Ep300
entrez
328572
canonical
uniprot
B2RWS6
canonical
ensembl
ENSMUSG00000055024
resolver
ensp
ENSMUSP00000066789
resolver
enst
ENSMUST00000068387
resolver
genesymbol
Ep300
resolver
genesymbol_syn
P300
resolver
uniprot
E9PYJ8
resolver
uniprot
Q8BJ14
resolver
uniprot_entry
EP300_MOUSE
resolver
uniprot_entry
Q8BJ14_MOUSE
resolver
uniprot_sec
E9PYJ8
resolver
amino_acid_sequence
MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDISQLQTSLGIVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQAMASQAQQNSPGLSLINSMVKSPMAQTGLTSPNMGIGSSGPNQGPTQSPAGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRPNMQYPNAGMGNAGSLLTEPLQQGSPQMGGQPGLRGPQPLKMGMMNNPSPYGSPYTQNSGQQIGASGLGLQIQTKTVLPNNLSPFAMDKKAVPGGGMPSMGQQPTPSVQQPGLVTPVAAGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNAGDKRNQQSILTGAPVGLGNPSSLGVGQQSTPSLSTVSQIDPSSIERAYAALGLPYQVNQIPPQPQVQAKNQQSQPSGQSPQGMRSVNNMSASPMGVNGGVGVQTPNLLSDSMLHSTINSQNPMMSENAGVASLGPLPTAAQPSSTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPNAPGMGPVPMNTGSNMGQQPTGMTTNGPVPDPSMIRGSVPNHMMPRMTPQPGLNQFGQMNMPQPPIGPRQPSPLQHHGQLAQSGSLNPPMGYGPRMQQASGQNQFLSQTQFTSQGMNVTNMPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPTLPQQAHQNSPSPVPSRTPTPHHTPPSIGNQPPPATAIPTPVPTPPAIPPGPQPPSLHPSSRQTPTPPTHLPPQVQPSLPAAPSADQSQQQPRSQQSTAVSVPTPTAPLLPPQPSTPLSQPAVSIEGQVSNPPSTSSTEVNSQTIPEKQPSQEVKMESKMEVDKPEPADAQPEDTKEAKGEDVKVEPTEMEERGPELKTDGKEEEEQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPSGFVCDGCLKKTARTRKENKLSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDILKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIACPAPNSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVAGQQQGLPSPTPATPTTPTGQQPATPQTPQPQPTSQPQPTPPNNMTPYLPRTQTTGPVSQGKAPGQVTPPTPPQTAQAPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPQMSPMAPMGMNPPPMARGPGGHLDPGIGPAGMQQQPPWAQGGMPQPQQMQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGVSPLKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANPNPQPLPGQPGMTQGQPGLQPPTMPGQQGVHSNPALQNMNPLQAGVQRAGLPQQQPQQQLQPPMGAMSPQAQQMNMNHNTMPSQFRDILRRQMMQQQGAGPGIGPGMANQFQQPQGIGYPPQQQQQQRMQHHMQQMQQGNMGQMGQLPQALGAEAGASLQAYQQRLLQQQMGSPAQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPGLVAAQAANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSSDNADLNSNLSQSTLDIH
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
2.3.1.48
uniprot
proteins
function
FUNCTION: Functions as a histone acetyltransferase and regulates transcription via chromatin remodeling (By similarity). Acetylates all four core histones in nucleosomes (By similarity). Histone acetylation gives an epigenetic tag for transcriptional activation (By similarity). 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 (By similarity). Mediates acetylation of histone H3 at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac, respectively) (By similarity). 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 (By similarity). Catalyzes formation of histone H4 acetyl-methylated at 'Lys-5' and 'Lys-12' (H4K5acme and H4K12acme, respectively) (By similarity). In response to DNA damage, catalyzes acetylation of histone H1 at 'Lys-75' (H1K75ac) following histone H1 deamidation by CTPS1, increasing chromatin accessibility to facilitate the recruitment of DNA repair proteins (By similarity). Also functions as acetyltransferase for non-histone targets, such as ALX1, HDAC1, PRDM16, PRMT1, SIRT2, STAT3, ZNF76 or GLUL (PubMed:28576496, PubMed:28883095, PubMed:35075301). Acetylates 'Lys-131' of ALX1 and acts as its coactivator (By similarity). Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function (By similarity). 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 (By similarity). Promotes chromatin acetylation in heat shock responsive HSP genes during the heat shock response (HSR), thereby stimulating HSR transcription (By similarity). Acetylates HDAC1 leading to its inactivation and modulation of transcription (By similarity). Acetylates 'Lys-247' of EGR2 (PubMed:28576496). Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2 (By similarity). 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 (By similarity). Promotes cardiac myocyte enlargement (By similarity). Can also mediate transcriptional repression (By similarity). Acetylates FOXO1 and enhances its transcriptional activity (By similarity). Acetylates STAT3 at different sites, promoting both STAT3 dimerization and activation and recruitment to chromatin (By similarity). Acetylates BCL6 which disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity (By similarity). 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 (By similarity). Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity (PubMed:14645221, PubMed:9512516). 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) (By similarity). Acetylates MEF2D (By similarity). 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 (PubMed:25200183). Acetylates PCK1 and promotes PCK1 anaplerotic activity (By similarity). Acetylates RXRA and RXRG (By similarity). Acetylates isoform M2 of PKM (PKM2), promoting its homodimerization and conversion into a protein kinase (By similarity). Acetylates RPTOR in response to leucine, leading to activation of the mTORC1 complex (By similarity). Acetylates RICTOR, leading to activation of the mTORC2 complex (By similarity). Mediates cAMP-gene regulation by binding specifically to phosphorylated CREBBP (PubMed:18486321, PubMed:24216764). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA), butanoyl-CoA (butyryl-CoA), 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), lactoyl-CoA, propanoyl-CoA (propionyl-CoA) or isonicotinyl-CoA, and is able to mediate protein crotonylation, butyrylation, 2-hydroxyisobutyrylation, lactylation, propionylation or isonicotinylation, respectively (PubMed:27105113). Acts as a histone crotonyltransferase; crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. Histone crotonyltransferase activity is dependent on the concentration of (2E)-butenoyl-CoA (crotonyl-CoA) substrate and such activity is weak when (2E)-butenoyl-CoA (crotonyl-CoA) concentration is low (By similarity). Also acts as a histone butyryltransferase; butyrylation marks active promoters (PubMed:27105113). Catalyzes histone lactylation in macrophages by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription (By similarity). Acts as a protein-lysine 2-hydroxyisobutyryltransferase; regulates glycolysis by mediating 2-hydroxyisobutyrylation of glycolytic enzymes. Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q09472, ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:18486321, ECO:0000269|PubMed:20810990, ECO:0000269|PubMed:24216764, ECO:0000269|PubMed:25200183, ECO:0000269|PubMed:27105113, ECO:0000269|PubMed:28576496, ECO:0000269|PubMed:28883095, ECO:0000269|PubMed:35075301, ECO:0000269|PubMed:9512516, ECO:0000305|PubMed:20955178}.
uniprot
proteins
mass_dalton
263305
uniprot
proteins
post_translational_modification
PTM: Acetylated on Lys at up to 17 positions by intermolecular autocatalysis. Deacetylated in the transcriptional repression domain (CRD1) by SIRT1, preferentially at Lys-1019. Deacetylated by SIRT2, preferentially at Lys-419, Lys-424, Lys-1541, Lys-1545, Lys-1548, Lys-1698, Lys-1703 and Lys-1706. {ECO:0000250|UniProtKB:Q09472}.; PTM: Citrullinated at Arg-2143 by PADI4, which impairs methylation by CARM1 and promotes interaction with NCOA2/GRIP1. {ECO:0000250|UniProtKB:Q09472}.; PTM: Methylated at Arg-581 and Arg-605 in the KIX domain by CARM1, which blocks association with CREB, inhibits CREB signaling and activates apoptotic response. Also methylated at Arg-2143 by CARM1, which impairs interaction with NCOA2/GRIP1 (By similarity). {ECO:0000250|UniProtKB:Q09472}.; PTM: Sumoylated; sumoylation in the transcriptional repression domain (CRD1) mediates transcriptional repression. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3 (By similarity). {ECO:0000250|UniProtKB:Q09472}.; PTM: Probable target of ubiquitination by FBXO3, leading to rapid proteasome-dependent degradation. {ECO:0000250|UniProtKB:Q09472}.; PTM: Phosphorylation at Ser-89 by AMPK reduces interaction with nuclear receptors, such as PPARG (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q09472}.
uniprot
proteins
pubmed
10593900
uniprot
proteins
pubmed
10722728
uniprot
proteins
pubmed
11115394
uniprot
proteins
pubmed
12709428
uniprot
proteins
pubmed
14645221
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15601857
uniprot
proteins
pubmed
16917507
uniprot
proteins
pubmed
18486321
uniprot
proteins
pubmed
19324970
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20810990
uniprot
proteins
pubmed
20940255
uniprot
proteins
pubmed
20955178
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24216764
uniprot
proteins
pubmed
25200183
uniprot
proteins
pubmed
27105113
uniprot
proteins
pubmed
28576496
uniprot
proteins
pubmed
28883095
uniprot
proteins
pubmed
35075301
uniprot
proteins
pubmed
9512516
uniprot
proteins
sequence_length
2412
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q09472}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00311, ECO:0000269|PubMed:19324970}. Note=In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Colocalizes with ROCK2 in the nucleus. Localizes to sites of DNA damage. {ECO:0000250|UniProtKB:Q09472}.
uniprot
proteins