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Histone acetyltransferase p300 (p300 HAT) (EC 2.3.1.48) (E1A-associated protein p300)

 EP300_HUMAN             Reviewed;        2414 AA.
Q09472; B1AKC2;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 2.
30-AUG-2017, entry version 222.
RecName: Full=Histone acetyltransferase p300;
Short=p300 HAT;
EC=2.3.1.48 {ECO:0000269|PubMed:23415232, ECO:0000269|PubMed:23934153, ECO:0000269|PubMed:8945521};
AltName: Full=E1A-associated protein p300;
Name=EP300; Synonyms=P300;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-2223.
PubMed=7523245; DOI=10.1101/gad.8.8.869;
Eckner R., Ewen M.E., Newsome D., Gerdes M., Decaprio J.A.,
Lawrence J.B., Livingston D.M.;
"Molecular cloning and functional analysis of the adenovirus E1A-
associated 300-kD protein (p300) reveals a protein with properties of
a transcriptional adaptor.";
Genes Dev. 8:869-884(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 27-42, AND CHROMOSOMAL TRANSLOCATION
WITH KAT6A.
PubMed=10824998;
DOI=10.1002/(SICI)1098-2264(200006)28:2<138::AID-GCC2>3.0.CO;2-2;
Chaffanet M., Gressin L., Preudhomme C., Soenen-Cornu V., Birnbaum D.,
Pebusque M.-J.;
"MOZ is fused to p300 in an acute monocytic leukemia with t(8;22).";
Genes Chromosomes Cancer 28:138-144(2000).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 552-660.
PubMed=7870179; DOI=10.1038/374085a0;
Lundblad J.R., Kwok R.P.S., Laurance M.E., Harter M.L., Goodman R.H.;
"Adenoviral E1A-associated protein p300 as a functional homologue of
the transcriptional co-activator CBP.";
Nature 374:85-88(1995).
[6]
PARTIAL PROTEIN SEQUENCE, INTERACTION WITH CARM1, METHYLATION AT
ARG-580 AND ARG-604, AND FUNCTION.
PubMed=11701890; DOI=10.1126/science.1065961;
Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M.,
Evans R.M.;
"A transcriptional switch mediated by cofactor methylation.";
Science 294:2507-2511(2001).
[7]
CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=8945521; DOI=10.1016/S0092-8674(00)82001-2;
Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., Nakatani Y.;
"The transcriptional coactivators p300 and CBP are histone
acetyltransferases.";
Cell 87:953-959(1996).
[8]
INTERACTION WITH PCAF.
PubMed=8684459; DOI=10.1038/382319a0;
Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y.;
"A p300/CBP-associated factor that competes with the adenoviral
oncoprotein E1A.";
Nature 382:319-324(1996).
[9]
INTERACTION WITH HIF1A AND CREBBP.
PubMed=8917528; DOI=10.1073/pnas.93.23.12969;
Arany Z., Huang L.E., Eckner R., Bhattacharya S., Jiang C.,
Goldberg M.A., Bunn H.F., Livingston D.M.;
"An essential role for p300/CBP in the cellular response to hypoxia.";
Proc. Natl. Acad. Sci. U.S.A. 93:12969-12973(1996).
[10]
INTERACTION WITH HTLV-1 TAX.
PubMed=9528808; DOI=10.1128/MCB.18.4.2392;
Bex F., Yin M.-J., Burny A., Gaynor R.B.;
"Differential transcriptional activation by human T-cell leukemia
virus type 1 Tax mutants is mediated by distinct interactions with
CREB binding protein and p300.";
Mol. Cell. Biol. 18:2392-2405(1998).
[11]
INTERACTION WITH NR3C1.
PubMed=9590696; DOI=10.1038/30032;
Fryer C.J., Archer T.K.;
"Chromatin remodelling by the glucocorticoid receptor requires the
BRG1 complex.";
Nature 393:88-91(1998).
[12]
INTERACTION WITH HIV-1 TAT.
PubMed=10545121; DOI=10.1093/emboj/18.21.6106;
Kiernan R.E., Vanhulle C., Schiltz L., Adam E., Xiao H., Maudoux F.,
Calomme C., Burny A., Nakatani Y., Jeang K.-T., Benkirane M.,
Van Lint C.;
"HIV-1 tat transcriptional activity is regulated by acetylation.";
EMBO J. 18:6106-6118(1999).
[13]
INTERACTION WITH CITED2 AND HIF1A, AND MUTAGENESIS OF 371-THR--LEU-376
AND 413-VAL--LYS-418.
PubMed=9887100; DOI=10.1101/gad.13.1.64;
Bhattacharya S., Michels C.M., Leung M.K., Arany Z.P., Kung A.L.,
Livingston D.M.;
"Functional role of p35srj, a novel p300/CBP binding protein, during
transactivation by HIF-1.";
Genes Dev. 13:64-75(1999).
[14]
INTERACTION WITH RORA.
PubMed=9862959; DOI=10.1093/nar/27.2.411;
Lau P., Bailey P., Dowhan D.H., Muscat G.E.;
"Exogenous expression of a dominant negative RORalpha1 vector in
muscle cells impairs differentiation: RORalpha1 directly interacts
with p300 and myoD.";
Nucleic Acids Res. 27:411-420(1999).
[15]
INTERACTION WITH CITED1.
PubMed=10722728; DOI=10.1074/jbc.275.12.8825;
Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S.,
Roberts A.B., Isselbacher K.J., Shioda T.;
"The MSG1 non-DNA-binding transactivator binds to the p300/CBP
coactivators, enhancing their functional link to the Smad
transcription factors.";
J. Biol. Chem. 275:8825-8834(2000).
[16]
FUNCTION IN TRANSCRIPTIONAL REPRESSION.
PubMed=10733570; DOI=10.1128/MCB.20.8.2676-2686.2000;
Snowden A.W., Anderson L.A., Webster G.A., Perkins N.D.;
"A novel transcriptional repression domain mediates p21(WAF1/CIP1)
induction of p300 transactivation.";
Mol. Cell. Biol. 20:2676-2686(2000).
[17]
ERRATUM.
Snowden A.W., Anderson L.A., Webster G.A., Perkins N.D.;
Mol. Cell. Biol. 20:5360-5360(2000).
[18]
INTERACTION WITH EID1.
PubMed=11073989; DOI=10.1128/MCB.20.23.8889-8902.2000;
Miyake S., Sellers W.R., Safran M., Li X., Zhao W., Grossman S.R.,
Gan J., DeCaprio J.A., Adams P.D., Kaelin W.G. Jr.;
"Cells degrade a novel inhibitor of differentiation with E1A-like
properties upon exiting the cell cycle.";
Mol. Cell. Biol. 20:8889-8902(2000).
[19]
INTERACTION WITH EID1.
PubMed=11073990; DOI=10.1128/MCB.20.23.8903-8915.2000;
MacLellan W.R., Xiao G., Abdellatif M., Schneider M.D.;
"A novel Rb- and p300-binding protein inhibits transactivation by
MyoD.";
Mol. Cell. Biol. 20:8903-8915(2000).
[20]
INTERACTION WITH NCOA6.
PubMed=10823961; DOI=10.1073/pnas.97.11.6212;
Ko L., Cardona G.R., Chin W.W.;
"Thyroid hormone receptor-binding protein, an LXXLL motif-containing
protein, functions as a general coactivator.";
Proc. Natl. Acad. Sci. U.S.A. 97:6212-6217(2000).
[21]
INTERACTION WITH HIV-1 TAT.
PubMed=11080476; DOI=10.1006/viro.2000.0593;
Deng L., de la Fuente C., Fu P., Wang L., Donnelly R., Wade J.D.,
Lambert P., Li H., Lee C.-G., Kashanchi F.;
"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of
integrated HIV-1 genome and enhances binding to core histones.";
Virology 277:278-295(2000).
[22]
INTERACTION WITH ESR1.
PubMed=11581164; DOI=10.1101/gad.906301;
Yahata T., Shao W., Endoh H., Hur J., Coser K.R., Sun H., Ueda Y.,
Kato S., Isselbacher K.J., Brown M., Shioda T.;
"Selective coactivation of estrogen-dependent transcription by CITED1
CBP/p300-binding protein.";
Genes Dev. 15:2598-2612(2001).
[23]
PHOSPHORYLATION AT SER-89, MUTAGENESIS OF SER-89, AND INTERACTION WITH
PPARG.
PubMed=11518699; DOI=10.1074/jbc.C100316200;
Yang W., Hong Y.H., Shen X.Q., Frankowski C., Camp H.S., Leff T.;
"Regulation of transcription by AMP-activated protein kinase:
phosphorylation of p300 blocks its interaction with nuclear
receptors.";
J. Biol. Chem. 276:38341-38344(2001).
[24]
INTERACTION WITH SRCAP.
PubMed=11581372; DOI=10.1128/JVI.75.21.10033-10040.2001;
Xu X., Chackalaparampil I., Monroy M.A., Cannella M.T., Pesek E.,
Chrivia J., Yaciuk P.;
"Adenovirus DNA binding protein interacts with the SNF2-related CBP
activator protein (SrCap) and inhibits SrCap-mediated transcription.";
J. Virol. 75:10033-10040(2001).
[25]
INTERACTION WITH HTLV-1 TAX.
PubMed=11463834; DOI=10.1128/MCB.21.16.5520-5530.2001;
Scoggin K.E.S., Ulloa A., Nyborg J.K.;
"The oncoprotein Tax binds the SRC-1-interacting domain of CBP/p300 to
mediate transcriptional activation.";
Mol. Cell. Biol. 21:5520-5530(2001).
[26]
INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P30II.
PubMed=11559821; DOI=10.1128/JVI.75.20.9885-9895.2001;
Zhang W., Nisbet J.W., Albrecht B., Ding W., Kashanchi F.,
Bartoe J.T., Lairmore M.D.;
"Human T-lymphotropic virus type 1 p30(II) regulates gene
transcription by binding CREB binding protein/p300.";
J. Virol. 75:9885-9895(2001).
[27]
INTERACTION WITH TRERF1.
PubMed=11349124; DOI=10.1074/jbc.M100113200;
Gizard F., Lavallee B., DeWitte F., Hum D.W.;
"A novel zinc finger protein TReP-132 interacts with CBP/p300 to
regulate human CYP11A1 gene expression.";
J. Biol. Chem. 276:33881-33892(2001).
[28]
INTERACTION WITH PELP1.
PubMed=11481323; DOI=10.1074/jbc.M103783200;
Vadlamudi R.K., Wang R.-A., Mazumdar A., Kim Y.-S., Shin J., Sahin A.,
Kumar R.;
"Molecular cloning and characterization of PELP1, a novel human
coregulator of estrogen receptor alpha.";
J. Biol. Chem. 276:38272-38279(2001).
[29]
INTERACTION WITH DTX1.
PubMed=11564735; DOI=10.1074/jbc.M105245200;
Yamamoto N., Yamamoto S., Inagaki F., Kawaichi M., Fukamizu A.,
Kishi N., Matsuno K., Nakamura K., Weinmaster G., Okano H.,
Nakafuku M.;
"Role of Deltex-1 as a transcriptional regulator downstream of the
Notch receptor.";
J. Biol. Chem. 276:45031-45040(2001).
[30]
FUNCTION, AND INTERACTION WITH FEN1.
PubMed=11430825; DOI=10.1016/S1097-2765(01)00272-6;
Hasan S., Stucki M., Hassa P.O., Imhof R., Gehrig P., Hunziker P.,
Hubscher U., Hottiger M.O.;
"Regulation of human flap endonuclease-1 activity by acetylation
through the transcriptional coactivator p300.";
Mol. Cell 7:1221-1231(2001).
[31]
INTERACTION WITH HADV5 E1A.
PubMed=11433299; DOI=10.1038/35083062;
Chan H.M., Krstic-Demonacos M., Smith L., Demonacos C.,
La Thangue N.B.;
"Acetylation control of the retinoblastoma tumour-suppressor
protein.";
Nat. Cell Biol. 3:667-674(2001).
[32]
INTERACTION WITH SPIB.
PubMed=11864910;
Yamamoto H., Kihara-Negishi F., Yamada T., Suzuki M., Nakano T.,
Oikawa T.;
"Interaction between the hematopoietic Ets transcription factor Spi-B
and the coactivator CREB-binding protein associated with negative
cross-talk with c-Myb.";
Cell Growth Differ. 13:69-75(2002).
[33]
INTERACTION WITH CITED4.
PubMed=11744733; DOI=10.1074/jbc.M110850200;
Braganca J., Swingler T., Marques F.I.R., Jones T., Eloranta J.J.,
Hurst H.C., Shioda T., Bhattacharya S.;
"Human CREB-binding protein/p300-interacting transactivator with ED-
rich tail (CITED) 4, a new member of the CITED family, functions as a
co-activator for transcription factor AP-2.";
J. Biol. Chem. 277:8559-8565(2002).
[34]
IDENTIFICATION IN A COMPLEX WITH CARM1 AND NCOA2.
PubMed=11997499; DOI=10.1128/MCB.22.11.3621-3632.2002;
Lee Y.-H., Koh S.S., Zhang X., Cheng X., Stallcup M.R.;
"Synergy among nuclear receptor coactivators: selective requirement
for protein methyltransferase and acetyltransferase activities.";
Mol. Cell. Biol. 22:3621-3632(2002).
[35]
FUNCTION IN BCL6 ACETYLATION.
PubMed=12402037; DOI=10.1038/ng1018;
Bereshchenko O.R., Gu W., Dalla-Favera R.;
"Acetylation inactivates the transcriptional repressor BCL6.";
Nat. Genet. 32:606-613(2002).
[36]
INTERACTION WITH ING4 AND ING5.
PubMed=12750254;
Shiseki M., Nagashima M., Pedeux R.M., Kitahama-Shiseki M., Miura K.,
Okamura S., Onogi H., Higashimoto Y., Appella E., Yokota J.,
Harris C.C.;
"p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity.";
Cancer Res. 63:2373-2378(2003).
[37]
PHOSPHORYLATION, AND INTERACTION WITH TCF7L2 AND LEF1.
PubMed=12446687; DOI=10.1074/jbc.M210081200;
Hecht A., Stemmler M.P.;
"Identification of a promoter-specific transcriptional activation
domain at the C-terminus of the Wnt effector protein T-cell factor
4.";
J. Biol. Chem. 278:3776-3785(2003).
[38]
FUNCTION, INTERACTION WITH CITED2 AND TFAP2A, AND MUTAGENESIS OF
ASP-1399.
PubMed=12586840; DOI=10.1074/jbc.M208144200;
Braganca J., Eloranta J.J., Bamforth S.D., Ibbitt J.C., Hurst H.C.,
Bhattacharya S.;
"Physical and functional interactions among AP-2 transcription
factors, p300/CREB-binding protein, and CITED2.";
J. Biol. Chem. 278:16021-16029(2003).
[39]
INTERACTION WITH SP3.
PubMed=12837748; DOI=10.1074/jbc.M305961200;
Ammanamanchi S., Freeman J.W., Brattain M.G.;
"Acetylated SP3 is a transcriptional activator.";
J. Biol. Chem. 278:35775-35780(2003).
[40]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ALX1, AND REGION.
PubMed=12929931; DOI=10.1359/jbmr.2003.18.8.1419;
Iioka T., Furukawa K., Yamaguchi A., Shindo H., Yamashita S.,
Tsukazaki T.;
"P300/CBP acts as a coactivator to cartilage homeoprotein-1 (Cart1),
paired-like homeoprotein, through acetylation of the conserved lysine
residue adjacent to the homeodomain.";
J. Bone Miner. Res. 18:1419-1429(2003).
[41]
INTERACTION WITH SATB1.
PubMed=14605447; DOI=10.1111/j.1348-0421.2003.tb03438.x;
Fujii Y., Kumatori A., Nakamura M.;
"SATB1 makes a complex with p300 and represses gp91(phox) promoter
activity.";
Microbiol. Immunol. 47:803-811(2003).
[42]
SUMOYLATION AT LYS-1020 AND LYS-1024, AND MUTAGENESIS OF LYS-1020 AND
LYS-1024.
PubMed=12718889; DOI=10.1016/S1097-2765(03)00141-2;
Girdwood D., Bumpass D., Vaughan O.A., Thain A., Anderson L.A.,
Snowden A.W., Garcia-Wilson E., Perkins N.D., Hay R.T.;
"P300 transcriptional repression is mediated by SUMO modification.";
Mol. Cell 11:1043-1054(2003).
[43]
INTERACTION WITH DDX5.
PubMed=12527917; DOI=10.1038/sj.onc.1206067;
Rossow K.L., Janknecht R.;
"Synergism between p68 RNA helicase and the transcriptional
coactivators CBP and p300.";
Oncogene 22:151-156(2003).
[44]
INTERACTION WITH TP53, AND FUNCTION.
PubMed=15186775; DOI=10.1016/j.cell.2004.05.009;
An W., Kim J., Roeder R.G.;
"Ordered cooperative functions of PRMT1, p300, and CARM1 in
transcriptional activation by p53.";
Cell 117:735-748(2004).
[45]
INTERACTION WITH SRY.
PubMed=15297880; DOI=10.1038/sj.emboj.7600352;
Thevenet L., Mejean C., Moniot B., Bonneaud N., Galeotti N.,
Aldrian-Herrada G., Poulat F., Berta P., Benkirane M.,
Boizet-Bonhoure B.;
"Regulation of human SRY subcellular distribution by its
acetylation/deacetylation.";
EMBO J. 23:3336-3345(2004).
[46]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NPAS2;
ARNTL/BMAL1 AND CLOCK.
PubMed=14645221; DOI=10.1074/jbc.M311973200;
Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M.,
Chakravarti D., FitzGerald G.A., McNamara P.;
"Histone acetyltransferase-dependent chromatin remodeling and the
vascular clock.";
J. Biol. Chem. 279:7091-7097(2004).
[47]
INTERACTION WITH ELF3.
PubMed=15075319; DOI=10.1074/jbc.M401356200;
Wang H., Fang R., Cho J.-Y., Libermann T.A., Oettgen P.;
"Positive and negative modulation of the transcriptional activity of
the ETS factor ESE-1 through interaction with p300, CREB-binding
protein, and Ku 70/86.";
J. Biol. Chem. 279:25241-25250(2004).
[48]
INTERACTION WITH IRF1.
PubMed=15509808; DOI=10.1128/MCB.24.22.10083-10098.2004;
Dornan D., Eckert M., Wallace M., Shimizu H., Ramsay E., Hupp T.R.,
Ball K.L.;
"Interferon regulatory factor 1 binding to p300 stimulates DNA-
dependent acetylation of p53.";
Mol. Cell. Biol. 24:10083-10098(2004).
[49]
ACETYLATION AT LYS-1499; LYS-1549; LYS-1554; LYS-1558 AND LYS-1560.
PubMed=15004546; DOI=10.1038/nsmb740;
Thompson P.R., Wang D., Wang L., Fulco M., Pediconi N., Zhang D.,
An W., Ge Q., Roeder R.G., Wong J., Levrero M., Sartorelli V.,
Cotter R.J., Cole P.A.;
"Regulation of the p300 HAT domain via a novel activation loop.";
Nat. Struct. Mol. Biol. 11:308-315(2004).
[50]
INTERACTION WITH NEUROD1 AND TCF3.
PubMed=14752053; DOI=10.1210/me.2003-0311;
Kim J.Y., Chu K., Kim H.J., Seong H.A., Park K.C., Sanyal S.,
Takeda J., Ha H., Shong M., Tsai M.J., Choi H.S.;
"Orphan nuclear receptor small heterodimer partner, a novel
corepressor for a basic helix-loop-helix transcription factor
BETA2/neuroD.";
Mol. Endocrinol. 18:776-790(2004).
[51]
INTERACTION WITH SS18L1/CREST.
PubMed=14716005; DOI=10.1126/science.1089845;
Aizawa H., Hu S.-C., Bobb K., Balakrishnan K., Ince G., Gurevich I.,
Cowan M., Ghosh A.;
"Dendrite development regulated by CREST, a calcium-regulated
transcriptional activator.";
Science 303:197-202(2004).
[52]
INVOLVEMENT IN RSTS2.
PubMed=15706485; DOI=10.1086/429130;
Roelfsema J.H., White S.J., Ariyuerek Y., Bartholdi D., Niedrist D.,
Papadia F., Bacino C.A., den Dunnen J.T., van Ommen G.-J.B.,
Breuning M.H., Hennekam R.C., Peters D.J.M.;
"Genetic heterogeneity in Rubinstein-Taybi syndrome: mutations in both
the CBP and EP300 genes cause disease.";
Am. J. Hum. Genet. 76:572-580(2005).
[53]
DEACETYLATION BY SIRT1, ACETYLATION AT LYS-1020 AND LYS-1024, AND
MUTAGENESIS OF LYS-1020 AND LYS-1024.
PubMed=15632193; DOI=10.1074/jbc.M408748200;
Bouras T., Fu M., Sauve A.A., Wang F., Quong A.A., Perkins N.D.,
Hay R.T., Gu W., Pestell R.G.;
"SIRT1 deacetylation and repression of p300 involves lysine residues
1020/1024 within the cell cycle regulatory domain 1.";
J. Biol. Chem. 280:10264-10276(2005).
[54]
INTERACTION WITH FOXO1, FUNCTION, AND MUTAGENESIS OF ASP-1399.
PubMed=15890677; DOI=10.1210/me.2004-0292;
Perrot V., Rechler M.M.;
"The coactivator p300 directly acetylates the forkhead transcription
factor Foxo1 and stimulates Foxo1-induced transcription.";
Mol. Endocrinol. 19:2283-2298(2005).
[55]
METHYLATION AT ARG-2142, CITRULLINATION AT ARG-2142, INTERACTION WITH
NCOA2, AND MUTAGENESIS OF ARG-2056; ARG-2088 AND ARG-2142.
PubMed=15731352; DOI=10.1073/pnas.0407159102;
Lee Y.-H., Coonrod S.A., Kraus W.L., Jelinek M.A., Stallcup M.R.;
"Regulation of coactivator complex assembly and function by protein
arginine methylation and demethylimination.";
Proc. Natl. Acad. Sci. U.S.A. 102:3611-3616(2005).
[56]
SUBCELLULAR LOCATION, INTERACTION WITH ROCK2, AND PHOSPHORYLATION AT
SER-89.
PubMed=16574662; DOI=10.1074/jbc.M510954200;
Tanaka T., Nishimura D., Wu R.C., Amano M., Iso T., Kedes L.,
Nishida H., Kaibuchi K., Hamamori Y.;
"Nuclear Rho kinase, ROCK2, targets p300 acetyltransferase.";
J. Biol. Chem. 281:15320-15329(2006).
[57]
INTERACTION WITH CITED1.
PubMed=16864582; DOI=10.1074/jbc.M602631200;
Shi G., Boyle S.C., Sparrow D.B., Dunwoodie S.L., Shioda T.,
de Caestecker M.P.;
"The transcriptional activity of CITED1 is regulated by
phosphorylation in a cell cycle-dependent manner.";
J. Biol. Chem. 281:27426-27435(2006).
[58]
ACETYLATION AT LYS-1336 AND LYS-1473, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=17065153; DOI=10.1074/jbc.M608813200;
Karanam B., Jiang L., Wang L., Kelleher N.L., Cole P.A.;
"Kinetic and mass spectrometric analysis of p300 histone
acetyltransferase domain autoacetylation.";
J. Biol. Chem. 281:40292-40301(2006).
[59]
FUNCTION IN ACETYLATION OF HDAC1.
PubMed=16762839; DOI=10.1016/j.molcel.2006.04.019;
Qiu Y., Zhao Y., Becker M., John S., Parekh B.S., Huang S.,
Hendarwanto A., Martinez E.D., Chen Y., Lu H., Adkins N.L.,
Stavreva D.A., Wiench M., Georgel P.T., Schiltz R.L., Hager G.L.;
"HDAC1 acetylation is linked to progressive modulation of steroid
receptor-induced gene transcription.";
Mol. Cell 22:669-679(2006).
[60]
INTERACTION WITH SP1.
PubMed=16478997; DOI=10.1128/MCB.26.5.1770-1785.2006;
Hung J.J., Wang Y.T., Chang W.C.;
"Sp1 deacetylation induced by phorbol ester recruits p300 to activate
12(S)-lipoxygenase gene transcription.";
Mol. Cell. Biol. 26:1770-1785(2006).
[61]
FUNCTION, AND INTERACTION WITH MTA1.
PubMed=16617102; DOI=10.1073/pnas.0601989103;
Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P.,
Zhang H., Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
"MTA1, a transcriptional activator of breast cancer amplified sequence
3.";
Proc. Natl. Acad. Sci. U.S.A. 103:6670-6675(2006).
[62]
ERRATUM.
Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P.,
Zhang H., Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
Proc. Natl. Acad. Sci. U.S.A. 110:4147-4148(2013).
[63]
INTERACTION WITH DDIT3.
PubMed=17872950; DOI=10.1074/jbc.M703735200;
Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H.;
"Critical and functional regulation of CHOP (C/EBP homologous protein)
through the N-terminal portion.";
J. Biol. Chem. 282:35687-35694(2007).
[64]
INTERACTION WITH DDX17.
PubMed=17226766; DOI=10.1002/jcb.21250;
Shin S., Janknecht R.;
"Concerted activation of the Mdm2 promoter by p72 RNA helicase and the
coactivators p300 and P/CAF.";
J. Cell. Biochem. 101:1252-1265(2007).
[65]
FUNCTION IN ACETYLATION OF SIRT2.
PubMed=18722353; DOI=10.1016/j.bbrc.2008.08.042;
Han Y., Jin Y.H., Kim Y.J., Kang B.Y., Choi H.J., Kim D.W., Yeo C.Y.,
Lee K.Y.;
"Acetylation of Sirt2 by p300 attenuates its deacetylase activity.";
Biochem. Biophys. Res. Commun. 375:576-580(2008).
[66]
PHOSPHORYLATION BY HIPK2.
PubMed=18695000; DOI=10.1182/blood-2008-01-134122;
Wee H.-J., Voon D.C.-C., Bae S.-C., Ito Y.;
"PEBP2-beta/CBF-beta-dependent phosphorylation of RUNX1 and p300 by
HIPK2: implications for leukemogenesis.";
Blood 112:3777-3787(2008).
[67]
FBXO3-MEDIATED DEGRADATION.
PubMed=18809579; DOI=10.1128/MCB.00897-08;
Shima Y., Shima T., Chiba T., Irimura T., Pandolfi P.P.,
Kitabayashi I.;
"PML activates transcription by protecting HIPK2 and p300 from
SCFFbx3-mediated degradation.";
Mol. Cell. Biol. 28:7126-7138(2008).
[68]
ACETYLATION AT LYS-418; LYS-423; LYS-1542; LYS-1546; LYS-1549;
LYS-1699; LYS-1704 AND LYS-1707, DEACETYLATION BY SIRT2, AND FUNCTION
IN TRANSCRIPTIONAL REGULATION.
PubMed=18995842; DOI=10.1016/j.molcel.2008.09.018;
Black J.C., Mosley A., Kitada T., Washburn M., Carey M.;
"The SIRT2 deacetylase regulates autoacetylation of p300.";
Mol. Cell 32:449-455(2008).
[69]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[70]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[71]
INTERACTION WITH SENP3, AND SUMOYLATION.
PubMed=19680224; DOI=10.1038/emboj.2009.210;
Huang C., Han Y., Wang Y., Sun X., Yan S., Yeh E.T.H., Chen Y.,
Cang H., Li H., Shi G., Cheng J., Tang X., Yi J.;
"SENP3 is responsible for HIF-1 transactivation under mild oxidative
stress via p300 de-SUMOylation.";
EMBO J. 28:2748-2762(2009).
[72]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[73]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-636; LYS-977; LYS-1542;
LYS-1546; LYS-1554; LYS-1555; LYS-1558; LYS-1560 AND LYS-1583, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[74]
IDENTIFICATION IN COMPLEX WITH CCNT1; CDK9 AND GATA4.
PubMed=20081228; DOI=10.1074/jbc.M109.070458;
Sunagawa Y., Morimoto T., Takaya T., Kaichi S., Wada H., Kawamura T.,
Fujita M., Shimatsu A., Kita T., Hasegawa K.;
"Cyclin-dependent kinase-9 is a component of the p300/GATA4 complex
required for phenylephrine-induced hypertrophy in cardiomyocytes.";
J. Biol. Chem. 285:9556-9568(2010).
[75]
FUNCTION IN ACETYLATION OF MEF2D.
PubMed=21030595; DOI=10.1074/jbc.M110.153270;
Chini C.C., Escande C., Nin V., Chini E.N.;
"HDAC3 is negatively regulated by the nuclear protein DBC1.";
J. Biol. Chem. 285:40830-40837(2010).
[76]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[77]
FUNCTION IN ACETYLATION OF XBP1.
PubMed=20955178; DOI=10.1042/BJ20101293;
Wang F.M., Chen Y.J., Ouyang H.J.;
"Regulation of unfolded protein response modulator XBP1s by
acetylation and deacetylation.";
Biochem. J. 433:245-252(2011).
[78]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1038, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[79]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[80]
INTERACTION WITH ALKBH4.
PubMed=23145062; DOI=10.1371/journal.pone.0049045;
Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M.,
Meza-Zepeda L.A., Falnes P.O.;
"Human ALKBH4 interacts with proteins associated with transcription.";
PLoS ONE 7:E49045-E49045(2012).
[81]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=23415232; DOI=10.1016/j.cell.2013.01.032;
Tropberger P., Pott S., Keller C., Kamieniarz-Gdula K., Caron M.,
Richter F., Li G., Mittler G., Liu E.T., Buhler M., Margueron R.,
Schneider R.;
"Regulation of transcription through acetylation of H3K122 on the
lateral surface of the histone octamer.";
Cell 152:859-872(2013).
[82]
FUNCTION AS ACETYLTRANSFERASE OF H3K27.
PubMed=23911289; DOI=10.1016/j.celrep.2013.06.016;
Hatzi K., Jiang Y., Huang C., Garrett-Bakelman F., Gearhart M.D.,
Giannopoulou E.G., Zumbo P., Kirouac K., Bhaskara S., Polo J.M.,
Kormaksson M., Mackerell A.D. Jr., Xue F., Mason C.E., Hiebert S.W.,
Prive G.G., Cerchietti L., Bardwell V.J., Elemento O., Melnick A.;
"A hybrid mechanism of action for BCL6 in B cells defined by formation
of functionally distinct complexes at enhancers and promoters.";
Cell Rep. 4:578-588(2013).
[83]
INTERACTION WITH KLF15.
PubMed=23999430; DOI=10.1172/JCI68552;
Lu Y., Zhang L., Liao X., Sangwung P., Prosdocimo D.A., Zhou G.,
Votruba A.R., Brian L., Han Y.J., Gao H., Wang Y., Shimizu K.,
Weinert-Stein K., Khrestian M., Simon D.I., Freedman N.J., Jain M.K.;
"Kruppel-like factor 15 is critical for vascular inflammation.";
J. Clin. Invest. 123:4232-4241(2013).
[84]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1038 AND SER-1726, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[85]
INTERACTION WITH HDAC4 AND HDAC5.
PubMed=24413532; DOI=10.1158/0008-5472.CAN-13-2020;
Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y.,
Kim Y.N., Seong J.K., Lee M.O.;
"Differential regulation of estrogen receptor alpha expression in
breast cancer cells by metastasis-associated protein 1.";
Cancer Res. 74:1484-1494(2014).
[86]
INTERACTION WITH ZNF451, AND FUNCTION.
PubMed=24324267; DOI=10.1074/jbc.M113.526905;
Feng Y., Wu H., Xu Y., Zhang Z., Liu T., Lin X., Feng X.H.;
"Zinc finger protein 451 is a novel Smad corepressor in transforming
growth factor-beta signaling.";
J. Biol. Chem. 289:2072-2083(2014).
[87]
INTERACTION WITH ZBTB48.
PubMed=24382891; DOI=10.1074/jbc.M113.526855;
Yoon J.H., Choi W.I., Jeon B.N., Koh D.I., Kim M.K., Kim M.H., Kim J.,
Hur S.S., Kim K.S., Hur M.W.;
"Human Kruppel-related 3 (HKR3) is a novel transcription activator of
alternate reading frame (ARF) gene.";
J. Biol. Chem. 289:4018-4031(2014).
[88]
ACETYLATION, DEACETYLATION BY SIRT2, AND INTERACTION WITH EP300.
PubMed=24177535; DOI=10.1016/j.jmb.2013.10.027;
Rack J.G., Vanlinden M.R., Lutter T., Aasland R., Ziegler M.;
"Constitutive nuclear localization of an alternatively spliced
sirtuin-2 isoform.";
J. Mol. Biol. 426:1677-1691(2014).
[89]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1038, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[90]
INTERACTION WITH TRIP4.
PubMed=25219498; DOI=10.1016/j.molcel.2014.08.007;
Yoo H.M., Kang S.H., Kim J.Y., Lee J.E., Seong M.W., Lee S.W.,
Ka S.H., Sou Y.S., Komatsu M., Tanaka K., Lee S.T., Noh D.Y.,
Baek S.H., Jeon Y.J., Chung C.H.;
"Modification of ASC1 by UFM1 is crucial for ERalpha transactivation
and breast cancer development.";
Mol. Cell 56:261-274(2014).
[91]
FUNCTION AS ACETYLTRANSFERASE OF PCNA, AND INTERACTION WITH PCNA.
PubMed=24939902; DOI=10.1093/nar/gku533;
Cazzalini O., Sommatis S., Tillhon M., Dutto I., Bachi A., Rapp A.,
Nardo T., Scovassi A.I., Necchi D., Cardoso M.C., Stivala L.A.,
Prosperi E.;
"CBP and p300 acetylate PCNA to link its degradation with nucleotide
excision repair synthesis.";
Nucleic Acids Res. 42:8433-8448(2014).
[92]
INTERACTION WITH ZBTB49.
PubMed=25245946; DOI=10.1093/nar/gku857;
Jeon B.N., Kim M.K., Yoon J.H., Kim M.Y., An H., Noh H.J., Choi W.I.,
Koh D.I., Hur M.W.;
"Two ZNF509 (ZBTB49) isoforms induce cell-cycle arrest by activating
transcription of p21/CDKN1A and RB upon exposure to genotoxic
stress.";
Nucleic Acids Res. 42:11447-11461(2014).
[93]
INTERACTION WITH HSF1.
PubMed=27189267; DOI=10.1038/srep26294;
Pan X.Y., Zhao W., Zeng X.Y., Lin J., Li M.M., Shen X.T., Liu S.W.;
"Heat shock factor 1 mediates latent HIV reactivation.";
Sci. Rep. 6:26294-26294(2016).
[94]
STRUCTURE BY NMR OF 302-418 IN COMPLEX WITH HIF1A PEPTIDE AND ZINC
IONS.
PubMed=11959990; DOI=10.1073/pnas.082117899;
Freedman S.J., Sun Z.-Y.J., Poy F., Kung A.L., Livingston D.M.,
Wagner G., Eck M.J.;
"Structural basis for recruitment of CBP/p300 by hypoxia-inducible
factor-1 alpha.";
Proc. Natl. Acad. Sci. U.S.A. 99:5367-5372(2002).
[95]
STRUCTURE BY NMR OF 323-423 IN COMPLEX WITH 216-259 OF CITED2 AND ZINC
IONS, INTERACTION WITH CITED2, AND MUTAGENESIS OF LEU-344 AND LEU-345.
PubMed=12778114; DOI=10.1038/nsb936;
Freedman S.J., Sun Z.Y., Kung A.L., France D.S., Wagner G., Eck M.J.;
"Structural basis for negative regulation of hypoxia-inducible factor-
1alpha by CITED2.";
Nat. Struct. Biol. 10:504-512(2003).
[96]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1287-1666 IN COMPLEX WITH
LYS-COA, AND MUTAGENESIS OF THR-1357; SER-1396; TYR-1397; GLU-1505;
ASP-1625 AND ASP-1628.
PubMed=18273021; DOI=10.1038/nature06546;
Liu X., Wang L., Zhao K., Thompson P.R., Hwang Y., Marmorstein R.,
Cole P.A.;
"The structural basis of protein acetylation by the p300/CBP
transcriptional coactivator.";
Nature 451:846-850(2008).
[97]
STRUCTURE BY NMR OF 1723-1812, AND INTERACTION WITH TP53.
PubMed=19217391; DOI=10.1016/j.str.2008.12.009;
Feng H., Jenkins L.M.M., Durell S.R., Hayashi R., Mazur S.J.,
Cherry S., Tropea J.E., Miller M., Wlodawer A., Appella E., Bai Y.;
"Structural basis for p300 Taz2-p53 TAD1 binding and modulation by
phosphorylation.";
Structure 17:202-210(2009).
[98]
X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 1040-1161.
PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
Gingras A.C., Arrowsmith C.H., Knapp S.;
"Histone recognition and large-scale structural analysis of the human
bromodomain family.";
Cell 149:214-231(2012).
[99]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1043-1519 AND 1581-1666 OF
MUTANT PHE-1467 IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY, FUNCTION,
AUTOACETYLATION, AND MUTAGENESIS OF PHE-1170; CYS-1204; GLU-1242;
ASP-1399; TYR-1467 AND 1645-ARG-ARG-1646.
PubMed=23934153; DOI=10.1038/nsmb.2642;
Delvecchio M., Gaucher J., Aguilar-Gurrieri C., Ortega E., Panne D.;
"Structure of the p300 catalytic core and implications for chromatin
targeting and HAT regulation.";
Nat. Struct. Mol. Biol. 20:1040-1046(2013).
[100]
X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 1287-1664 OF MUTANT PHE-1467
IN COMPLEX WITH ACETYL-COA AND COENZYME A.
PubMed=24819397; DOI=10.1021/bi500380f;
Maksimoska J., Segura-Pena D., Cole P.A., Marmorstein R.;
"Structure of the p300 histone acetyltransferase bound to acetyl-
coenzyme A and its analogues.";
Biochemistry 53:3415-3422(2014).
[101]
VARIANTS PRO-827; GLY-1013; TYR-1650 AND GLN-2221, AND POSSIBLE
INVOLVEMENT IN CANCER.
PubMed=10700188; DOI=10.1038/73536;
Gayther S.A., Batley S.J., Linger L., Bannister A., Thorpe K.,
Chin S.-F., Daigo Y., Russell P., Wilson A., Sowter H.M.,
Delhanty J.D.A., Ponder B.A.J., Kouzarides T., Caldas C.;
"Mutations truncating the EP300 acetylase in human cancers.";
Nat. Genet. 24:300-303(2000).
[102]
VARIANT ILE-1511.
PubMed=24476420; DOI=10.1111/cge.12348;
Negri G., Milani D., Colapietro P., Forzano F., Della Monica M.,
Rusconi D., Consonni L., Caffi L.G., Finelli P., Scarano G.,
Magnani C., Selicorni A., Spena S., Larizza L., Gervasini C.;
"Clinical and molecular characterization of Rubinstein-Taybi syndrome
patients carrying distinct novel mutations of the EP300 gene.";
Clin. Genet. 87:148-154(2015).
-!- FUNCTION: Functions as histone acetyltransferase and regulates
transcription via chromatin remodeling. Acetylates all four core
histones in nucleosomes. Histone acetylation gives an epigenetic
tag for transcriptional activation. Mediates cAMP-gene regulation
by binding specifically to phosphorylated CREB protein. Mediates
acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification
that localizes at the surface of the histone octamer and
stimulates transcription, possibly by promoting nucleosome
instability. Mediates acetylation of histone H3 at 'Lys-27'
(H3K27ac). Also functions as acetyltransferase for nonhistone
targets. Acetylates 'Lys-131' of ALX1 and acts as its coactivator.
Acetylates SIRT2 and is proposed to indirectly increase the
transcriptional activity of TP53 through acetylation and
subsequent attenuation of SIRT2 deacetylase function. Acetylates
HDAC1 leading to its inactivation and modulation of transcription.
Acts as a TFAP2A-mediated transcriptional coactivator in presence
of CITED2. Plays a role as a coactivator of NEUROD1-dependent
transcription of the secretin and p21 genes and controls terminal
differentiation of cells in the intestinal epithelium. Promotes
cardiac myocyte enlargement. Can also mediate transcriptional
repression. Binds to and may be involved in the transforming
capacity of the adenovirus E1A protein. In case of HIV-1
infection, it is recruited by the viral protein Tat. Regulates
Tat's transactivating activity and may help inducing chromatin
remodeling of proviral genes. Acetylates FOXO1 and enhances its
transcriptional activity. Acetylates BCL6 wich disrupts its
ability to recruit histone deacetylases and hinders its
transcriptional repressor activity. Participates in CLOCK or
NPAS2-regulated rhythmic gene transcription; exhibits a circadian
association with CLOCK or NPAS2, correlating with increase in
PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter.
Acetylates MTA1 at 'Lys-626' which is essential for its
transcriptional coactivator activity (PubMed:10733570,
PubMed:11430825, PubMed:11701890, PubMed:12402037,
PubMed:12586840, PubMed:12929931, PubMed:14645221,
PubMed:15186775, PubMed:15890677, PubMed:16617102,
PubMed:16762839, PubMed:18722353, PubMed:18995842,
PubMed:23415232, PubMed:23911289, PubMed:23934153,
PubMed:8945521). Acetylates XBP1 isoform 2; acetylation increases
protein stability of XBP1 isoform 2 and enhances its
transcriptional activity (PubMed:20955178). Acetylates PCNA;
acetylation promotes removal of chromatin-bound PCNA and its
degradation during nucleotide excision repair (NER)
(PubMed:24939902). Acetylates MEF2D. {ECO:0000269|PubMed:10733570,
ECO:0000269|PubMed:11430825, ECO:0000269|PubMed:11701890,
ECO:0000269|PubMed:12402037, ECO:0000269|PubMed:12586840,
ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:14645221,
ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15890677,
ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:16762839,
ECO:0000269|PubMed:18722353, ECO:0000269|PubMed:18995842,
ECO:0000269|PubMed:21030595, ECO:0000269|PubMed:23415232,
ECO:0000269|PubMed:23911289, ECO:0000269|PubMed:23934153,
ECO:0000269|PubMed:24939902, ECO:0000269|PubMed:8945521,
ECO:0000305|PubMed:20955178}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine. {ECO:0000269|PubMed:23415232,
ECO:0000269|PubMed:23934153, ECO:0000269|PubMed:8945521}.
-!- SUBUNIT: Interacts with phosphorylated CREB1. Interacts with
HIF1A; the interaction is stimulated in response to hypoxia and
inhibited by CITED2. Interacts (via N-terminus) with TFAP2A (via
N-terminus); the interaction requires CITED2. Interacts (via CH1
domain) with CITED2 (via C-terminus). Interacts with CITED1
(unphosphorylated form preferentially and via C-terminus).
Interacts with ESR1; the interaction is estrogen-dependent and
enhanced by CITED1. Interacts with DTX1, EID1, ELF3, FEN1, LEF1,
NCOA1, NCOA6, NR3C1, PCAF, PELP1, PRDM6, SP1, SP3, SPIB, SRY,
TCF7L2, TP53, DDX5, DDX17, SATB1, SRCAP, TTC5, JMY and TRERF1. The
TAZ-type 1 domain interacts with HIF1A. Probably part of a complex
with HIF1A and CREBBP. Part of a complex containing CARM1 and
NCOA2/GRIP1. Interacts with ING4 and this interaction may be
indirect. Interacts with ING5. Interacts with the C-terminal
region of CITED4. Non-sumoylated EP300 preferentially interacts
with SENP3. Interacts with SS18L1/CREST. Interacts with ALX1 (via
homeobox domain). Interacts with NEUROD1; the interaction is
inhibited by NR0B2. Interacts with TCF3. Interacts (via CREB-
binding domain) with MYOCD (via C-terminus). Binds to HIPK2.
Interacts with ROCK2 and PPARG. Forms a complex made of CDK9,
CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy in
cardiomyocytes. Interacts with IRF1 and this interaction enhances
acetylation of p53/TP53 and stimulation of its activity. Interacts
with FOXO1; the interaction acetylates FOXO1 and enhances its
transcriptional activity. Interacts with ALKBH4 and DDIT3/CHOP.
Interacts with KLF15. Interacts with CEBPB and RORA. Interacts
with HTLV-1 Tax and p30II. Interacts with and acetylates HIV-1
Tat. Interacts with NPAS2, ARNTL/BMAL1 and CLOCK. Interacts with
SIRT2 isoform 1, isoform 2 and isoform 5. Interacts with MTA1.
Interacts with HDAC4 and HDAC5 in the presence of TFAP2C
(PubMed:10545121, PubMed:10722728, PubMed:10823961,
PubMed:11073989, PubMed:11073990, PubMed:11080476,
PubMed:11349124, PubMed:11430825, PubMed:11463834,
PubMed:11481323, PubMed:11518699, PubMed:11559821,
PubMed:11564735, PubMed:11581164, PubMed:11581372,
PubMed:11701890, PubMed:11744733, PubMed:11864910,
PubMed:11959990, PubMed:11997499, PubMed:12446687,
PubMed:12527917, PubMed:12586840, PubMed:12750254,
PubMed:12778114, PubMed:12837748, PubMed:12929931,
PubMed:14605447, PubMed:14645221, PubMed:14716005,
PubMed:14752053, PubMed:15075319, PubMed:15186775,
PubMed:15297880, PubMed:15509808, PubMed:15731352,
PubMed:15890677, PubMed:16478997, PubMed:16574662,
PubMed:16617102, PubMed:16864582, PubMed:17226766,
PubMed:17872950, PubMed:18273021, PubMed:19217391,
PubMed:19680224, PubMed:20081228, PubMed:23145062,
PubMed:23999430, PubMed:24177535, PubMed:24413532, PubMed:8684459,
PubMed:8917528, PubMed:9528808, PubMed:9590696, PubMed:9862959,
PubMed:9887100). Interacts with TRIP4 (PubMed:25219498). Directly
interacts with ZBTB49; this interaction leads to synergistic
transactivation of CDKN1A (PubMed:25245946). Interacts with NR4A3
(By similarity). Interacts with ZNF451 (PubMed:24324267).
Interacts with human adenovirus 5 E1A protein; this interaction
stimulates the acetylation of RB1 by recruiting EP300 and RB1 into
a multimeric-protein complex (PubMed:11433299). Interacts with
ATF5; EP300 is required for ATF5 and CEBPB interaction and DNA
binding (By similarity). Interacts with HSF1 (PubMed:27189267).
Interacts with ZBTB48/TZAP (PubMed:24382891).
{ECO:0000250|UniProtKB:B2RWS6, ECO:0000269|PubMed:10545121,
ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:10823961,
ECO:0000269|PubMed:11073989, ECO:0000269|PubMed:11073990,
ECO:0000269|PubMed:11080476, ECO:0000269|PubMed:11349124,
ECO:0000269|PubMed:11430825, ECO:0000269|PubMed:11433299,
ECO:0000269|PubMed:11463834, ECO:0000269|PubMed:11481323,
ECO:0000269|PubMed:11518699, ECO:0000269|PubMed:11559821,
ECO:0000269|PubMed:11564735, ECO:0000269|PubMed:11581164,
ECO:0000269|PubMed:11581372, ECO:0000269|PubMed:11701890,
ECO:0000269|PubMed:11744733, ECO:0000269|PubMed:11864910,
ECO:0000269|PubMed:11959990, ECO:0000269|PubMed:11997499,
ECO:0000269|PubMed:12446687, ECO:0000269|PubMed:12527917,
ECO:0000269|PubMed:12586840, ECO:0000269|PubMed:12750254,
ECO:0000269|PubMed:12778114, ECO:0000269|PubMed:12837748,
ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:14605447,
ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:14716005,
ECO:0000269|PubMed:14752053, ECO:0000269|PubMed:15075319,
ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15297880,
ECO:0000269|PubMed:15509808, ECO:0000269|PubMed:15731352,
ECO:0000269|PubMed:15890677, ECO:0000269|PubMed:16478997,
ECO:0000269|PubMed:16574662, ECO:0000269|PubMed:16617102,
ECO:0000269|PubMed:16864582, ECO:0000269|PubMed:17226766,
ECO:0000269|PubMed:17872950, ECO:0000269|PubMed:18273021,
ECO:0000269|PubMed:19217391, ECO:0000269|PubMed:19680224,
ECO:0000269|PubMed:20081228, ECO:0000269|PubMed:23145062,
ECO:0000269|PubMed:23999430, ECO:0000269|PubMed:24177535,
ECO:0000269|PubMed:24382891, ECO:0000269|PubMed:24413532,
ECO:0000269|PubMed:25219498, ECO:0000269|PubMed:25245946,
ECO:0000269|PubMed:27189267, ECO:0000269|PubMed:8684459,
ECO:0000269|PubMed:8917528, ECO:0000269|PubMed:9528808,
ECO:0000269|PubMed:9590696, ECO:0000269|PubMed:9862959,
ECO:0000269|PubMed:9887100}.
-!- INTERACTION:
P03070:- (xeno); NbExp=2; IntAct=EBI-447295, EBI-617698;
P03255:- (xeno); NbExp=3; IntAct=EBI-447295, EBI-2603114;
P03255-2:- (xeno); NbExp=3; IntAct=EBI-447295, EBI-6859460;
P03259:- (xeno); NbExp=3; IntAct=EBI-447295, EBI-6947456;
Q9NXW9:ALKBH4; NbExp=4; IntAct=EBI-447295, EBI-8637516;
P27695:APEX1; NbExp=8; IntAct=EBI-447295, EBI-1048805;
Q9UBL3:ASH2L; NbExp=5; IntAct=EBI-447295, EBI-540797;
K4P3M7:BICP0 (xeno); NbExp=4; IntAct=EBI-447295, EBI-11296047;
Q9NPI1:BRD7; NbExp=3; IntAct=EBI-447295, EBI-711221;
P24941:CDK2; NbExp=5; IntAct=EBI-447295, EBI-375096;
Q99967:CITED2; NbExp=3; IntAct=EBI-447295, EBI-937732;
P61201:COPS2; NbExp=2; IntAct=EBI-447295, EBI-1050386;
P16220:CREB1; NbExp=2; IntAct=EBI-447295, EBI-711855;
Q01147:Creb1 (xeno); NbExp=2; IntAct=EBI-447295, EBI-2291098;
P17844:DDX5; NbExp=4; IntAct=EBI-447295, EBI-351962;
P03122:E2 (xeno); NbExp=3; IntAct=EBI-447295, EBI-7028618;
P06422:E2 (xeno); NbExp=7; IntAct=EBI-447295, EBI-7136851;
P06790:E2 (xeno); NbExp=6; IntAct=EBI-447295, EBI-7010629;
P03372:ESR1; NbExp=2; IntAct=EBI-447295, EBI-78473;
Q00403:GTF2B; NbExp=2; IntAct=EBI-447295, EBI-389564;
Q16665:HIF1A; NbExp=16; IntAct=EBI-447295, EBI-447269;
Q61221:Hif1a (xeno); NbExp=2; IntAct=EBI-447295, EBI-298954;
Q9H2X6:HIPK2; NbExp=4; IntAct=EBI-447295, EBI-348345;
Q9QXM1:Jmy (xeno); NbExp=16; IntAct=EBI-447295, EBI-866001;
Q92831:KAT2B; NbExp=2; IntAct=EBI-447295, EBI-477430;
P55209:NAP1L1; NbExp=3; IntAct=EBI-447295, EBI-356392;
O60934:NBN; NbExp=5; IntAct=EBI-447295, EBI-494844;
Q9Y6Q9:NCOA3; NbExp=2; IntAct=EBI-447295, EBI-81196;
P20265:POU3F2; NbExp=3; IntAct=EBI-447295, EBI-1167176;
Q96KQ4:PPP1R13B; NbExp=2; IntAct=EBI-447295, EBI-1105153;
Q8WUF5:PPP1R13L; NbExp=2; IntAct=EBI-447295, EBI-5550163;
Q13761:RUNX3; NbExp=7; IntAct=EBI-447295, EBI-925990;
Q96EB6:SIRT1; NbExp=2; IntAct=EBI-447295, EBI-1802965;
Q13309:SKP2; NbExp=3; IntAct=EBI-447295, EBI-456291;
O95863:SNAI1; NbExp=3; IntAct=EBI-447295, EBI-1045459;
P42226:STAT6; NbExp=2; IntAct=EBI-447295, EBI-1186478;
P04608:tat (xeno); NbExp=3; IntAct=EBI-447295, EBI-6164389;
P05549:TFAP2A; NbExp=7; IntAct=EBI-447295, EBI-347351;
P04637:TP53; NbExp=10; IntAct=EBI-447295, EBI-366083;
Q13625:TP53BP2; NbExp=2; IntAct=EBI-447295, EBI-77642;
P11473:VDR; NbExp=3; IntAct=EBI-447295, EBI-286357;
P67809:YBX1; NbExp=2; IntAct=EBI-447295, EBI-354065;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In the presence of
ALX1 relocalizes from the cytoplasm to the nucleus. Colocalizes
with ROCK2 in the nucleus.
-!- DOMAIN: The CRD1 domain (cell cycle regulatory domain 1) mediates
transcriptional repression of a subset of p300 responsive genes;
it can be de-repressed by CDKN1A/p21WAF1 at least at some
promoters. It conatins sumoylation and acetylation sites and the
same lysine residues may be targeted for the respective
modifications. It is proposed that deacetylation by SIRT1 allows
sumoylation leading to suppressed activity.
-!- PTM: Acetylated on Lys at up to 17 positions by intermolecular
autocatalysis. Deacetylated in the transcriptional repression
domain (CRD1) by SIRT1, preferentially at Lys-1020. Deacetylated
by SIRT2, preferentially at Lys-418, Lys-423, Lys-1542, Lys-1546,
Lys-1549, Lys-1699, Lys-1704 and Lys-1707.
{ECO:0000269|PubMed:15004546, ECO:0000269|PubMed:15632193,
ECO:0000269|PubMed:17065153, ECO:0000269|PubMed:18995842,
ECO:0000269|PubMed:23934153, ECO:0000269|PubMed:24177535}.
-!- PTM: Citrullinated at Arg-2142 by PADI4, which impairs methylation
by CARM1 and promotes interaction with NCOA2/GRIP1.
{ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:15731352}.
-!- PTM: Methylated at Arg-580 and Arg-604 in the KIX domain by CARM1,
which blocks association with CREB, inhibits CREB signaling and
activates apoptotic response. Also methylated at Arg-2142 by
CARM1, which impairs interaction with NCOA2/GRIP1.
{ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:15731352}.
-!- PTM: Sumoylated; sumoylation in the transcriptional repression
domain (CRD1) mediates transcriptional repression. Desumoylated by
SENP3 through the removal of SUMO2 and SUMO3.
{ECO:0000269|PubMed:12718889, ECO:0000269|PubMed:19680224}.
-!- PTM: Probable target of ubiquitination by FBXO3, leading to rapid
proteasome-dependent degradation.
-!- PTM: Phosphorylated by HIPK2 in a RUNX1-dependent manner. This
phosphorylation that activates EP300 happens when RUNX1 is
associated with DNA and CBFB. Phosphorylated by ROCK2 and this
enhances its activity. Phosphorylation at Ser-89 by AMPK reduces
interaction with nuclear receptors, such as PPARG.
{ECO:0000269|PubMed:11518699, ECO:0000269|PubMed:12446687,
ECO:0000269|PubMed:16574662, ECO:0000269|PubMed:18695000}.
-!- DISEASE: Note=Defects in EP300 may play a role in epithelial
cancer.
-!- DISEASE: Note=Chromosomal aberrations involving EP300 may be a
cause of acute myeloid leukemias. Translocation t(8;22)(p11;q13)
with KAT6A.
-!- DISEASE: Rubinstein-Taybi syndrome 2 (RSTS2) [MIM:613684]: A
disorder characterized by craniofacial abnormalities, postnatal
growth deficiency, broad thumbs, broad big toes, mental
retardation and a propensity for development of malignancies. Some
individuals with RSTS2 have less severe mental impairment, more
severe microcephaly, and a greater degree of changes in facial
bone structure than RSTS1 patients. {ECO:0000269|PubMed:15706485}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/P300ID97.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=P300/CBP entry;
URL="https://en.wikipedia.org/wiki/P300/CBP";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U01877; AAA18639.1; -; mRNA.
EMBL; AL080243; CAH70384.1; -; Genomic_DNA.
EMBL; AL035658; CAH70384.1; JOINED; Genomic_DNA.
EMBL; AL096765; CAH70384.1; JOINED; Genomic_DNA.
EMBL; AL096765; CAH73688.1; -; Genomic_DNA.
EMBL; AL035658; CAH73688.1; JOINED; Genomic_DNA.
EMBL; AL080243; CAH73688.1; JOINED; Genomic_DNA.
EMBL; AL035658; CAI23037.1; -; Genomic_DNA.
EMBL; AL080243; CAI23037.1; JOINED; Genomic_DNA.
EMBL; AL096765; CAI23037.1; JOINED; Genomic_DNA.
EMBL; CH471095; EAW60408.1; -; Genomic_DNA.
CCDS; CCDS14010.1; -.
PIR; A54277; A54277.
RefSeq; NP_001420.2; NM_001429.3.
UniGene; Hs.517517; -.
UniGene; Hs.655211; -.
PDB; 1L3E; NMR; -; B=323-423.
PDB; 1P4Q; NMR; -; B=323-423.
PDB; 2K8F; NMR; -; A=1723-1812.
PDB; 2MH0; NMR; -; B=1723-1812.
PDB; 2MZD; NMR; -; A=1723-1812.
PDB; 3BIY; X-ray; 1.70 A; A=1287-1666.
PDB; 3I3J; X-ray; 2.33 A; A/B/C/D/E/F/G/H/I/J/K/L=1040-1161.
PDB; 3IO2; X-ray; 2.50 A; A=1723-1836.
PDB; 3P57; X-ray; 2.19 A; P=1726-1835.
PDB; 3T92; X-ray; 1.50 A; A=1723-1818.
PDB; 4BHW; X-ray; 2.80 A; A/B=1043-1519, A/B=1581-1666.
PDB; 4PZR; X-ray; 2.10 A; A=1287-1664.
PDB; 4PZS; X-ray; 1.94 A; A=1287-1664.
PDB; 4PZT; X-ray; 2.80 A; A=1287-1664.
PDB; 5BT3; X-ray; 1.05 A; A=1048-1161.
PDB; 5LKT; X-ray; 2.04 A; A=1043-1519, A=1581-1666.
PDB; 5LKU; X-ray; 3.50 A; A=1043-1519, A=1581-1666.
PDB; 5LKX; X-ray; 2.52 A; A=1043-1519, A=1581-1666.
PDB; 5LKZ; X-ray; 2.50 A; A=1043-1519, A=1581-1666.
PDBsum; 1L3E; -.
PDBsum; 1P4Q; -.
PDBsum; 2K8F; -.
PDBsum; 2MH0; -.
PDBsum; 2MZD; -.
PDBsum; 3BIY; -.
PDBsum; 3I3J; -.
PDBsum; 3IO2; -.
PDBsum; 3P57; -.
PDBsum; 3T92; -.
PDBsum; 4BHW; -.
PDBsum; 4PZR; -.
PDBsum; 4PZS; -.
PDBsum; 4PZT; -.
PDBsum; 5BT3; -.
PDBsum; 5LKT; -.
PDBsum; 5LKU; -.
PDBsum; 5LKX; -.
PDBsum; 5LKZ; -.
DisProt; DP00633; -.
ProteinModelPortal; Q09472; -.
SMR; Q09472; -.
BioGrid; 108347; 495.
DIP; DIP-257N; -.
IntAct; Q09472; 190.
MINT; MINT-104535; -.
STRING; 9606.ENSP00000263253; -.
BindingDB; Q09472; -.
ChEMBL; CHEMBL3784; -.
GuidetoPHARMACOLOGY; 2735; -.
iPTMnet; Q09472; -.
PhosphoSitePlus; Q09472; -.
BioMuta; EP300; -.
DMDM; 223590203; -.
EPD; Q09472; -.
MaxQB; Q09472; -.
PaxDb; Q09472; -.
PeptideAtlas; Q09472; -.
PRIDE; Q09472; -.
Ensembl; ENST00000263253; ENSP00000263253; ENSG00000100393.
GeneID; 2033; -.
KEGG; hsa:2033; -.
UCSC; uc003azl.5; human.
CTD; 2033; -.
DisGeNET; 2033; -.
GeneCards; EP300; -.
GeneCards; MIR1281; -.
GeneReviews; EP300; -.
H-InvDB; HIX0203186; -.
HGNC; HGNC:3373; EP300.
HPA; CAB000146; -.
HPA; HPA003128; -.
HPA; HPA004112; -.
MalaCards; EP300; -.
MIM; 602700; gene.
MIM; 613684; phenotype.
neXtProt; NX_Q09472; -.
OpenTargets; ENSG00000100393; -.
Orphanet; 353284; Rubinstein-Taybi syndrome due to EP300 haploinsufficiency.
PharmGKB; PA27807; -.
eggNOG; KOG1778; Eukaryota.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00760000119206; -.
HOGENOM; HOG000111353; -.
HOVERGEN; HBG000185; -.
InParanoid; Q09472; -.
KO; K04498; -.
OMA; GQVSNPP; -.
OrthoDB; EOG091G0L04; -.
PhylomeDB; Q09472; -.
TreeFam; TF101097; -.
BRENDA; 2.3.1.48; 2681.
Reactome; R-HSA-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
Reactome; R-HSA-1368082; RORA activates gene expression.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-HSA-156711; Polo-like kinase mediated events.
Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2197563; NOTCH2 intracellular domain regulates transcription.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-3371568; Attenuation phase.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-HSA-5689901; Metalloprotease DUBs.
Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
Reactome; R-HSA-6782135; Dual incision in TC-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation.
Reactome; R-HSA-6811555; PI5P Regulates TP53 Acetylation.
Reactome; R-HSA-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
Reactome; R-HSA-8941856; RUNX3 regulates NOTCH signaling.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8951936; RUNX3 regulates p14-ARF.
Reactome; R-HSA-918233; TRAF3-dependent IRF activation pathway.
Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SignaLink; Q09472; -.
SIGNOR; Q09472; -.
ChiTaRS; EP300; human.
EvolutionaryTrace; Q09472; -.
GeneWiki; EP300; -.
GenomeRNAi; 2033; -.
PRO; PR:Q09472; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100393; -.
CleanEx; HS_EP300; -.
ExpressionAtlas; Q09472; baseline and differential.
Genevisible; Q09472; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000123; C:histone acetyltransferase complex; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB.
GO; GO:0033613; F:activating transcription factor binding; IPI:UniProtKB.
GO; GO:0050681; F:androgen receptor binding; IPI:BHF-UCL.
GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IDA:UniProtKB.
GO; GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB.
GO; GO:0002039; F:p53 binding; IEA:Ensembl.
GO; GO:0034212; F:peptide N-acetyltransferase activity; TAS:Reactome.
GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; TAS:Reactome.
GO; GO:0097157; F:pre-mRNA intronic binding; IEA:Ensembl.
GO; GO:0008022; F:protein C-terminus binding; IDA:MGI.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:BHF-UCL.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IEA:Ensembl.
GO; GO:0016746; F:transferase activity, transferring acyl groups; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0043969; P:histone H2B acetylation; IDA:UniProtKB.
GO; GO:0043967; P:histone H4 acetylation; IMP:UniProtKB.
GO; GO:0018393; P:internal peptidyl-lysine acetylation; IDA:UniProtKB.
GO; GO:0006475; P:internal protein amino acid acetylation; IDA:UniProtKB.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:UniProtKB.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0010742; P:macrophage derived foam cell differentiation; IDA:UniProtKB.
GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
GO; GO:0030220; P:platelet formation; IEA:Ensembl.
GO; GO:0043923; P:positive regulation by host of viral transcription; IDA:BHF-UCL.
GO; GO:0045815; P:positive regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0006990; P:positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response; ISS:UniProtKB.
GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
GO; GO:0006473; P:protein acetylation; IDA:UniProtKB.
GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0010506; P:regulation of autophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0051726; P:regulation of cell cycle; TAS:Reactome.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0090043; P:regulation of tubulin deacetylation; IDA:UniProtKB.
GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd15802; RING_CBP-p300; 1.
Gene3D; 1.10.1630.10; -; 1.
Gene3D; 1.20.1020.10; -; 3.
Gene3D; 1.20.920.10; -; 1.
InterPro; IPR001487; Bromodomain.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR031162; CBP_P300_HAT.
InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
InterPro; IPR003101; KIX_dom.
InterPro; IPR009110; Nuc_rcpt_coact.
InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
InterPro; IPR010303; RING_CBP-p300.
InterPro; IPR000197; Znf_TAZ.
InterPro; IPR000433; Znf_ZZ.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF09030; Creb_binding; 1.
Pfam; PF06001; DUF902; 1.
Pfam; PF08214; HAT_KAT11; 1.
Pfam; PF02172; KIX; 1.
Pfam; PF02135; zf-TAZ; 2.
Pfam; PF00569; ZZ; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 1.
SMART; SM01250; KAT11; 1.
SMART; SM00551; ZnF_TAZ; 2.
SMART; SM00291; ZnF_ZZ; 1.
SUPFAM; SSF47040; SSF47040; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF57933; SSF57933; 2.
SUPFAM; SSF69125; SSF69125; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS51727; CBP_P300_HAT; 1.
PROSITE; PS50952; KIX; 1.
PROSITE; PS50134; ZF_TAZ; 2.
PROSITE; PS01357; ZF_ZZ_1; 1.
PROSITE; PS50135; ZF_ZZ_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Acyltransferase; Biological rhythms;
Bromodomain; Cell cycle; Chromosomal rearrangement; Citrullination;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Host-virus interaction; Isopeptide bond;
Metal-binding; Methylation; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transcription; Transcription regulation;
Transferase; Ubl conjugation; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
CHAIN 2 2414 Histone acetyltransferase p300.
/FTId=PRO_0000211193.
DOMAIN 566 645 KIX. {ECO:0000255|PROSITE-
ProRule:PRU00311}.
DOMAIN 1067 1139 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 1287 1663 CBP/p300-type HAT. {ECO:0000255|PROSITE-
ProRule:PRU01065}.
ZN_FING 331 417 TAZ-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00203}.
ZN_FING 1664 1707 ZZ-type. {ECO:0000255|PROSITE-
ProRule:PRU00228}.
ZN_FING 1728 1809 TAZ-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00203}.
REGION 2 149 Interaction with RORA.
{ECO:0000269|PubMed:9862959}.
REGION 2 139 Interaction with ALX1.
{ECO:0000269|PubMed:12929931}.
REGION 1017 1029 CRD1; mediates transcriptional
repression.
REGION 1397 1399 Interaction with histone.
{ECO:0000269|PubMed:18273021}.
REGION 1398 1400 Acetyl-CoA binding.
{ECO:0000269|PubMed:24819397}.
REGION 1410 1411 Acetyl-CoA binding.
{ECO:0000269|PubMed:24819397}.
REGION 1572 1818 Binding region for E1A adenovirus.
REGION 2003 2212 Interaction with HTLV-1 Tax.
REGION 2041 2240 Interaction with NCOA2.
{ECO:0000269|PubMed:15731352}.
MOTIF 11 17 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 797 800 Poly-Ser.
COMPBIAS 1519 1526 Poly-Glu.
COMPBIAS 2066 2069 Poly-Gln.
COMPBIAS 2190 2195 Poly-Gln.
METAL 347 347 Zinc 1.
METAL 351 351 Zinc 1.
METAL 364 364 Zinc 1.
METAL 369 369 Zinc 1.
METAL 378 378 Zinc 2.
METAL 382 382 Zinc 2.
METAL 388 388 Zinc 2.
METAL 393 393 Zinc 2.
METAL 402 402 Zinc 3.
METAL 406 406 Zinc 3.
METAL 411 411 Zinc 3.
METAL 414 414 Zinc 3.
BINDING 1457 1457 Acetyl-CoA; via carbonyl oxygen.
{ECO:0000269|PubMed:24819397}.
BINDING 1462 1462 Acetyl-CoA.
{ECO:0000269|PubMed:24819397}.
BINDING 1466 1466 Acetyl-CoA.
{ECO:0000269|PubMed:24819397}.
SITE 31 32 Breakpoint for translocation to form
KAT6A-EP300 and EP300-KAT6A.
SITE 2088 2088 Interaction with NCOA2.
SITE 2142 2142 Interaction with NCOA2.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
MOD_RES 89 89 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:11518699,
ECO:0000269|PubMed:16574662}.
MOD_RES 418 418 N6-acetyllysine.
{ECO:0000269|PubMed:18995842}.
MOD_RES 423 423 N6-acetyllysine.
{ECO:0000269|PubMed:18995842}.
MOD_RES 499 499 Phosphoserine.
{ECO:0000250|UniProtKB:B2RWS6}.
MOD_RES 580 580 Omega-N-methylated arginine; by CARM1.
{ECO:0000269|PubMed:11701890}.
MOD_RES 604 604 Omega-N-methylated arginine; by CARM1.
{ECO:0000269|PubMed:11701890}.
MOD_RES 636 636 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 977 977 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1020 1020 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:15632193}.
MOD_RES 1024 1024 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:15632193}.
MOD_RES 1038 1038 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1180 1180 N6-acetyllysine.
{ECO:0000250|UniProtKB:B2RWS6}.
MOD_RES 1336 1336 N6-acetyllysine.
{ECO:0000269|PubMed:17065153}.
MOD_RES 1473 1473 N6-acetyllysine.
{ECO:0000269|PubMed:17065153}.
MOD_RES 1499 1499 N6-acetyllysine; by autocatalysis.
{ECO:0000269|PubMed:15004546}.
MOD_RES 1542 1542 N6-acetyllysine.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:18995842}.
MOD_RES 1546 1546 N6-acetyllysine.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:18995842}.
MOD_RES 1549 1549 N6-acetyllysine; by autocatalysis.
{ECO:0000269|PubMed:15004546,
ECO:0000269|PubMed:18995842}.
MOD_RES 1554 1554 N6-acetyllysine; by autocatalysis.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:15004546}.
MOD_RES 1555 1555 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1558 1558 N6-acetyllysine.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:15004546}.
MOD_RES 1560 1560 N6-acetyllysine; by autocatalysis.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:15004546}.
MOD_RES 1583 1583 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1699 1699 N6-acetyllysine.
{ECO:0000269|PubMed:18995842}.
MOD_RES 1704 1704 N6-acetyllysine.
{ECO:0000269|PubMed:18995842}.
MOD_RES 1707 1707 N6-acetyllysine.
{ECO:0000269|PubMed:18995842}.
MOD_RES 1726 1726 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2142 2142 Asymmetric dimethylarginine; by CARM1;
alternate. {ECO:0000269|PubMed:15731352}.
MOD_RES 2142 2142 Citrulline; by PADI4; alternate.
{ECO:0000269|PubMed:15731352}.
CROSSLNK 1020 1020 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 1024 1024 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
VARIANT 289 289 M -> V (in dbSNP:rs2230111).
/FTId=VAR_055554.
VARIANT 827 827 L -> P (in a breast cancer sample).
{ECO:0000269|PubMed:10700188}.
/FTId=VAR_014428.
VARIANT 997 997 I -> V (in dbSNP:rs20551).
/FTId=VAR_020425.
VARIANT 1013 1013 E -> G (in a breast cancer sample).
{ECO:0000269|PubMed:10700188}.
/FTId=VAR_014429.
VARIANT 1511 1511 N -> I. {ECO:0000269|PubMed:24476420}.
/FTId=VAR_074021.
VARIANT 1650 1650 S -> Y (in a pancreatic cancer sample).
{ECO:0000269|PubMed:10700188}.
/FTId=VAR_014430.
VARIANT 2174 2174 T -> S (in dbSNP:rs5758252).
/FTId=VAR_038376.
VARIANT 2221 2221 P -> Q (in a colorectal cancer sample;
dbSNP:rs28937578).
{ECO:0000269|PubMed:10700188}.
/FTId=VAR_014431.
VARIANT 2223 2223 Q -> P (in dbSNP:rs1046088).
{ECO:0000269|PubMed:7523245}.
/FTId=VAR_038377.
MUTAGEN 89 89 S->A: Abolishes AMPK-mediated
phosphorylation.
{ECO:0000269|PubMed:11518699}.
MUTAGEN 89 89 S->D: Phosphomimetic mutant that leads to
descreased interaction with nuclear
receptors. {ECO:0000269|PubMed:11518699}.
MUTAGEN 344 344 L->A: Inhibits interaction with HIF1A and
transcription activation; when associated
with A-345.
{ECO:0000269|PubMed:12778114}.
MUTAGEN 345 345 L->A: Inhibits interaction with HIF1A and
transcription activation; when associated
with A-344.
{ECO:0000269|PubMed:12778114}.
MUTAGEN 371 376 TMKNVL->NAAIRS: Inhibits interaction with
HIF1A. Reduces interaction with CITED2.
{ECO:0000269|PubMed:9887100}.
MUTAGEN 413 418 VCLPLK->NAAIRS: Inhibits interaction with
HIF1A. Does not inhibit interaction with
CITED2. {ECO:0000269|PubMed:9887100}.
MUTAGEN 1020 1020 K->A: Abolishes sumoylation and
transcriptional repression when
associated with A-1024.
{ECO:0000269|PubMed:12718889,
ECO:0000269|PubMed:15632193}.
MUTAGEN 1020 1020 K->R: Abolishes sumoylation and
transcriptional repression; when
associated with R-1024.
{ECO:0000269|PubMed:12718889,
ECO:0000269|PubMed:15632193}.
MUTAGEN 1024 1024 K->A: Abolishes sumoylation and
transcriptional repression; when
associated with A-1020.
{ECO:0000269|PubMed:12718889,
ECO:0000269|PubMed:15632193}.
MUTAGEN 1024 1024 K->R: Abolishes sumoylation and
transcriptional repression; when
associated with R-1020.
{ECO:0000269|PubMed:12718889,
ECO:0000269|PubMed:15632193}.
MUTAGEN 1170 1170 F->E: Increased acetyltransferase
activity. {ECO:0000269|PubMed:23934153}.
MUTAGEN 1204 1204 C->R: Increased acetyltransferase
activity. {ECO:0000269|PubMed:23934153}.
MUTAGEN 1242 1242 E->K: Increased acetyltransferase
activity. {ECO:0000269|PubMed:23934153}.
MUTAGEN 1357 1357 T->L: 40% decrease in activity.
{ECO:0000269|PubMed:18273021}.
MUTAGEN 1357 1357 T->R: 40% decrease in activity. 90%
decrease in activity; when associated
with R-1505; R-1625 and R-1628.
{ECO:0000269|PubMed:18273021}.
MUTAGEN 1396 1396 S->R: Loss of activity; when associated
with R-1397.
{ECO:0000269|PubMed:18273021}.
MUTAGEN 1396 1396 S->W: Loss of activity; when associated
with W-1396.
{ECO:0000269|PubMed:18273021}.
MUTAGEN 1397 1397 Y->R: Loss of activity; when associated
with R-1396.
{ECO:0000269|PubMed:18273021}.
MUTAGEN 1397 1397 Y->W: Loss of activity; when associated
with W-1397.
{ECO:0000269|PubMed:18273021}.
MUTAGEN 1399 1399 D->Y: Abolishes autoacetylation. Does not
interact with TFAP2A and inhibits
transcriptional coactivation of TFAP2A by
CITED2. Does not inhibit interaction with
CITED2, DNA-binding of TFAP2A or nuclear
localization of TFAP2A or CITED2. No
enhancement of FOXO1-mediated
transcriptional activity. No inhibition
of insulin-mediated translocation to the
cytoplasm. {ECO:0000269|PubMed:12586840,
ECO:0000269|PubMed:15890677,
ECO:0000269|PubMed:23934153}.
MUTAGEN 1467 1467 Y->F: Abolishes autoacetylation. Loss of
acetyltransferase activity.
{ECO:0000269|PubMed:23934153}.
MUTAGEN 1505 1505 E->R: 90% decrease in activity; when
associated with R-1625 and R-1628. 90%
decrease in activity; when associated
with R-1357; R-1625 and R-1628.
{ECO:0000269|PubMed:18273021}.
MUTAGEN 1625 1625 D->R: 70% decrease in activity; when
associated with R-1628. 90% decrease in
activity; when associated with R-1505 and
R-1628. 90% decrease in activity; when
associated with R-1357; R-1505 and R-
1628. {ECO:0000269|PubMed:18273021}.
MUTAGEN 1628 1628 D->R: 70% decrease in activity; when
associated with R-1625. 90% decrease in
activity; when associated with E-1505 and
R-1625. 90% decrease in activity; when
associated with R-1357; R-1505 and R-
1625. {ECO:0000269|PubMed:18273021}.
MUTAGEN 1645 1646 RR->EE: Increased acetyltransferase
activity. {ECO:0000269|PubMed:23934153}.
MUTAGEN 2056 2056 R->K: No effect on interaction with
NCOA2. {ECO:0000269|PubMed:15731352}.
MUTAGEN 2088 2088 R->K: Abolishes interaction with NCOA2.
{ECO:0000269|PubMed:15731352}.
MUTAGEN 2142 2142 R->K: Strongly reduces interaction with
NCOA2. {ECO:0000269|PubMed:15731352}.
CONFLICT 169 169 M -> T (in Ref. 1; AAA18639).
{ECO:0000305}.
CONFLICT 204 204 N -> D (in Ref. 1; AAA18639).
{ECO:0000305}.
CONFLICT 928 928 T -> N (in Ref. 1; AAA18639).
{ECO:0000305}.
CONFLICT 1924 1924 A -> T (in Ref. 1; AAA18639).
{ECO:0000305}.
HELIX 332 334 {ECO:0000244|PDB:1L3E}.
HELIX 335 355 {ECO:0000244|PDB:1L3E}.
TURN 356 358 {ECO:0000244|PDB:1L3E}.
HELIX 367 379 {ECO:0000244|PDB:1L3E}.
STRAND 386 389 {ECO:0000244|PDB:1L3E}.
HELIX 391 405 {ECO:0000244|PDB:1L3E}.
STRAND 408 410 {ECO:0000244|PDB:1P4Q}.
HELIX 414 418 {ECO:0000244|PDB:1L3E}.
HELIX 1051 1066 {ECO:0000244|PDB:5BT3}.
TURN 1069 1072 {ECO:0000244|PDB:5BT3}.
HELIX 1073 1075 {ECO:0000244|PDB:5BT3}.
HELIX 1081 1084 {ECO:0000244|PDB:5BT3}.
HELIX 1089 1092 {ECO:0000244|PDB:5BT3}.
HELIX 1099 1107 {ECO:0000244|PDB:5BT3}.
HELIX 1114 1131 {ECO:0000244|PDB:5BT3}.
HELIX 1137 1160 {ECO:0000244|PDB:5BT3}.
STRAND 1180 1182 {ECO:0000244|PDB:5LKX}.
STRAND 1189 1194 {ECO:0000244|PDB:5LKT}.
TURN 1195 1197 {ECO:0000244|PDB:5LKT}.
STRAND 1198 1201 {ECO:0000244|PDB:5LKT}.
HELIX 1202 1207 {ECO:0000244|PDB:5LKT}.
STRAND 1210 1215 {ECO:0000244|PDB:5LKT}.
STRAND 1218 1221 {ECO:0000244|PDB:4BHW}.
STRAND 1224 1227 {ECO:0000244|PDB:5LKT}.
HELIX 1228 1230 {ECO:0000244|PDB:5LKT}.
STRAND 1231 1236 {ECO:0000244|PDB:5LKT}.
STRAND 1244 1246 {ECO:0000244|PDB:5LKT}.
TURN 1248 1250 {ECO:0000244|PDB:5LKT}.
STRAND 1253 1255 {ECO:0000244|PDB:5LKT}.
HELIX 1256 1259 {ECO:0000244|PDB:5LKT}.
TURN 1263 1265 {ECO:0000244|PDB:5LKT}.
HELIX 1273 1278 {ECO:0000244|PDB:5LKT}.
HELIX 1297 1313 {ECO:0000244|PDB:3BIY}.
STRAND 1321 1334 {ECO:0000244|PDB:3BIY}.
HELIX 1339 1342 {ECO:0000244|PDB:3BIY}.
TURN 1343 1347 {ECO:0000244|PDB:3BIY}.
STRAND 1351 1366 {ECO:0000244|PDB:3BIY}.
STRAND 1369 1381 {ECO:0000244|PDB:3BIY}.
STRAND 1392 1400 {ECO:0000244|PDB:3BIY}.
HELIX 1407 1409 {ECO:0000244|PDB:3BIY}.
HELIX 1410 1428 {ECO:0000244|PDB:3BIY}.
STRAND 1432 1436 {ECO:0000244|PDB:3BIY}.
STRAND 1446 1450 {ECO:0000244|PDB:3BIY}.
HELIX 1460 1476 {ECO:0000244|PDB:3BIY}.
STRAND 1482 1485 {ECO:0000244|PDB:3BIY}.
HELIX 1486 1493 {ECO:0000244|PDB:3BIY}.
HELIX 1498 1500 {ECO:0000244|PDB:3BIY}.
HELIX 1508 1517 {ECO:0000244|PDB:3BIY}.
HELIX 1582 1590 {ECO:0000244|PDB:3BIY}.
HELIX 1592 1594 {ECO:0000244|PDB:3BIY}.
STRAND 1595 1601 {ECO:0000244|PDB:3BIY}.
HELIX 1603 1606 {ECO:0000244|PDB:3BIY}.
HELIX 1622 1624 {ECO:0000244|PDB:3BIY}.
STRAND 1625 1627 {ECO:0000244|PDB:3BIY}.
HELIX 1628 1636 {ECO:0000244|PDB:3BIY}.
HELIX 1644 1662 {ECO:0000244|PDB:3BIY}.
TURN 1726 1728 {ECO:0000244|PDB:2MZD}.
HELIX 1730 1747 {ECO:0000244|PDB:3T92}.
HELIX 1756 1770 {ECO:0000244|PDB:3T92}.
TURN 1774 1778 {ECO:0000244|PDB:3T92}.
HELIX 1780 1793 {ECO:0000244|PDB:3T92}.
STRAND 1799 1802 {ECO:0000244|PDB:2MZD}.
HELIX 1806 1818 {ECO:0000244|PDB:3T92}.
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


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