EP300_MOUSE
ID EP300_MOUSE Reviewed; 2412 AA.
AC B2RWS6; E9PYJ8;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Histone acetyltransferase p300;
DE Short=p300 HAT;
DE EC=2.3.1.48 {ECO:0000269|PubMed:28576496};
DE AltName: Full=E1A-associated protein p300;
DE AltName: Full=Histone butyryltransferase p300;
DE EC=2.3.1.- {ECO:0000269|PubMed:27105113};
DE AltName: Full=Histone crotonyltransferase p300;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q09472};
DE AltName: Full=Protein 2-hydroxyisobutyryltransferase p300 {ECO:0000250|UniProtKB:Q09472};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q09472};
DE AltName: Full=Protein lactyltransferas p300;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q09472};
DE AltName: Full=Protein propionyltransferase p300;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q09472};
GN Name=Ep300; Synonyms=P300;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND INTERACTION WITH NEUROD1.
RX PubMed=9512516; DOI=10.1101/gad.12.6.820;
RA Mutoh H., Naya F.J., Tsai M.J., Leiter A.B.;
RT "The basic helix-loop-helix protein BETA2 interacts with p300 to coordinate
RT differentiation of secretin-expressing enteroendocrine cells.";
RL Genes Dev. 12:820-830(1998).
RN [4]
RP INTERACTION WITH CITED2.
RX PubMed=10593900; DOI=10.1074/jbc.274.51.36159;
RA Glenn D.J., Maurer R.A.;
RT "MRG1 binds to the LIM domain of Lhx2 and may function as a coactivator to
RT stimulate glycoprotein hormone alpha-subunit gene expression.";
RL J. Biol. Chem. 274:36159-36167(1999).
RN [5]
RP INTERACTION WITH CITED1.
RX PubMed=10722728; DOI=10.1074/jbc.275.12.8825;
RA Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S., Roberts A.B.,
RA Isselbacher K.J., Shioda T.;
RT "The MSG1 non-DNA-binding transactivator binds to the p300/CBP
RT coactivators, enhancing their functional link to the Smad transcription
RT factors.";
RL J. Biol. Chem. 275:8825-8834(2000).
RN [6]
RP INTERACTION WITH NR4A3.
RX PubMed=12709428; DOI=10.1074/jbc.m300088200;
RA Wansa K.D., Harris J.M., Yan G., Ordentlich P., Muscat G.E.;
RT "The AF-1 domain of the orphan nuclear receptor NOR-1 mediates trans-
RT activation, coactivator recruitment, and activation by the purine anti-
RT metabolite 6-mercaptopurine.";
RL J. Biol. Chem. 278:24776-24790(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH NPAS2.
RX PubMed=14645221; DOI=10.1074/jbc.m311973200;
RA Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M.,
RA Chakravarti D., FitzGerald G.A., McNamara P.;
RT "Histone acetyltransferase-dependent chromatin remodeling and the vascular
RT clock.";
RL J. Biol. Chem. 279:7091-7097(2004).
RN [8]
RP INTERACTION WITH MYOCD.
RX PubMed=15601857; DOI=10.1128/mcb.25.1.364-376.2005;
RA Cao D., Wang Z., Zhang C.L., Oh J., Xing W., Li S., Richardson J.A.,
RA Wang D.Z., Olson E.N.;
RT "Modulation of smooth muscle gene expression by association of histone
RT acetyltransferases and deacetylases with myocardin.";
RL Mol. Cell. Biol. 25:364-376(2005).
RN [9]
RP INTERACTION WITH HIPK2, AND PHOSPHORYLATION BY HIPK2.
RX PubMed=16917507; DOI=10.1038/sj.emboj.7601273;
RA Aikawa Y., Nguyen L.A., Isono K., Takakura N., Tagata Y., Schmitz M.L.,
RA Koseki H., Kitabayashi I.;
RT "Roles of HIPK1 and HIPK2 in AML1- and p300-dependent transcription,
RT hematopoiesis and blood vessel formation.";
RL EMBO J. 25:3955-3965(2006).
RN [10]
RP FUNCTION, AND INTERACTION WITH CEBPB.
RX PubMed=18486321; DOI=10.1016/j.mce.2008.03.009;
RA Cesena T.I., Cui T.X., Subramanian L., Fulton C.T., Iniguez-Lluhi J.A.,
RA Kwok R.P., Schwartz J.;
RT "Acetylation and deacetylation regulate CCAAT/enhancer binding protein beta
RT at K39 in mediating gene transcription.";
RL Mol. Cell. Endocrinol. 289:94-101(2008).
RN [11]
RP INTERACTION WITH CEBPB, AND SUBCELLULAR LOCATION.
RX PubMed=19324970; DOI=10.1210/me.2008-0277;
RA Ohoka N., Kato S., Takahashi Y., Hayashi H., Sato R.;
RT "The orphan nuclear receptor RORalpha restrains adipocyte differentiation
RT through a reduction of C/EBPbeta activity and perilipin gene expression.";
RL Mol. Endocrinol. 23:759-771(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP INTERACTION WITH RB1.
RX PubMed=20940255; DOI=10.1242/jcs.068924;
RA Pickard A., Wong P.P., McCance D.J.;
RT "Acetylation of Rb by PCAF is required for nuclear localization and
RT keratinocyte differentiation.";
RL J. Cell Sci. 123:3718-3726(2010).
RN [14]
RP FUNCTION IN ACETYLATION OF ZBTB7B.
RX PubMed=20810990; DOI=10.4049/jimmunol.1001462;
RA Zhang M., Zhang J., Rui J., Liu X.;
RT "p300-mediated acetylation stabilizes the Th-inducing POK factor.";
RL J. Immunol. 185:3960-3969(2010).
RN [15]
RP FUNCTION IN ACETYLATION OF XBP1.
RX PubMed=20955178; DOI=10.1042/bj20101293;
RA Wang F.M., Chen Y.J., Ouyang H.J.;
RT "Regulation of unfolded protein response modulator XBP1s by acetylation and
RT deacetylation.";
RL Biochem. J. 433:245-252(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1179; LYS-1557 AND LYS-1559, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [17]
RP FUNCTION.
RX PubMed=25200183; DOI=10.1016/j.cmet.2014.08.001;
RA Ryu D., Jo Y.S., Lo Sasso G., Stein S., Zhang H., Perino A., Lee J.U.,
RA Zeviani M., Romand R., Hottiger M.O., Schoonjans K., Auwerx J.;
RT "A SIRT7-dependent acetylation switch of GABPbeta1 controls mitochondrial
RT function.";
RL Cell Metab. 20:856-869(2014).
RN [18]
RP FUNCTION, AND INTERACTION WITH ATF5 AND CEBPB.
RX PubMed=24216764; DOI=10.1128/mcb.00956-13;
RA Zhao Y., Zhang Y.D., Zhang Y.Y., Qian S.W., Zhang Z.C., Li S.F., Guo L.,
RA Liu Y., Wen B., Lei Q.Y., Tang Q.Q., Li X.;
RT "p300-dependent acetylation of activating transcription factor 5 enhances
RT C/EBPbeta transactivation of C/EBPalpha during 3T3-L1 differentiation.";
RL Mol. Cell. Biol. 34:315-324(2014).
RN [19]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014;
RA Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z.,
RA Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J.,
RA Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C., Panne D.,
RA Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.;
RT "Dynamic competing histone H4 K5K8 acetylation and butyrylation are
RT hallmarks of highly active gene promoters.";
RL Mol. Cell 62:169-180(2016).
RN [20]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28576496; DOI=10.1016/j.bbrc.2017.05.170;
RA Noritsugu K., Ito A., Nakao Y., Yoshida M.;
RT "Identification of zinc finger transcription factor EGR2 as a novel
RT acetylated protein.";
RL Biochem. Biophys. Res. Commun. 489:455-459(2017).
RN [21]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28883095; DOI=10.1242/jcs.206904;
RA Lai Y., Li J., Li X., Zou C.;
RT "Lipopolysaccharide modulates p300 and Sirt1 to promote PRMT1 stability via
RT an SCFFbxl17-recognized acetyldegron.";
RL J. Cell Sci. 130:3578-3587(2017).
CC -!- FUNCTION: Functions as histone acetyltransferase and regulates
CC transcription via chromatin remodeling (By similarity). Acetylates all
CC four core histones in nucleosomes (By similarity). Histone acetylation
CC gives an epigenetic tag for transcriptional activation (By similarity).
CC Mediates cAMP-gene regulation by binding specifically to phosphorylated
CC CREB protein (PubMed:18486321, PubMed:24216764). Mediates acetylation
CC of histone H3 at 'Lys-122' (H3K122ac), a modification that localizes at
CC the surface of the histone octamer and stimulates transcription,
CC possibly by promoting nucleosome instability (By similarity). Mediates
CC acetylation of histone H3 at 'Lys-27' (H3K27ac) (By similarity). Also
CC functions as acetyltransferase for non-histone targets, such as ALX1,
CC HDAC1, PRMT1 or SIRT2 (PubMed:28883095, PubMed:28576496). Acetylates
CC 'Lys-131' of ALX1 and acts as its coactivator (By similarity).
CC Acetylates SIRT2 and is proposed to indirectly increase the
CC transcriptional activity of TP53 through acetylation and subsequent
CC attenuation of SIRT2 deacetylase function (By similarity). Following
CC DNA damage, forms a stress-responsive p53/TP53 coactivator complex with
CC JMY which mediates p53/TP53 acetylation, thereby increasing p53/TP53-
CC dependent transcription and apoptosis (By similarity). Promotes
CC chromatin acetylation in heat shock responsive HSP genes during the
CC heat shock response (HSR), thereby stimulating HSR transcription (By
CC similarity). Acetylates HDAC1 leading to its inactivation and
CC modulation of transcription (By similarity). Acetylates 'Lys-247' of
CC EGR2 (PubMed:28576496). Acts as a TFAP2A-mediated transcriptional
CC coactivator in presence of CITED2 (By similarity). Plays a role as a
CC coactivator of NEUROD1-dependent transcription of the secretin and p21
CC genes and controls terminal differentiation of cells in the intestinal
CC epithelium (By similarity). Promotes cardiac myocyte enlargement (By
CC similarity). Can also mediate transcriptional repression (By
CC similarity). Acetylates FOXO1 and enhances its transcriptional activity
CC (By similarity). Acetylates BCL6 wich disrupts its ability to recruit
CC histone deacetylases and hinders its transcriptional repressor activity
CC (By similarity). Participates in CLOCK or NPAS2-regulated rhythmic gene
CC transcription; exhibits a circadian association with CLOCK or NPAS2,
CC correlating with increase in PER1/2 mRNA and histone H3 acetylation on
CC the PER1/2 promoter (By similarity). Acetylates MTA1 at 'Lys-626' which
CC is essential for its transcriptional coactivator activity
CC (PubMed:14645221, PubMed:9512516). Acetylates XBP1 isoform 2;
CC acetylation increases protein stability of XBP1 isoform 2 and enhances
CC its transcriptional activity (PubMed:20955178). Acetylates PCNA;
CC acetylation promotes removal of chromatin-bound PCNA and its
CC degradation during nucleotide excision repair (NER) (By similarity).
CC Acetylates MEF2D (By similarity). Acetylates and stabilizes ZBTB7B
CC protein by antagonizing ubiquitin conjugation and degradation, this
CC mechanism may be involved in CD4/CD8 lineage differentiation
CC (PubMed:20810990). Acetylates GABPB1, impairing GABPB1
CC heterotetramerization and activity (PubMed:25200183). Acetylates PCK1
CC and promotes PCK1 anaplerotic activity (By similarity). Acetylates RXRA
CC and RXRG (By similarity). Acetylates isoform M2 of PKM (PKM2),
CC promoting its homodimerization and conversion into a protein kinase (By
CC similarity). In addition to protein acetyltransferase, can use
CC different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-
CC CoA), butanoyl-CoA (butyryl-CoA), 2-hydroxyisobutanoyl-CoA (2-
CC hydroxyisobutyryl-CoA), lactoyl-CoA or propanoyl-CoA (propionyl-CoA),
CC and is able to mediate protein crotonylation, butyrylation, 2-
CC hydroxyisobutyrylation, lactylation or propionylation, respectively
CC (PubMed:27105113). Acts as a histone crotonyltransferase; crotonylation
CC marks active promoters and enhancers and confers resistance to
CC transcriptional repressors. Histone crotonyltransferase activity is
CC dependent on the concentration of (2E)-butenoyl-CoA (crotonyl-CoA)
CC substrate and such activity is weak when (2E)-butenoyl-CoA (crotonyl-
CC CoA) concentration is low (By similarity). Also acts as a histone
CC butyryltransferase; butyrylation marks active promoters
CC (PubMed:27105113). Catalyzes histone lactylation in macrophages by
CC using lactoyl-CoA directly derived from endogenous or exogenous
CC lactate, leading to stimulates gene transcription (By similarity). Acts
CC as a protein-lysine 2-hydroxyisobutyryltransferase; regulates
CC glycolysis by mediating 2-hydroxyisobutyrylation of glycolytic enzymes.
CC Functions as a transcriptional coactivator for SMAD4 in the TGF-beta
CC signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q09472,
CC ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:18486321,
CC ECO:0000269|PubMed:20810990, ECO:0000269|PubMed:24216764,
CC ECO:0000269|PubMed:25200183, ECO:0000269|PubMed:27105113,
CC ECO:0000269|PubMed:28576496, ECO:0000269|PubMed:28883095,
CC ECO:0000269|PubMed:9512516, ECO:0000305|PubMed:20955178}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000269|PubMed:28576496, ECO:0000305|PubMed:28883095};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC Evidence={ECO:0000250|UniProtKB:Q09472};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-butanoyl-
CC L-lysyl-[protein]; Xref=Rhea:RHEA:53912, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:13708, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57371, ChEBI:CHEBI:137955;
CC Evidence={ECO:0000269|PubMed:27105113};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-
CC (2E)-butenoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:53908, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:137954; Evidence={ECO:0000250|UniProtKB:Q09472};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + propanoyl-CoA = CoA + H(+) + N(6)-
CC propanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54020, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:13758, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:138019; Evidence={ECO:0000250|UniProtKB:Q09472};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H(+) +
CC N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:24180,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:131780,
CC ChEBI:CHEBI:144968; Evidence={ECO:0000250|UniProtKB:Q09472};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181;
CC Evidence={ECO:0000250|UniProtKB:Q09472};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + lactoyl-CoA = CoA + H(+) + N(6)-lactoyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:61996, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:16001, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57382, ChEBI:CHEBI:145324;
CC Evidence={ECO:0000250|UniProtKB:Q09472};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61997;
CC Evidence={ECO:0000250|UniProtKB:Q09472};
CC -!- SUBUNIT: Interacts with HIF1A; the interaction is stimulated in
CC response to hypoxia and inhibited by CITED2. Probably part of a complex
CC with HIF1A and CREBBP. Interacts (via N-terminus) with TFAP2A (via N-
CC terminus); the interaction requires CITED2 (By similarity). Interacts
CC (via CH1 domain) with CITED2 (via C-terminus) (PubMed:10593900).
CC Interacts with CITED1 (unphosphorylated form preferentially and via C-
CC terminus) (PubMed:10722728). Interacts with ESR1; the interaction is
CC estrogen-dependent and enhanced by CITED1 (By similarity). Interacts
CC with HIPK2 (PubMed:16917507). Interacts with DTX1, EID1, ELF3, FEN1,
CC LEF1, NCOA1, NCOA6, NR3C1, PCAF, PELP1, PRDM6, SP1, SP3, SPIB, SRY,
CC TCF7L2, DDX5, DDX17, SATB1, SRCAP and TRERF1 (By similarity). Interacts
CC with JMY, the complex activates p53/TP53 transcriptional activity.
CC Interacts with TTC5/STRAP; the interaction facilitates the association
CC between JMY and p300/EP300 cofactors. Interacts with p53/TP53; the
CC interation is facilitated by TTC5/STRAP. Forms a complex with
CC TTC5/STRAP and HSF1; these interactions augment chromatin-bound HSF1
CC and p300/EP300 histone acetyltransferase activity (By similarity). Part
CC of a complex containing CARM1 and NCOA2/GRIP1. Interacts with ING4 and
CC this interaction may be indirect. Interacts with ING5. Interacts with
CC the C-terminal region of CITED4. Non-sumoylated EP300 preferentially
CC interacts with SENP3. Interacts with SS18L1/CREST. Interacts with ALX1
CC (via homeobox domain) (By similarity). Interacts with NEUROD1; the
CC interaction is inhibited by NR0B2 (PubMed:9512516). Interacts with TCF3
CC (By similarity). Interacts (via CREB-binding domain) with MYOCD (via C-
CC terminus) (PubMed:15601857). Interacts with ROCK2 and PPARG. Forms a
CC complex made of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates
CC hypertrophy in cardiomyocytes. Interacts with IRF1 and this interaction
CC enhances acetylation of p53/TP53 and stimulation of its activity.
CC Interacts with FOXO1; the interaction acetylates FOXO1 and enhances its
CC transcriptional activity. Interacts with ALKBH4 and DDIT3/CHOP.
CC Interacts with KLF15 (By similarity). Interacts with CEBPB and RORA
CC (PubMed:18486321, PubMed:24216764). Interacts with NPAS2, ARNTL/BMAL1
CC and CLOCK. Interacts with SIRT2 isoform 1, isoform 2 and isoform 5.
CC Interacts with MTA1. Interacts with HDAC4 and HDAC5 in the presence of
CC TFAP2C. Interacts with TRIP4 (By similarity). Interacts with NPAS2
CC (PubMed:14645221). Directly interacts with ZBTB49; this interaction
CC leads to synergistic transactivation of CDKN1A (By similarity).
CC Interacts with NR4A3 (PubMed:12709428). Interacts with ZNF451 (By
CC similarity). Interacts with ATF5; EP300 is required for ATF5 and CEBPB
CC interaction and DNA binding (PubMed:24216764). Interacts with HSF1.
CC Interacts with ZBTB48/TZAP. Interacts with STAT1; the interaction is
CC enhanced upon IFN-gamma stimulation. Interacts with HNRNPU (via C-
CC terminus); this interaction enhances DNA-binding of HNRNPU to nuclear
CC scaffold/matrix attachment region (S/MAR) elements. Interacts with
CC BCL11B. Interacts with SMAD4; negatively regulated by ZBTB7A. Interacts
CC with DUX4 (via C-terminus). Interacts with NUPR1; this interaction
CC enhances the effect of EP300 on PAX2 transcription factor activity.
CC Interacts with RXRA; the interaction is decreased by 9-cis retinoic
CC acid. NR4A1 competes with EP300 for interaction with RXRA and thereby
CC attenuates EP300 mediated acetylation of RXRA (By similarity).
CC Interacts with RB1 (PubMed:20940255). Interacts with DDX3X; this
CC interaction may facilitate HNF4A acetylation. Interacts with SOX9.
CC Interacts with ATF4; EP300/p300 stabilizes ATF4 and increases its
CC transcriptional activity independently of its catalytic activity by
CC preventing its ubiquitination (By similarity). Interacts with KAT5;
CC promoting KAT5 autoacetylation (By similarity).
CC {ECO:0000250|UniProtKB:Q09472, ECO:0000269|PubMed:10593900,
CC ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:12709428,
CC ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:15601857,
CC ECO:0000269|PubMed:16917507, ECO:0000269|PubMed:18486321,
CC ECO:0000269|PubMed:19324970, ECO:0000269|PubMed:20940255,
CC ECO:0000269|PubMed:24216764, ECO:0000269|PubMed:9512516}.
CC -!- INTERACTION:
CC B2RWS6; P02340: Tp53; NbExp=3; IntAct=EBI-3953360, EBI-474016;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q09472}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00311, ECO:0000269|PubMed:19324970}.
CC Note=In the presence of ALX1 relocalizes from the cytoplasm to the
CC nucleus. Colocalizes with ROCK2 in the nucleus.
CC {ECO:0000250|UniProtKB:Q09472}.
CC -!- DOMAIN: The CRD1 domain (cell cycle regulatory domain 1) mediates
CC transcriptional repression of a subset of p300 responsive genes; it can
CC be de-repressed by CDKN1A/p21WAF1 at least at some promoters. It
CC conatins sumoylation and acetylation sites and the same lysine residues
CC may be targeted for the respective modifications. It is proposed that
CC deacetylation by SIRT1 allows sumoylation leading to suppressed
CC activity (By similarity). {ECO:0000250|UniProtKB:Q09472}.
CC -!- PTM: Acetylated on Lys at up to 17 positions by intermolecular
CC autocatalysis. Deacetylated in the transcriptional repression domain
CC (CRD1) by SIRT1, preferentially at Lys-1019. Deacetylated by SIRT2,
CC preferentially at Lys-419, Lys-424, Lys-1541, Lys-1545, Lys-1548, Lys-
CC 1698, Lys-1703 and Lys-1706. {ECO:0000250|UniProtKB:Q09472}.
CC -!- PTM: Citrullinated at Arg-2143 by PADI4, which impairs methylation by
CC CARM1 and promotes interaction with NCOA2/GRIP1.
CC {ECO:0000250|UniProtKB:Q09472}.
CC -!- PTM: Methylated at Arg-581 and Arg-605 in the KIX domain by CARM1,
CC which blocks association with CREB, inhibits CREB signaling and
CC activates apoptotic response. Also methylated at Arg-2143 by CARM1,
CC which impairs interaction with NCOA2/GRIP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q09472}.
CC -!- PTM: Sumoylated; sumoylation in the transcriptional repression domain
CC (CRD1) mediates transcriptional repression. Desumoylated by SENP3
CC through the removal of SUMO2 and SUMO3 (By similarity).
CC {ECO:0000250|UniProtKB:Q09472}.
CC -!- PTM: Probable target of ubiquitination by FBXO3, leading to rapid
CC proteasome-dependent degradation. {ECO:0000250|UniProtKB:Q09472}.
CC -!- PTM: Phosphorylation at Ser-89 by AMPK reduces interaction with nuclear
CC receptors, such as PPARG (By similarity). Phosphorylated by HIPK2 in a
CC RUNX1-dependent manner. This phosphorylation that activates EP300
CC happens when RUNX1 is associated with DNA and CBFB. Phosphorylated by
CC ROCK2 and this enhances its activity (By similarity).
CC {ECO:0000250|UniProtKB:Q09472}.
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DR EMBL; AC102262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC160528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC144976; AAI44977.1; -; mRNA.
DR EMBL; BC150681; AAI50682.1; -; mRNA.
DR CCDS; CCDS37149.1; -.
DR RefSeq; NP_808489.4; NM_177821.6.
DR AlphaFoldDB; B2RWS6; -.
DR BMRB; B2RWS6; -.
DR SMR; B2RWS6; -.
DR BioGRID; 236625; 89.
DR CORUM; B2RWS6; -.
DR DIP; DIP-60610N; -.
DR IntAct; B2RWS6; 9.
DR MINT; B2RWS6; -.
DR STRING; 10090.ENSMUSP00000066789; -.
DR iPTMnet; B2RWS6; -.
DR PhosphoSitePlus; B2RWS6; -.
DR SwissPalm; B2RWS6; -.
DR EPD; B2RWS6; -.
DR PaxDb; B2RWS6; -.
DR PeptideAtlas; B2RWS6; -.
DR PRIDE; B2RWS6; -.
DR ProteomicsDB; 275928; -.
DR Antibodypedia; 296; 1061 antibodies from 40 providers.
DR DNASU; 328572; -.
DR Ensembl; ENSMUST00000068387; ENSMUSP00000066789; ENSMUSG00000055024.
DR GeneID; 328572; -.
DR KEGG; mmu:328572; -.
DR UCSC; uc007wws.1; mouse.
DR CTD; 2033; -.
DR MGI; MGI:1276116; Ep300.
DR VEuPathDB; HostDB:ENSMUSG00000055024; -.
DR eggNOG; KOG1778; Eukaryota.
DR GeneTree; ENSGT00940000155497; -.
DR HOGENOM; CLU_000162_2_0_1; -.
DR InParanoid; B2RWS6; -.
DR OMA; GQPGMNI; -.
DR OrthoDB; 236283at2759; -.
DR PhylomeDB; B2RWS6; -.
DR TreeFam; TF101097; -.
DR BRENDA; 2.3.1.48; 3474.
DR Reactome; R-MMU-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-MMU-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-MMU-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
DR Reactome; R-MMU-3371568; Attenuation phase.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-MMU-5689901; Metalloprotease DUBs.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-MMU-6804760; Regulation of TP53 Activity through Methylation.
DR Reactome; R-MMU-6811555; PI5P Regulates TP53 Acetylation.
DR Reactome; R-MMU-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-MMU-8941856; RUNX3 regulates NOTCH signaling.
DR Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-MMU-8951936; RUNX3 regulates p14-ARF.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR Reactome; R-MMU-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-MMU-918233; TRAF3-dependent IRF activation pathway.
DR Reactome; R-MMU-933541; TRAF6 mediated IRF7 activation.
DR Reactome; R-MMU-9617629; Regulation of FOXO transcriptional activity by acetylation.
DR Reactome; R-MMU-9701898; STAT3 nuclear events downstream of ALK signaling.
DR Reactome; R-MMU-9759194; Nuclear events mediated by NFE2L2.
DR BioGRID-ORCS; 328572; 18 hits in 82 CRISPR screens.
DR ChiTaRS; Ep300; mouse.
DR PRO; PR:B2RWS6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; B2RWS6; protein.
DR Bgee; ENSMUSG00000055024; Expressed in embryonic post-anal tail and 221 other tissues.
DR ExpressionAtlas; B2RWS6; baseline and differential.
DR Genevisible; B2RWS6; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:UniProtKB.
DR GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; ISO:MGI.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; ISO:MGI.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0140069; F:histone butyryltransferase activity; IDA:UniProtKB.
DR GO; GO:0140068; F:histone crotonyltransferase activity; ISS:UniProtKB.
DR GO; GO:0120301; F:histone lactyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; ISS:UniProtKB.
DR GO; GO:0051059; F:NF-kappaB binding; ISO:MGI.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:0002039; F:p53 binding; IPI:MGI.
DR GO; GO:0106226; F:peptide 2-hydroxyisobutyryltransferase activity; IEA:RHEA.
DR GO; GO:0140065; F:peptide butyryltransferase activity; ISO:MGI.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IDA:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0061920; F:protein propionyltransferase activity; ISS:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI.
DR GO; GO:0097677; F:STAT family protein binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; IMP:MGI.
DR GO; GO:0002209; P:behavioral defense response; IMP:ARUK-UCL.
DR GO; GO:0051216; P:cartilage development; NAS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IDA:UniProtKB.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; ISS:UniProtKB.
DR GO; GO:0060325; P:face morphogenesis; IMP:ARUK-UCL.
DR GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
DR GO; GO:0043969; P:histone H2B acetylation; ISS:UniProtKB.
DR GO; GO:0097043; P:histone H3-K56 acetylation; IDA:MGI.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; ISO:MGI.
DR GO; GO:0006475; P:internal protein amino acid acetylation; ISS:UniProtKB.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:MGI.
DR GO; GO:0007611; P:learning or memory; IMP:ARUK-UCL.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0010742; P:macrophage derived foam cell differentiation; ISS:UniProtKB.
DR GO; GO:0035855; P:megakaryocyte development; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:ARUK-UCL.
DR GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; ISS:UniProtKB.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; ISO:MGI.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0018394; P:peptidyl-lysine acetylation; ISO:MGI.
DR GO; GO:0140067; P:peptidyl-lysine butyrylation; IDA:UniProtKB.
DR GO; GO:0140066; P:peptidyl-lysine crotonylation; ISS:UniProtKB.
DR GO; GO:0061921; P:peptidyl-lysine propionylation; ISS:UniProtKB.
DR GO; GO:0030220; P:platelet formation; IMP:MGI.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:MGI.
DR GO; GO:1905636; P:positive regulation of RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006990; P:positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0006473; P:protein acetylation; IDA:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; ISO:MGI.
DR GO; GO:0006110; P:regulation of glycolytic process; ISS:UniProtKB.
DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; ISS:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
DR GO; GO:0001756; P:somitogenesis; IGI:MGI.
DR GO; GO:0036268; P:swimming; IMP:ARUK-UCL.
DR GO; GO:0001966; P:thigmotaxis; IMP:ARUK-UCL.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI.
DR CDD; cd15802; RING_CBP-p300; 1.
DR Gene3D; 1.10.1630.10; -; 1.
DR Gene3D; 1.10.246.20; -; 1.
DR Gene3D; 1.20.1020.10; -; 2.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 2.10.110.40; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR003101; KIX_dom.
DR InterPro; IPR036529; KIX_dom_sf.
DR InterPro; IPR009110; Nuc_rcpt_coact.
DR InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
DR InterPro; IPR037073; Nuc_rcpt_coact_CREBbp_sf.
DR InterPro; IPR010303; RING_CBP-p300.
DR InterPro; IPR038547; RING_CBP-p300_sf.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; PTHR13808; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF09030; Creb_binding; 1.
DR Pfam; PF06001; DUF902; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF02172; KIX; 1.
DR Pfam; PF02135; zf-TAZ; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47040; SSF47040; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57933; SSF57933; 2.
DR SUPFAM; SSF69125; SSF69125; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS50952; KIX; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Biological rhythms; Bromodomain; Cell cycle;
KW Citrullination; Coiled coil; Cytoplasm; Differentiation; Isopeptide bond;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Transferase;
KW Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT CHAIN 2..2412
FT /note="Histone acetyltransferase p300"
FT /id="PRO_0000409386"
FT DOMAIN 567..646
FT /note="KIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00311"
FT DOMAIN 1066..1138
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 1286..1662
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01065"
FT ZN_FING 332..418
FT /note="TAZ-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT ZN_FING 1664..1712
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1727..1808
FT /note="TAZ-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..149
FT /note="Interaction with RORA"
FT REGION 2..139
FT /note="Interaction with ALX1"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT REGION 130..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1028
FT /note="CRD1; mediates transcriptional repression"
FT /evidence="ECO:0000250"
FT REGION 1396..1398
FT /note="Interaction with histone"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT REGION 1519..1577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1830..1925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1991..2011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2042..2237
FT /note="Interaction with NCOA2"
FT /evidence="ECO:0000250"
FT REGION 2094..2133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2192..2236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2263..2348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1510..1539
FT /evidence="ECO:0000255"
FT MOTIF 11..17
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 776..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..900
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..1028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1519..1546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1564
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1850..1885
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1886..1904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1905..1925
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1996..2011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2106..2133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2203..2236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2263..2307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2308..2339
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1397..1399
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1409..1410
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1456
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1461
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1465
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1669
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1672
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1682
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1685
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1691
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1694
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1700
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1702
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT SITE 2089
FT /note="Interaction with NCOA2"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT SITE 2143
FT /note="Interaction with NCOA2"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 89
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 419
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 424
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 581
FT /note="Asymmetric dimethylarginine; by CARM1"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 605
FT /note="Asymmetric dimethylarginine; by CARM1"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 637
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 976
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 1019
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 1023
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 1037
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 1179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1335
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 1472
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 1498
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 1541
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 1545
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 1548
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 1553
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 1554
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 1557
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1559
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1582
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 1698
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 1703
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 1706
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 1725
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 2143
FT /note="Asymmetric dimethylarginine; by CARM1; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT MOD_RES 2143
FT /note="Citrulline; by PADI4; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT CROSSLNK 1019
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT CROSSLNK 1023
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT CONFLICT 677
FT /note="G -> E (in Ref. 2; AAI44977/AAI50682)"
FT /evidence="ECO:0000305"
FT CONFLICT 2217
FT /note="Q -> QQQQ (in Ref. 2; AAI44977/AAI50682)"
FT /evidence="ECO:0000305"
SQ 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
