVQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPGLVAAQANPMEQGHFASPDQNSMLSQLASNPGMANL | ||||||
Compositional bias | 2311-2342 | Pro residues | ||||
Sequence: QPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSP | ||||||
Compositional bias | 2362-2385 | Polar residues | ||||
Sequence: GHFASPDQNSMLSQLASNPGMANL |
Domain
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.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,414
- Mass (Da)264,161
- Last updated2009-02-10 v2
- Checksum8E869E1F174A6FEB
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0U1RR87 | A0A0U1RR87_HUMAN | EP300 | 187 | ||
A0A994J6T4 | A0A994J6T4_HUMAN | EP300 | 634 | ||
A0A669KB12 | A0A669KB12_HUMAN | EP300 | 2388 | ||
A0A994J3N7 | A0A994J3N7_HUMAN | EP300 | 473 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 169 | in Ref. 1; AAA18639 | ||||
Sequence: M → T | ||||||
Compositional bias | 196-234 | Polar residues | ||||
Sequence: IGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQT | ||||||
Sequence conflict | 204 | in Ref. 1; AAA18639 | ||||
Sequence: N → D | ||||||
Compositional bias | 753-811 | Polar residues | ||||
Sequence: PRMQQPSNQGQFLPQTQFPSQGMNVTNIPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPG | ||||||
Compositional bias | 827-849 | Pro residues | ||||
Sequence: LHQNSPSPVPSRTPTPHHTPPSI | ||||||
Compositional bias | 857-895 | Pro residues | ||||
Sequence: TTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQ | ||||||
Compositional bias | 896-926 | Polar residues | ||||
Sequence: QVQPSLPAAPSADQPQQQPRSQQSTAASVPT | ||||||
Sequence conflict | 928 | in Ref. 1; AAA18639 | ||||
Sequence: T → N | ||||||
Compositional bias | 941-971 | Polar residues | ||||
Sequence: SQPAVSIEGQVSNPPSTSSTEVNSQAIAEKQ | ||||||
Compositional bias | 974-1029 | Basic and acidic residues | ||||
Sequence: QEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELKTEIKEEEDQ | ||||||
Compositional bias | 1520-1547 | Basic and acidic residues | ||||
Sequence: LEQEEEERKREENTSNESTDVTKGDSKN | ||||||
Compositional bias | 1548-1565 | Basic residues | ||||
Sequence: AKKKNNKKTSKNKSSLSR | ||||||
Compositional bias | 1851-1886 | Pro residues | ||||
Sequence: TPATPTTPTGQQPTTPQTPQPTSQPQPTPPNSMPPY | ||||||
Compositional bias | 1909-1924 | Pro residues | ||||
Sequence: TPPQTAQPPLPGPPPA | ||||||
Sequence conflict | 1924 | in Ref. 1; AAA18639 | ||||
Sequence: A → T | ||||||
Compositional bias | 1989-2010 | Polar residues | ||||
Sequence: MQQQPPWSQGGLPQPQQLQSGM | ||||||
Compositional bias | 2100-2114 | Pro residues | ||||
Sequence: IPGQPGMPQGQPGLQ | ||||||
Compositional bias | 2115-2163 | Polar residues | ||||
Sequence: PPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGGMSP | ||||||
Compositional bias | 2206-2237 | Polar residues | ||||
Sequence: ANHNQFQQPQGVGYPPQQQQRMQHHMQQMQQG | ||||||
Compositional bias | 2267-2310 | Polar residues | ||||
Sequence: QQMGSPVQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSP | ||||||
Compositional bias | 2311-2342 | Pro residues | ||||
Sequence: QPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSP | ||||||
Compositional bias | 2362-2385 | Polar residues | ||||
Sequence: GHFASPDQNSMLSQLASNPGMANL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U01877 EMBL· GenBank· DDBJ | AAA18639.1 EMBL· GenBank· DDBJ | mRNA | ||
AL080243 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL096765 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL035658 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471095 EMBL· GenBank· DDBJ | EAW60408.1 EMBL· GenBank· DDBJ | Genomic DNA |