EP300_HUMAN
ID EP300_HUMAN Reviewed; 2414 AA.
AC Q09472; B1AKC2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 261.
DE RecName: Full=Histone acetyltransferase p300;
DE Short=p300 HAT;
DE EC=2.3.1.48 {ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:23415232, ECO:0000269|PubMed:23934153, ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:8945521};
DE AltName: Full=E1A-associated protein p300;
DE AltName: Full=Histone butyryltransferase p300;
DE EC=2.3.1.- {ECO:0000269|PubMed:17267393};
DE AltName: Full=Histone crotonyltransferase p300;
DE EC=2.3.1.- {ECO:0000269|PubMed:25818647};
DE AltName: Full=Protein 2-hydroxyisobutyryltransferase p300;
DE EC=2.3.1.- {ECO:0000269|PubMed:29775581};
DE AltName: Full=Protein lactyltransferas p300;
DE EC=2.3.1.- {ECO:0000269|PubMed:31645732};
DE AltName: Full=Protein propionyltransferase p300;
DE EC=2.3.1.- {ECO:0000269|PubMed:17267393};
GN Name=EP300; Synonyms=P300;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-2223.
RX PubMed=7523245; DOI=10.1101/gad.8.8.869;
RA Eckner R., Ewen M.E., Newsome D., Gerdes M., Decaprio J.A., Lawrence J.B.,
RA Livingston D.M.;
RT "Molecular cloning and functional analysis of the adenovirus E1A-associated
RT 300-kD protein (p300) reveals a protein with properties of a
RT transcriptional adaptor.";
RL Genes Dev. 8:869-884(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-42, AND CHROMOSOMAL TRANSLOCATION WITH
RP KAT6A.
RX PubMed=10824998;
RX DOI=10.1002/(sici)1098-2264(200006)28:2<138::aid-gcc2>3.0.co;2-2;
RA Chaffanet M., Gressin L., Preudhomme C., Soenen-Cornu V., Birnbaum D.,
RA Pebusque M.-J.;
RT "MOZ is fused to p300 in an acute monocytic leukemia with t(8;22).";
RL Genes Chromosomes Cancer 28:138-144(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 552-660.
RX PubMed=7870179; DOI=10.1038/374085a0;
RA Lundblad J.R., Kwok R.P.S., Laurance M.E., Harter M.L., Goodman R.H.;
RT "Adenoviral E1A-associated protein p300 as a functional homologue of the
RT transcriptional co-activator CBP.";
RL Nature 374:85-88(1995).
RN [6]
RP PARTIAL PROTEIN SEQUENCE, INTERACTION WITH CARM1, METHYLATION AT ARG-580
RP AND ARG-604, AND FUNCTION.
RX PubMed=11701890; DOI=10.1126/science.1065961;
RA Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M.,
RA Evans R.M.;
RT "A transcriptional switch mediated by cofactor methylation.";
RL Science 294:2507-2511(2001).
RN [7]
RP INTERACTION WITH JMY.
RX PubMed=10518217; DOI=10.1016/s1097-2765(00)80338-x;
RA Shikama N., Lee C.-W., France S., Delavaine L., Lyon J.,
RA Krstic-Demonacos M., La Thangue N.B.;
RT "A novel cofactor for p300 that regulates the p53 response.";
RL Mol. Cell 4:365-376(1999).
RN [8]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=8945521; DOI=10.1016/s0092-8674(00)82001-2;
RA Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., Nakatani Y.;
RT "The transcriptional coactivators p300 and CBP are histone
RT acetyltransferases.";
RL Cell 87:953-959(1996).
RN [9]
RP INTERACTION WITH PCAF.
RX PubMed=8684459; DOI=10.1038/382319a0;
RA Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y.;
RT "A p300/CBP-associated factor that competes with the adenoviral oncoprotein
RT E1A.";
RL Nature 382:319-324(1996).
RN [10]
RP INTERACTION WITH HIF1A AND CREBBP.
RX PubMed=8917528; DOI=10.1073/pnas.93.23.12969;
RA Arany Z., Huang L.E., Eckner R., Bhattacharya S., Jiang C., Goldberg M.A.,
RA Bunn H.F., Livingston D.M.;
RT "An essential role for p300/CBP in the cellular response to hypoxia.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:12969-12973(1996).
RN [11]
RP INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION).
RX PubMed=9528808; DOI=10.1128/mcb.18.4.2392;
RA Bex F., Yin M.-J., Burny A., Gaynor R.B.;
RT "Differential transcriptional activation by human T-cell leukemia virus
RT type 1 Tax mutants is mediated by distinct interactions with CREB binding
RT protein and p300.";
RL Mol. Cell. Biol. 18:2392-2405(1998).
RN [12]
RP INTERACTION WITH NR3C1.
RX PubMed=9590696; DOI=10.1038/30032;
RA Fryer C.J., Archer T.K.;
RT "Chromatin remodelling by the glucocorticoid receptor requires the BRG1
RT complex.";
RL Nature 393:88-91(1998).
RN [13]
RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION), AND FUNCTION (MICROBIAL
RP INFECTION).
RX PubMed=10545121; DOI=10.1093/emboj/18.21.6106;
RA Kiernan R.E., Vanhulle C., Schiltz L., Adam E., Xiao H., Maudoux F.,
RA Calomme C., Burny A., Nakatani Y., Jeang K.-T., Benkirane M., Van Lint C.;
RT "HIV-1 tat transcriptional activity is regulated by acetylation.";
RL EMBO J. 18:6106-6118(1999).
RN [14]
RP INTERACTION WITH CITED2 AND HIF1A, AND MUTAGENESIS OF 371-THR--LEU-376 AND
RP 413-VAL--LYS-418.
RX PubMed=9887100; DOI=10.1101/gad.13.1.64;
RA Bhattacharya S., Michels C.M., Leung M.K., Arany Z.P., Kung A.L.,
RA Livingston D.M.;
RT "Functional role of p35srj, a novel p300/CBP binding protein, during
RT transactivation by HIF-1.";
RL Genes Dev. 13:64-75(1999).
RN [15]
RP INTERACTION WITH RORA.
RX PubMed=9862959; DOI=10.1093/nar/27.2.411;
RA Lau P., Bailey P., Dowhan D.H., Muscat G.E.;
RT "Exogenous expression of a dominant negative RORalpha1 vector in muscle
RT cells impairs differentiation: RORalpha1 directly interacts with p300 and
RT myoD.";
RL Nucleic Acids Res. 27:411-420(1999).
RN [16]
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 [17]
RP FUNCTION IN TRANSCRIPTIONAL REPRESSION.
RX PubMed=10733570; DOI=10.1128/mcb.20.8.2676-2686.2000;
RA Snowden A.W., Anderson L.A., Webster G.A., Perkins N.D.;
RT "A novel transcriptional repression domain mediates p21(WAF1/CIP1)
RT induction of p300 transactivation.";
RL Mol. Cell. Biol. 20:2676-2686(2000).
RN [18]
RP ERRATUM OF PUBMED:10733570.
RA Snowden A.W., Anderson L.A., Webster G.A., Perkins N.D.;
RL Mol. Cell. Biol. 20:5360-5360(2000).
RN [19]
RP INTERACTION WITH EID1.
RX PubMed=11073989; DOI=10.1128/mcb.20.23.8889-8902.2000;
RA Miyake S., Sellers W.R., Safran M., Li X., Zhao W., Grossman S.R., Gan J.,
RA DeCaprio J.A., Adams P.D., Kaelin W.G. Jr.;
RT "Cells degrade a novel inhibitor of differentiation with E1A-like
RT properties upon exiting the cell cycle.";
RL Mol. Cell. Biol. 20:8889-8902(2000).
RN [20]
RP INTERACTION WITH EID1.
RX PubMed=11073990; DOI=10.1128/mcb.20.23.8903-8915.2000;
RA MacLellan W.R., Xiao G., Abdellatif M., Schneider M.D.;
RT "A novel Rb- and p300-binding protein inhibits transactivation by MyoD.";
RL Mol. Cell. Biol. 20:8903-8915(2000).
RN [21]
RP INTERACTION WITH NCOA6.
RX PubMed=10823961; DOI=10.1073/pnas.97.11.6212;
RA Ko L., Cardona G.R., Chin W.W.;
RT "Thyroid hormone receptor-binding protein, an LXXLL motif-containing
RT protein, functions as a general coactivator.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:6212-6217(2000).
RN [22]
RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION), AND FUNCTION (MICROBIAL
RP INFECTION).
RX PubMed=11080476; DOI=10.1006/viro.2000.0593;
RA Deng L., de la Fuente C., Fu P., Wang L., Donnelly R., Wade J.D.,
RA Lambert P., Li H., Lee C.-G., Kashanchi F.;
RT "Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated
RT HIV-1 genome and enhances binding to core histones.";
RL Virology 277:278-295(2000).
RN [23]
RP INTERACTION WITH ESR1.
RX PubMed=11581164; DOI=10.1101/gad.906301;
RA Yahata T., Shao W., Endoh H., Hur J., Coser K.R., Sun H., Ueda Y., Kato S.,
RA Isselbacher K.J., Brown M., Shioda T.;
RT "Selective coactivation of estrogen-dependent transcription by CITED1
RT CBP/p300-binding protein.";
RL Genes Dev. 15:2598-2612(2001).
RN [24]
RP PHOSPHORYLATION AT SER-89, MUTAGENESIS OF SER-89, AND INTERACTION WITH
RP PPARG.
RX PubMed=11518699; DOI=10.1074/jbc.c100316200;
RA Yang W., Hong Y.H., Shen X.Q., Frankowski C., Camp H.S., Leff T.;
RT "Regulation of transcription by AMP-activated protein kinase:
RT phosphorylation of p300 blocks its interaction with nuclear receptors.";
RL J. Biol. Chem. 276:38341-38344(2001).
RN [25]
RP INTERACTION WITH SRCAP.
RX PubMed=11581372; DOI=10.1128/jvi.75.21.10033-10040.2001;
RA Xu X., Chackalaparampil I., Monroy M.A., Cannella M.T., Pesek E.,
RA Chrivia J., Yaciuk P.;
RT "Adenovirus DNA binding protein interacts with the SNF2-related CBP
RT activator protein (SrCap) and inhibits SrCap-mediated transcription.";
RL J. Virol. 75:10033-10040(2001).
RN [26]
RP FUNCTION, AND INTERACTION WITH TTC5 AND JMY.
RX PubMed=11511361; DOI=10.1016/s1097-2765(01)00277-5;
RA Demonacos C., Krstic-Demonacos M., La Thangue N.B.;
RT "A TPR motif cofactor contributes to p300 activity in the p53 response.";
RL Mol. Cell 8:71-84(2001).
RN [27]
RP INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION).
RX PubMed=11463834; DOI=10.1128/mcb.21.16.5520-5530.2001;
RA Scoggin K.E.S., Ulloa A., Nyborg J.K.;
RT "The oncoprotein Tax binds the SRC-1-interacting domain of CBP/p300 to
RT mediate transcriptional activation.";
RL Mol. Cell. Biol. 21:5520-5530(2001).
RN [28]
RP INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P30II (MICROBIAL INFECTION).
RX PubMed=11559821; DOI=10.1128/jvi.75.20.9885-9895.2001;
RA Zhang W., Nisbet J.W., Albrecht B., Ding W., Kashanchi F., Bartoe J.T.,
RA Lairmore M.D.;
RT "Human T-lymphotropic virus type 1 p30(II) regulates gene transcription by
RT binding CREB binding protein/p300.";
RL J. Virol. 75:9885-9895(2001).
RN [29]
RP INTERACTION WITH TRERF1.
RX PubMed=11349124; DOI=10.1074/jbc.m100113200;
RA Gizard F., Lavallee B., DeWitte F., Hum D.W.;
RT "A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate
RT human CYP11A1 gene expression.";
RL J. Biol. Chem. 276:33881-33892(2001).
RN [30]
RP INTERACTION WITH PELP1.
RX PubMed=11481323; DOI=10.1074/jbc.m103783200;
RA Vadlamudi R.K., Wang R.-A., Mazumdar A., Kim Y.-S., Shin J., Sahin A.,
RA Kumar R.;
RT "Molecular cloning and characterization of PELP1, a novel human coregulator
RT of estrogen receptor alpha.";
RL J. Biol. Chem. 276:38272-38279(2001).
RN [31]
RP INTERACTION WITH DTX1.
RX PubMed=11564735; DOI=10.1074/jbc.m105245200;
RA Yamamoto N., Yamamoto S., Inagaki F., Kawaichi M., Fukamizu A., Kishi N.,
RA Matsuno K., Nakamura K., Weinmaster G., Okano H., Nakafuku M.;
RT "Role of Deltex-1 as a transcriptional regulator downstream of the Notch
RT receptor.";
RL J. Biol. Chem. 276:45031-45040(2001).
RN [32]
RP FUNCTION, AND INTERACTION WITH FEN1.
RX PubMed=11430825; DOI=10.1016/s1097-2765(01)00272-6;
RA Hasan S., Stucki M., Hassa P.O., Imhof R., Gehrig P., Hunziker P.,
RA Hubscher U., Hottiger M.O.;
RT "Regulation of human flap endonuclease-1 activity by acetylation through
RT the transcriptional coactivator p300.";
RL Mol. Cell 7:1221-1231(2001).
RN [33]
RP INTERACTION WITH HADV5 E1A (MICROBIAL INFECTION).
RX PubMed=11433299; DOI=10.1038/35083062;
RA Chan H.M., Krstic-Demonacos M., Smith L., Demonacos C., La Thangue N.B.;
RT "Acetylation control of the retinoblastoma tumour-suppressor protein.";
RL Nat. Cell Biol. 3:667-674(2001).
RN [34]
RP INTERACTION WITH SPIB.
RX PubMed=11864910;
RA Yamamoto H., Kihara-Negishi F., Yamada T., Suzuki M., Nakano T., Oikawa T.;
RT "Interaction between the hematopoietic Ets transcription factor Spi-B and
RT the coactivator CREB-binding protein associated with negative cross-talk
RT with c-Myb.";
RL Cell Growth Differ. 13:69-75(2002).
RN [35]
RP INTERACTION WITH CITED4.
RX PubMed=11744733; DOI=10.1074/jbc.m110850200;
RA Braganca J., Swingler T., Marques F.I.R., Jones T., Eloranta J.J.,
RA Hurst H.C., Shioda T., Bhattacharya S.;
RT "Human CREB-binding protein/p300-interacting transactivator with ED-rich
RT tail (CITED) 4, a new member of the CITED family, functions as a co-
RT activator for transcription factor AP-2.";
RL J. Biol. Chem. 277:8559-8565(2002).
RN [36]
RP INTERACTION WITH NUPR1.
RX PubMed=11940591; DOI=10.1074/jbc.m201657200;
RA Hoffmeister A., Ropolo A., Vasseur S., Mallo G.V., Bodeker H.,
RA Ritz-Laser B., Dressler G.R., Vaccaro M.I., Dagorn J.C., Moreno S.,
RA Iovanna J.L.;
RT "The HMG-I/Y-related protein p8 binds to p300 and Pax2 trans-activation
RT domain-interacting protein to regulate the trans-activation activity of the
RT Pax2A and Pax2B transcription factors on the glucagon gene promoter.";
RL J. Biol. Chem. 277:22314-22319(2002).
RN [37]
RP INTERACTION WITH HNRNPU.
RX PubMed=11909954; DOI=10.1128/mcb.22.8.2598-2606.2002;
RA Martens J.H., Verlaan M., Kalkhoven E., Dorsman J.C., Zantema A.;
RT "Scaffold/matrix attachment region elements interact with a p300-scaffold
RT attachment factor A complex and are bound by acetylated nucleosomes.";
RL Mol. Cell. Biol. 22:2598-2606(2002).
RN [38]
RP IDENTIFICATION IN A COMPLEX WITH CARM1 AND NCOA2.
RX PubMed=11997499; DOI=10.1128/mcb.22.11.3621-3632.2002;
RA Lee Y.-H., Koh S.S., Zhang X., Cheng X., Stallcup M.R.;
RT "Synergy among nuclear receptor coactivators: selective requirement for
RT protein methyltransferase and acetyltransferase activities.";
RL Mol. Cell. Biol. 22:3621-3632(2002).
RN [39]
RP FUNCTION IN BCL6 ACETYLATION.
RX PubMed=12402037; DOI=10.1038/ng1018;
RA Bereshchenko O.R., Gu W., Dalla-Favera R.;
RT "Acetylation inactivates the transcriptional repressor BCL6.";
RL Nat. Genet. 32:606-613(2002).
RN [40]
RP INTERACTION WITH ING4 AND ING5.
RX PubMed=12750254;
RA Shiseki M., Nagashima M., Pedeux R.M., Kitahama-Shiseki M., Miura K.,
RA Okamura S., Onogi H., Higashimoto Y., Appella E., Yokota J., Harris C.C.;
RT "p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity.";
RL Cancer Res. 63:2373-2378(2003).
RN [41]
RP PHOSPHORYLATION, AND INTERACTION WITH TCF7L2 AND LEF1.
RX PubMed=12446687; DOI=10.1074/jbc.m210081200;
RA Hecht A., Stemmler M.P.;
RT "Identification of a promoter-specific transcriptional activation domain at
RT the C-terminus of the Wnt effector protein T-cell factor 4.";
RL J. Biol. Chem. 278:3776-3785(2003).
RN [42]
RP FUNCTION, INTERACTION WITH CITED2 AND TFAP2A, AND MUTAGENESIS OF ASP-1399.
RX PubMed=12586840; DOI=10.1074/jbc.m208144200;
RA Braganca J., Eloranta J.J., Bamforth S.D., Ibbitt J.C., Hurst H.C.,
RA Bhattacharya S.;
RT "Physical and functional interactions among AP-2 transcription factors,
RT p300/CREB-binding protein, and CITED2.";
RL J. Biol. Chem. 278:16021-16029(2003).
RN [43]
RP INTERACTION WITH SOX9.
RX PubMed=12732631; DOI=10.1074/jbc.m303471200;
RA Tsuda M., Takahashi S., Takahashi Y., Asahara H.;
RT "Transcriptional co-activators CREB-binding protein and p300 regulate
RT chondrocyte-specific gene expression via association with Sox9.";
RL J. Biol. Chem. 278:27224-27229(2003).
RN [44]
RP INTERACTION WITH SP3.
RX PubMed=12837748; DOI=10.1074/jbc.m305961200;
RA Ammanamanchi S., Freeman J.W., Brattain M.G.;
RT "Acetylated SP3 is a transcriptional activator.";
RL J. Biol. Chem. 278:35775-35780(2003).
RN [45]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ALX1, AND REGION.
RX PubMed=12929931; DOI=10.1359/jbmr.2003.18.8.1419;
RA Iioka T., Furukawa K., Yamaguchi A., Shindo H., Yamashita S., Tsukazaki T.;
RT "P300/CBP acts as a coactivator to cartilage homeoprotein-1 (Cart1),
RT paired-like homeoprotein, through acetylation of the conserved lysine
RT residue adjacent to the homeodomain.";
RL J. Bone Miner. Res. 18:1419-1429(2003).
RN [46]
RP INTERACTION WITH SATB1.
RX PubMed=14605447; DOI=10.1111/j.1348-0421.2003.tb03438.x;
RA Fujii Y., Kumatori A., Nakamura M.;
RT "SATB1 makes a complex with p300 and represses gp91(phox) promoter
RT activity.";
RL Microbiol. Immunol. 47:803-811(2003).
RN [47]
RP SUMOYLATION AT LYS-1020 AND LYS-1024, AND MUTAGENESIS OF LYS-1020 AND
RP LYS-1024.
RX PubMed=12718889; DOI=10.1016/s1097-2765(03)00141-2;
RA Girdwood D., Bumpass D., Vaughan O.A., Thain A., Anderson L.A.,
RA Snowden A.W., Garcia-Wilson E., Perkins N.D., Hay R.T.;
RT "P300 transcriptional repression is mediated by SUMO modification.";
RL Mol. Cell 11:1043-1054(2003).
RN [48]
RP INTERACTION WITH DDX5.
RX PubMed=12527917; DOI=10.1038/sj.onc.1206067;
RA Rossow K.L., Janknecht R.;
RT "Synergism between p68 RNA helicase and the transcriptional coactivators
RT CBP and p300.";
RL Oncogene 22:151-156(2003).
RN [49]
RP INTERACTION WITH TP53, AND FUNCTION.
RX PubMed=15186775; DOI=10.1016/j.cell.2004.05.009;
RA An W., Kim J., Roeder R.G.;
RT "Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional
RT activation by p53.";
RL Cell 117:735-748(2004).
RN [50]
RP INTERACTION WITH SRY.
RX PubMed=15297880; DOI=10.1038/sj.emboj.7600352;
RA Thevenet L., Mejean C., Moniot B., Bonneaud N., Galeotti N.,
RA Aldrian-Herrada G., Poulat F., Berta P., Benkirane M., Boizet-Bonhoure B.;
RT "Regulation of human SRY subcellular distribution by its
RT acetylation/deacetylation.";
RL EMBO J. 23:3336-3345(2004).
RN [51]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NPAS2; ARNTL/BMAL1 AND
RP CLOCK.
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 [52]
RP INTERACTION WITH ELF3.
RX PubMed=15075319; DOI=10.1074/jbc.m401356200;
RA Wang H., Fang R., Cho J.-Y., Libermann T.A., Oettgen P.;
RT "Positive and negative modulation of the transcriptional activity of the
RT ETS factor ESE-1 through interaction with p300, CREB-binding protein, and
RT Ku 70/86.";
RL J. Biol. Chem. 279:25241-25250(2004).
RN [53]
RP INTERACTION WITH IRF1.
RX PubMed=15509808; DOI=10.1128/mcb.24.22.10083-10098.2004;
RA Dornan D., Eckert M., Wallace M., Shimizu H., Ramsay E., Hupp T.R.,
RA Ball K.L.;
RT "Interferon regulatory factor 1 binding to p300 stimulates DNA-dependent
RT acetylation of p53.";
RL Mol. Cell. Biol. 24:10083-10098(2004).
RN [54]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH TTC5 AND TP53.
RX PubMed=15448695; DOI=10.1038/ncb1170;
RA Demonacos C., Krstic-Demonacos M., Smith L., Xu D., O'Connor D.P.,
RA Jansson M., La Thangue N.B.;
RT "A new effector pathway links ATM kinase with the DNA damage response.";
RL Nat. Cell Biol. 6:968-976(2004).
RN [55]
RP ACETYLATION AT LYS-1499; LYS-1549; LYS-1554; LYS-1558 AND LYS-1560.
RX PubMed=15004546; DOI=10.1038/nsmb740;
RA Thompson P.R., Wang D., Wang L., Fulco M., Pediconi N., Zhang D., An W.,
RA Ge Q., Roeder R.G., Wong J., Levrero M., Sartorelli V., Cotter R.J.,
RA Cole P.A.;
RT "Regulation of the p300 HAT domain via a novel activation loop.";
RL Nat. Struct. Mol. Biol. 11:308-315(2004).
RN [56]
RP INTERACTION WITH NEUROD1 AND TCF3.
RX PubMed=14752053; DOI=10.1210/me.2003-0311;
RA Kim J.Y., Chu K., Kim H.J., Seong H.A., Park K.C., Sanyal S., Takeda J.,
RA Ha H., Shong M., Tsai M.J., Choi H.S.;
RT "Orphan nuclear receptor small heterodimer partner, a novel corepressor for
RT a basic helix-loop-helix transcription factor BETA2/neuroD.";
RL Mol. Endocrinol. 18:776-790(2004).
RN [57]
RP INTERACTION WITH SS18L1/CREST.
RX PubMed=14716005; DOI=10.1126/science.1089845;
RA Aizawa H., Hu S.-C., Bobb K., Balakrishnan K., Ince G., Gurevich I.,
RA Cowan M., Ghosh A.;
RT "Dendrite development regulated by CREST, a calcium-regulated
RT transcriptional activator.";
RL Science 303:197-202(2004).
RN [58]
RP INVOLVEMENT IN RSTS2.
RX PubMed=15706485; DOI=10.1086/429130;
RA Roelfsema J.H., White S.J., Ariyuerek Y., Bartholdi D., Niedrist D.,
RA Papadia F., Bacino C.A., den Dunnen J.T., van Ommen G.-J.B., Breuning M.H.,
RA Hennekam R.C., Peters D.J.M.;
RT "Genetic heterogeneity in Rubinstein-Taybi syndrome: mutations in both the
RT CBP and EP300 genes cause disease.";
RL Am. J. Hum. Genet. 76:572-580(2005).
RN [59]
RP DEACETYLATION BY SIRT1, ACETYLATION AT LYS-1020 AND LYS-1024, AND
RP MUTAGENESIS OF LYS-1020 AND LYS-1024.
RX PubMed=15632193; DOI=10.1074/jbc.m408748200;
RA Bouras T., Fu M., Sauve A.A., Wang F., Quong A.A., Perkins N.D., Hay R.T.,
RA Gu W., Pestell R.G.;
RT "SIRT1 deacetylation and repression of p300 involves lysine residues
RT 1020/1024 within the cell cycle regulatory domain 1.";
RL J. Biol. Chem. 280:10264-10276(2005).
RN [60]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ATF4.
RX PubMed=16219772; DOI=10.1074/jbc.m505294200;
RA Lassot I., Estrabaud E., Emiliani S., Benkirane M., Benarous R.,
RA Margottin-Goguet F.;
RT "p300 modulates ATF4 stability and transcriptional activity independently
RT of its acetyltransferase domain.";
RL J. Biol. Chem. 280:41537-41545(2005).
RN [61]
RP INTERACTION WITH FOXO1, FUNCTION, AND MUTAGENESIS OF ASP-1399.
RX PubMed=15890677; DOI=10.1210/me.2004-0292;
RA Perrot V., Rechler M.M.;
RT "The coactivator p300 directly acetylates the forkhead transcription factor
RT Foxo1 and stimulates Foxo1-induced transcription.";
RL Mol. Endocrinol. 19:2283-2298(2005).
RN [62]
RP METHYLATION AT ARG-2142, CITRULLINATION AT ARG-2142, INTERACTION WITH
RP NCOA2, AND MUTAGENESIS OF ARG-2056; ARG-2088 AND ARG-2142.
RX PubMed=15731352; DOI=10.1073/pnas.0407159102;
RA Lee Y.-H., Coonrod S.A., Kraus W.L., Jelinek M.A., Stallcup M.R.;
RT "Regulation of coactivator complex assembly and function by protein
RT arginine methylation and demethylimination.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3611-3616(2005).
RN [63]
RP INTERACTION WITH BCL11B.
RX PubMed=16809611; DOI=10.1182/blood-2006-05-021790;
RA Cismasiu V.B., Ghanta S., Duque J., Albu D.I., Chen H.M., Kasturi R.,
RA Avram D.;
RT "BCL11B participates in the activation of IL2 gene expression in CD4+ T
RT lymphocytes.";
RL Blood 108:2695-2702(2006).
RN [64]
RP SUBCELLULAR LOCATION, INTERACTION WITH ROCK2, AND PHOSPHORYLATION AT
RP SER-89.
RX PubMed=16574662; DOI=10.1074/jbc.m510954200;
RA Tanaka T., Nishimura D., Wu R.C., Amano M., Iso T., Kedes L., Nishida H.,
RA Kaibuchi K., Hamamori Y.;
RT "Nuclear Rho kinase, ROCK2, targets p300 acetyltransferase.";
RL J. Biol. Chem. 281:15320-15329(2006).
RN [65]
RP INTERACTION WITH CITED1.
RX PubMed=16864582; DOI=10.1074/jbc.m602631200;
RA Shi G., Boyle S.C., Sparrow D.B., Dunwoodie S.L., Shioda T.,
RA de Caestecker M.P.;
RT "The transcriptional activity of CITED1 is regulated by phosphorylation in
RT a cell cycle-dependent manner.";
RL J. Biol. Chem. 281:27426-27435(2006).
RN [66]
RP ACETYLATION AT LYS-1336 AND LYS-1473, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=17065153; DOI=10.1074/jbc.m608813200;
RA Karanam B., Jiang L., Wang L., Kelleher N.L., Cole P.A.;
RT "Kinetic and mass spectrometric analysis of p300 histone acetyltransferase
RT domain autoacetylation.";
RL J. Biol. Chem. 281:40292-40301(2006).
RN [67]
RP FUNCTION IN ACETYLATION OF HDAC1.
RX PubMed=16762839; DOI=10.1016/j.molcel.2006.04.019;
RA Qiu Y., Zhao Y., Becker M., John S., Parekh B.S., Huang S., Hendarwanto A.,
RA Martinez E.D., Chen Y., Lu H., Adkins N.L., Stavreva D.A., Wiench M.,
RA Georgel P.T., Schiltz R.L., Hager G.L.;
RT "HDAC1 acetylation is linked to progressive modulation of steroid receptor-
RT induced gene transcription.";
RL Mol. Cell 22:669-679(2006).
RN [68]
RP INTERACTION WITH SP1.
RX PubMed=16478997; DOI=10.1128/mcb.26.5.1770-1785.2006;
RA Hung J.J., Wang Y.T., Chang W.C.;
RT "Sp1 deacetylation induced by phorbol ester recruits p300 to activate
RT 12(S)-lipoxygenase gene transcription.";
RL Mol. Cell. Biol. 26:1770-1785(2006).
RN [69]
RP FUNCTION, AND INTERACTION WITH MTA1.
RX PubMed=16617102; DOI=10.1073/pnas.0601989103;
RA Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H.,
RA Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
RT "MTA1, a transcriptional activator of breast cancer amplified sequence 3.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6670-6675(2006).
RN [70]
RP ERRATUM OF PUBMED:16617102.
RA Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H.,
RA Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
RL Proc. Natl. Acad. Sci. U.S.A. 110:4147-4148(2013).
RN [71]
RP INTERACTION WITH DDIT3.
RX PubMed=17872950; DOI=10.1074/jbc.m703735200;
RA Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H.;
RT "Critical and functional regulation of CHOP (C/EBP homologous protein)
RT through the N-terminal portion.";
RL J. Biol. Chem. 282:35687-35694(2007).
RN [72]
RP INTERACTION WITH DDX17.
RX PubMed=17226766; DOI=10.1002/jcb.21250;
RA Shin S., Janknecht R.;
RT "Concerted activation of the Mdm2 promoter by p72 RNA helicase and the
RT coactivators p300 and P/CAF.";
RL J. Cell. Biochem. 101:1252-1265(2007).
RN [73]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17267393; DOI=10.1074/mcp.m700021-mcp200;
RA Chen Y., Sprung R., Tang Y., Ball H., Sangras B., Kim S.C., Falck J.R.,
RA Peng J., Gu W., Zhao Y.;
RT "Lysine propionylation and butyrylation are novel post-translational
RT modifications in histones.";
RL Mol. Cell. Proteomics 6:812-819(2007).
RN [74]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH RXRA, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF ASP-1399.
RX PubMed=17761950; DOI=10.1210/me.2007-0107;
RA Zhao W.X., Tian M., Zhao B.X., Li G.D., Liu B., Zhan Y.Y., Chen H.Z.,
RA Wu Q.;
RT "Orphan receptor TR3 attenuates the p300-induced acetylation of retinoid X
RT receptor-alpha.";
RL Mol. Endocrinol. 21:2877-2889(2007).
RN [75]
RP FUNCTION IN ACETYLATION OF SIRT2.
RX PubMed=18722353; DOI=10.1016/j.bbrc.2008.08.042;
RA Han Y., Jin Y.H., Kim Y.J., Kang B.Y., Choi H.J., Kim D.W., Yeo C.Y.,
RA Lee K.Y.;
RT "Acetylation of Sirt2 by p300 attenuates its deacetylase activity.";
RL Biochem. Biophys. Res. Commun. 375:576-580(2008).
RN [76]
RP PHOSPHORYLATION BY HIPK2.
RX PubMed=18695000; DOI=10.1182/blood-2008-01-134122;
RA Wee H.-J., Voon D.C.-C., Bae S.-C., Ito Y.;
RT "PEBP2-beta/CBF-beta-dependent phosphorylation of RUNX1 and p300 by HIPK2:
RT implications for leukemogenesis.";
RL Blood 112:3777-3787(2008).
RN [77]
RP FUNCTION, AND INTERACTION WITH TTC5 AND HSF1.
RX PubMed=18451878; DOI=10.1038/embor.2008.70;
RA Xu D., Zalmas L.P., La Thangue N.B.;
RT "A transcription cofactor required for the heat-shock response.";
RL EMBO Rep. 9:662-669(2008).
RN [78]
RP INTERACTION WITH HUMAN T-CELL LEUKEMIA VIRUS 1/HTLV-1 PROTEIN HBZ.
RX PubMed=18599479; DOI=10.1074/jbc.m803116200;
RA Clerc I., Polakowski N., Andre-Arpin C., Cook P., Barbeau B., Mesnard J.M.,
RA Lemasson I.;
RT "An interaction between the human T cell leukemia virus type 1 basic
RT leucine zipper factor (HBZ) and the KIX domain of p300/CBP contributes to
RT the down-regulation of tax-dependent viral transcription by HBZ.";
RL J. Biol. Chem. 283:23903-23913(2008).
RN [79]
RP FBXO3-MEDIATED DEGRADATION.
RX PubMed=18809579; DOI=10.1128/mcb.00897-08;
RA Shima Y., Shima T., Chiba T., Irimura T., Pandolfi P.P., Kitabayashi I.;
RT "PML activates transcription by protecting HIPK2 and p300 from SCFFbx3-
RT mediated degradation.";
RL Mol. Cell. Biol. 28:7126-7138(2008).
RN [80]
RP ACETYLATION AT LYS-418; LYS-423; LYS-1542; LYS-1546; LYS-1549; LYS-1699;
RP LYS-1704 AND LYS-1707, DEACETYLATION BY SIRT2, AND FUNCTION IN
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=18995842; DOI=10.1016/j.molcel.2008.09.018;
RA Black J.C., Mosley A., Kitada T., Washburn M., Carey M.;
RT "The SIRT2 deacetylase regulates autoacetylation of p300.";
RL Mol. Cell 32:449-455(2008).
RN [81]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [82]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [83]
RP INTERACTION WITH SENP3, AND SUMOYLATION.
RX PubMed=19680224; DOI=10.1038/emboj.2009.210;
RA Huang C., Han Y., Wang Y., Sun X., Yan S., Yeh E.T.H., Chen Y., Cang H.,
RA Li H., Shi G., Cheng J., Tang X., Yi J.;
RT "SENP3 is responsible for HIF-1 transactivation under mild oxidative stress
RT via p300 de-SUMOylation.";
RL EMBO J. 28:2748-2762(2009).
RN [84]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [85]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-636; LYS-977; LYS-1542; LYS-1546;
RP LYS-1554; LYS-1555; LYS-1558; LYS-1560 AND LYS-1583, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [86]
RP SUBCELLULAR LOCATION.
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 [87]
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 [88]
RP IDENTIFICATION IN COMPLEX WITH CCNT1; CDK9 AND GATA4.
RX PubMed=20081228; DOI=10.1074/jbc.m109.070458;
RA Sunagawa Y., Morimoto T., Takaya T., Kaichi S., Wada H., Kawamura T.,
RA Fujita M., Shimatsu A., Kita T., Hasegawa K.;
RT "Cyclin-dependent kinase-9 is a component of the p300/GATA4 complex
RT required for phenylephrine-induced hypertrophy in cardiomyocytes.";
RL J. Biol. Chem. 285:9556-9568(2010).
RN [89]
RP FUNCTION IN ACETYLATION OF MEF2D.
RX PubMed=21030595; DOI=10.1074/jbc.m110.153270;
RA Chini C.C., Escande C., Nin V., Chini E.N.;
RT "HDAC3 is negatively regulated by the nuclear protein DBC1.";
RL J. Biol. Chem. 285:40830-40837(2010).
RN [90]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [91]
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 [92]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1038, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [93]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [94]
RP INTERACTION WITH ALKBH4.
RX PubMed=23145062; DOI=10.1371/journal.pone.0049045;
RA Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A.,
RA Falnes P.O.;
RT "Human ALKBH4 interacts with proteins associated with transcription.";
RL PLoS ONE 7:E49045-E49045(2012).
RN [95]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23415232; DOI=10.1016/j.cell.2013.01.032;
RA Tropberger P., Pott S., Keller C., Kamieniarz-Gdula K., Caron M.,
RA Richter F., Li G., Mittler G., Liu E.T., Buhler M., Margueron R.,
RA Schneider R.;
RT "Regulation of transcription through acetylation of H3K122 on the lateral
RT surface of the histone octamer.";
RL Cell 152:859-872(2013).
RN [96]
RP FUNCTION AS ACETYLTRANSFERASE OF H3K27.
RX PubMed=23911289; DOI=10.1016/j.celrep.2013.06.016;
RA Hatzi K., Jiang Y., Huang C., Garrett-Bakelman F., Gearhart M.D.,
RA Giannopoulou E.G., Zumbo P., Kirouac K., Bhaskara S., Polo J.M.,
RA Kormaksson M., Mackerell A.D. Jr., Xue F., Mason C.E., Hiebert S.W.,
RA Prive G.G., Cerchietti L., Bardwell V.J., Elemento O., Melnick A.;
RT "A hybrid mechanism of action for BCL6 in B cells defined by formation of
RT functionally distinct complexes at enhancers and promoters.";
RL Cell Rep. 4:578-588(2013).
RN [97]
RP INTERACTION WITH KLF15.
RX PubMed=23999430; DOI=10.1172/jci68552;
RA Lu Y., Zhang L., Liao X., Sangwung P., Prosdocimo D.A., Zhou G.,
RA Votruba A.R., Brian L., Han Y.J., Gao H., Wang Y., Shimizu K.,
RA Weinert-Stein K., Khrestian M., Simon D.I., Freedman N.J., Jain M.K.;
RT "Kruppel-like factor 15 is critical for vascular inflammation.";
RL J. Clin. Invest. 123:4232-4241(2013).
RN [98]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1038 AND SER-1726, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [99]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24120661; DOI=10.1016/j.molcel.2013.09.004;
RA Lv L., Xu Y.P., Zhao D., Li F.L., Wang W., Sasaki N., Jiang Y., Zhou X.,
RA Li T.T., Guan K.L., Lei Q.Y., Xiong Y.;
RT "Mitogenic and oncogenic stimulation of K433 acetylation promotes PKM2
RT protein kinase activity and nuclear localization.";
RL Mol. Cell 52:340-352(2013).
RN [100]
RP INTERACTION WITH HDAC4 AND HDAC5.
RX PubMed=24413532; DOI=10.1158/0008-5472.can-13-2020;
RA Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y.,
RA Kim Y.N., Seong J.K., Lee M.O.;
RT "Differential regulation of estrogen receptor alpha expression in breast
RT cancer cells by metastasis-associated protein 1.";
RL Cancer Res. 74:1484-1494(2014).
RN [101]
RP INTERACTION WITH KAT5, AND MUTAGENESIS OF PHE-1504.
RX PubMed=24835996; DOI=10.1016/j.celrep.2014.04.021;
RA Xiao Y., Nagai Y., Deng G., Ohtani T., Zhu Z., Zhou Z., Zhang H., Ji M.Q.,
RA Lough J.W., Samanta A., Hancock W.W., Greene M.I.;
RT "Dynamic interactions between TIP60 and p300 regulate FOXP3 function
RT through a structural switch defined by a single lysine on TIP60.";
RL Cell Rep. 7:1471-1480(2014).
RN [102]
RP INTERACTION WITH ZNF451, AND FUNCTION.
RX PubMed=24324267; DOI=10.1074/jbc.m113.526905;
RA Feng Y., Wu H., Xu Y., Zhang Z., Liu T., Lin X., Feng X.H.;
RT "Zinc finger protein 451 is a novel Smad corepressor in transforming growth
RT factor-beta signaling.";
RL J. Biol. Chem. 289:2072-2083(2014).
RN [103]
RP INTERACTION WITH ZBTB48.
RX PubMed=24382891; DOI=10.1074/jbc.m113.526855;
RA Yoon J.H., Choi W.I., Jeon B.N., Koh D.I., Kim M.K., Kim M.H., Kim J.,
RA Hur S.S., Kim K.S., Hur M.W.;
RT "Human Kruppel-related 3 (HKR3) is a novel transcription activator of
RT alternate reading frame (ARF) gene.";
RL J. Biol. Chem. 289:4018-4031(2014).
RN [104]
RP ACETYLATION, DEACETYLATION BY SIRT2, AND INTERACTION WITH EP300.
RX PubMed=24177535; DOI=10.1016/j.jmb.2013.10.027;
RA Rack J.G., Vanlinden M.R., Lutter T., Aasland R., Ziegler M.;
RT "Constitutive nuclear localization of an alternatively spliced sirtuin-2
RT isoform.";
RL J. Mol. Biol. 426:1677-1691(2014).
RN [105]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1038, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [106]
RP INTERACTION WITH TRIP4.
RX PubMed=25219498; DOI=10.1016/j.molcel.2014.08.007;
RA Yoo H.M., Kang S.H., Kim J.Y., Lee J.E., Seong M.W., Lee S.W., Ka S.H.,
RA Sou Y.S., Komatsu M., Tanaka K., Lee S.T., Noh D.Y., Baek S.H., Jeon Y.J.,
RA Chung C.H.;
RT "Modification of ASC1 by UFM1 is crucial for ERalpha transactivation and
RT breast cancer development.";
RL Mol. Cell 56:261-274(2014).
RN [107]
RP FUNCTION AS ACETYLTRANSFERASE OF PCNA, AND INTERACTION WITH PCNA.
RX PubMed=24939902; DOI=10.1093/nar/gku533;
RA Cazzalini O., Sommatis S., Tillhon M., Dutto I., Bachi A., Rapp A.,
RA Nardo T., Scovassi A.I., Necchi D., Cardoso M.C., Stivala L.A.,
RA Prosperi E.;
RT "CBP and p300 acetylate PCNA to link its degradation with nucleotide
RT excision repair synthesis.";
RL Nucleic Acids Res. 42:8433-8448(2014).
RN [108]
RP INTERACTION WITH ZBTB49.
RX PubMed=25245946; DOI=10.1093/nar/gku857;
RA Jeon B.N., Kim M.K., Yoon J.H., Kim M.Y., An H., Noh H.J., Choi W.I.,
RA Koh D.I., Hur M.W.;
RT "Two ZNF509 (ZBTB49) isoforms induce cell-cycle arrest by activating
RT transcription of p21/CDKN1A and RB upon exposure to genotoxic stress.";
RL Nucleic Acids Res. 42:11447-11461(2014).
RN [109]
RP FUNCTION, AND INTERACTION WITH SMAD4.
RX PubMed=25514493; DOI=10.1016/j.bbagrm.2014.12.008;
RA Yang Y., Cui J., Xue F., Zhang C., Mei Z., Wang Y., Bi M., Shan D.,
RA Meredith A., Li H., Xu Z.Q.;
RT "Pokemon (FBI-1) interacts with Smad4 to repress TGF-beta-induced
RT transcriptional responses.";
RL Biochim. Biophys. Acta 1849:270-281(2015).
RN [110]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=25818647; DOI=10.1016/j.molcel.2015.02.029;
RA Sabari B.R., Tang Z., Huang H., Yong-Gonzalez V., Molina H., Kong H.E.,
RA Dai L., Shimada M., Cross J.R., Zhao Y., Roeder R.G., Allis C.D.;
RT "Intracellular crotonyl-CoA stimulates transcription through p300-catalyzed
RT histone crotonylation.";
RL Mol. Cell 58:203-215(2015).
RN [111]
RP INTERACTION WITH STAT1.
RX PubMed=26479788; DOI=10.1038/ni.3279;
RA Zhang Y., Mao D., Roswit W.T., Jin X., Patel A.C., Patel D.A., Agapov E.,
RA Wang Z., Tidwell R.M., Atkinson J.J., Huang G., McCarthy R., Yu J.,
RA Yun N.E., Paessler S., Lawson T.G., Omattage N.S., Brett T.J.,
RA Holtzman M.J.;
RT "PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C
RT protease to enhance interferon signaling and control viral infection.";
RL Nat. Immunol. 16:1215-1227(2015).
RN [112]
RP INTERACTION WITH BCL11B.
RX PubMed=27959755; DOI=10.1056/nejmoa1509164;
RA Punwani D., Zhang Y., Yu J., Cowan M.J., Rana S., Kwan A., Adhikari A.N.,
RA Lizama C.O., Mendelsohn B.A., Fahl S.P., Chellappan A., Srinivasan R.,
RA Brenner S.E., Wiest D.L., Puck J.M.;
RT "Multisystem anomalies in severe combined immunodeficiency with mutant
RT BCL11B.";
RL N. Engl. J. Med. 375:2165-2176(2016).
RN [113]
RP INTERACTION WITH DUX4.
RX PubMed=26951377; DOI=10.1093/nar/gkw141;
RA Choi S.H., Gearhart M.D., Cui Z., Bosnakovski D., Kim M., Schennum N.,
RA Kyba M.;
RT "DUX4 recruits p300/CBP through its C-terminus and induces global H3K27
RT acetylation changes.";
RL Nucleic Acids Res. 44:5161-5173(2016).
RN [114]
RP INTERACTION WITH HSF1.
RX PubMed=27189267; DOI=10.1038/srep26294;
RA Pan X.Y., Zhao W., Zeng X.Y., Lin J., Li M.M., Shen X.T., Liu S.W.;
RT "Heat shock factor 1 mediates latent HIV reactivation.";
RL Sci. Rep. 6:26294-26294(2016).
RN [115]
RP INTERACTION WITH DDX3X.
RX PubMed=28128295; DOI=10.1038/srep41452;
RA Tsai T.Y., Wang W.T., Li H.K., Chen W.J., Tsai Y.H., Chao C.H.,
RA Wu Lee Y.H.;
RT "RNA helicase DDX3 maintains lipid homeostasis through upregulation of the
RT microsomal triglyceride transfer protein by interacting with HNF4 and
RT SHP.";
RL Sci. Rep. 7:41452-41452(2017).
RN [116]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-1399.
RX PubMed=29775581; DOI=10.1016/j.molcel.2018.04.011;
RA Huang H., Tang S., Ji M., Tang Z., Shimada M., Liu X., Qi S.,
RA Locasale J.W., Roeder R.G., Zhao Y., Li X.;
RT "p300-mediated lysine 2-hydroxyisobutyrylation regulates glycolysis.";
RL Mol. Cell 70:663-678(2018).
RN [117]
RP FUNCTION IN ACETYLATION OF PCK1.
RX PubMed=30193097; DOI=10.1016/j.molcel.2018.07.031;
RA Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F.,
RA Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.;
RT "Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme
RT activity between gluconeogenic and anaplerotic reactions.";
RL Mol. Cell 71:718-732(2018).
RN [118]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31645732; DOI=10.1038/s41586-019-1678-1;
RA Zhang D., Tang Z., Huang H., Zhou G., Cui C., Weng Y., Liu W., Kim S.,
RA Lee S., Perez-Neut M., Ding J., Czyz D., Hu R., Ye Z., He M., Zheng Y.G.,
RA Shuman H.A., Dai L., Ren B., Roeder R.G., Becker L., Zhao Y.;
RT "Metabolic regulation of gene expression by histone lactylation.";
RL Nature 574:575-580(2019).
RN [119]
RP STRUCTURE BY NMR OF 302-418 IN COMPLEX WITH HIF1A PEPTIDE AND ZINC IONS.
RX PubMed=11959990; DOI=10.1073/pnas.082117899;
RA Freedman S.J., Sun Z.-Y.J., Poy F., Kung A.L., Livingston D.M., Wagner G.,
RA Eck M.J.;
RT "Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1
RT alpha.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5367-5372(2002).
RN [120]
RP STRUCTURE BY NMR OF 323-423 IN COMPLEX WITH 216-259 OF CITED2 AND ZINC
RP IONS, INTERACTION WITH CITED2, AND MUTAGENESIS OF LEU-344 AND LEU-345.
RX PubMed=12778114; DOI=10.1038/nsb936;
RA Freedman S.J., Sun Z.Y., Kung A.L., France D.S., Wagner G., Eck M.J.;
RT "Structural basis for negative regulation of hypoxia-inducible factor-
RT 1alpha by CITED2.";
RL Nat. Struct. Biol. 10:504-512(2003).
RN [121]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1287-1666 IN COMPLEX WITH LYS-COA,
RP AND MUTAGENESIS OF THR-1357; SER-1396; TYR-1397; GLU-1505; ASP-1625 AND
RP ASP-1628.
RX PubMed=18273021; DOI=10.1038/nature06546;
RA Liu X., Wang L., Zhao K., Thompson P.R., Hwang Y., Marmorstein R.,
RA Cole P.A.;
RT "The structural basis of protein acetylation by the p300/CBP
RT transcriptional coactivator.";
RL Nature 451:846-850(2008).
RN [122]
RP STRUCTURE BY NMR OF 1723-1812, AND INTERACTION WITH TP53.
RX PubMed=19217391; DOI=10.1016/j.str.2008.12.009;
RA Feng H., Jenkins L.M.M., Durell S.R., Hayashi R., Mazur S.J., Cherry S.,
RA Tropea J.E., Miller M., Wlodawer A., Appella E., Bai Y.;
RT "Structural basis for p300 Taz2-p53 TAD1 binding and modulation by
RT phosphorylation.";
RL Structure 17:202-210(2009).
RN [123]
RP X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 1040-1161.
RX PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
RA Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
RA Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
RA Gingras A.C., Arrowsmith C.H., Knapp S.;
RT "Histone recognition and large-scale structural analysis of the human
RT bromodomain family.";
RL Cell 149:214-231(2012).
RN [124]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1043-1519 AND 1581-1666 OF MUTANT
RP PHE-1467 IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY, FUNCTION,
RP AUTOACETYLATION, AND MUTAGENESIS OF PHE-1170; CYS-1204; GLU-1242; ASP-1399;
RP TYR-1467 AND 1645-ARG-ARG-1646.
RX PubMed=23934153; DOI=10.1038/nsmb.2642;
RA Delvecchio M., Gaucher J., Aguilar-Gurrieri C., Ortega E., Panne D.;
RT "Structure of the p300 catalytic core and implications for chromatin
RT targeting and HAT regulation.";
RL Nat. Struct. Mol. Biol. 20:1040-1046(2013).
RN [125]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 1287-1664 OF MUTANT PHE-1467 IN
RP COMPLEX WITH ACETYL-COA AND COENZYME A.
RX PubMed=24819397; DOI=10.1021/bi500380f;
RA Maksimoska J., Segura-Pena D., Cole P.A., Marmorstein R.;
RT "Structure of the p300 histone acetyltransferase bound to acetyl-coenzyme A
RT and its analogues.";
RL Biochemistry 53:3415-3422(2014).
RN [126]
RP VARIANTS PRO-827; GLY-1013; TYR-1650 AND GLN-2221, AND POSSIBLE INVOLVEMENT
RP IN CANCER.
RX PubMed=10700188; DOI=10.1038/73536;
RA Gayther S.A., Batley S.J., Linger L., Bannister A., Thorpe K., Chin S.-F.,
RA Daigo Y., Russell P., Wilson A., Sowter H.M., Delhanty J.D.A.,
RA Ponder B.A.J., Kouzarides T., Caldas C.;
RT "Mutations truncating the EP300 acetylase in human cancers.";
RL Nat. Genet. 24:300-303(2000).
RN [127]
RP VARIANT ILE-1511.
RX PubMed=24476420; DOI=10.1111/cge.12348;
RA Negri G., Milani D., Colapietro P., Forzano F., Della Monica M.,
RA Rusconi D., Consonni L., Caffi L.G., Finelli P., Scarano G., Magnani C.,
RA Selicorni A., Spena S., Larizza L., Gervasini C.;
RT "Clinical and molecular characterization of Rubinstein-Taybi syndrome
RT patients carrying distinct novel mutations of the EP300 gene.";
RL Clin. Genet. 87:148-154(2015).
RN [128]
RP VARIANT ARG-2007.
RX PubMed=29053796; DOI=10.1093/brain/awx251;
RA Nibbeling E.A.R., Duarri A., Verschuuren-Bemelmans C.C., Fokkens M.R.,
RA Karjalainen J.M., Smeets C.J.L.M., de Boer-Bergsma J.J., van der Vries G.,
RA Dooijes D., Bampi G.B., van Diemen C., Brunt E., Ippel E., Kremer B.,
RA Vlak M., Adir N., Wijmenga C., van de Warrenburg B.P.C., Franke L.,
RA Sinke R.J., Verbeek D.S.;
RT "Exome sequencing and network analysis identifies shared mechanisms
RT underlying spinocerebellar ataxia.";
RL Brain 140:2860-2878(2017).
RN [129]
RP VARIANTS MKHK2 PRO-1824 AND ARG-1831 DEL, AND INVOLVEMENT IN MKHK2.
RX PubMed=29460469; DOI=10.1002/ajmg.a.38626;
RG DDD study;
RA Menke L.A., Gardeitchik T., Hammond P., Heimdal K.R., Houge G.,
RA Hufnagel S.B., Ji J., Johansson S., Kant S.G., Kinning E., Leon E.L.,
RA Newbury-Ecob R., Paolacci S., Pfundt R., Ragge N.K., Rinne T.,
RA Ruivenkamp C., Saitta S.C., Sun Y., Tartaglia M., Terhal P.A.,
RA van Essen A.J., Vigeland M.D., Xiao B., Hennekam R.C.;
RT "Further delineation of an entity caused by CREBBP and EP300 mutations but
RT not resembling Rubinstein-Taybi syndrome.";
RL Am. J. Med. Genet. A 176:862-876(2018).
CC -!- FUNCTION: Functions as histone acetyltransferase and regulates
CC transcription via chromatin remodeling (PubMed:23415232,
CC PubMed:23934153, PubMed:8945521). Acetylates all four core histones in
CC nucleosomes. Histone acetylation gives an epigenetic tag for
CC transcriptional activation (PubMed:23415232, PubMed:23934153,
CC PubMed:8945521). Mediates cAMP-gene regulation by binding specifically
CC to phosphorylated CREB protein. Mediates acetylation of histone H3 at
CC 'Lys-122' (H3K122ac), a modification that localizes at the surface of
CC the histone octamer and stimulates transcription, possibly by promoting
CC nucleosome instability. Mediates acetylation of histone H3 at 'Lys-27'
CC (H3K27ac) (PubMed:23911289). Also functions as acetyltransferase for
CC non-histone targets, such as ALX1, HDAC1, PRMT1 or SIRT2
CC (PubMed:12929931, PubMed:16762839, PubMed:18722353). Acetylates 'Lys-
CC 131' of ALX1 and acts as its coactivator (PubMed:12929931). Acetylates
CC SIRT2 and is proposed to indirectly increase the transcriptional
CC activity of p53/TP53 through acetylation and subsequent attenuation of
CC SIRT2 deacetylase function (PubMed:18722353). Following DNA damage,
CC forms a stress-responsive p53/TP53 coactivator complex with JMY which
CC mediates p53/TP53 acetylation, thereby increasing p53/TP53-dependent
CC transcription and apoptosis (PubMed:11511361, PubMed:15448695).
CC Promotes chromatin acetylation in heat shock responsive HSP genes
CC during the heat shock response (HSR), thereby stimulating HSR
CC transcription (PubMed:18451878). Acetylates HDAC1 leading to its
CC inactivation and modulation of transcription (PubMed:16762839).
CC Acetylates 'Lys-247' of EGR2 (By similarity). Acts as a TFAP2A-mediated
CC transcriptional coactivator in presence of CITED2 (PubMed:12586840).
CC Plays a role as a coactivator of NEUROD1-dependent transcription of the
CC secretin and p21 genes and controls terminal differentiation of cells
CC in the intestinal epithelium. Promotes cardiac myocyte enlargement. Can
CC also mediate transcriptional repression. Acetylates FOXO1 and enhances
CC its transcriptional activity (PubMed:15890677). Acetylates BCL6 wich
CC disrupts its ability to recruit histone deacetylases and hinders its
CC transcriptional repressor activity (PubMed:12402037). Participates in
CC CLOCK or NPAS2-regulated rhythmic gene transcription; exhibits a
CC circadian association with CLOCK or NPAS2, correlating with increase in
CC PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter
CC (PubMed:14645221). Acetylates MTA1 at 'Lys-626' which is essential for
CC its transcriptional coactivator activity (PubMed:16617102). Acetylates
CC XBP1 isoform 2; acetylation increases protein stability of XBP1 isoform
CC 2 and enhances its transcriptional activity (PubMed:20955178).
CC Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA
CC and its degradation during nucleotide excision repair (NER)
CC (PubMed:24939902). Acetylates MEF2D (PubMed:21030595). Acetylates and
CC stabilizes ZBTB7B protein by antagonizing ubiquitin conjugation and
CC degradation, this mechanism may be involved in CD4/CD8 lineage
CC differentiation (PubMed:20810990). Acetylates GABPB1, impairing GABPB1
CC heterotetramerization and activity (By similarity). Acetylates PCK1 and
CC promotes PCK1 anaplerotic activity (PubMed:30193097). Acetylates RXRA
CC and RXRG (PubMed:17761950). Acetylates isoform M2 of PKM (PKM2),
CC promoting its homodimerization and conversion into a protein kinase
CC (PubMed:24120661). 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:17267393, PubMed:25818647, PubMed:29775581, PubMed:31645732).
CC Acts as a histone crotonyltransferase; crotonylation marks active
CC promoters and enhancers and confers resistance to transcriptional
CC repressors (PubMed:25818647). 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 (PubMed:25818647). Also acts as a histone
CC butyryltransferase; butyrylation marks active promoters
CC (PubMed:17267393). Catalyzes histone lactylation in macrophages by
CC using lactoyl-CoA directly derived from endogenous or exogenous
CC lactate, leading to stimulates gene transcription (PubMed:31645732).
CC Acts as a protein-lysine 2-hydroxyisobutyryltransferase; regulates
CC glycolysis by mediating 2-hydroxyisobutyrylation of glycolytic enzymes
CC (PubMed:29775581). Functions as a transcriptional coactivator for SMAD4
CC in the TGF-beta signaling pathway (PubMed:25514493).
CC {ECO:0000250|UniProtKB:B2RWS6, ECO:0000269|PubMed:10733570,
CC ECO:0000269|PubMed:11430825, ECO:0000269|PubMed:11511361,
CC ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:12402037,
CC ECO:0000269|PubMed:12586840, ECO:0000269|PubMed:12929931,
CC ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:15186775,
CC ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:15890677,
CC ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:16762839,
CC ECO:0000269|PubMed:17267393, ECO:0000269|PubMed:17761950,
CC ECO:0000269|PubMed:18451878, ECO:0000269|PubMed:18722353,
CC ECO:0000269|PubMed:18995842, ECO:0000269|PubMed:20810990,
CC ECO:0000269|PubMed:21030595, ECO:0000269|PubMed:23415232,
CC ECO:0000269|PubMed:23911289, ECO:0000269|PubMed:23934153,
CC ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:24939902,
CC ECO:0000269|PubMed:25514493, ECO:0000269|PubMed:25818647,
CC ECO:0000269|PubMed:29775581, ECO:0000269|PubMed:30193097,
CC ECO:0000269|PubMed:31645732, ECO:0000269|PubMed:8945521,
CC ECO:0000305|PubMed:20955178}.
CC -!- FUNCTION: (Microbial infection) In case of HIV-1 infection, it is
CC recruited by the viral protein Tat. Regulates Tat's transactivating
CC activity and may help inducing chromatin remodeling of proviral genes.
CC Binds to and may be involved in the transforming capacity of the
CC adenovirus E1A protein. {ECO:0000269|PubMed:10545121,
CC ECO:0000269|PubMed:11080476}.
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:15448695, ECO:0000269|PubMed:17761950,
CC ECO:0000269|PubMed:23415232, ECO:0000269|PubMed:23934153,
CC ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:8945521};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC Evidence={ECO:0000305|PubMed:15448695};
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:0000269|PubMed:25818647};
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:0000250|UniProtKB:B2RWS6};
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:0000269|PubMed:17267393};
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:0000269|PubMed:29775581};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181;
CC Evidence={ECO:0000269|PubMed:29775581};
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:0000269|PubMed:31645732};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61997;
CC Evidence={ECO:0000269|PubMed:31645732};
CC -!- SUBUNIT: Interacts with HIF1A; the interaction is stimulated in
CC response to hypoxia and inhibited by CITED2 (PubMed:9887100,
CC PubMed:11959990). Probably part of a complex with HIF1A and CREBBP
CC (PubMed:8917528). Interacts (via N-terminus) with TFAP2A (via N-
CC terminus); the interaction requires CITED2 (PubMed:12586840). Interacts
CC (via CH1 domain) with CITED2 (via C-terminus) (PubMed:12586840,
CC PubMed:12778114). Interacts with CITED1 (unphosphorylated form
CC preferentially and via C-terminus) (PubMed:10722728, PubMed:16864582).
CC Interacts with ESR1; the interaction is estrogen-dependent and enhanced
CC by CITED1 (PubMed:11581164). Interacts with HIPK2 (By similarity).
CC Interacts with DTX1, EID1, ELF3, FEN1, LEF1, NCOA1, NCOA6, NR3C1, PCAF,
CC PELP1, PRDM6, SP1, SP3, SPIB, SRY, TCF7L2, DDX5, DDX17, SATB1, SRCAP
CC and TRERF1 (PubMed:11073989, PubMed:11073990, PubMed:10823961,
CC PubMed:11349124, PubMed:11430825, PubMed:11481323, PubMed:11564735,
CC PubMed:11581372, PubMed:11864910, PubMed:12446687, PubMed:12527917,
CC PubMed:12837748, PubMed:14605447, PubMed:15075319, PubMed:15297880,
CC PubMed:16478997, PubMed:8684459, PubMed:17226766, PubMed:9590696).
CC Interacts with JMY, the complex activates p53/TP53 transcriptional
CC activity (PubMed:10518217, PubMed:11511361). Interacts with TTC5/STRAP;
CC the interaction facilitates the association between JMY and p300/EP300
CC cofactors (PubMed:11511361). Interacts with p53/TP53; the interation is
CC facilitated by TTC5/STRAP (PubMed:15186775, PubMed:15448695,
CC PubMed:19217391). Forms a complex with TTC5/STRAP and HSF1; these
CC interactions augment chromatin-bound HSF1 and p300/EP300 histone
CC acetyltransferase activity (PubMed:18451878). Part of a complex
CC containing CARM1 and NCOA2/GRIP1 (PubMed:11701890, PubMed:11997499,
CC PubMed:15731352). Interacts with ING4 and this interaction may be
CC indirect (PubMed:12750254). Interacts with ING5 (PubMed:12750254).
CC Interacts with the C-terminal region of CITED4 (PubMed:11744733). Non-
CC sumoylated EP300 preferentially interacts with SENP3 (PubMed:19680224).
CC Interacts with SS18L1/CREST (PubMed:14716005). Interacts with ALX1 (via
CC homeobox domain) (PubMed:12929931). Interacts with NEUROD1; the
CC interaction is inhibited by NR0B2 (PubMed:14752053). Interacts with
CC TCF3 (PubMed:14752053). Interacts (via CREB-binding domain) with MYOCD
CC (via C-terminus) (By similarity). Interacts with ROCK2 and PPARG
CC (PubMed:11518699, PubMed:16574662). Forms a complex made of CDK9,
CC CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy in
CC cardiomyocytes (PubMed:20081228). Interacts with IRF1 and this
CC interaction enhances acetylation of p53/TP53 and stimulation of its
CC activity (PubMed:15509808). Interacts with FOXO1; the interaction
CC acetylates FOXO1 and enhances its transcriptional activity
CC (PubMed:15890677). Interacts with ALKBH4 and DDIT3/CHOP
CC (PubMed:17872950, PubMed:23145062). Interacts with KLF15
CC (PubMed:23999430). Interacts with CEBPB and RORA (PubMed:9862959).
CC Interacts with NPAS2, ARNTL/BMAL1 and CLOCK (PubMed:14645221).
CC Interacts with SIRT2 isoform 1, isoform 2 and isoform 5
CC (PubMed:24177535). Interacts with MTA1 (PubMed:16617102). Interacts
CC with HDAC4 and HDAC5 in the presence of TFAP2C (PubMed:24413532).
CC Interacts with TRIP4 (PubMed:25219498). Directly interacts with ZBTB49;
CC this interaction leads to synergistic transactivation of CDKN1A
CC (PubMed:25245946). Interacts with NR4A3 (By similarity). Interacts with
CC ZNF451 (PubMed:24324267). Interacts with ATF5; EP300 is required for
CC ATF5 and CEBPB interaction and DNA binding (By similarity). Interacts
CC with HSF1 (PubMed:27189267). Interacts with ZBTB48/TZAP
CC (PubMed:24382891). Interacts with STAT1; the interaction is enhanced
CC upon IFN-gamma stimulation (PubMed:26479788). Interacts with HNRNPU
CC (via C-terminus); this interaction enhances DNA-binding of HNRNPU to
CC nuclear scaffold/matrix attachment region (S/MAR) elements
CC (PubMed:11909954). Interacts with BCL11B (PubMed:27959755,
CC PubMed:16809611). Interacts with SMAD4; negatively regulated by ZBTB7A
CC (PubMed:25514493). Interacts with DUX4 (via C-terminus)
CC (PubMed:26951377). Interacts with NUPR1; this interaction enhances the
CC effect of EP300 on PAX2 transcription factor activity
CC (PubMed:11940591). Interacts with RXRA; the interaction is decreased by
CC 9-cis retinoic acid (PubMed:17761950). NR4A1 competes with EP300 for
CC interaction with RXRA and thereby attenuates EP300 mediated acetylation
CC of RXRA (PubMed:17761950). Interacts with RB1 (By similarity).
CC Interacts with DDX3X; this interaction may facilitate HNF4A acetylation
CC (PubMed:28128295). Interacts with SOX9 (PubMed:12732631). Interacts
CC with ATF4; EP300/p300 stabilizes ATF4 and increases its transcriptional
CC activity independently of its catalytic activity by preventing its
CC ubiquitination (PubMed:16219772). Interacts with KAT5; promoting KAT5
CC autoacetylation (PubMed:24835996). {ECO:0000250|UniProtKB:B2RWS6,
CC ECO:0000269|PubMed:10518217, ECO:0000269|PubMed:10722728,
CC ECO:0000269|PubMed:10823961, ECO:0000269|PubMed:11073989,
CC ECO:0000269|PubMed:11073990, ECO:0000269|PubMed:11349124,
CC ECO:0000269|PubMed:11430825, ECO:0000269|PubMed:11481323,
CC ECO:0000269|PubMed:11511361, ECO:0000269|PubMed:11518699,
CC ECO:0000269|PubMed:11564735, ECO:0000269|PubMed:11581164,
CC ECO:0000269|PubMed:11581372, ECO:0000269|PubMed:11701890,
CC ECO:0000269|PubMed:11744733, ECO:0000269|PubMed:11864910,
CC ECO:0000269|PubMed:11909954, ECO:0000269|PubMed:11940591,
CC ECO:0000269|PubMed:11959990, ECO:0000269|PubMed:11997499,
CC ECO:0000269|PubMed:12446687, ECO:0000269|PubMed:12527917,
CC ECO:0000269|PubMed:12586840, ECO:0000269|PubMed:12732631,
CC ECO:0000269|PubMed:12750254, ECO:0000269|PubMed:12778114,
CC ECO:0000269|PubMed:12837748, ECO:0000269|PubMed:12929931,
CC ECO:0000269|PubMed:14605447, ECO:0000269|PubMed:14645221,
CC ECO:0000269|PubMed:14716005, ECO:0000269|PubMed:14752053,
CC ECO:0000269|PubMed:15075319, ECO:0000269|PubMed:15186775,
CC ECO:0000269|PubMed:15297880, ECO:0000269|PubMed:15448695,
CC ECO:0000269|PubMed:15509808, ECO:0000269|PubMed:15731352,
CC ECO:0000269|PubMed:15890677, ECO:0000269|PubMed:16219772,
CC ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:16574662,
CC ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:16809611,
CC ECO:0000269|PubMed:16864582, ECO:0000269|PubMed:17226766,
CC ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:17872950,
CC ECO:0000269|PubMed:18451878, ECO:0000269|PubMed:19217391,
CC ECO:0000269|PubMed:19680224, ECO:0000269|PubMed:20081228,
CC ECO:0000269|PubMed:23145062, ECO:0000269|PubMed:23999430,
CC ECO:0000269|PubMed:24177535, ECO:0000269|PubMed:24382891,
CC ECO:0000269|PubMed:24413532, ECO:0000269|PubMed:24835996,
CC ECO:0000269|PubMed:25219498, ECO:0000269|PubMed:25245946,
CC ECO:0000269|PubMed:25514493, ECO:0000269|PubMed:26479788,
CC ECO:0000269|PubMed:26951377, ECO:0000269|PubMed:27189267,
CC ECO:0000269|PubMed:27959755, ECO:0000269|PubMed:28128295,
CC ECO:0000269|PubMed:8684459, ECO:0000269|PubMed:8917528,
CC ECO:0000269|PubMed:9590696, ECO:0000269|PubMed:9862959,
CC ECO:0000269|PubMed:9887100}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus 5 E1A
CC protein; this interaction stimulates the acetylation of RB1 by
CC recruiting EP300 and RB1 into a multimeric-protein complex.
CC {ECO:0000269|PubMed:11433299}.
CC -!- SUBUNIT: (Microbial infection) Interacts with and acetylates HIV-1 Tat.
CC {ECO:0000269|PubMed:10545121, ECO:0000269|PubMed:11080476,
CC ECO:0000269|PubMed:9528808}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 proteins Tax,
CC p30II and HBZ. {ECO:0000269|PubMed:11463834,
CC ECO:0000269|PubMed:11559821, ECO:0000269|PubMed:18599479}.
CC -!- INTERACTION:
CC Q09472; Q9NXW9: ALKBH4; NbExp=4; IntAct=EBI-447295, EBI-8637516;
CC Q09472; P27695: APEX1; NbExp=8; IntAct=EBI-447295, EBI-1048805;
CC Q09472; Q9UBL3: ASH2L; NbExp=5; IntAct=EBI-447295, EBI-540797;
CC Q09472; Q8WXX7: AUTS2; NbExp=3; IntAct=EBI-447295, EBI-2875359;
CC Q09472; Q9NPI1: BRD7; NbExp=3; IntAct=EBI-447295, EBI-711221;
CC Q09472; P24941: CDK2; NbExp=6; IntAct=EBI-447295, EBI-375096;
CC Q09472; Q99967: CITED2; NbExp=3; IntAct=EBI-447295, EBI-937732;
CC Q09472; P61201: COPS2; NbExp=2; IntAct=EBI-447295, EBI-1050386;
CC Q09472; P16220-1: CREB1; NbExp=2; IntAct=EBI-447295, EBI-26386865;
CC Q09472; P17844: DDX5; NbExp=4; IntAct=EBI-447295, EBI-351962;
CC Q09472; Q01844: EWSR1; NbExp=2; IntAct=EBI-447295, EBI-739737;
CC Q09472; P35637: FUS; NbExp=4; IntAct=EBI-447295, EBI-400434;
CC Q09472; Q00403: GTF2B; NbExp=2; IntAct=EBI-447295, EBI-389564;
CC Q09472; Q16665: HIF1A; NbExp=20; IntAct=EBI-447295, EBI-447269;
CC Q09472; Q9H2X6: HIPK2; NbExp=4; IntAct=EBI-447295, EBI-348345;
CC Q09472; Q92831: KAT2B; NbExp=2; IntAct=EBI-447295, EBI-477430;
CC Q09472; P55209: NAP1L1; NbExp=3; IntAct=EBI-447295, EBI-356392;
CC Q09472; O60934: NBN; NbExp=5; IntAct=EBI-447295, EBI-494844;
CC Q09472; P20265: POU3F2; NbExp=3; IntAct=EBI-447295, EBI-1167176;
CC Q09472; Q96KQ4: PPP1R13B; NbExp=2; IntAct=EBI-447295, EBI-1105153;
CC Q09472; Q8WUF5: PPP1R13L; NbExp=2; IntAct=EBI-447295, EBI-5550163;
CC Q09472; Q13761: RUNX3; NbExp=7; IntAct=EBI-447295, EBI-925990;
CC Q09472; Q96EB6: SIRT1; NbExp=4; IntAct=EBI-447295, EBI-1802965;
CC Q09472; Q13309: SKP2; NbExp=3; IntAct=EBI-447295, EBI-456291;
CC Q09472; O95863: SNAI1; NbExp=3; IntAct=EBI-447295, EBI-1045459;
CC Q09472; P42226: STAT6; NbExp=2; IntAct=EBI-447295, EBI-1186478;
CC Q09472; Q9UL17: TBX21; NbExp=5; IntAct=EBI-447295, EBI-3922312;
CC Q09472; P56279: TCL1A; NbExp=4; IntAct=EBI-447295, EBI-749995;
CC Q09472; P05549: TFAP2A; NbExp=7; IntAct=EBI-447295, EBI-347351;
CC Q09472; P04637: TP53; NbExp=21; IntAct=EBI-447295, EBI-366083;
CC Q09472; Q13625: TP53BP2; NbExp=2; IntAct=EBI-447295, EBI-77642;
CC Q09472; O15350: TP73; NbExp=2; IntAct=EBI-447295, EBI-389606;
CC Q09472; P11473: VDR; NbExp=3; IntAct=EBI-447295, EBI-286357;
CC Q09472; P67809: YBX1; NbExp=2; IntAct=EBI-447295, EBI-354065;
CC Q09472; K4P3M7: BICP0; Xeno; NbExp=4; IntAct=EBI-447295, EBI-11296047;
CC Q09472; P03122: E2; Xeno; NbExp=3; IntAct=EBI-447295, EBI-7028618;
CC Q09472; P06422: E2; Xeno; NbExp=7; IntAct=EBI-447295, EBI-7136851;
CC Q09472; P06790: E2; Xeno; NbExp=6; IntAct=EBI-447295, EBI-7010629;
CC Q09472; Q61221: Hif1a; Xeno; NbExp=2; IntAct=EBI-447295, EBI-298954;
CC Q09472; Q9QXM1: Jmy; Xeno; NbExp=16; IntAct=EBI-447295, EBI-866001;
CC Q09472; P04608: tat; Xeno; NbExp=3; IntAct=EBI-447295, EBI-6164389;
CC Q09472; P03070; Xeno; NbExp=2; IntAct=EBI-447295, EBI-617698;
CC Q09472; P03255; Xeno; NbExp=3; IntAct=EBI-447295, EBI-2603114;
CC Q09472; P03255-2; Xeno; NbExp=3; IntAct=EBI-447295, EBI-6859460;
CC Q09472; P03259; Xeno; NbExp=3; IntAct=EBI-447295, EBI-6947456;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12929931,
CC ECO:0000269|PubMed:20940255}. Nucleus {ECO:0000269|PubMed:12929931,
CC ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:16219772,
CC ECO:0000269|PubMed:16574662, ECO:0000269|PubMed:17761950,
CC ECO:0000269|PubMed:20940255}. Chromosome {ECO:0000269|PubMed:14645221,
CC ECO:0000269|PubMed:25818647}. Note=Localizes to active chromatin:
CC Colocalizes with histone H3 acetylated and/or crotonylated at 'Lys-18'
CC (H3K18ac and H3K18cr, respectively) (PubMed:25818647). In the presence
CC of ALX1 relocalizes from the cytoplasm to the nucleus. Colocalizes with
CC ROCK2 in the nucleus (PubMed:12929931). {ECO:0000269|PubMed:12929931,
CC ECO:0000269|PubMed:25818647}.
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.
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-1020. Deacetylated by SIRT2,
CC preferentially at Lys-418, Lys-423, Lys-1542, Lys-1546, Lys-1549, Lys-
CC 1699, Lys-1704 and Lys-1707. {ECO:0000269|PubMed:15004546,
CC ECO:0000269|PubMed:15632193, ECO:0000269|PubMed:17065153,
CC ECO:0000269|PubMed:18995842, ECO:0000269|PubMed:23934153,
CC ECO:0000269|PubMed:24177535}.
CC -!- PTM: Citrullinated at Arg-2142 by PADI4, which impairs methylation by
CC CARM1 and promotes interaction with NCOA2/GRIP1.
CC {ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:15731352}.
CC -!- PTM: Methylated at Arg-580 and Arg-604 in the KIX domain by CARM1,
CC which blocks association with CREB, inhibits CREB signaling and
CC activates apoptotic response. Also methylated at Arg-2142 by CARM1,
CC which impairs interaction with NCOA2/GRIP1.
CC {ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:15731352}.
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. {ECO:0000269|PubMed:12718889,
CC ECO:0000269|PubMed:19680224}.
CC -!- PTM: Probable target of ubiquitination by FBXO3, leading to rapid
CC proteasome-dependent degradation.
CC -!- PTM: Phosphorylated by HIPK2 in a RUNX1-dependent manner. This
CC phosphorylation that activates EP300 happens when RUNX1 is associated
CC with DNA and CBFB. Phosphorylated by ROCK2 and this enhances its
CC activity. Phosphorylation at Ser-89 by AMPK reduces interaction with
CC nuclear receptors, such as PPARG. {ECO:0000269|PubMed:11518699,
CC ECO:0000269|PubMed:12446687, ECO:0000269|PubMed:16574662,
CC ECO:0000269|PubMed:18695000}.
CC -!- DISEASE: Note=Defects in EP300 may play a role in epithelial cancer.
CC -!- DISEASE: Note=Chromosomal aberrations involving EP300 may be a cause of
CC acute myeloid leukemias. Translocation t(8;22)(p11;q13) with KAT6A.
CC -!- DISEASE: Rubinstein-Taybi syndrome 2 (RSTS2) [MIM:613684]: A disorder
CC characterized by craniofacial abnormalities, postnatal growth
CC deficiency, broad thumbs, broad big toes, intellectual disability and a
CC propensity for development of malignancies. Some individuals with RSTS2
CC have less severe mental impairment, more severe microcephaly, and a
CC greater degree of changes in facial bone structure than RSTS1 patients.
CC {ECO:0000269|PubMed:15706485}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Menke-Hennekam syndrome 2 (MKHK2) [MIM:618333]: A form of
CC Menke-Hennekam syndrome, a congenital autosomal dominant disease
CC characterized by developmental delay, growth retardation, and
CC craniofacial dysmorphism. Patients have intellectual disability of
CC variable severity, speech delay, autistic behavior, short stature and
CC microcephaly. Main facial characteristics include short palpebral
CC fissures, telecanthi, depressed nasal ridge, short nose, anteverted
CC nares, short columella and long philtrum.
CC {ECO:0000269|PubMed:29460469}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/P300ID97.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=P300/CBP entry;
CC URL="https://en.wikipedia.org/wiki/P300/CBP";
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DR EMBL; U01877; AAA18639.1; -; mRNA.
DR EMBL; AL080243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL096765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60408.1; -; Genomic_DNA.
DR CCDS; CCDS14010.1; -.
DR PIR; A54277; A54277.
DR RefSeq; NP_001420.2; NM_001429.3.
DR PDB; 1L3E; NMR; -; B=323-423.
DR PDB; 1P4Q; NMR; -; B=323-423.
DR PDB; 2K8F; NMR; -; A=1723-1812.
DR PDB; 2MH0; NMR; -; B=1723-1812.
DR PDB; 2MZD; NMR; -; A=1723-1812.
DR PDB; 3BIY; X-ray; 1.70 A; A=1287-1666.
DR PDB; 3I3J; X-ray; 2.33 A; A/B/C/D/E/F/G/H/I/J/K/L=1040-1161.
DR PDB; 3IO2; X-ray; 2.50 A; A=1723-1836.
DR PDB; 3P57; X-ray; 2.19 A; P=1726-1835.
DR PDB; 3T92; X-ray; 1.50 A; A=1723-1818.
DR PDB; 4BHW; X-ray; 2.80 A; A/B=1043-1519, A/B=1581-1666.
DR PDB; 4PZR; X-ray; 2.10 A; A=1287-1664.
DR PDB; 4PZS; X-ray; 1.94 A; A=1287-1664.
DR PDB; 4PZT; X-ray; 2.80 A; A=1287-1664.
DR PDB; 5BT3; X-ray; 1.05 A; A=1048-1161.
DR PDB; 5KJ2; X-ray; 1.95 A; A=1287-1522, A=1555-1666.
DR PDB; 5LKT; X-ray; 2.04 A; A=1043-1519, A=1581-1666.
DR PDB; 5LKU; X-ray; 3.50 A; A=1043-1519, A=1581-1666.
DR PDB; 5LKX; X-ray; 2.52 A; A=1043-1519, A=1581-1666.
DR PDB; 5LKZ; X-ray; 2.50 A; A=1043-1519, A=1581-1666.
DR PDB; 5LPK; X-ray; 2.10 A; A/B/C/D/E/F/G=1040-1161.
DR PDB; 5LPM; X-ray; 1.50 A; A/B=1048-1161.
DR PDB; 5NU5; X-ray; 1.60 A; A/B=1048-1161.
DR PDB; 5XZC; EM; 10.70 A; A=1046-1664.
DR PDB; 6DS6; X-ray; 1.95 A; A=1661-1713.
DR PDB; 6FGN; NMR; -; A=1723-1812.
DR PDB; 6FGS; NMR; -; A=1723-1812.
DR PDB; 6GYR; X-ray; 3.10 A; A/B/C/D=1046-1664.
DR PDB; 6GYT; X-ray; 2.50 A; A/B=1047-1168.
DR PDB; 6K4N; EM; 9.80 A; A=1046-1664.
DR PDB; 6PF1; X-ray; 2.32 A; A/B=1287-1663.
DR PDB; 6PGU; X-ray; 1.72 A; A/B=1287-1519, A/B=1582-1663.
DR PDB; 6V8B; X-ray; 3.13 A; A=1287-1666.
DR PDB; 6V8K; X-ray; 1.84 A; A=1287-1519, A=1581-1663.
DR PDB; 6V8N; X-ray; 2.30 A; A=1287-1666.
DR PDB; 6V90; X-ray; 2.04 A; A=1287-1666.
DR PDB; 7LJE; X-ray; 2.61 A; A/B/C/D=1287-1666.
DR PDBsum; 1L3E; -.
DR PDBsum; 1P4Q; -.
DR PDBsum; 2K8F; -.
DR PDBsum; 2MH0; -.
DR PDBsum; 2MZD; -.
DR PDBsum; 3BIY; -.
DR PDBsum; 3I3J; -.
DR PDBsum; 3IO2; -.
DR PDBsum; 3P57; -.
DR PDBsum; 3T92; -.
DR PDBsum; 4BHW; -.
DR PDBsum; 4PZR; -.
DR PDBsum; 4PZS; -.
DR PDBsum; 4PZT; -.
DR PDBsum; 5BT3; -.
DR PDBsum; 5KJ2; -.
DR PDBsum; 5LKT; -.
DR PDBsum; 5LKU; -.
DR PDBsum; 5LKX; -.
DR PDBsum; 5LKZ; -.
DR PDBsum; 5LPK; -.
DR PDBsum; 5LPM; -.
DR PDBsum; 5NU5; -.
DR PDBsum; 5XZC; -.
DR PDBsum; 6DS6; -.
DR PDBsum; 6FGN; -.
DR PDBsum; 6FGS; -.
DR PDBsum; 6GYR; -.
DR PDBsum; 6GYT; -.
DR PDBsum; 6K4N; -.
DR PDBsum; 6PF1; -.
DR PDBsum; 6PGU; -.
DR PDBsum; 6V8B; -.
DR PDBsum; 6V8K; -.
DR PDBsum; 6V8N; -.
DR PDBsum; 6V90; -.
DR PDBsum; 7LJE; -.
DR AlphaFoldDB; Q09472; -.
DR BMRB; Q09472; -.
DR SMR; Q09472; -.
DR BioGRID; 108347; 1342.
DR CORUM; Q09472; -.
DR DIP; DIP-257N; -.
DR IntAct; Q09472; 247.
DR MINT; Q09472; -.
DR STRING; 9606.ENSP00000263253; -.
DR BindingDB; Q09472; -.
DR ChEMBL; CHEMBL3784; -.
DR GuidetoPHARMACOLOGY; 2735; -.
DR MoonDB; Q09472; Predicted.
DR GlyGen; Q09472; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q09472; -.
DR MetOSite; Q09472; -.
DR PhosphoSitePlus; Q09472; -.
DR BioMuta; EP300; -.
DR DMDM; 223590203; -.
DR CPTAC; CPTAC-1240; -.
DR EPD; Q09472; -.
DR jPOST; Q09472; -.
DR MassIVE; Q09472; -.
DR MaxQB; Q09472; -.
DR PaxDb; Q09472; -.
DR PeptideAtlas; Q09472; -.
DR PRIDE; Q09472; -.
DR ProteomicsDB; 58723; -.
DR ABCD; Q09472; 1 sequenced antibody.
DR Antibodypedia; 296; 1061 antibodies from 40 providers.
DR DNASU; 2033; -.
DR Ensembl; ENST00000263253.9; ENSP00000263253.7; ENSG00000100393.14.
DR GeneID; 2033; -.
DR KEGG; hsa:2033; -.
DR MANE-Select; ENST00000263253.9; ENSP00000263253.7; NM_001429.4; NP_001420.2.
DR UCSC; uc003azl.5; human.
DR CTD; 2033; -.
DR DisGeNET; 2033; -.
DR GeneCards; EP300; -.
DR GeneReviews; EP300; -.
DR HGNC; HGNC:3373; EP300.
DR HPA; ENSG00000100393; Low tissue specificity.
DR MalaCards; EP300; -.
DR MIM; 602700; gene.
DR MIM; 613684; phenotype.
DR MIM; 618333; phenotype.
DR neXtProt; NX_Q09472; -.
DR OpenTargets; ENSG00000100393; -.
DR Orphanet; 353284; Rubinstein-Taybi syndrome due to EP300 haploinsufficiency.
DR PharmGKB; PA27807; -.
DR VEuPathDB; HostDB:ENSG00000100393; -.
DR eggNOG; KOG1778; Eukaryota.
DR GeneTree; ENSGT00940000155497; -.
DR HOGENOM; CLU_000162_2_0_1; -.
DR InParanoid; Q09472; -.
DR OMA; GQPGMNI; -.
DR OrthoDB; 236283at2759; -.
DR PhylomeDB; Q09472; -.
DR TreeFam; TF101097; -.
DR BRENDA; 2.3.1.48; 2681.
DR PathwayCommons; Q09472; -.
DR Reactome; R-HSA-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR Reactome; R-HSA-1368082; RORA activates gene expression.
DR Reactome; R-HSA-156711; Polo-like kinase mediated events.
DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-210744; Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-2197563; NOTCH2 intracellular domain regulates transcription.
DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR Reactome; R-HSA-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-3371568; Attenuation phase.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-HSA-5689901; Metalloprotease DUBs.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation.
DR Reactome; R-HSA-6811555; PI5P Regulates TP53 Acetylation.
DR Reactome; R-HSA-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-HSA-8941856; RUNX3 regulates NOTCH signaling.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8951936; RUNX3 regulates p14-ARF.
DR Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-9013695; NOTCH4 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR Reactome; R-HSA-918233; TRAF3-dependent IRF activation pathway.
DR Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
DR Reactome; R-HSA-9614657; FOXO-mediated transcription of cell death genes.
DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR Reactome; R-HSA-9617629; Regulation of FOXO transcriptional activity by acetylation.
DR Reactome; R-HSA-9701898; STAT3 nuclear events downstream of ALK signaling.
DR Reactome; R-HSA-9707616; Heme signaling.
DR Reactome; R-HSA-9759194; Nuclear events mediated by NFE2L2.
DR SignaLink; Q09472; -.
DR SIGNOR; Q09472; -.
DR BioGRID-ORCS; 2033; 201 hits in 1120 CRISPR screens.
DR ChiTaRS; EP300; human.
DR EvolutionaryTrace; Q09472; -.
DR GeneWiki; EP300; -.
DR GenomeRNAi; 2033; -.
DR Pharos; Q09472; Tchem.
DR PRO; PR:Q09472; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q09472; protein.
DR Bgee; ENSG00000100393; Expressed in colonic epithelium and 211 other tissues.
DR ExpressionAtlas; Q09472; baseline and differential.
DR Genevisible; Q09472; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; ISS:ARUK-UCL.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; IDA:GO_Central.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IDA:GO_Central.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0140069; F:histone butyryltransferase activity; IEA:Ensembl.
DR GO; GO:0140068; F:histone crotonyltransferase activity; IDA:UniProtKB.
DR GO; GO:0120301; F:histone lactyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IDA:UniProtKB.
DR GO; GO:0051059; F:NF-kappaB binding; IPI:ARUK-UCL.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IPI:BHF-UCL.
DR GO; GO:0016922; F:nuclear receptor binding; IPI:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR GO; GO:0106226; F:peptide 2-hydroxyisobutyryltransferase activity; IEA:RHEA.
DR GO; GO:0140065; F:peptide butyryltransferase activity; IDA:UniProtKB.
DR GO; GO:0034212; F:peptide N-acetyltransferase activity; TAS:Reactome.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IDA:MGI.
DR GO; GO:0061920; F:protein propionyltransferase activity; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0097677; F:STAT family protein binding; IPI:UniProtKB.
DR GO; GO:0048156; F:tau protein binding; NAS:ARUK-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR GO; GO:0002209; P:behavioral defense response; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; IDA:UniProtKB.
DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
DR GO; GO:0043969; P:histone H2B acetylation; IDA:UniProtKB.
DR GO; GO:0097043; P:histone H3-K56 acetylation; IEA:Ensembl.
DR GO; GO:0043967; P:histone H4 acetylation; IMP:UniProtKB.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; IDA:UniProtKB.
DR GO; GO:0006475; P:internal protein amino acid acetylation; IDA:UniProtKB.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:UniProtKB.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0010742; P:macrophage derived foam cell differentiation; IDA:UniProtKB.
DR GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; IDA:UniProtKB.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IDA:UniProtKB.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; TAS:ARUK-UCL.
DR GO; GO:0018394; P:peptidyl-lysine acetylation; IDA:ARUK-UCL.
DR GO; GO:0140067; P:peptidyl-lysine butyrylation; IDA:UniProtKB.
DR GO; GO:0140066; P:peptidyl-lysine crotonylation; IDA:UniProtKB.
DR GO; GO:0061921; P:peptidyl-lysine propionylation; IDA:UniProtKB.
DR GO; GO:0030220; P:platelet formation; IEA:Ensembl.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; IDA:BHF-UCL.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:ARUK-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:ARUK-UCL.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:ARUK-UCL.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:1905636; P:positive regulation of RNA polymerase II regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
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; ISS: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; IMP:UniProtKB.
DR GO; GO:0006473; P:protein acetylation; IDA:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0010506; P:regulation of autophagy; TAS:ParkinsonsUK-UCL.
DR GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
DR GO; GO:0006110; P:regulation of glycolytic process; IDA:UniProtKB.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISS:UniProtKB.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; IDA:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0036268; P:swimming; IEA:Ensembl.
DR GO; GO:0001966; P:thigmotaxis; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR CDD; cd15802; RING_CBP-p300; 1.
DR DisProt; DP00633; -.
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 IDEAL; IID00070; -.
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 3D-structure; Acetylation; Acyltransferase; Biological rhythms;
KW Bromodomain; Cell cycle; Chromosomal rearrangement; Chromosome;
KW Citrullination; Cytoplasm; Direct protein sequencing; Disease variant;
KW Host-virus interaction; Intellectual disability; 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:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..2414
FT /note="Histone acetyltransferase p300"
FT /id="PRO_0000211193"
FT DOMAIN 566..645
FT /note="KIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00311"
FT DOMAIN 1067..1139
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 1287..1663
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01065"
FT ZN_FING 331..417
FT /note="TAZ-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT ZN_FING 1665..1713
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1728..1809
FT /note="TAZ-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..149
FT /note="Interaction with RORA"
FT /evidence="ECO:0000269|PubMed:9862959"
FT REGION 2..139
FT /note="Interaction with ALX1"
FT /evidence="ECO:0000269|PubMed:12929931"
FT REGION 133..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1029
FT /note="CRD1; mediates transcriptional repression"
FT REGION 1397..1399
FT /note="Interaction with histone"
FT /evidence="ECO:0000269|PubMed:18273021"
FT REGION 1520..1578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1572..1818
FT /note="Binding region for E1A adenovirus"
FT REGION 1833..1924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1980..2010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2003..2212
FT /note="Interaction with HTLV-1 Tax"
FT REGION 2041..2240
FT /note="Interaction with NCOA2"
FT /evidence="ECO:0000269|PubMed:15731352"
FT REGION 2094..2163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2186..2237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2267..2385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 11..17
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 196..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..849
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..895
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1520..1547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1548..1565
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1851..1886
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1909..1924
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1989..2010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2100..2114
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2115..2163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2206..2237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2267..2310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2311..2342
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2362..2385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11959990,
FT ECO:0000269|PubMed:12778114"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11959990,
FT ECO:0000269|PubMed:12778114"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11959990,
FT ECO:0000269|PubMed:12778114"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11959990,
FT ECO:0000269|PubMed:12778114"
FT BINDING 378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11959990,
FT ECO:0000269|PubMed:12778114"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11959990,
FT ECO:0000269|PubMed:12778114"
FT BINDING 388
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11959990,
FT ECO:0000269|PubMed:12778114"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11959990,
FT ECO:0000269|PubMed:12778114"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11959990,
FT ECO:0000269|PubMed:12778114"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11959990,
FT ECO:0000269|PubMed:12778114"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11959990,
FT ECO:0000269|PubMed:12778114"
FT BINDING 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11959990,
FT ECO:0000269|PubMed:12778114"
FT BINDING 1398..1400
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:24819397"
FT BINDING 1410..1411
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:24819397"
FT BINDING 1457
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:24819397"
FT BINDING 1462
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:24819397"
FT BINDING 1466
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:24819397"
FT BINDING 1670
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1673
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1683
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1686
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1692
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1695
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1701
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1703
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT SITE 31..32
FT /note="Breakpoint for translocation to form KAT6A-EP300 and
FT EP300-KAT6A"
FT SITE 2088
FT /note="Interaction with NCOA2"
FT SITE 2142
FT /note="Interaction with NCOA2"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 89
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000269|PubMed:11518699,
FT ECO:0000269|PubMed:16574662"
FT MOD_RES 418
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18995842"
FT MOD_RES 423
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18995842"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RWS6"
FT MOD_RES 580
FT /note="Asymmetric dimethylarginine; by CARM1"
FT /evidence="ECO:0000269|PubMed:11701890"
FT MOD_RES 604
FT /note="Asymmetric dimethylarginine; by CARM1"
FT /evidence="ECO:0000269|PubMed:11701890"
FT MOD_RES 636
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 977
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1020
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:15632193"
FT MOD_RES 1024
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:15632193"
FT MOD_RES 1038
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1180
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:B2RWS6"
FT MOD_RES 1336
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17065153"
FT MOD_RES 1473
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17065153"
FT MOD_RES 1499
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:15004546"
FT MOD_RES 1542
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18995842,
FT ECO:0007744|PubMed:19608861"
FT MOD_RES 1546
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18995842,
FT ECO:0007744|PubMed:19608861"
FT MOD_RES 1549
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:15004546,
FT ECO:0000269|PubMed:18995842"
FT MOD_RES 1554
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:15004546,
FT ECO:0007744|PubMed:19608861"
FT MOD_RES 1555
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1558
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15004546,
FT ECO:0007744|PubMed:19608861"
FT MOD_RES 1560
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:15004546,
FT ECO:0007744|PubMed:19608861"
FT MOD_RES 1583
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1699
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18995842"
FT MOD_RES 1704
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18995842"
FT MOD_RES 1707
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18995842"
FT MOD_RES 1726
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2142
FT /note="Asymmetric dimethylarginine; by CARM1; alternate"
FT /evidence="ECO:0000269|PubMed:15731352"
FT MOD_RES 2142
FT /note="Citrulline; by PADI4; alternate"
FT /evidence="ECO:0000269|PubMed:15731352"
FT CROSSLNK 1020
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:12718889"
FT CROSSLNK 1024
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:12718889"
FT VARIANT 289
FT /note="M -> V (in dbSNP:rs2230111)"
FT /id="VAR_055554"
FT VARIANT 827
FT /note="L -> P (in a breast cancer sample)"
FT /evidence="ECO:0000269|PubMed:10700188"
FT /id="VAR_014428"
FT VARIANT 997
FT /note="I -> V (in dbSNP:rs20551)"
FT /id="VAR_020425"
FT VARIANT 1013
FT /note="E -> G (in a breast cancer sample;
FT dbSNP:rs1234168115)"
FT /evidence="ECO:0000269|PubMed:10700188"
FT /id="VAR_014429"
FT VARIANT 1511
FT /note="N -> I"
FT /evidence="ECO:0000269|PubMed:24476420"
FT /id="VAR_074021"
FT VARIANT 1650
FT /note="S -> Y (in a pancreatic cancer sample)"
FT /evidence="ECO:0000269|PubMed:10700188"
FT /id="VAR_014430"
FT VARIANT 1824
FT /note="Q -> P (in MKHK2; dbSNP:rs1569120903)"
FT /evidence="ECO:0000269|PubMed:29460469"
FT /id="VAR_081986"
FT VARIANT 1831
FT /note="Missing (in MKHK2)"
FT /evidence="ECO:0000269|PubMed:29460469"
FT /id="VAR_081987"
FT VARIANT 2007
FT /note="Q -> R (found in a patient with spinocerebellar
FT ataxia; unknown pathological significance;
FT dbSNP:rs763892493)"
FT /evidence="ECO:0000269|PubMed:29053796"
FT /id="VAR_080731"
FT VARIANT 2174
FT /note="T -> S (in dbSNP:rs5758252)"
FT /id="VAR_038376"
FT VARIANT 2221
FT /note="P -> Q (in a colorectal cancer sample;
FT dbSNP:rs28937578)"
FT /evidence="ECO:0000269|PubMed:10700188"
FT /id="VAR_014431"
FT VARIANT 2223
FT /note="Q -> P (in dbSNP:rs1046088)"
FT /evidence="ECO:0000269|PubMed:7523245"
FT /id="VAR_038377"
FT MUTAGEN 89
FT /note="S->A: Abolishes AMPK-mediated phosphorylation."
FT /evidence="ECO:0000269|PubMed:11518699"
FT MUTAGEN 89
FT /note="S->D: Phosphomimetic mutant that leads to descreased
FT interaction with nuclear receptors."
FT /evidence="ECO:0000269|PubMed:11518699"
FT MUTAGEN 344
FT /note="L->A: Inhibits interaction with HIF1A and
FT transcription activation; when associated with A-345."
FT /evidence="ECO:0000269|PubMed:12778114"
FT MUTAGEN 345
FT /note="L->A: Inhibits interaction with HIF1A and
FT transcription activation; when associated with A-344."
FT /evidence="ECO:0000269|PubMed:12778114"
FT MUTAGEN 371..376
FT /note="TMKNVL->NAAIRS: Inhibits interaction with HIF1A.
FT Reduces interaction with CITED2."
FT /evidence="ECO:0000269|PubMed:9887100"
FT MUTAGEN 413..418
FT /note="VCLPLK->NAAIRS: Inhibits interaction with HIF1A.
FT Does not inhibit interaction with CITED2."
FT /evidence="ECO:0000269|PubMed:9887100"
FT MUTAGEN 1020
FT /note="K->A: Abolishes sumoylation and transcriptional
FT repression when associated with A-1024."
FT /evidence="ECO:0000269|PubMed:12718889,
FT ECO:0000269|PubMed:15632193"
FT MUTAGEN 1020
FT /note="K->R: Abolishes sumoylation and transcriptional
FT repression; when associated with R-1024."
FT /evidence="ECO:0000269|PubMed:12718889,
FT ECO:0000269|PubMed:15632193"
FT MUTAGEN 1024
FT /note="K->A: Abolishes sumoylation and transcriptional
FT repression; when associated with A-1020."
FT /evidence="ECO:0000269|PubMed:12718889,
FT ECO:0000269|PubMed:15632193"
FT MUTAGEN 1024
FT /note="K->R: Abolishes sumoylation and transcriptional
FT repression; when associated with R-1020."
FT /evidence="ECO:0000269|PubMed:12718889,
FT ECO:0000269|PubMed:15632193"
FT MUTAGEN 1170
FT /note="F->E: Increased acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:23934153"
FT MUTAGEN 1204
FT /note="C->R: Increased acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:23934153"
FT MUTAGEN 1242
FT /note="E->K: Increased acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:23934153"
FT MUTAGEN 1357
FT /note="T->L: 40% decrease in activity."
FT /evidence="ECO:0000269|PubMed:18273021"
FT MUTAGEN 1357
FT /note="T->R: 40% decrease in activity. 90% decrease in
FT activity; when associated with R-1505; R-1625 and R-1628."
FT /evidence="ECO:0000269|PubMed:18273021"
FT MUTAGEN 1396
FT /note="S->R: Loss of activity; when associated with R-
FT 1397."
FT /evidence="ECO:0000269|PubMed:18273021"
FT MUTAGEN 1396
FT /note="S->W: Loss of activity; when associated with W-
FT 1396."
FT /evidence="ECO:0000269|PubMed:18273021"
FT MUTAGEN 1397
FT /note="Y->R: Loss of activity; when associated with R-
FT 1396."
FT /evidence="ECO:0000269|PubMed:18273021"
FT MUTAGEN 1397
FT /note="Y->W: Loss of activity; when associated with W-
FT 1397."
FT /evidence="ECO:0000269|PubMed:18273021"
FT MUTAGEN 1399
FT /note="D->Y: Abolished acetyltransferase and
FT acyltransferase activities. Abolishes autoacetylation. Does
FT not interact with TFAP2A and inhibits transcriptional
FT coactivation of TFAP2A by CITED2. Does not inhibit
FT interaction with CITED2, DNA-binding of TFAP2A or nuclear
FT localization of TFAP2A or CITED2. No enhancement of FOXO1-
FT mediated transcriptional activity. No inhibition of
FT insulin-mediated translocation to the cytoplasm. No
FT acetylation of RXRA."
FT /evidence="ECO:0000269|PubMed:12586840,
FT ECO:0000269|PubMed:15890677, ECO:0000269|PubMed:17761950,
FT ECO:0000269|PubMed:23934153, ECO:0000269|PubMed:29775581"
FT MUTAGEN 1467
FT /note="Y->F: Abolishes autoacetylation. Loss of
FT acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:23934153"
FT MUTAGEN 1504
FT /note="F->A: Abolished acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:24835996"
FT MUTAGEN 1505
FT /note="E->R: 90% decrease in activity; when associated with
FT R-1625 and R-1628. 90% decrease in activity; when
FT associated with R-1357; R-1625 and R-1628."
FT /evidence="ECO:0000269|PubMed:18273021"
FT MUTAGEN 1625
FT /note="D->R: 70% decrease in activity; when associated with
FT R-1628. 90% decrease in activity; when associated with R-
FT 1505 and R-1628. 90% decrease in activity; when associated
FT with R-1357; R-1505 and R-1628."
FT /evidence="ECO:0000269|PubMed:18273021"
FT MUTAGEN 1628
FT /note="D->R: 70% decrease in activity; when associated with
FT R-1625. 90% decrease in activity; when associated with E-
FT 1505 and R-1625. 90% decrease in activity; when associated
FT with R-1357; R-1505 and R-1625."
FT /evidence="ECO:0000269|PubMed:18273021"
FT MUTAGEN 1645..1646
FT /note="RR->EE: Increased acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:23934153"
FT MUTAGEN 2056
FT /note="R->K: No effect on interaction with NCOA2."
FT /evidence="ECO:0000269|PubMed:15731352"
FT MUTAGEN 2088
FT /note="R->K: Abolishes interaction with NCOA2."
FT /evidence="ECO:0000269|PubMed:15731352"
FT MUTAGEN 2142
FT /note="R->K: Strongly reduces interaction with NCOA2."
FT /evidence="ECO:0000269|PubMed:15731352"
FT CONFLICT 169
FT /note="M -> T (in Ref. 1; AAA18639)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="N -> D (in Ref. 1; AAA18639)"
FT /evidence="ECO:0000305"
FT CONFLICT 928
FT /note="T -> N (in Ref. 1; AAA18639)"
FT /evidence="ECO:0000305"
FT CONFLICT 1924
FT /note="A -> T (in Ref. 1; AAA18639)"
FT /evidence="ECO:0000305"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:1L3E"
FT HELIX 335..355
FT /evidence="ECO:0007829|PDB:1L3E"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:1L3E"
FT HELIX 367..379
FT /evidence="ECO:0007829|PDB:1L3E"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:1L3E"
FT HELIX 391..405
FT /evidence="ECO:0007829|PDB:1L3E"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:1P4Q"
FT HELIX 414..418
FT /evidence="ECO:0007829|PDB:1L3E"
FT HELIX 1051..1066
FT /evidence="ECO:0007829|PDB:5BT3"
FT TURN 1069..1072
FT /evidence="ECO:0007829|PDB:5BT3"
FT HELIX 1073..1075
FT /evidence="ECO:0007829|PDB:5BT3"
FT HELIX 1081..1084
FT /evidence="ECO:0007829|PDB:5BT3"
FT HELIX 1089..1092
FT /evidence="ECO:0007829|PDB:5BT3"
FT HELIX 1099..1107
FT /evidence="ECO:0007829|PDB:5BT3"
FT HELIX 1114..1131
FT /evidence="ECO:0007829|PDB:5BT3"
FT HELIX 1137..1160
FT /evidence="ECO:0007829|PDB:5BT3"
FT STRAND 1175..1177
FT /evidence="ECO:0007829|PDB:6GYR"
FT STRAND 1180..1182
FT /evidence="ECO:0007829|PDB:5LKX"
FT STRAND 1189..1194
FT /evidence="ECO:0007829|PDB:5LKT"
FT TURN 1195..1197
FT /evidence="ECO:0007829|PDB:5LKT"
FT STRAND 1198..1201
FT /evidence="ECO:0007829|PDB:5LKT"
FT HELIX 1202..1207
FT /evidence="ECO:0007829|PDB:5LKT"
FT STRAND 1210..1215
FT /evidence="ECO:0007829|PDB:5LKT"
FT STRAND 1218..1221
FT /evidence="ECO:0007829|PDB:4BHW"
FT STRAND 1224..1227
FT /evidence="ECO:0007829|PDB:5LKT"
FT HELIX 1228..1230
FT /evidence="ECO:0007829|PDB:5LKT"
FT STRAND 1231..1236
FT /evidence="ECO:0007829|PDB:5LKT"
FT STRAND 1244..1246
FT /evidence="ECO:0007829|PDB:5LKT"
FT TURN 1248..1250
FT /evidence="ECO:0007829|PDB:5LKT"
FT STRAND 1253..1255
FT /evidence="ECO:0007829|PDB:5LKT"
FT HELIX 1256..1259
FT /evidence="ECO:0007829|PDB:5LKT"
FT TURN 1263..1265
FT /evidence="ECO:0007829|PDB:5LKT"
FT HELIX 1273..1278
FT /evidence="ECO:0007829|PDB:5LKT"
FT TURN 1290..1292
FT /evidence="ECO:0007829|PDB:6V8K"
FT HELIX 1297..1313
FT /evidence="ECO:0007829|PDB:3BIY"
FT STRAND 1321..1334
FT /evidence="ECO:0007829|PDB:3BIY"
FT HELIX 1339..1342
FT /evidence="ECO:0007829|PDB:3BIY"
FT TURN 1343..1347
FT /evidence="ECO:0007829|PDB:3BIY"
FT STRAND 1351..1366
FT /evidence="ECO:0007829|PDB:3BIY"
FT STRAND 1369..1381
FT /evidence="ECO:0007829|PDB:3BIY"
FT STRAND 1383..1385
FT /evidence="ECO:0007829|PDB:6PF1"
FT STRAND 1392..1400
FT /evidence="ECO:0007829|PDB:3BIY"
FT HELIX 1407..1409
FT /evidence="ECO:0007829|PDB:3BIY"
FT HELIX 1410..1428
FT /evidence="ECO:0007829|PDB:3BIY"
FT STRAND 1432..1436
FT /evidence="ECO:0007829|PDB:3BIY"
FT STRAND 1446..1450
FT /evidence="ECO:0007829|PDB:3BIY"
FT HELIX 1460..1476
FT /evidence="ECO:0007829|PDB:3BIY"
FT STRAND 1482..1485
FT /evidence="ECO:0007829|PDB:3BIY"
FT HELIX 1486..1493
FT /evidence="ECO:0007829|PDB:3BIY"
FT HELIX 1498..1500
FT /evidence="ECO:0007829|PDB:3BIY"
FT HELIX 1508..1517
FT /evidence="ECO:0007829|PDB:3BIY"
FT HELIX 1582..1590
FT /evidence="ECO:0007829|PDB:3BIY"
FT HELIX 1592..1594
FT /evidence="ECO:0007829|PDB:3BIY"
FT STRAND 1595..1601
FT /evidence="ECO:0007829|PDB:3BIY"
FT HELIX 1603..1606
FT /evidence="ECO:0007829|PDB:3BIY"
FT HELIX 1622..1624
FT /evidence="ECO:0007829|PDB:3BIY"
FT STRAND 1625..1627
FT /evidence="ECO:0007829|PDB:3BIY"
FT HELIX 1628..1636
FT /evidence="ECO:0007829|PDB:3BIY"
FT HELIX 1644..1662
FT /evidence="ECO:0007829|PDB:3BIY"
FT TURN 1671..1673
FT /evidence="ECO:0007829|PDB:6DS6"
FT STRAND 1676..1688
FT /evidence="ECO:0007829|PDB:6DS6"
FT HELIX 1693..1696
FT /evidence="ECO:0007829|PDB:6DS6"
FT STRAND 1705..1708
FT /evidence="ECO:0007829|PDB:6DS6"
FT TURN 1726..1728
FT /evidence="ECO:0007829|PDB:2MZD"
FT HELIX 1730..1747
FT /evidence="ECO:0007829|PDB:3T92"
FT STRAND 1750..1752
FT /evidence="ECO:0007829|PDB:6FGN"
FT HELIX 1756..1770
FT /evidence="ECO:0007829|PDB:3T92"
FT TURN 1774..1778
FT /evidence="ECO:0007829|PDB:3T92"
FT HELIX 1780..1793
FT /evidence="ECO:0007829|PDB:3T92"
FT STRAND 1799..1802
FT /evidence="ECO:0007829|PDB:2MZD"
FT HELIX 1806..1818
FT /evidence="ECO:0007829|PDB:3T92"
SQ SEQUENCE 2414 AA; 264161 MW; 8E869E1F174A6FEB CRC64;
MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS TELGLTNGGD
INQLQTSLGM VQDAASKHKQ LSELLRSGSS PNLNMGVGGP GQVMASQAQQ SSPGLGLINS
MVKSPMTQAG LTSPNMGMGT SGPNQGPTQS TGMMNSPVNQ PAMGMNTGMN AGMNPGMLAA
GNGQGIMPNQ VMNGSIGAGR GRQNMQYPNP GMGSAGNLLT EPLQQGSPQM GGQTGLRGPQ
PLKMGMMNNP NPYGSPYTQN PGQQIGASGL GLQIQTKTVL SNNLSPFAMD KKAVPGGGMP
NMGQQPAPQV QQPGLVTPVA QGMGSGAHTA DPEKRKLIQQ QLVLLLHAHK CQRREQANGE
VRQCNLPHCR TMKNVLNHMT HCQSGKSCQV AHCASSRQII SHWKNCTRHD CPVCLPLKNA
GDKRNQQPIL TGAPVGLGNP SSLGVGQQSA PNLSTVSQID PSSIERAYAA LGLPYQVNQM
PTQPQVQAKN QQNQQPGQSP QGMRPMSNMS ASPMGVNGGV GVQTPSLLSD SMLHSAINSQ
NPMMSENASV PSLGPMPTAA QPSTTGIRKQ WHEDITQDLR NHLVHKLVQA IFPTPDPAAL
KDRRMENLVA YARKVEGDMY ESANNRAEYY HLLAEKIYKI QKELEEKRRT RLQKQNMLPN
AAGMVPVSMN PGPNMGQPQP GMTSNGPLPD PSMIRGSVPN QMMPRITPQS GLNQFGQMSM
AQPPIVPRQT PPLQHHGQLA QPGALNPPMG YGPRMQQPSN QGQFLPQTQF PSQGMNVTNI
PLAPSSGQAP VSQAQMSSSS CPVNSPIMPP GSQGSHIHCP QLPQPALHQN SPSPVPSRTP
TPHHTPPSIG AQQPPATTIP APVPTPPAMP PGPQSQALHP PPRQTPTPPT TQLPQQVQPS
LPAAPSADQP QQQPRSQQST AASVPTPTAP LLPPQPATPL SQPAVSIEGQ VSNPPSTSST
EVNSQAIAEK QPSQEVKMEA KMEVDQPEPA DTQPEDISES KVEDCKMEST ETEERSTELK
TEIKEEEDQP STSATQSSPA PGQSKKKIFK PEELRQALMP TLEALYRQDP ESLPFRQPVD
PQLLGIPDYF DIVKSPMDLS TIKRKLDTGQ YQEPWQYVDD IWLMFNNAWL YNRKTSRVYK
YCSKLSEVFE QEIDPVMQSL GYCCGRKLEF SPQTLCCYGK QLCTIPRDAT YYSYQNRYHF
CEKCFNEIQG ESVSLGDDPS QPQTTINKEQ FSKRKNDTLD PELFVECTEC GRKMHQICVL
HHEIIWPAGF VCDGCLKKSA RTRKENKFSA KRLPSTRLGT FLENRVNDFL RRQNHPESGE
VTVRVVHASD KTVEVKPGMK ARFVDSGEMA ESFPYRTKAL FAFEEIDGVD LCFFGMHVQE
YGSDCPPPNQ RRVYISYLDS VHFFRPKCLR TAVYHEILIG YLEYVKKLGY TTGHIWACPP
SEGDDYIFHC HPPDQKIPKP KRLQEWYKKM LDKAVSERIV HDYKDIFKQA TEDRLTSAKE
LPYFEGDFWP NVLEESIKEL EQEEEERKRE ENTSNESTDV TKGDSKNAKK KNNKKTSKNK
SSLSRGNKKK PGMPNVSNDL SQKLYATMEK HKEVFFVIRL IAGPAANSLP PIVDPDPLIP
CDLMDGRDAF LTLARDKHLE FSSLRRAQWS TMCMLVELHT QSQDRFVYTC NECKHHVETR
WHCTVCEDYD LCITCYNTKN HDHKMEKLGL GLDDESNNQQ AAATQSPGDS RRLSIQRCIQ
SLVHACQCRN ANCSLPSCQK MKRVVQHTKG CKRKTNGGCP ICKQLIALCC YHAKHCQENK
CPVPFCLNIK QKLRQQQLQH RLQQAQMLRR RMASMQRTGV VGQQQGLPSP TPATPTTPTG
QQPTTPQTPQ PTSQPQPTPP NSMPPYLPRT QAAGPVSQGK AAGQVTPPTP PQTAQPPLPG
PPPAAVEMAM QIQRAAETQR QMAHVQIFQR PIQHQMPPMT PMAPMGMNPP PMTRGPSGHL
EPGMGPTGMQ QQPPWSQGGL PQPQQLQSGM PRPAMMSVAQ HGQPLNMAPQ PGLGQVGISP
LKPGTVSQQA LQNLLRTLRS PSSPLQQQQV LSILHANPQL LAAFIKQRAA KYANSNPQPI
PGQPGMPQGQ PGLQPPTMPG QQGVHSNPAM QNMNPMQAGV QRAGLPQQQP QQQLQPPMGG
MSPQAQQMNM NHNTMPSQFR DILRRQQMMQ QQQQQGAGPG IGPGMANHNQ FQQPQGVGYP
PQQQQRMQHH MQQMQQGNMG QIGQLPQALG AEAGASLQAY QQRLLQQQMG SPVQPNPMSP
QQHMLPNQAQ SPHLQGQQIP NSLSNQVRSP QPVPSPRPQS QPPHSSPSPR MQPQPSPHHV
SPQTSSPHPG LVAAQANPME QGHFASPDQN SMLSQLASNP GMANLHGASA TDLGLSTDNS
DLNSNLSQST LDIH
