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 27-MAR-2024, entry version 270. DE RecName: Full=Histone acetyltransferase p300 {ECO:0000305}; DE Short=p300 HAT; DE EC=2.3.1.48 {ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:23415232, ECO:0000269|PubMed:23934153, ECO:0000269|PubMed:25818647, 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 {ECO:0000303|PubMed:15706485, ECO:0000312|HGNC:HGNC:3373}; GN Synonyms=P300 {ECO:0000303|PubMed:7523245}; 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 FUNCTION, AND 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, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION WITH RP NPAS2; BMAL1 AND 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 FUNCTION, AND 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 FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=16285960; DOI=10.1053/j.gastro.2005.07.055; RA Ray S., Boldogh I., Brasier A.R.; RT "STAT3 NH2-terminal acetylation is activated by the hepatic acute-phase RT response and required for IL-6 induction of angiotensinogen."; RL Gastroenterology 129:1616-1632(2005). RN [60] 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 [61] 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 [62] RP 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 [63] 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 [64] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=15653507; DOI=10.1126/science.1105166; RA Yuan Z.L., Guan Y.J., Chatterjee D., Chin Y.E.; RT "Stat3 dimerization regulated by reversible acetylation of a single lysine RT residue."; RL Science 307:269-273(2005). RN [65] 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 [66] 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 [67] 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 [68] 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 [69] 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 [70] 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 [71] 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 [72] 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 [73] 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 [74] 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 [75] 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 [76] 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 [77] 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 [78] 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 [79] 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 [80] 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 [81] RP FUNCTION, AND INTERACTION WITH STAT3. RX PubMed=18782771; DOI=10.1074/jbc.m805941200; RA Hou T., Ray S., Lee C., Brasier A.R.; RT "The STAT3 NH2-terminal domain stabilizes enhanceosome assembly by RT interacting with the p300 bromodomain."; RL J. Biol. Chem. 283:30725-30734(2008). RN [82] 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 [83] 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 [84] 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 [85] 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 [86] 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 [87] 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 [88] 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 [89] 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 [90] 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 [91] 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 [92] 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 [93] 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 [94] 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 [95] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=21131905; DOI=10.1038/emboj.2010.318; RA Jin Q., Yu L.R., Wang L., Zhang Z., Kasper L.H., Lee J.E., Wang C., RA Brindle P.K., Dent S.Y., Ge K.; RT "Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-mediated RT H3K18/27ac in nuclear receptor transactivation."; RL EMBO J. 30:249-262(2011). RN [96] 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 [97] 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 [98] 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 [99] 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 [100] 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 [101] 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 [102] 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 [103] 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 [104] 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 [105] 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 [106] 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 [107] 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 [108] 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 [109] 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 [110] 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 [111] 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 [112] 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 [113] 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 [114] RP SUBCELLULAR LOCATION. RX PubMed=25593309; DOI=10.1101/gad.252189.114; RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W., RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.; RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of RT transcription-associated DNA damage that promotes homologous RT recombination."; RL Genes Dev. 29:197-211(2015). RN [115] 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 [116] 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 [117] 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 [118] 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 [119] 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 [120] 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 [121] 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 [122] 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 [123] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=30197302; DOI=10.1016/j.cmet.2018.08.013; RA Son S.M., Park S.J., Lee H., Siddiqi F., Lee J.E., Menzies F.M., RA Rubinsztein D.C.; RT "Leucine signals to mTORC1 via its metabolite acetyl-coenzyme A."; RL Cell Metab. 29:192-201(2019). RN [124] 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 [125] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=32561715; DOI=10.1038/s41467-020-16886-2; RA Son S.M., Park S.J., Stamatakou E., Vicinanza M., Menzies F.M., RA Rubinsztein D.C.; RT "Leucine regulates autophagy via acetylation of the mTORC1 component RT raptor."; RL Nat. Commun. 11:3148-3148(2020). RN [126] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=37731000; DOI=10.1038/s41586-023-06565-9; RA Lu-Culligan W.J., Connor L.J., Xie Y., Ekundayo B.E., Rose B.T., RA Machyna M., Pintado-Urbanc A.P., Zimmer J.T., Vock I.W., Bhanu N.V., RA King M.C., Garcia B.A., Bleichert F., Simon M.D.; RT "Acetyl-methyllysine marks chromatin at active transcription start sites."; RL Nature 622:173-179(2023). RN [127] 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 [128] 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 [129] 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 [130] 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 [131] 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 [132] 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 [133] 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 [134] 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 [135] 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 [136] 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 [137] 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 a histone acetyltransferase and regulates CC transcription via chromatin remodeling (PubMed:23415232, CC PubMed:23934153, PubMed:8945521). Acetylates all four core histones in CC nucleosomes (PubMed:23415232, PubMed:23934153, PubMed:8945521). Histone CC acetylation gives an epigenetic tag for transcriptional activation CC (PubMed:23415232, PubMed:23934153, PubMed:8945521). Mediates CC acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification that CC localizes at the surface of the histone octamer and stimulates CC transcription, possibly by promoting nucleosome instability CC (PubMed:23415232). Mediates acetylation of histone H3 at 'Lys-18' and CC 'Lys-27' (H3K18ac and H3K27ac, respectively) (PubMed:21131905, CC PubMed:23911289). Also able to acetylate histone lysine residues that CC are already monomethylated on the same side chain to form N6-acetyl-N6- CC methyllysine (Kacme), an epigenetic mark of active chromatin associated CC with increased transcriptional initiation (PubMed:37731000). Catalyzes CC formation of histone H4 acetyl-methylated at 'Lys-5' and 'Lys-12' CC (H4K5acme and H4K12acme, respectively) (PubMed:37731000). Also CC functions as acetyltransferase for non-histone targets, such as ALX1, CC HDAC1, PRMT1, SIRT2 or STAT3 (PubMed:12929931, PubMed:16285960, CC PubMed:15653507, PubMed:16762839, PubMed:18722353, PubMed:18782771). CC Acetylates 'Lys-131' of ALX1 and acts as its coactivator CC (PubMed:12929931). Acetylates SIRT2 and is proposed to indirectly CC increase the transcriptional activity of p53/TP53 through acetylation CC and subsequent attenuation of SIRT2 deacetylase function CC (PubMed:18722353). Following DNA damage, forms a stress-responsive CC p53/TP53 coactivator complex with JMY which mediates p53/TP53 CC acetylation, thereby increasing p53/TP53-dependent transcription and CC apoptosis (PubMed:11511361, PubMed:15448695). Promotes chromatin CC acetylation in heat shock responsive HSP genes during the heat shock CC response (HSR), thereby stimulating HSR transcription CC (PubMed:18451878). Acetylates HDAC1 leading to its inactivation and CC modulation of transcription (PubMed:16762839). Acetylates 'Lys-247' of CC EGR2 (By similarity). Acts as a TFAP2A-mediated transcriptional CC coactivator in presence of CITED2 (PubMed:12586840). Plays a role as a CC coactivator of NEUROD1-dependent transcription of the secretin and p21 CC genes and controls terminal differentiation of cells in the intestinal CC epithelium. Promotes cardiac myocyte enlargement (PubMed:14752053). Can CC also mediate transcriptional repression. Acetylates FOXO1 and enhances CC its transcriptional activity (PubMed:15890677). Acetylates STAT3 at CC different sites, promoting both STAT3 dimerization and activation and CC recruitment to chromatin (PubMed:16285960, PubMed:15653507, CC PubMed:18782771). Acetylates BCL6 wich disrupts its ability to recruit CC histone deacetylases and hinders its transcriptional repressor activity CC (PubMed:12402037). Participates in CLOCK or NPAS2-regulated rhythmic CC gene transcription; exhibits a circadian association with CLOCK or CC NPAS2, correlating with increase in PER1/2 mRNA and histone H3 CC acetylation on the PER1/2 promoter (PubMed:14645221). Acetylates MTA1 CC at 'Lys-626' which is essential for its transcriptional coactivator CC activity (PubMed:16617102). Acetylates XBP1 isoform 2; acetylation CC increases protein stability of XBP1 isoform 2 and enhances its CC transcriptional activity (PubMed:20955178). Acetylates PCNA; CC acetylation promotes removal of chromatin-bound PCNA and its CC degradation during nucleotide excision repair (NER) (PubMed:24939902). CC Acetylates MEF2D (PubMed:21030595). Acetylates and stabilizes ZBTB7B CC protein by antagonizing ubiquitin conjugation and degradation, this CC mechanism may be involved in CD4/CD8 lineage differentiation CC (PubMed:20810990). Acetylates GABPB1, impairing GABPB1 CC heterotetramerization and activity (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). Acetylates RPTOR in response to leucine, leading to CC activation of the mTORC1 complex (PubMed:30197302, PubMed:32561715). CC Mediates cAMP-gene regulation by binding specifically to phosphorylated CC CREBBP (PubMed:8917528). In addition to protein acetyltransferase, can CC use 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:14752053, CC ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15448695, CC ECO:0000269|PubMed:15653507, ECO:0000269|PubMed:15890677, CC ECO:0000269|PubMed:16285960, ECO:0000269|PubMed:16617102, CC ECO:0000269|PubMed:16762839, ECO:0000269|PubMed:17267393, CC ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:18451878, CC ECO:0000269|PubMed:18722353, ECO:0000269|PubMed:18782771, CC ECO:0000269|PubMed:18995842, ECO:0000269|PubMed:20810990, CC ECO:0000269|PubMed:21030595, ECO:0000269|PubMed:21131905, CC ECO:0000269|PubMed:23415232, ECO:0000269|PubMed:23911289, CC ECO:0000269|PubMed:23934153, ECO:0000269|PubMed:24120661, CC ECO:0000269|PubMed:24939902, ECO:0000269|PubMed:25514493, CC ECO:0000269|PubMed:25818647, ECO:0000269|PubMed:29775581, CC ECO:0000269|PubMed:30193097, ECO:0000269|PubMed:30197302, CC ECO:0000269|PubMed:31645732, ECO:0000269|PubMed:32561715, CC ECO:0000269|PubMed:37731000, ECO:0000269|PubMed:8917528, CC ECO:0000269|PubMed:8945521, 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-[histone] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, CC Rhea:RHEA-COMP:11338, 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:14645221, ECO:0000269|PubMed:21131905, CC ECO:0000269|PubMed:23415232, ECO:0000269|PubMed:23934153, CC ECO:0000269|PubMed:25818647, ECO:0000269|PubMed:8945521}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; CC Evidence={ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:21131905, CC ECO:0000269|PubMed:23415232, ECO:0000269|PubMed:23934153, CC ECO:0000269|PubMed:25818647, ECO:0000269|PubMed:8945521}; 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; CC Evidence={ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:15653507, CC ECO:0000269|PubMed:16285960, ECO:0000269|PubMed:17761950, CC ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:30197302, CC ECO:0000269|PubMed:32561715}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949; CC Evidence={ECO:0000269|PubMed:15653507, ECO:0000269|PubMed:16285960, CC ECO:0000305|PubMed:15448695, ECO:0000305|PubMed:30197302, CC ECO:0000305|PubMed:32561715}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + N(6)-methyl-L-lysyl-[histone] = CoA + H(+) + CC N(6)-acetyl-N(6)-methyl-L-lysyl-[histone]; Xref=Rhea:RHEA:77775, CC Rhea:RHEA-COMP:9846, Rhea:RHEA-COMP:18984, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61929, CC ChEBI:CHEBI:197459; Evidence={ECO:0000269|PubMed:37731000}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77776; CC Evidence={ECO:0000269|PubMed:37731000}; 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 interaction CC is 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 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, BMAL1 and CLOCK (PubMed:14645221). Interacts with CC SIRT2 isoform 1, isoform 2 and isoform 5 (PubMed:24177535). Interacts CC with MTA1 (PubMed:16617102). Interacts with HDAC4 and HDAC5 in the CC presence of TFAP2C (PubMed:24413532). Interacts with TRIP4 CC (PubMed:25219498). Directly interacts with ZBTB49; this interaction CC leads to synergistic transactivation of CDKN1A (PubMed:25245946). CC Interacts with NR4A3 (By similarity). Interacts with ZNF451 CC (PubMed:24324267). Interacts with ATF5; EP300 is required for ATF5 and CC CEBPB interaction and DNA binding (By similarity). Interacts with HSF1 CC (PubMed:27189267). Interacts with ZBTB48/TZAP (PubMed:24382891). CC Interacts with STAT1; the interaction is enhanced upon IFN-gamma CC stimulation (PubMed:26479788). Interacts with HNRNPU (via C-terminus); CC this interaction enhances DNA-binding of HNRNPU to nuclear CC scaffold/matrix attachment region (S/MAR) elements (PubMed:11909954). CC Interacts with BCL11B (PubMed:27959755, PubMed:16809611). Interacts CC with SMAD4; negatively regulated by ZBTB7A (PubMed:25514493). Interacts CC with DUX4 (via C-terminus) (PubMed:26951377). Interacts with NUPR1; CC this interaction enhances the effect of EP300 on PAX2 transcription CC factor activity (PubMed:11940591). Interacts with RXRA; the interaction CC is decreased by 9-cis retinoic acid (PubMed:17761950). NR4A1 competes CC with EP300 for interaction with RXRA and thereby attenuates EP300 CC mediated acetylation of RXRA (PubMed:17761950). Interacts with RB1 (By CC similarity). Interacts with DDX3X; this interaction may facilitate CC HNF4A acetylation (PubMed:28128295). Interacts with SOX9 CC (PubMed:12732631). Interacts with ATF4; EP300/p300 stabilizes ATF4 and CC increases its transcriptional activity independently of its catalytic CC activity by preventing its ubiquitination (PubMed:16219772). Interacts CC with KAT5; promoting KAT5 autoacetylation (PubMed:24835996). Interacts CC (via bromo domain) with (acetylated) STAT3; interaction takes place CC following STAT3 acetylation by EP300 and promotes enhanceosome assembly CC (PubMed:18782771). {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:16219772, ECO:0000269|PubMed:16478997, CC ECO:0000269|PubMed:16574662, ECO:0000269|PubMed:16617102, CC ECO:0000269|PubMed:16809611, ECO:0000269|PubMed:16864582, CC ECO:0000269|PubMed:17226766, ECO:0000269|PubMed:17761950, CC ECO:0000269|PubMed:17872950, ECO:0000269|PubMed:18451878, CC ECO:0000269|PubMed:18782771, 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=6; 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, ECO:0000269|PubMed:25593309}. Chromosome CC {ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:25818647}. CC Note=Localizes to active chromatin: Colocalizes with histone H3 CC acetylated and/or crotonylated at 'Lys-18' (H3K18ac and H3K18cr, CC respectively) (PubMed:25818647). In the presence of ALX1 relocalizes CC from the cytoplasm to the nucleus. Colocalizes with ROCK2 in the CC nucleus (PubMed:12929931). Localizes to sites of DNA damage CC (PubMed:25593309). {ECO:0000269|PubMed:12929931, CC ECO:0000269|PubMed:25593309, 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 contains 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="https://atlasgeneticsoncology.org/gene/97/ep300"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=P300/CBP entry; CC URL="https://en.wikipedia.org/wiki/P300/CBP"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7QGS; X-ray; 2.00 A; A=330-420. DR PDB; 7SS8; X-ray; 2.15 A; A=1048-1519, A=1582-1664. DR PDB; 7SSK; X-ray; 2.36 A; A=1048-1519, A=1582-1664. DR PDB; 7SZQ; X-ray; 2.80 A; A=1279-1666. DR PDB; 7UGI; X-ray; 2.00 A; A/B=1048-1161. DR PDB; 7VHY; X-ray; 2.30 A; A/B=1159-1519, A/B=1581-1666. DR PDB; 7VHZ; X-ray; 2.00 A; A/B=1159-1519, A/B=1581-1666. DR PDB; 7VI0; X-ray; 2.10 A; A/B=1159-1519, A/B=1581-1666. DR PDB; 7W9V; EM; 3.95 A; K=1035-1519, K=1581-1720. DR PDB; 7XEZ; NMR; -; A=1723-1812. DR PDB; 7XFG; NMR; -; A=1723-1812. DR PDB; 8E1D; NMR; -; A=1723-1812. DR PDB; 8GZC; X-ray; 2.00 A; A/B=1159-1519, A/B=1581-1666. DR PDB; 8HAG; EM; 3.20 A; K=1048-1836. DR PDB; 8HAH; EM; 3.90 A; K=1048-1836. DR PDB; 8HAI; EM; 4.70 A; K=1048-1836. DR PDB; 8HAJ; EM; 4.80 A; K=1048-1836. DR PDB; 8HAK; EM; 4.50 A; N=1048-1836. 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 PDBsum; 7QGS; -. DR PDBsum; 7SS8; -. DR PDBsum; 7SSK; -. DR PDBsum; 7SZQ; -. DR PDBsum; 7UGI; -. DR PDBsum; 7VHY; -. DR PDBsum; 7VHZ; -. DR PDBsum; 7VI0; -. DR PDBsum; 7W9V; -. DR PDBsum; 7XEZ; -. DR PDBsum; 7XFG; -. DR PDBsum; 8E1D; -. DR PDBsum; 8GZC; -. DR PDBsum; 8HAG; -. DR PDBsum; 8HAH; -. DR PDBsum; 8HAI; -. DR PDBsum; 8HAJ; -. DR PDBsum; 8HAK; -. DR AlphaFoldDB; Q09472; -. DR BMRB; Q09472; -. DR EMDB; EMD-32373; -. DR EMDB; EMD-34588; -. DR EMDB; EMD-34589; -. DR EMDB; EMD-34591; -. DR EMDB; EMD-34592; -. DR EMDB; EMD-34594; -. DR EMDB; EMD-6261; -. DR EMDB; EMD-6262; -. DR EMDB; EMD-6263; -. DR EMDB; EMD-6791; -. DR EMDB; EMD-6792; -. DR SMR; Q09472; -. DR BioGRID; 108347; 1371. DR CORUM; Q09472; -. DR DIP; DIP-257N; -. DR IntAct; Q09472; 249. DR MINT; Q09472; -. DR STRING; 9606.ENSP00000263253; -. DR BindingDB; Q09472; -. DR ChEMBL; CHEMBL3784; -. DR GuidetoPHARMACOLOGY; 2735; -. DR MoonDB; Q09472; Predicted. DR GlyCosmos; Q09472; 3 sites, 1 glycan. DR GlyGen; Q09472; 4 sites, 1 O-linked glycan (4 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; 9606-ENSP00000263253; -. DR PeptideAtlas; Q09472; -. DR ProteomicsDB; 58723; -. DR Pumba; Q09472; -. DR ABCD; Q09472; 1 sequenced antibody. DR Antibodypedia; 296; 1177 antibodies from 40 providers. DR DNASU; 2033; -. DR Ensembl; ENST00000263253.9; ENSP00000263253.7; ENSG00000100393.15. 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 AGR; HGNC:3373; -. 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; NMNASPM; -. DR OrthoDB; 5490807at2759; -. 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-2173796; SMAD2/SMAD3:SMAD4 heterotrimer 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-9735871; SARS-CoV-1 targets host intracellular signalling and regulatory pathways. DR Reactome; R-HSA-9759194; Nuclear events mediated by NFE2L2. DR Reactome; R-HSA-9793380; Formation of paraxial mesoderm. DR Reactome; R-HSA-9818026; NFE2L2 regulating inflammation associated genes. DR Reactome; R-HSA-9818027; NFE2L2 regulating anti-oxidant/detoxification enzymes. DR Reactome; R-HSA-9818028; NFE2L2 regulates pentose phosphate pathway genes. DR Reactome; R-HSA-9818030; NFE2L2 regulating tumorigenic genes. DR Reactome; R-HSA-9818032; NFE2L2 regulating MDR associated enzymes. DR Reactome; R-HSA-9818035; NFE2L2 regulating ER-stress associated genes. DR Reactome; R-HSA-9818749; Regulation of NFE2L2 gene expression. DR Reactome; R-HSA-9819196; Zygotic genome activation (ZGA). DR SABIO-RK; Q09472; -. DR SignaLink; Q09472; -. DR SIGNOR; Q09472; -. DR BioGRID-ORCS; 2033; 223 hits in 1220 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 212 other cell types or tissues. DR ExpressionAtlas; Q09472; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:UniProt. DR GO; GO:0005737; C:cytoplasm; IDA:UniProt. 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:0140033; F:acetylation-dependent protein binding; IDA:UniProtKB. 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: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:0044013; F:histone H2B acetyltransferase activity; IDA:GO_Central. DR GO; GO:0010484; F:histone H3 acetyltransferase activity; IDA:GO_Central. DR GO; GO:0140908; F:histone H3K122 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0043993; F:histone H3K18 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0044017; F:histone H3K27 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0010485; F:histone H4 acetyltransferase activity; IDA:GO_Central. 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: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:0007249; P:canonical NF-kappaB signal transduction; IDA:ARUK-UCL. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0071233; P:cellular response to leucine; IDA:UniProtKB. DR GO; GO:0031669; P:cellular response to nutrient levels; IDA:UniProt. DR GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB. DR GO; GO:0007623; P:circadian rhythm; ISS: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: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:0010507; P:negative regulation of autophagy; IDA:UniProt. 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:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:ARUK-UCL. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:UniProt. DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IDA:UniProt. DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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:0045815; P:transcription initiation-coupled chromatin remodeling; IDA:UniProtKB. DR CDD; cd05495; Bromo_cbp_like; 1. DR CDD; cd20910; NCBD_CREBBP-p300_like; 1. DR CDD; cd15646; PHD_p300; 1. DR CDD; cd15802; RING_CBP-p300; 1. DR CDD; cd02337; ZZ_CBP; 1. DR DisProt; DP00633; -. DR Gene3D; 2.10.110.40; -; 1. DR Gene3D; 3.30.60.90; -; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 1. DR Gene3D; 1.10.246.20; Coactivator CBP, KIX domain; 1. DR Gene3D; 1.10.1630.10; Nuclear receptor coactivator, CREB-bp-like, interlocking domain; 1. DR Gene3D; 1.20.1020.10; TAZ domain; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; CBP/P300-RELATED; 1. DR PANTHER; PTHR13808:SF29; HISTONE ACETYLTRANSFERASE P300; 1. DR Pfam; PF00439; Bromodomain; 1. DR Pfam; PF09030; Creb_binding; 1. DR Pfam; PF08214; HAT_KAT11; 1. DR Pfam; PF02172; KIX; 1. DR Pfam; PF06001; RING_CBP-p300; 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; SSF47370; Bromodomain; 1. DR SUPFAM; SSF47040; Kix domain of CBP (creb binding protein); 1. DR SUPFAM; SSF69125; Nuclear receptor coactivator interlocking domain; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR SUPFAM; SSF57933; TAZ domain; 2. 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. DR Genevisible; Q09472; HS. 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; uncertain significance; 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 FT R-1397." FT /evidence="ECO:0000269|PubMed:18273021" FT MUTAGEN 1396 FT /note="S->W: Loss of activity; when associated with FT W-1396." FT /evidence="ECO:0000269|PubMed:18273021" FT MUTAGEN 1397 FT /note="Y->R: Loss of activity; when associated with FT R-1396." FT /evidence="ECO:0000269|PubMed:18273021" FT MUTAGEN 1397 FT /note="Y->W: Loss of activity; when associated with FT W-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 FT FOXO1-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 FT R-1505 and R-1628. 90% decrease in activity; when FT associated 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 FT E-1505 and R-1625. 90% decrease in activity; when FT associated 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..357 FT /evidence="ECO:0007829|PDB:7QGS" FT HELIX 369..381 FT /evidence="ECO:0007829|PDB:7QGS" FT HELIX 385..387 FT /evidence="ECO:0007829|PDB:7QGS" FT HELIX 393..405 FT /evidence="ECO:0007829|PDB:7QGS" FT STRAND 408..410 FT /evidence="ECO:0007829|PDB:1P4Q" FT TURN 412..414 FT /evidence="ECO:0007829|PDB:7QGS" FT HELIX 415..418 FT /evidence="ECO:0007829|PDB:7QGS" 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 1178..1180 FT /evidence="ECO:0007829|PDB:7VHZ" FT STRAND 1181..1185 FT /evidence="ECO:0007829|PDB:6GYR" FT STRAND 1190..1194 FT /evidence="ECO:0007829|PDB:7VHZ" FT TURN 1195..1197 FT /evidence="ECO:0007829|PDB:7VHZ" FT STRAND 1198..1201 FT /evidence="ECO:0007829|PDB:7VHZ" FT HELIX 1202..1206 FT /evidence="ECO:0007829|PDB:7VHZ" FT STRAND 1208..1215 FT /evidence="ECO:0007829|PDB:7VHZ" FT STRAND 1218..1221 FT /evidence="ECO:0007829|PDB:4BHW" FT STRAND 1224..1227 FT /evidence="ECO:0007829|PDB:7VHZ" FT HELIX 1228..1230 FT /evidence="ECO:0007829|PDB:7VHZ" FT STRAND 1231..1236 FT /evidence="ECO:0007829|PDB:7VHZ" FT STRAND 1244..1246 FT /evidence="ECO:0007829|PDB:7VHZ" FT TURN 1248..1250 FT /evidence="ECO:0007829|PDB:7VHZ" FT STRAND 1253..1255 FT /evidence="ECO:0007829|PDB:7VHZ" FT HELIX 1256..1259 FT /evidence="ECO:0007829|PDB:7VHZ" FT TURN 1263..1265 FT /evidence="ECO:0007829|PDB:7VHZ" FT HELIX 1273..1277 FT /evidence="ECO:0007829|PDB:7VHZ" FT TURN 1278..1280 FT /evidence="ECO:0007829|PDB:7VHZ" 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 1442..1444 FT /evidence="ECO:0007829|PDB:7VHZ" 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 //