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Histone acetyltransferase p300 (p300 HAT) (EC 2.3.1.48) (E1A-associated protein p300) (Histone butyryltransferase p300) (EC 2.3.1.-) (Histone crotonyltransferase p300) (EC 2.3.1.-) (Protein propionyltransferase p300) (EC 2.3.1.-)

 EP300_MOUSE             Reviewed;        2412 AA.
B2RWS6; E9PYJ8;
31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 2.
22-NOV-2017, entry version 99.
RecName: Full=Histone acetyltransferase p300;
Short=p300 HAT;
EC=2.3.1.48 {ECO:0000250|UniProtKB:Q09472};
AltName: Full=E1A-associated protein p300;
AltName: Full=Histone butyryltransferase p300;
EC=2.3.1.- {ECO:0000269|PubMed:27105113};
AltName: Full=Histone crotonyltransferase p300;
EC=2.3.1.- {ECO:0000250|UniProtKB:Q09472};
AltName: Full=Protein propionyltransferase p300;
EC=2.3.1.- {ECO:0000250|UniProtKB:Q09472};
Name=Ep300; Synonyms=P300;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, AND INTERACTION WITH NEUROD1.
PubMed=9512516; DOI=10.1101/gad.12.6.820;
Mutoh H., Naya F.J., Tsai M.J., Leiter A.B.;
"The basic helix-loop-helix protein BETA2 interacts with p300 to
coordinate differentiation of secretin-expressing enteroendocrine
cells.";
Genes Dev. 12:820-830(1998).
[4]
INTERACTION WITH CITED2.
PubMed=10593900; DOI=10.1074/jbc.274.51.36159;
Glenn D.J., Maurer R.A.;
"MRG1 binds to the LIM domain of Lhx2 and may function as a
coactivator to stimulate glycoprotein hormone alpha-subunit gene
expression.";
J. Biol. Chem. 274:36159-36167(1999).
[5]
INTERACTION WITH CITED1.
PubMed=10722728; DOI=10.1074/jbc.275.12.8825;
Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S.,
Roberts A.B., Isselbacher K.J., Shioda T.;
"The MSG1 non-DNA-binding transactivator binds to the p300/CBP
coactivators, enhancing their functional link to the Smad
transcription factors.";
J. Biol. Chem. 275:8825-8834(2000).
[6]
INTERACTION WITH NR4A3.
PubMed=12709428; DOI=10.1074/jbc.M300088200;
Wansa K.D., Harris J.M., Yan G., Ordentlich P., Muscat G.E.;
"The AF-1 domain of the orphan nuclear receptor NOR-1 mediates trans-
activation, coactivator recruitment, and activation by the purine
anti-metabolite 6-mercaptopurine.";
J. Biol. Chem. 278:24776-24790(2003).
[7]
FUNCTION, AND INTERACTION WITH NPAS2.
PubMed=14645221; DOI=10.1074/jbc.M311973200;
Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M.,
Chakravarti D., FitzGerald G.A., McNamara P.;
"Histone acetyltransferase-dependent chromatin remodeling and the
vascular clock.";
J. Biol. Chem. 279:7091-7097(2004).
[8]
INTERACTION WITH MYOCD.
PubMed=15601857; DOI=10.1128/MCB.25.1.364-376.2005;
Cao D., Wang Z., Zhang C.L., Oh J., Xing W., Li S., Richardson J.A.,
Wang D.Z., Olson E.N.;
"Modulation of smooth muscle gene expression by association of histone
acetyltransferases and deacetylases with myocardin.";
Mol. Cell. Biol. 25:364-376(2005).
[9]
INTERACTION WITH HIPK2, AND PHOSPHORYLATION BY HIPK2.
PubMed=16917507; DOI=10.1038/sj.emboj.7601273;
Aikawa Y., Nguyen L.A., Isono K., Takakura N., Tagata Y.,
Schmitz M.L., Koseki H., Kitabayashi I.;
"Roles of HIPK1 and HIPK2 in AML1- and p300-dependent transcription,
hematopoiesis and blood vessel formation.";
EMBO J. 25:3955-3965(2006).
[10]
FUNCTION, AND INTERACTION WITH CEBPB.
PubMed=18486321; DOI=10.1016/j.mce.2008.03.009;
Cesena T.I., Cui T.X., Subramanian L., Fulton C.T.,
Iniguez-Lluhi J.A., Kwok R.P., Schwartz J.;
"Acetylation and deacetylation regulate CCAAT/enhancer binding protein
beta at K39 in mediating gene transcription.";
Mol. Cell. Endocrinol. 289:94-101(2008).
[11]
INTERACTION WITH CEBPB, AND SUBCELLULAR LOCATION.
PubMed=19324970; DOI=10.1210/me.2008-0277;
Ohoka N., Kato S., Takahashi Y., Hayashi H., Sato R.;
"The orphan nuclear receptor RORalpha restrains adipocyte
differentiation through a reduction of C/EBPbeta activity and
perilipin gene expression.";
Mol. Endocrinol. 23:759-771(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
FUNCTION IN ACETYLATION OF XBP1.
PubMed=20955178; DOI=10.1042/BJ20101293;
Wang F.M., Chen Y.J., Ouyang H.J.;
"Regulation of unfolded protein response modulator XBP1s by
acetylation and deacetylation.";
Biochem. J. 433:245-252(2011).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1179; LYS-1557 AND LYS-1559,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[15]
FUNCTION, AND INTERACTION WITH ATF5 AND CEBPB.
PubMed=24216764; DOI=10.1128/MCB.00956-13;
Zhao Y., Zhang Y.D., Zhang Y.Y., Qian S.W., Zhang Z.C., Li S.F.,
Guo L., Liu Y., Wen B., Lei Q.Y., Tang Q.Q., Li X.;
"p300-dependent acetylation of activating transcription factor 5
enhances C/EBPbeta transactivation of C/EBPalpha during 3T3-L1
differentiation.";
Mol. Cell. Biol. 34:315-324(2014).
[16]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014;
Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z.,
Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J.,
Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C.,
Panne D., Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.;
"Dynamic competing histone H4 K5K8 acetylation and butyrylation are
hallmarks of highly active gene promoters.";
Mol. Cell 62:169-180(2016).
-!- FUNCTION: Functions as 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 cAMP-gene regulation by binding
specifically to phosphorylated CREB protein (PubMed:18486321,
PubMed:24216764). 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-27' (H3K27ac) (By similarity).
Also functions as acetyltransferase for nonhistone targets (By
similarity). 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). Acetylates HDAC1 leading to its
inactivation and modulation of transcription (By similarity). 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 BCL6 wich 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). 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: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 (E)-but-2-enoyl-CoA (crotonyl-CoA)
concentration is low (By similarity). Also acts as a histone
butyryltransferase; butyrylation marks active promoters
(PubMed:27105113). {ECO:0000250|UniProtKB:Q09472,
ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:18486321,
ECO:0000269|PubMed:24216764, ECO:0000269|PubMed:27105113,
ECO:0000269|PubMed:9512516, ECO:0000305|PubMed:20955178}.
-!- CATALYTIC ACTIVITY: Butanoyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-butanoyl-L-lysine. {ECO:0000269|PubMed:27105113}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine. {ECO:0000250|UniProtKB:Q09472}.
-!- CATALYTIC ACTIVITY: (2E)-butenoyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-(2E)-butenoyl-L-lysine.
{ECO:0000250|UniProtKB:Q09472}.
-!- CATALYTIC ACTIVITY: Propanoyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-propanoyl-L-lysine. {ECO:0000250|UniProtKB:Q09472}.
-!- SUBUNIT: 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 HIPK2, 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
with PPARG. Forms a complex made of CDK9, CCNT1/cyclin-T1, EP300
and GATA4 that stimulates hypertrophy in cardiomyocytes. Interacts
with CITED1 and CITED2. Interacts with ROCK2. Interacts with
NEUROD1. Interacts (via CREB-binding domain) with MYOCD (via C-
terminus). 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
(PubMed:18486321, PubMed:24216764). Interacts with ARNTL/BMAL1 and
CLOCK (By similarity). Interacts with SIRT2. Interacts with MTA1.
Interacts with HDAC4 and HDAC5 in the presence of TFAP2C (By
similarity). Interacts with TRIP4 (By similarity). Interacts with
NPAS2. Directly interacts with ZBTB49; this interaction leads to
synergistic transactivation of CDKN1A (By similarity). Interacts
with NR4A3 (PubMed:12709428). Interacts with ATF5; EP300 is
required for ATF5 and CEBPB interaction and DNA binding
(PubMed:24216764). Interacts with ZNF451 (By similarity).
Interacts with HSF1 (By similarity). Interacts with ZBTB48/TZAP
(By similarity). Interacts with STAT1; the interaction is enhanced
upon IFN-gamma stimulation (By similarity). Interacts with HNRNPU
(via C-terminus); this interaction enhances DNA-binding of HNRNPU
to nuclear scaffold/matrix attachment region (S/MAR) elements (By
similarity). {ECO:0000250|UniProtKB:Q09472,
ECO:0000269|PubMed:10593900, ECO:0000269|PubMed:10722728,
ECO:0000269|PubMed:12709428, ECO:0000269|PubMed:14645221,
ECO:0000269|PubMed:15601857, ECO:0000269|PubMed:16917507,
ECO:0000269|PubMed:18486321, ECO:0000269|PubMed:19324970,
ECO:0000269|PubMed:24216764, ECO:0000269|PubMed:9512516}.
-!- INTERACTION:
P02340:Tp53; NbExp=3; IntAct=EBI-3953360, EBI-474016;
-!- 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. {ECO:0000250|UniProtKB:Q09472}.
-!- 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 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 (By similarity).
{ECO:0000250}.
-!- 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}.
-!- 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}.
-!- 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}.
-!- PTM: Probable target of ubiquitination by FBXO3, leading to rapid
proteasome-dependent degradation. {ECO:0000250}.
-!- 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}.
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EMBL; AC102262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC160528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC144976; AAI44977.1; -; mRNA.
EMBL; BC150681; AAI50682.1; -; mRNA.
CCDS; CCDS37149.1; -.
RefSeq; NP_808489.4; NM_177821.6.
UniGene; Mm.258397; -.
ProteinModelPortal; B2RWS6; -.
SMR; B2RWS6; -.
BioGrid; 236625; 52.
CORUM; B2RWS6; -.
DIP; DIP-60610N; -.
IntAct; B2RWS6; 8.
STRING; 10090.ENSMUSP00000066789; -.
iPTMnet; B2RWS6; -.
PhosphoSitePlus; B2RWS6; -.
EPD; B2RWS6; -.
PaxDb; B2RWS6; -.
PeptideAtlas; B2RWS6; -.
PRIDE; B2RWS6; -.
Ensembl; ENSMUST00000068387; ENSMUSP00000066789; ENSMUSG00000055024.
GeneID; 328572; -.
KEGG; mmu:328572; -.
UCSC; uc007wws.1; mouse.
CTD; 2033; -.
MGI; MGI:1276116; Ep300.
eggNOG; KOG1778; Eukaryota.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00760000119206; -.
HOGENOM; HOG000111353; -.
HOVERGEN; HBG000185; -.
InParanoid; B2RWS6; -.
KO; K04498; -.
OMA; GQVSNPP; -.
OrthoDB; EOG091G0L04; -.
PhylomeDB; B2RWS6; -.
Reactome; R-MMU-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
Reactome; R-MMU-1368092; Rora activates gene expression.
Reactome; R-MMU-1368110; Bmal1:Clock,Npas2 activates circadian gene expression.
Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-MMU-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-MMU-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
Reactome; R-MMU-3371568; Attenuation phase.
Reactome; R-MMU-442533; Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-MMU-5689901; Metalloprotease DUBs.
Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-MMU-6782135; Dual incision in TC-NER.
Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-MMU-6804760; Regulation of TP53 Activity through Methylation.
Reactome; R-MMU-6811555; PI5P Regulates TP53 Acetylation.
Reactome; R-MMU-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
Reactome; R-MMU-8941856; RUNX3 regulates NOTCH signaling.
Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-MMU-8951936; RUNX3 regulates p14-ARF.
Reactome; R-MMU-918233; TRAF3-dependent IRF activation pathway.
Reactome; R-MMU-933541; TRAF6 mediated IRF7 activation.
Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
ChiTaRS; Ep300; mouse.
PRO; PR:B2RWS6; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000055024; -.
ExpressionAtlas; B2RWS6; baseline and differential.
Genevisible; B2RWS6; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0000123; C:histone acetyltransferase complex; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0005667; C:transcription factor complex; IDA:UniProtKB.
GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB.
GO; GO:0033613; F:activating transcription factor binding; ISO:MGI.
GO; GO:0050681; F:androgen receptor binding; ISO:MGI.
GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
GO; GO:0001047; F:core promoter binding; ISO:MGI.
GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
GO; GO:0140069; F:histone butyryltransferase activity; IDA:UniProtKB.
GO; GO:0140068; F:histone crotonyltransferase activity; ISS:UniProtKB.
GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; ISS:UniProtKB.
GO; GO:0035257; F:nuclear hormone receptor binding; ISO:MGI.
GO; GO:0002039; F:p53 binding; IPI:MGI.
GO; GO:0140065; F:peptide butyryltransferase activity; ISO:MGI.
GO; GO:0097157; F:pre-mRNA intronic binding; IDA:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0061920; F:protein propionyltransferase activity; ISS:UniProtKB.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:MGI.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:MGI.
GO; GO:0097677; F:STAT family protein binding; ISO:MGI.
GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:MGI.
GO; GO:0016746; F:transferase activity, transferring acyl groups; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
GO; GO:0030183; P:B cell differentiation; IMP:MGI.
GO; GO:0051216; P:cartilage development; NAS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
GO; GO:0007623; P:circadian rhythm; IDA:UniProtKB.
GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
GO; GO:0043969; P:histone H2B acetylation; ISS:UniProtKB.
GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
GO; GO:0018393; P:internal peptidyl-lysine acetylation; ISO:MGI.
GO; GO:0006475; P:internal protein amino acid acetylation; ISS:UniProtKB.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:MGI.
GO; GO:0030324; P:lung development; IMP:MGI.
GO; GO:0010742; P:macrophage derived foam cell differentiation; ISS:UniProtKB.
GO; GO:0035855; P:megakaryocyte development; IMP:MGI.
GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
GO; GO:0140067; P:peptidyl-lysine butyrylation; IDA:UniProtKB.
GO; GO:0140066; P:peptidyl-lysine crotonylation; ISS:UniProtKB.
GO; GO:0061921; P:peptidyl-lysine propionylation; ISS:UniProtKB.
GO; GO:0030220; P:platelet formation; IMP:MGI.
GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IGI:MGI.
GO; GO:0045815; P:positive regulation of gene expression, epigenetic; ISS:UniProtKB.
GO; GO:0032092; P:positive regulation of protein binding; IDA:MGI.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0006990; P:positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006473; P:protein acetylation; IDA:UniProtKB.
GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
GO; GO:0060765; P:regulation of androgen receptor signaling pathway; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0090043; P:regulation of tubulin deacetylation; ISS:UniProtKB.
GO; GO:0043627; P:response to estrogen; ISS:UniProtKB.
GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
GO; GO:0001756; P:somitogenesis; IGI:MGI.
CDD; cd15802; RING_CBP-p300; 1.
Gene3D; 1.10.1630.10; -; 1.
Gene3D; 1.20.1020.10; -; 2.
Gene3D; 1.20.920.10; -; 1.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR031162; CBP_P300_HAT.
InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
InterPro; IPR003101; KIX_dom.
InterPro; IPR036529; KIX_dom_sf.
InterPro; IPR009110; Nuc_rcpt_coact.
InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
InterPro; IPR037073; Nuc_rcpt_coact_CREBbp_sf.
InterPro; IPR010303; RING_CBP-p300.
InterPro; IPR035898; TAZ_dom_sf.
InterPro; IPR000197; Znf_TAZ.
InterPro; IPR000433; Znf_ZZ.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF09030; Creb_binding; 1.
Pfam; PF06001; DUF902; 1.
Pfam; PF08214; HAT_KAT11; 1.
Pfam; PF02172; KIX; 1.
Pfam; PF02135; zf-TAZ; 2.
Pfam; PF00569; ZZ; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 1.
SMART; SM01250; KAT11; 1.
SMART; SM00551; ZnF_TAZ; 2.
SMART; SM00291; ZnF_ZZ; 1.
SUPFAM; SSF47040; SSF47040; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF57933; SSF57933; 2.
SUPFAM; SSF69125; SSF69125; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS51727; CBP_P300_HAT; 1.
PROSITE; PS50952; KIX; 1.
PROSITE; PS50134; ZF_TAZ; 2.
PROSITE; PS01357; ZF_ZZ_1; 1.
PROSITE; PS50135; ZF_ZZ_2; 1.
1: Evidence at protein level;
Acetylation; Acyltransferase; Biological rhythms; Bromodomain;
Cell cycle; Citrullination; Coiled coil; Complete proteome; Cytoplasm;
Differentiation; Isopeptide bond; Metal-binding; Methylation; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation; Transferase; Ubl conjugation; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q09472}.
CHAIN 2 2412 Histone acetyltransferase p300.
/FTId=PRO_0000409386.
DOMAIN 567 646 KIX. {ECO:0000255|PROSITE-
ProRule:PRU00311}.
DOMAIN 1066 1138 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 1286 1662 CBP/p300-type HAT. {ECO:0000255|PROSITE-
ProRule:PRU01065}.
ZN_FING 332 418 TAZ-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00203}.
ZN_FING 1663 1706 ZZ-type. {ECO:0000255|PROSITE-
ProRule:PRU00228}.
ZN_FING 1727 1808 TAZ-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00203}.
REGION 2 149 Interaction with RORA.
REGION 2 139 Interaction with ALX1.
{ECO:0000250|UniProtKB:Q09472}.
REGION 1016 1028 CRD1; mediates transcriptional
repression. {ECO:0000250}.
REGION 1396 1398 Interaction with histone.
{ECO:0000250|UniProtKB:Q09472}.
REGION 1397 1399 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q09472}.
REGION 1409 1410 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q09472}.
REGION 2042 2237 Interaction with NCOA2. {ECO:0000250}.
COILED 1510 1539 {ECO:0000255}.
MOTIF 11 17 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 660 942 Pro-rich.
COMPBIAS 798 801 Poly-Ser.
COMPBIAS 1518 1525 Poly-Glu.
METAL 348 348 Zinc 1. {ECO:0000250}.
METAL 352 352 Zinc 1. {ECO:0000250}.
METAL 365 365 Zinc 1. {ECO:0000250}.
METAL 370 370 Zinc 1. {ECO:0000250}.
METAL 379 379 Zinc 2. {ECO:0000250}.
METAL 383 383 Zinc 2. {ECO:0000250}.
METAL 389 389 Zinc 2. {ECO:0000250}.
METAL 394 394 Zinc 2. {ECO:0000250}.
METAL 403 403 Zinc 3. {ECO:0000250}.
METAL 407 407 Zinc 3. {ECO:0000250}.
METAL 412 412 Zinc 3. {ECO:0000250}.
METAL 415 415 Zinc 3. {ECO:0000250}.
BINDING 1456 1456 Acetyl-CoA; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q09472}.
BINDING 1461 1461 Acetyl-CoA.
{ECO:0000250|UniProtKB:Q09472}.
BINDING 1465 1465 Acetyl-CoA.
{ECO:0000250|UniProtKB:Q09472}.
SITE 2089 2089 Interaction with NCOA2. {ECO:0000250}.
SITE 2143 2143 Interaction with NCOA2. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 89 89 Phosphoserine; by AMPK.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 419 419 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 424 424 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 500 500 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 581 581 Omega-N-methylated arginine; by CARM1.
{ECO:0000250}.
MOD_RES 605 605 Omega-N-methylated arginine; by CARM1.
{ECO:0000250}.
MOD_RES 637 637 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 976 976 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 1019 1019 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 1023 1023 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 1037 1037 Phosphoserine.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 1179 1179 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1335 1335 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 1472 1472 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 1498 1498 N6-acetyllysine; by autocatalysis.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 1541 1541 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 1545 1545 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 1548 1548 N6-acetyllysine; by autocatalysis.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 1553 1553 N6-acetyllysine; by autocatalysis.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 1554 1554 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 1557 1557 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1559 1559 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1582 1582 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 1698 1698 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 1703 1703 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 1706 1706 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 1725 1725 Phosphoserine.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 2143 2143 Asymmetric dimethylarginine; by CARM1;
alternate.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 2143 2143 Citrulline; by PADI4; alternate.
{ECO:0000250}.
CROSSLNK 1019 1019 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 1023 1023 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CONFLICT 677 677 G -> E (in Ref. 2; AAI44977/AAI50682).
{ECO:0000305}.
CONFLICT 2217 2217 Q -> QQQQ (in Ref. 2; AAI44977/AAI50682).
{ECO:0000305}.
SEQUENCE 2412 AA; 263305 MW; 0E9B2D9508237671 CRC64;
MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS TELGLTNGGD
ISQLQTSLGI VQDAASKHKQ LSELLRSGSS PNLNMGVGGP GQAMASQAQQ NSPGLSLINS
MVKSPMAQTG LTSPNMGIGS SGPNQGPTQS PAGMMNSPVN QPAMGMNTGM NAGMNPGMLA
AGNGQGIMPN QVMNGSIGAG RGRPNMQYPN AGMGNAGSLL TEPLQQGSPQ MGGQPGLRGP
QPLKMGMMNN PSPYGSPYTQ NSGQQIGASG LGLQIQTKTV LPNNLSPFAM DKKAVPGGGM
PSMGQQPTPS VQQPGLVTPV AAGMGSGAHT ADPEKRKLIQ QQLVLLLHAH KCQRREQANG
EVRQCNLPHC RTMKNVLNHM THCQSGKSCQ VAHCASSRQI ISHWKNCTRH DCPVCLPLKN
AGDKRNQQSI LTGAPVGLGN PSSLGVGQQS TPSLSTVSQI DPSSIERAYA ALGLPYQVNQ
IPPQPQVQAK NQQSQPSGQS PQGMRSVNNM SASPMGVNGG VGVQTPNLLS DSMLHSTINS
QNPMMSENAG VASLGPLPTA AQPSSTGIRK QWHEDITQDL RNHLVHKLVQ AIFPTPDPAA
LKDRRMENLV AYARKVEGDM YESANNRAEY YHLLAEKIYK IQKELEEKRR TRLQKQNMLP
NAPGMGPVPM NTGSNMGQQP TGMTTNGPVP DPSMIRGSVP NHMMPRMTPQ PGLNQFGQMN
MPQPPIGPRQ PSPLQHHGQL AQSGSLNPPM GYGPRMQQAS GQNQFLSQTQ FTSQGMNVTN
MPLAPSSGQA PVSQAQMSSS SCPVNSPIMP PGSQGSHIHC PTLPQQAHQN SPSPVPSRTP
TPHHTPPSIG NQPPPATAIP TPVPTPPAIP PGPQPPSLHP SSRQTPTPPT HLPPQVQPSL
PAAPSADQSQ QQPRSQQSTA VSVPTPTAPL LPPQPSTPLS QPAVSIEGQV SNPPSTSSTE
VNSQTIPEKQ PSQEVKMESK MEVDKPEPAD AQPEDTKEAK GEDVKVEPTE MEERGPELKT
DGKEEEEQPS TSATQSSPAP GQSKKKIFKP EELRQALMPT LEALYRQDPE SLPFRQPVDP
QLLGIPDYFD IVKSPMDLST IKRKLDTGQY QEPWQYIDDI WLMFNNAWLY NRKTSRVYKY
CSKLSEVFEQ EIDPVMQSLG YCCGRKLEFS PQTLCCYGKQ LCTIPRDATY YSYQNRYHFC
EKCFNEIQGE SVSLGDDPSQ PQTTINKEQF SKRKNDTLDP ELFVECTECG RKMHQICVLH
HEIIWPSGFV CDGCLKKTAR TRKENKLSAK RLPSTRLGTF LENRVNDFLR RQNHPESGEV
TVRVVHASDK TVEVKPGMKA RFVDSGEMAE SFPYRTKALF AFEEIDGVDL CFFGMHVQEY
GSDCPPPNQR RVYISYLDSV HFFRPKCLRT AVYHEILIGY LEYVKKLGYT TGHIWACPPS
EGDDYIFHCH PPDQKIPKPK RLQEWYKKML DKAVSERIVH DYKDILKQAT EDRLTSAKEL
PYFEGDFWPN VLEESIKELE QEEEERKREE NTSNESTDVT KGDSKNAKKK NNKKTSKNKS
SLSRGNKKKP GMPNVSNDLS QKLYATMEKH KEVFFVIRLI ACPAPNSLPP IVDPDPLIPC
DLMDGRDAFL TLARDKHLEF SSLRRAQWST MCMLVELHTQ SQDRFVYTCN ECKHHVETRW
HCTVCEDYDL CITCYNTKNH DHKMEKLGLG LDDESNNQQA AATQSPGDSR RLSIQRCIQS
LVHACQCRNA NCSLPSCQKM KRVVQHTKGC KRKTNGGCPI CKQLIALCCY HAKHCQENKC
PVPFCLNIKQ KLRQQQLQHR LQQAQMLRRR MASMQRTGVA GQQQGLPSPT PATPTTPTGQ
QPATPQTPQP QPTSQPQPTP PNNMTPYLPR TQTTGPVSQG KAPGQVTPPT PPQTAQAPLP
GPPPAAVEMA MQIQRAAETQ RQMAHVQIFQ RPIQHQMPQM SPMAPMGMNP PPMARGPGGH
LDPGIGPAGM QQQPPWAQGG MPQPQQMQSG MPRPAMMSVA QHGQPLNMAP QPGLGQVGVS
PLKPGTVSQQ ALQNLLRTLR SPSSPLQQQQ VLSILHANPQ LLAAFIKQRA AKYANPNPQP
LPGQPGMTQG QPGLQPPTMP GQQGVHSNPA LQNMNPLQAG VQRAGLPQQQ PQQQLQPPMG
AMSPQAQQMN MNHNTMPSQF RDILRRQMMQ QQGAGPGIGP GMANQFQQPQ GIGYPPQQQQ
QQRMQHHMQQ MQQGNMGQMG QLPQALGAEA GASLQAYQQR LLQQQMGSPA QPNPMSPQQH
MLPNQAQSPH LQGQQIPNSL SNQVRSPQPV PSPRPQSQPP HSSPSPRMQP QPSPHHVSPQ
TSSPHPGLVA AQAANPMEQG HFASPDQNSM LSQLASNPGM ANLHGASATD LGLSSDNADL
NSNLSQSTLD IH


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