UniProtKB - Q09472 (EP300_HUMAN)

>sp|Q09472|EP300_HUMAN Histone acetyltransferase p300 OS=Homo sapiens OX=9606 GN=EP300 PE=1 SV=2
MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGD
INQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQSSPGLGLINS
MVKSPMTQAGLTSPNMGMGTSGPNQGPTQSTGMMNSPVNQPAMGMNTGMNAGMNPGMLAA
GNGQGIMPNQVMNGSIGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQ
PLKMGMMNNPNPYGSPYTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAMDKKAVPGGGMP
NMGQQPAPQVQQPGLVTPVAQGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGE
VRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNA
GDKRNQQPILTGAPVGLGNPSSLGVGQQSAPNLSTVSQIDPSSIERAYAALGLPYQVNQM
PTQPQVQAKNQQNQQPGQSPQGMRPMSNMSASPMGVNGGVGVQTPSLLSDSMLHSAINSQ
NPMMSENASVPSLGPMPTAAQPSTTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAAL
KDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPN
AAGMVPVSMNPGPNMGQPQPGMTSNGPLPDPSMIRGSVPNQMMPRITPQSGLNQFGQMSM
AQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNI
PLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTP
TPHHTPPSIGAQQPPATTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQQVQPS
LPAAPSADQPQQQPRSQQSTAASVPTPTAPLLPPQPATPLSQPAVSIEGQVSNPPSTSST
EVNSQAIAEKQPSQEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELK
TEIKEEEDQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVD
PQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYK
YCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHF
CEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVL
HHEIIWPAGFVCDGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGE
VTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQE
YGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPP
SEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKE
LPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNK
SSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIP
CDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETR
WHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQ
SLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENK
CPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVVGQQQGLPSPTPATPTTPTG
QQPTTPQTPQPTSQPQPTPPNSMPPYLPRTQAAGPVSQGKAAGQVTPPTPPQTAQPPLPG
PPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPPMTPMAPMGMNPPPMTRGPSGHL
EPGMGPTGMQQQPPWSQGGLPQPQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGISP
LKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPI
PGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGG
MSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGMANHNQFQQPQGVGYP
PQQQQRMQHHMQQMQQGNMGQIGQLPQALGAEAGASLQAYQQRLLQQQMGSPVQPNPMSP
QQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHV
SPQTSSPHPGLVAAQANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNS
DLNSNLSQSTLDIH

Entry version 240 (10 Apr 2019)
Sequence version 2 (10 Feb 2009)
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Protein

Histone acetyltransferase p300

Gene

EP300

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Functions as histone acetyltransferase and regulates transcription via chromatin remodeling (PubMed:23415232, PubMed:23934153, PubMed:8945521). Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation (PubMed:23415232, PubMed:23934153, PubMed:8945521). Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. 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-27' (H3K27ac) (PubMed:23911289). Also functions as acetyltransferase for non-histone targets, such as ALX1, HDAC1, PRMT1 or SIRT2 (PubMed:12929931, PubMed:16762839, PubMed:18722353). Acetylates 'Lys-131' of ALX1 and acts as its coactivator (PubMed:12929931). Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function (PubMed:18722353). Acetylates HDAC1 leading to its inactivation and modulation of transcription (PubMed:16762839). 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. Can also mediate transcriptional repression. Acetylates FOXO1 and enhances its transcriptional activity (PubMed:15890677). 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 degragation, this mechanism may be involved in CD4/CD8 lineage differentiation (PubMed:20810990). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA), butanoyl-CoA (butyryl-CoA) or propanoyl-CoA (propionyl-CoA), and is able to mediate protein crotonylation, butyrylation or propionylation, respectively (PubMed:25818647, PubMed:17267393). 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 (E)-but-2-enoyl-CoA (crotonyl-CoA) concentration is low (PubMed:25818647). Also acts as a histone butyryltransferase; butyrylation marks active promoters (PubMed:17267393). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (PubMed:25514493). Acetylates PCK1 and promotes PCK1 anaplerotic activity (PubMed:30193097).By similarity1 Publication24 Publications

(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.2 Publications

Catalytic activityⁱ

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	347	Zinc 1	1
Metal bindingⁱ	351	Zinc 1	1
Metal bindingⁱ	364	Zinc 1	1
Metal bindingⁱ	369	Zinc 1	1
Metal bindingⁱ	378	Zinc 2	1
Metal bindingⁱ	382	Zinc 2	1
Metal bindingⁱ	388	Zinc 2	1
Metal bindingⁱ	393	Zinc 2	1
Metal bindingⁱ	402	Zinc 3	1
Metal bindingⁱ	406	Zinc 3	1
Metal bindingⁱ	411	Zinc 3	1
Metal bindingⁱ	414	Zinc 3	1
Binding siteⁱ	1457	Acetyl-CoA; via carbonyl oxygen1 Publication	1
Binding siteⁱ	1462	Acetyl-CoA1 Publication	1
Binding siteⁱ	1466	Acetyl-CoA1 Publication	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Zinc fingerⁱ	331 – 417	TAZ-type 1PROSITE-ProRule annotationAdd BLAST	87
Zinc fingerⁱ	1664 – 1707	ZZ-typePROSITE-ProRule annotationAdd BLAST	44
Zinc fingerⁱ	1728 – 1809	TAZ-type 2PROSITE-ProRule annotationAdd BLAST	82

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Acyltransferase, Transferase
Biological process	Biological rhythms, Cell cycle, Host-virus interaction, Transcription, Transcription regulation
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

BRENDAⁱ	2.3.1.48 2681
Reactomeⁱ	R-HSA-1234158 Regulation of gene expression by Hypoxia-inducible Factor R-HSA-1368082 RORA activates gene expression 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-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-400253 Circadian Clock 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-6781823 Formation of TC-NER Pre-Incision Complex R-HSA-6781827 Transcription-Coupled Nucleotide Excision Repair (TC-NER) R-HSA-6782135 Dual incision in TC-NER R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER 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 R-HSA-9013508 NOTCH3 Intracellular Domain Regulates Transcription R-HSA-9013695 NOTCH4 Intracellular Domain Regulates Transcription R-HSA-9018519 Estrogen-dependent gene expression R-HSA-918233 TRAF3-dependent IRF activation pathway R-HSA-933541 TRAF6 mediated IRF7 activation R-HSA-9614657 FOXO-mediated transcription of cell death genes R-HSA-9617629 Regulation of FOXO transcriptional activity by acetylation
SignaLinkⁱ	Q09472
SIGNORⁱ	Q09472

Protein family/group databases

MoonDBⁱ	Q09472 Predicted

MoonDBⁱ

Q09472 Predicted

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Histone acetyltransferase p300 (EC:2.3.1.483 Publications) Short name: p300 HAT Alternative name(s): E1A-associated protein p300 Histone butyryltransferase p300 (EC:2.3.1.-1 Publication) Histone crotonyltransferase p300 (EC:2.3.1.-1 Publication) Protein propionyltransferase p300 (EC:2.3.1.-1 Publication)
Gene namesⁱ	Name:EP300 Synonyms:P300
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 22

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000100393.10
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:3373 EP300
MIMⁱ	602700 gene
neXtProtⁱ	NX_Q09472

Keywords - Cellular componentⁱ

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechⁱ

Involvement in diseaseⁱ

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)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by craniofacial abnormalities, postnatal growth deficiency, broad thumbs, broad big toes, mental retardation 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.

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	89	S → A: Abolishes AMPK-mediated phosphorylation. 1 Publication	1
Mutagenesisⁱ	89	S → D: Phosphomimetic mutant that leads to descreased interaction with nuclear receptors. 1 Publication	1
Mutagenesisⁱ	344	L → A: Inhibits interaction with HIF1A and transcription activation; when associated with A-345. 1 Publication	1
Mutagenesisⁱ	345	L → A: Inhibits interaction with HIF1A and transcription activation; when associated with A-344. 1 Publication	1
Mutagenesisⁱ	371 – 376	TMKNVL → NAAIRS: Inhibits interaction with HIF1A. Reduces interaction with CITED2. 1 Publication	6
Mutagenesisⁱ	413 – 418	VCLPLK → NAAIRS: Inhibits interaction with HIF1A. Does not inhibit interaction with CITED2. 1 Publication	6
Mutagenesisⁱ	1020	K → A: Abolishes sumoylation and transcriptional repression when associated with A-1024. 2 Publications	1
Mutagenesisⁱ	1020	K → R: Abolishes sumoylation and transcriptional repression; when associated with R-1024. 2 Publications	1
Mutagenesisⁱ	1024	K → A: Abolishes sumoylation and transcriptional repression; when associated with A-1020. 2 Publications	1
Mutagenesisⁱ	1024	K → R: Abolishes sumoylation and transcriptional repression; when associated with R-1020. 2 Publications	1
Mutagenesisⁱ	1170	F → E: Increased acetyltransferase activity. 1 Publication	1
Mutagenesisⁱ	1204	C → R: Increased acetyltransferase activity. 1 Publication	1
Mutagenesisⁱ	1242	E → K: Increased acetyltransferase activity. 1 Publication	1
Mutagenesisⁱ	1357	T → L: 40% decrease in activity. 1 Publication	1
Mutagenesisⁱ	1357	T → R: 40% decrease in activity. 90% decrease in activity; when associated with R-1505; R-1625 and R-1628. 1 Publication	1
Mutagenesisⁱ	1396	S → R: Loss of activity; when associated with R-1397. 1 Publication	1
Mutagenesisⁱ	1396	S → W: Loss of activity; when associated with W-1396. 1 Publication	1
Mutagenesisⁱ	1397	Y → R: Loss of activity; when associated with R-1396. 1 Publication	1
Mutagenesisⁱ	1397	Y → W: Loss of activity; when associated with W-1397. 1 Publication	1
Mutagenesisⁱ	1399	D → Y: 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. 3 Publications	1
Mutagenesisⁱ	1467	Y → F: Abolishes autoacetylation. Loss of acetyltransferase activity. 1 Publication	1
Mutagenesisⁱ	1505	E → R: 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. 1 Publication	1
Mutagenesisⁱ	1625	D → R: 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. 1 Publication	1
Mutagenesisⁱ	1628	D → R: 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. 1 Publication	1
Mutagenesisⁱ	1645 – 1646	RR → EE: Increased acetyltransferase activity. 1 Publication	2
Mutagenesisⁱ	2056	R → K: No effect on interaction with NCOA2. 1 Publication	1
Mutagenesisⁱ	2088	R → K: Abolishes interaction with NCOA2. 1 Publication	1
Mutagenesisⁱ	2142	R → K: Strongly reduces interaction with NCOA2. 1 Publication	1

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	31 – 32	Breakpoint for translocation to form KAT6A-EP300 and EP300-KAT6A		2

Keywords - Diseaseⁱ

Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	2033
GeneReviewsⁱ	EP300
MalaCards human disease database More...MalaCardsⁱ	EP300
MIMⁱ	613684 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000100393
Orphanetⁱ	353284 Rubinstein-Taybi syndrome due to EP300 haploinsufficiency
PharmGKBⁱ	PA27807

Chemistry databases

ChEMBLⁱ	CHEMBL3784
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2735

Polymorphism and mutation databases

BioMutaⁱ	EP300
DMDMⁱ	223590203

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources
ChainⁱPRO_0000211193	2 – 2414	Histone acetyltransferase p300Add BLAST		2413

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylalanineCombined sources	1
Modified residueⁱ	89	Phosphoserine; by AMPK2 Publications	1
Modified residueⁱ	418	N6-acetyllysine1 Publication	1
Modified residueⁱ	423	N6-acetyllysine1 Publication	1
Modified residueⁱ	499	PhosphoserineBy similarity	1
Modified residueⁱ	580	Omega-N-methylated arginine; by CARM11 Publication	1
Modified residueⁱ	604	Omega-N-methylated arginine; by CARM11 Publication	1
Modified residueⁱ	636	N6-acetyllysineCombined sources	1
Modified residueⁱ	977	N6-acetyllysineCombined sources	1
Modified residueⁱ	1020	N6-acetyllysine; alternate1 Publication	1
Cross-linkⁱ	1020	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Modified residueⁱ	1024	N6-acetyllysine; alternate1 Publication	1
Cross-linkⁱ	1024	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Modified residueⁱ	1038	PhosphoserineCombined sources	1
Modified residueⁱ	1180	N6-acetyllysineBy similarity	1
Modified residueⁱ	1336	N6-acetyllysine1 Publication	1
Modified residueⁱ	1473	N6-acetyllysine1 Publication	1
Modified residueⁱ	1499	N6-acetyllysine; by autocatalysis1 Publication	1
Modified residueⁱ	1542	N6-acetyllysineCombined sources1 Publication	1
Modified residueⁱ	1546	N6-acetyllysineCombined sources1 Publication	1
Modified residueⁱ	1549	N6-acetyllysine; by autocatalysis2 Publications	1
Modified residueⁱ	1554	N6-acetyllysine; by autocatalysisCombined sources1 Publication	1
Modified residueⁱ	1555	N6-acetyllysineCombined sources	1
Modified residueⁱ	1558	N6-acetyllysineCombined sources1 Publication	1
Modified residueⁱ	1560	N6-acetyllysine; by autocatalysisCombined sources1 Publication	1
Modified residueⁱ	1583	N6-acetyllysineCombined sources	1
Modified residueⁱ	1699	N6-acetyllysine1 Publication	1
Modified residueⁱ	1704	N6-acetyllysine1 Publication	1
Modified residueⁱ	1707	N6-acetyllysine1 Publication	1
Modified residueⁱ	1726	PhosphoserineCombined sources	1
Modified residueⁱ	2142	Asymmetric dimethylarginine; by CARM1; alternate1 Publication	1
Modified residueⁱ	2142	Citrulline; by PADI4; alternate1 Publication	1

Post-translational modificationⁱ

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-1707.6 Publications

Citrullinated at Arg-2142 by PADI4, which impairs methylation by CARM1 and promotes interaction with NCOA2/GRIP1.2 Publications

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/GRIP1.2 Publications

Sumoylated; sumoylation in the transcriptional repression domain (CRD1) mediates transcriptional repression. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3.2 Publications

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.4 Publications

Keywords - PTMⁱ

Acetylation, Citrullination, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	Q09472
jPOSTⁱ	Q09472
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q09472
PaxDbⁱ	Q09472
PeptideAtlas More...PeptideAtlasⁱ	Q09472
PRIDEⁱ	Q09472
ProteomicsDBⁱ	58723

PTM databases

iPTMnetⁱ	Q09472
PhosphoSitePlusⁱ	Q09472

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000100393 Expressed in 233 organ(s), highest expression level in kidney
ExpressionAtlasⁱ	Q09472 baseline and differential
Genevisibleⁱ	Q09472 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB000146 HPA003128 HPA004112

HPAⁱ

CAB000146
HPA003128
HPA004112

Interactionⁱ

Subunit structureⁱ

Interacts with phosphorylated CREB1. Interacts with HIF1A; the interaction is stimulated in response to hypoxia and inhibited by CITED2. 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 DTX1, EID1, ELF3, FEN1, LEF1, NCOA1, NCOA6, NR3C1, PCAF, PELP1, PRDM6, SP1, SP3, SPIB, SRY, TCF7L2, TP53, DDX5, DDX17, SATB1, SRCAP, TTC5, JMY and TRERF1. The TAZ-type 1 domain interacts with HIF1A. Probably part of a complex with HIF1A and CREBBP. 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). Binds to HIPK2. 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 FOXO1; the interaction acetylates FOXO1 and enhances its transcriptional activity. Interacts with ALKBH4 and DDIT3/CHOP. Interacts with KLF15. Interacts with CEBPB and RORA. Interacts with p30II. Interacts with NPAS2, ARNTL/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 (PubMed:10722728, PubMed:10823961, PubMed:11073989, PubMed:11073990, PubMed:11349124, PubMed:11430825, PubMed:11481323, PubMed:11518699, PubMed:11559821, PubMed:11564735, PubMed:11581164, PubMed:11581372, PubMed:11701890, PubMed:11744733, PubMed:11864910, PubMed:11959990, PubMed:11997499, PubMed:12446687, PubMed:12527917, PubMed:12586840, PubMed:12750254, PubMed:12778114, PubMed:12837748, PubMed:12929931, PubMed:14605447, PubMed:14645221, PubMed:14716005, PubMed:14752053, PubMed:15075319, PubMed:15186775, PubMed:15297880, PubMed:15509808, PubMed:15731352, PubMed:15890677, PubMed:16478997, PubMed:16574662, PubMed:16617102, PubMed:16864582, PubMed:17226766, PubMed:17872950, PubMed:18273021, PubMed:19217391, PubMed:19680224, PubMed:20081228, PubMed:23145062, PubMed:23999430, PubMed:24177535, PubMed:24413532, PubMed:8684459, PubMed:8917528, PubMed:9528808, PubMed:9590696, PubMed:9862959, PubMed:9887100). 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:27959755, PubMed:16809611). 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).By similarity64 Publications

(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.1 Publication

(Microbial infection) Interacts with and acetylates HIV-1 Tat.3 Publications

(Microbial infection) Interacts with HTLV-1 proteins Tax, p30II and HBZ.3 Publications

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	2088	Interaction with NCOA2		1
Siteⁱ	2142	Interaction with NCOA2		1

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
	P03070	2	EBI-447295,EBI-617698	From Simian virus 40.
	P03255	3	EBI-447295,EBI-2603114	From Human adenovirus C serotype 5.
	P03255-2	3	EBI-447295,EBI-6859460	From a different organism.
	P03259	3	EBI-447295,EBI-6947456	From Human adenovirus A serotype 12.
ALKBH4	Q9NXW9	4	EBI-447295,EBI-8637516
APEX1	P27695	8	EBI-447295,EBI-1048805
ASH2L	Q9UBL3	5	EBI-447295,EBI-540797
AUTS2	Q8WXX7	3	EBI-447295,EBI-2875359
BICP0	K4P3M7	4	EBI-447295,EBI-11296047	From Bovine herpesvirus type 1.1.
BRD7	Q9NPI1	3	EBI-447295,EBI-711221
CDK2	P24941	5	EBI-447295,EBI-375096
CITED2	Q99967	3	EBI-447295,EBI-937732
COPS2	P61201	2	EBI-447295,EBI-1050386
CREB1	P16220	2	EBI-447295,EBI-711855
Creb1	Q01147	2	EBI-447295,EBI-2291098	From Mus musculus.
DDX5	P17844	4	EBI-447295,EBI-351962
E2	P03122	3	EBI-447295,EBI-7028618	From Bovine papillomavirus type 1.
E2	P06422	7	EBI-447295,EBI-7136851	From Human papillomavirus type 8.
E2	P06790	6	EBI-447295,EBI-7010629	From Human papillomavirus type 18.
ESR1	P03372	2	EBI-447295,EBI-78473
EWSR1	Q01844	2	EBI-447295,EBI-739737
FUS	P35637	4	EBI-447295,EBI-400434
GTF2B	Q00403	2	EBI-447295,EBI-389564
HIF1A	Q16665	20	EBI-447295,EBI-447269
Hif1a	Q61221	2	EBI-447295,EBI-298954	From Mus musculus.
HIPK2	Q9H2X6	4	EBI-447295,EBI-348345
Jmy	Q9QXM1	16	EBI-447295,EBI-866001	From Mus musculus.
KAT2B	Q92831	2	EBI-447295,EBI-477430
NAP1L1	P55209	3	EBI-447295,EBI-356392
NBN	O60934	5	EBI-447295,EBI-494844
NCOA3	Q9Y6Q9	2	EBI-447295,EBI-81196
POU3F2	P20265	3	EBI-447295,EBI-1167176
PPP1R13B	Q96KQ4	2	EBI-447295,EBI-1105153
PPP1R13L	Q8WUF5	2	EBI-447295,EBI-5550163
RUNX3	Q13761	7	EBI-447295,EBI-925990
SIRT1	Q96EB6	4	EBI-447295,EBI-1802965
SKP2	Q13309	3	EBI-447295,EBI-456291
SNAI1	O95863	3	EBI-447295,EBI-1045459
STAT6	P42226	2	EBI-447295,EBI-1186478
tat	P04608	3	EBI-447295,EBI-6164389	From Human immunodeficiency virus type 1 group M subtype B (isolate HXB2).
TBX21	Q9UL17	5	EBI-447295,EBI-3922312
TCL1A	P56279	4	EBI-447295,EBI-749995
TFAP2A	P05549	7	EBI-447295,EBI-347351
TP53	P04637	20	EBI-447295,EBI-366083
TP53BP2	Q13625	2	EBI-447295,EBI-77642
TP73	O15350	2	EBI-447295,EBI-389606
VDR	P11473	3	EBI-447295,EBI-286357
YBX1	P67809	2	EBI-447295,EBI-354065

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	108347, 523 interactors
CORUMⁱ	Q09472
Database of interacting proteins More...DIPⁱ	DIP-257N
IntActⁱ	Q09472, 197 interactors
Molecular INTeraction database More...MINTⁱ	Q09472
STRINGⁱ	9606.ENSP00000263253

Chemistry databases

BindingDBⁱ	Q09472

BindingDBⁱ

Q09472

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	332 – 334	Combined sources	3
Helixⁱ	335 – 355	Combined sources	21
Turnⁱ	356 – 358	Combined sources	3
Helixⁱ	367 – 379	Combined sources	13
Beta strandⁱ	386 – 389	Combined sources	4
Helixⁱ	391 – 405	Combined sources	15
Beta strandⁱ	408 – 410	Combined sources	3
Helixⁱ	414 – 418	Combined sources	5
Helixⁱ	1051 – 1066	Combined sources	16
Turnⁱ	1069 – 1072	Combined sources	4
Helixⁱ	1073 – 1075	Combined sources	3
Helixⁱ	1081 – 1084	Combined sources	4
Helixⁱ	1089 – 1092	Combined sources	4
Helixⁱ	1099 – 1107	Combined sources	9
Helixⁱ	1114 – 1131	Combined sources	18
Helixⁱ	1137 – 1160	Combined sources	24
Helixⁱ	1165 – 1168	Combined sources	4
Beta strandⁱ	1175 – 1177	Combined sources	3
Turnⁱ	1178 – 1180	Combined sources	3
Helixⁱ	1182 – 1190	Combined sources	9
Helixⁱ	1197 – 1205	Combined sources	9
Helixⁱ	1208 – 1216	Combined sources	9
Beta strandⁱ	1218 – 1221	Combined sources	4
Helixⁱ	1225 – 1245	Combined sources	21
Turnⁱ	1248 – 1250	Combined sources	3
Beta strandⁱ	1255 – 1257	Combined sources	3
Beta strandⁱ	1264 – 1272	Combined sources	9
Helixⁱ	1273 – 1278	Combined sources	6
Helixⁱ	1290 – 1292	Combined sources	3
Helixⁱ	1297 – 1313	Combined sources	17
Beta strandⁱ	1321 – 1334	Combined sources	14
Turnⁱ	1336 – 1338	Combined sources	3
Helixⁱ	1339 – 1342	Combined sources	4
Turnⁱ	1343 – 1347	Combined sources	5
Beta strandⁱ	1351 – 1366	Combined sources	16
Beta strandⁱ	1369 – 1381	Combined sources	13
Beta strandⁱ	1392 – 1400	Combined sources	9
Helixⁱ	1407 – 1409	Combined sources	3
Helixⁱ	1410 – 1428	Combined sources	19
Beta strandⁱ	1432 – 1436	Combined sources	5
Beta strandⁱ	1446 – 1450	Combined sources	5
Turnⁱ	1453 – 1455	Combined sources	3
Helixⁱ	1460 – 1476	Combined sources	17
Beta strandⁱ	1482 – 1485	Combined sources	4
Helixⁱ	1486 – 1493	Combined sources	8
Helixⁱ	1498 – 1500	Combined sources	3
Helixⁱ	1508 – 1517	Combined sources	10
Helixⁱ	1582 – 1590	Combined sources	9
Helixⁱ	1592 – 1594	Combined sources	3
Beta strandⁱ	1595 – 1601	Combined sources	7
Helixⁱ	1603 – 1606	Combined sources	4
Helixⁱ	1622 – 1624	Combined sources	3
Beta strandⁱ	1625 – 1627	Combined sources	3
Helixⁱ	1628 – 1636	Combined sources	9
Helixⁱ	1644 – 1662	Combined sources	19
Turnⁱ	1671 – 1673	Combined sources	3
Beta strandⁱ	1676 – 1688	Combined sources	13
Helixⁱ	1693 – 1696	Combined sources	4
Beta strandⁱ	1705 – 1708	Combined sources	4
Turnⁱ	1726 – 1728	Combined sources	3
Helixⁱ	1730 – 1747	Combined sources	18
Beta strandⁱ	1750 – 1752	Combined sources	3
Helixⁱ	1756 – 1770	Combined sources	15
Turnⁱ	1774 – 1778	Combined sources	5
Helixⁱ	1780 – 1793	Combined sources	14
Beta strandⁱ	1799 – 1802	Combined sources	4
Helixⁱ	1806 – 1818	Combined sources	13

Show more details

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1L3E	NMR	-	B	323-423	[»]
	1P4Q	NMR	-	B	323-423	[»]
	2K8F	NMR	-	A	1723-1812	[»]
	2MH0	NMR	-	B	1723-1812	[»]
	2MZD	NMR	-	A	1723-1812	[»]
	3BIY	X-ray	1.70	A	1287-1666	[»]
	3I3J	X-ray	2.33	A/B/C/D/E/F/G/H/I/J/K/L	1040-1161	[»]
	3IO2	X-ray	2.50	A	1723-1836	[»]
	3P57	X-ray	2.19	P	1726-1835	[»]
	3T92	X-ray	1.50	A	1723-1818	[»]
	4BHW	X-ray	2.80	A/B	1043-1519	[»]
				A/B	1581-1666	[»]
	4PZR	X-ray	2.10	A	1287-1664	[»]
	4PZS	X-ray	1.94	A	1287-1664	[»]
	4PZT	X-ray	2.80	A	1287-1664	[»]
	5BT3	X-ray	1.05	A	1048-1161	[»]
	5KJ2	X-ray	1.95	A	1287-1522	[»]
				A	1555-1666	[»]
	5LKT	X-ray	2.04	A	1043-1519	[»]
				A	1581-1666	[»]
	5LKU	X-ray	3.50	A	1043-1519	[»]
				A	1581-1666	[»]
	5LKX	X-ray	2.52	A	1043-1519	[»]
				A	1581-1666	[»]
	5LKZ	X-ray	2.50	A	1043-1519	[»]
				A	1581-1666	[»]
	5LPK	X-ray	2.10	A/B/C/D/E/F/G	1040-1161	[»]
	5LPM	X-ray	1.50	A/B	1048-1161	[»]
	5NU5	X-ray	1.60	A/B	1048-1161	[»]
	5XZC	electron microscopy	10.70	A	1046-1664	[»]
	5XZS	electron microscopy	9.80	A	1046-1664	[»]
	6DS6	X-ray	1.95	A	1661-1713	[»]
	6FGN	NMR	-	A	1723-1812	[»]
	6FGS	NMR	-	A	1723-1812	[»]
	6GYR	X-ray	3.10	A/B/C/D	1046-1664	[»]
	6GYT	X-ray	2.50	A/B	1047-1168	[»]
Database of protein disorder More...DisProtⁱ	DP00633
ProteinModelPortalⁱ	Q09472
SMRⁱ	Q09472
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q09472

EvolutionaryTraceⁱ

Q09472

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	566 – 645	KIXPROSITE-ProRule annotationAdd BLAST	80
Domainⁱ	1067 – 1139	BromoPROSITE-ProRule annotationAdd BLAST	73
Domainⁱ	1287 – 1663	CBP/p300-type HATPROSITE-ProRule annotationAdd BLAST	377

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	2 – 149	Interaction with RORA1 PublicationAdd BLAST	148
Regionⁱ	2 – 139	Interaction with ALX11 PublicationAdd BLAST	138
Regionⁱ	1017 – 1029	CRD1; mediates transcriptional repressionAdd BLAST	13
Regionⁱ	1397 – 1399	Interaction with histone1 Publication	3
Regionⁱ	1398 – 1400	Acetyl-CoA binding1 Publication	3
Regionⁱ	1410 – 1411	Acetyl-CoA binding1 Publication	2
Regionⁱ	1572 – 1818	Binding region for E1A adenovirusAdd BLAST	247
Regionⁱ	2003 – 2212	Interaction with HTLV-1 TaxAdd BLAST	210
Regionⁱ	2041 – 2240	Interaction with NCOA21 PublicationAdd BLAST	200

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	11 – 17	Nuclear localization signalSequence analysis		7

Compositional bias

Feature key	Position(s)	DescriptionActions	Length
Compositional biasⁱ	797 – 800	Poly-Ser	4
Compositional biasⁱ	1519 – 1526	Poly-Glu	8
Compositional biasⁱ	2066 – 2069	Poly-Gln	4
Compositional biasⁱ	2190 – 2195	Poly-Gln	6

Domainⁱ

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 conatins 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.

Zinc finger

Feature key	Position(s)	DescriptionActions	Length
Zinc fingerⁱ	331 – 417	TAZ-type 1PROSITE-ProRule annotationAdd BLAST	87
Zinc fingerⁱ	1664 – 1707	ZZ-typePROSITE-ProRule annotationAdd BLAST	44
Zinc fingerⁱ	1728 – 1809	TAZ-type 2PROSITE-ProRule annotationAdd BLAST	82

Keywords - Domainⁱ

Bromodomain, Repeat, Zinc-finger

Phylogenomic databases

eggNOGⁱ	KOG1778 Eukaryota COG5076 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000155497
HOGENOMⁱ	HOG000111353
HOVERGENⁱ	HBG000185
InParanoidⁱ	Q09472
KEGG Orthology (KO) More...KOⁱ	K04498
OMAⁱ	QPGLNQF
Database of Orthologous Groups More...OrthoDBⁱ	135929at2759
PhylomeDBⁱ	Q09472
TreeFamⁱ	TF101097

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd15802 RING_CBP-p300, 1 hit
Gene3Dⁱ	1.10.1630.10, 1 hit 1.20.1020.10, 2 hits 1.20.920.10, 1 hit 2.10.110.40, 1 hit 3.30.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR001487 Bromodomain IPR036427 Bromodomain-like_sf IPR018359 Bromodomain_CS IPR031162 CBP_P300_HAT IPR013178 Histone_AcTrfase_Rtt109/CBP IPR003101 KIX_dom IPR036529 KIX_dom_sf IPR009110 Nuc_rcpt_coact IPR014744 Nuc_rcpt_coact_CREBbp IPR037073 Nuc_rcpt_coact_CREBbp_sf IPR010303 RING_CBP-p300 IPR038547 RING_CBP-p300_sf IPR035898 TAZ_dom_sf IPR013083 Znf_RING/FYVE/PHD IPR000197 Znf_TAZ IPR000433 Znf_ZZ
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00439 Bromodomain, 1 hit PF09030 Creb_binding, 1 hit PF06001 DUF902, 1 hit PF08214 HAT_KAT11, 1 hit PF02172 KIX, 1 hit PF02135 zf-TAZ, 2 hits PF00569 ZZ, 1 hit
PRINTSⁱ	PR00503 BROMODOMAIN
SMARTⁱ	View protein in SMART SM00297 BROMO, 1 hit SM01250 KAT11, 1 hit SM00551 ZnF_TAZ, 2 hits SM00291 ZnF_ZZ, 1 hit
SUPFAMⁱ	SSF47040 SSF47040, 1 hit SSF47370 SSF47370, 1 hit SSF57933 SSF57933, 2 hits SSF69125 SSF69125, 1 hit
PROSITEⁱ	View protein in PROSITE PS00633 BROMODOMAIN_1, 1 hit PS50014 BROMODOMAIN_2, 1 hit PS51727 CBP_P300_HAT, 1 hit PS50952 KIX, 1 hit PS50134 ZF_TAZ, 2 hits PS01357 ZF_ZZ_1, 1 hit PS50135 ZF_ZZ_2, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show all Align All

Q09472-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS 
        60         70         80         90        100
TELGLTNGGD INQLQTSLGM VQDAASKHKQ LSELLRSGSS PNLNMGVGGP 
       110        120        130        140        150
GQVMASQAQQ SSPGLGLINS MVKSPMTQAG LTSPNMGMGT SGPNQGPTQS 
       160        170        180        190        200
TGMMNSPVNQ PAMGMNTGMN AGMNPGMLAA GNGQGIMPNQ VMNGSIGAGR 
       210        220        230        240        250
GRQNMQYPNP GMGSAGNLLT EPLQQGSPQM GGQTGLRGPQ PLKMGMMNNP 
       260        270        280        290        300
NPYGSPYTQN PGQQIGASGL GLQIQTKTVL SNNLSPFAMD KKAVPGGGMP 
       310        320        330        340        350
NMGQQPAPQV QQPGLVTPVA QGMGSGAHTA DPEKRKLIQQ QLVLLLHAHK 
       360        370        380        390        400
CQRREQANGE VRQCNLPHCR TMKNVLNHMT HCQSGKSCQV AHCASSRQII 
       410        420        430        440        450
SHWKNCTRHD CPVCLPLKNA GDKRNQQPIL TGAPVGLGNP SSLGVGQQSA 
       460        470        480        490        500
PNLSTVSQID PSSIERAYAA LGLPYQVNQM PTQPQVQAKN QQNQQPGQSP 
       510        520        530        540        550
QGMRPMSNMS ASPMGVNGGV GVQTPSLLSD SMLHSAINSQ NPMMSENASV 
       560        570        580        590        600
PSLGPMPTAA QPSTTGIRKQ WHEDITQDLR NHLVHKLVQA IFPTPDPAAL 
       610        620        630        640        650
KDRRMENLVA YARKVEGDMY ESANNRAEYY HLLAEKIYKI QKELEEKRRT 
       660        670        680        690        700
RLQKQNMLPN AAGMVPVSMN PGPNMGQPQP GMTSNGPLPD PSMIRGSVPN 
       710        720        730        740        750
QMMPRITPQS GLNQFGQMSM AQPPIVPRQT PPLQHHGQLA QPGALNPPMG 
       760        770        780        790        800
YGPRMQQPSN QGQFLPQTQF PSQGMNVTNI PLAPSSGQAP VSQAQMSSSS 
       810        820        830        840        850
CPVNSPIMPP GSQGSHIHCP QLPQPALHQN SPSPVPSRTP TPHHTPPSIG 
       860        870        880        890        900
AQQPPATTIP APVPTPPAMP PGPQSQALHP PPRQTPTPPT TQLPQQVQPS 
       910        920        930        940        950
LPAAPSADQP QQQPRSQQST AASVPTPTAP LLPPQPATPL SQPAVSIEGQ 
       960        970        980        990       1000
VSNPPSTSST EVNSQAIAEK QPSQEVKMEA KMEVDQPEPA DTQPEDISES 
      1010       1020       1030       1040       1050
KVEDCKMEST ETEERSTELK TEIKEEEDQP STSATQSSPA PGQSKKKIFK 
      1060       1070       1080       1090       1100
PEELRQALMP TLEALYRQDP ESLPFRQPVD PQLLGIPDYF DIVKSPMDLS 
      1110       1120       1130       1140       1150
TIKRKLDTGQ YQEPWQYVDD IWLMFNNAWL YNRKTSRVYK YCSKLSEVFE 
      1160       1170       1180       1190       1200
QEIDPVMQSL GYCCGRKLEF SPQTLCCYGK QLCTIPRDAT YYSYQNRYHF 
      1210       1220       1230       1240       1250
CEKCFNEIQG ESVSLGDDPS QPQTTINKEQ FSKRKNDTLD PELFVECTEC 
      1260       1270       1280       1290       1300
GRKMHQICVL HHEIIWPAGF VCDGCLKKSA RTRKENKFSA KRLPSTRLGT 
      1310       1320       1330       1340       1350
FLENRVNDFL RRQNHPESGE VTVRVVHASD KTVEVKPGMK ARFVDSGEMA 
      1360       1370       1380       1390       1400
ESFPYRTKAL FAFEEIDGVD LCFFGMHVQE YGSDCPPPNQ RRVYISYLDS 
      1410       1420       1430       1440       1450
VHFFRPKCLR TAVYHEILIG YLEYVKKLGY TTGHIWACPP SEGDDYIFHC 
      1460       1470       1480       1490       1500
HPPDQKIPKP KRLQEWYKKM LDKAVSERIV HDYKDIFKQA TEDRLTSAKE 
      1510       1520       1530       1540       1550
LPYFEGDFWP NVLEESIKEL EQEEEERKRE ENTSNESTDV TKGDSKNAKK 
      1560       1570       1580       1590       1600
KNNKKTSKNK SSLSRGNKKK PGMPNVSNDL SQKLYATMEK HKEVFFVIRL 
      1610       1620       1630       1640       1650
IAGPAANSLP PIVDPDPLIP CDLMDGRDAF LTLARDKHLE FSSLRRAQWS 
      1660       1670       1680       1690       1700
TMCMLVELHT QSQDRFVYTC NECKHHVETR WHCTVCEDYD LCITCYNTKN 
      1710       1720       1730       1740       1750
HDHKMEKLGL GLDDESNNQQ AAATQSPGDS RRLSIQRCIQ SLVHACQCRN 
      1760       1770       1780       1790       1800
ANCSLPSCQK MKRVVQHTKG CKRKTNGGCP ICKQLIALCC YHAKHCQENK 
      1810       1820       1830       1840       1850
CPVPFCLNIK QKLRQQQLQH RLQQAQMLRR RMASMQRTGV VGQQQGLPSP 
      1860       1870       1880       1890       1900
TPATPTTPTG QQPTTPQTPQ PTSQPQPTPP NSMPPYLPRT QAAGPVSQGK 
      1910       1920       1930       1940       1950
AAGQVTPPTP PQTAQPPLPG PPPAAVEMAM QIQRAAETQR QMAHVQIFQR 
      1960       1970       1980       1990       2000
PIQHQMPPMT PMAPMGMNPP PMTRGPSGHL EPGMGPTGMQ QQPPWSQGGL 
      2010       2020       2030       2040       2050
PQPQQLQSGM PRPAMMSVAQ HGQPLNMAPQ PGLGQVGISP LKPGTVSQQA 
      2060       2070       2080       2090       2100
LQNLLRTLRS PSSPLQQQQV LSILHANPQL LAAFIKQRAA KYANSNPQPI 
      2110       2120       2130       2140       2150
PGQPGMPQGQ PGLQPPTMPG QQGVHSNPAM QNMNPMQAGV QRAGLPQQQP 
      2160       2170       2180       2190       2200
QQQLQPPMGG MSPQAQQMNM NHNTMPSQFR DILRRQQMMQ QQQQQGAGPG 
      2210       2220       2230       2240       2250
IGPGMANHNQ FQQPQGVGYP PQQQQRMQHH MQQMQQGNMG QIGQLPQALG 
      2260       2270       2280       2290       2300
AEAGASLQAY QQRLLQQQMG SPVQPNPMSP QQHMLPNQAQ SPHLQGQQIP 
      2310       2320       2330       2340       2350
NSLSNQVRSP QPVPSPRPQS QPPHSSPSPR MQPQPSPHHV SPQTSSPHPG 
      2360       2370       2380       2390       2400
LVAAQANPME QGHFASPDQN SMLSQLASNP GMANLHGASA TDLGLSTDNS 
      2410 
DLNSNLSQST LDIH

Length:2,414

Mass (Da):264,161

Last modified:February 10, 2009 - v2

Checksum:ⁱ8E869E1F174A6FEB

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

A0A0U1RQG3	A0A0U1RQG3_HUMAN	Histone acetyltransferase p300 Histone acetyltransferase p300	EP300	133	Annotation score:
A0A0U1RR87	A0A0U1RR87_HUMAN	Histone acetyltransferase p300 Histone acetyltransferase p300	EP300	187	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	169	M → T in AAA18639 (PubMed:7523245).Curated	1
Sequence conflictⁱ	204	N → D in AAA18639 (PubMed:7523245).Curated	1
Sequence conflictⁱ	928	T → N in AAA18639 (PubMed:7523245).Curated	1
Sequence conflictⁱ	1924	A → T in AAA18639 (PubMed:7523245).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_055554	289	M → V. Corresponds to variant dbSNP:rs2230111EnsemblClinVar.	1
Natural variantⁱVAR_014428	827	L → P in a breast cancer sample. 1 Publication	1
Natural variantⁱVAR_020425	997	I → V. Corresponds to variant dbSNP:rs20551EnsemblClinVar.	1
Natural variantⁱVAR_014429	1013	E → G in a breast cancer sample. 1 PublicationCorresponds to variant dbSNP:rs1234168115Ensembl.	1
Natural variantⁱVAR_074021	1511	N → I1 Publication	1
Natural variantⁱVAR_014430	1650	S → Y in a pancreatic cancer sample. 1 Publication	1
Natural variantⁱVAR_080731	2007	Q → R Found in a patient with spinocerebellar ataxia; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs763892493Ensembl.	1
Natural variantⁱVAR_038376	2174	T → S. Corresponds to variant dbSNP:rs5758252Ensembl.	1
Natural variantⁱVAR_014431	2221	P → Q in a colorectal cancer sample. 1 PublicationCorresponds to variant dbSNP:rs28937578EnsemblClinVar.	1
Natural variantⁱVAR_038377	2223	Q → P1 PublicationCorresponds to variant dbSNP:rs1046088EnsemblClinVar.	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U01877 mRNA Translation: AAA18639.1 AL080243 Genomic DNA No translation available. AL096765 Genomic DNA No translation available. AL035658 Genomic DNA No translation available. CH471095 Genomic DNA Translation: EAW60408.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS14010.1
PIRⁱ	A54277
NCBI Reference Sequences More...RefSeqⁱ	NP_001420.2, NM_001429.3
UniGeneⁱ	Hs.517517 Hs.655211

Genome annotation databases

Ensemblⁱ	ENST00000263253; ENSP00000263253; ENSG00000100393
GeneIDⁱ	2033
KEGGⁱ	hsa:2033
UCSC genome browser More...UCSCⁱ	uc003azl.5 human

Keywords - Coding sequence diversityⁱ

Chromosomal rearrangement, Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q09472 (EP300_HUMAN)

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Histone acetyltransferase p300

EP300

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

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Cytosol

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

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Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Sites

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Motif

Compositional bias

Zinc finger

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ