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CREB-binding protein (EC 2.3.1.48)

 CBP_HUMAN               Reviewed;        2442 AA.
Q92793; D3DUC9; O00147; Q16376; Q4LE28;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
05-DEC-2018, entry version 229.
RecName: Full=CREB-binding protein;
EC=2.3.1.48 {ECO:0000269|PubMed:24616510};
Name=CREBBP; Synonyms=CBP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9238046; DOI=10.1073/pnas.94.16.8732;
Sobulo O.M., Borrow J., Tomek R., Reshimi S., Harden A.,
Schlegelberger B., Housman D., Doggett N.A., Rowley J.D.,
Zeleznik-Le N.J.;
"MLL is fused to CBP, a histone acetyltransferase, in therapy-related
acute myeloid leukemia with a t(11;16)(q23;p13.3).";
Proc. Natl. Acad. Sci. U.S.A. 94:8732-8737(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9177780; DOI=10.1006/geno.1997.4699;
Giles R.H., Petrij F., Dauwerse H.G., den Hollander A.I.,
Lushnikova T., van Ommen G.J.B., Goodman R.H., Deaven L.L.,
Doggett N.A., Peters D.J.M., Breuning M.H.;
"Construction of a 1.2-Mb contig surrounding, and molecular analysis
of, the human CREB-binding protein (CBP/CREBBP) gene on chromosome
16p13.3.";
Genomics 42:96-114(1997).
[3]
SEQUENCE REVISION TO 1724-1725; 1789 AND 1812.
Petrij F., den Hollander A.I., Chrivia J.C.;
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
"Preparation of a set of expression-ready clones of mammalian long
cDNAs encoding large proteins by the ORF trap cloning method.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-405, AND CHROMOSOMAL TRANSLOCATION
WITH KAT6A.
PubMed=8782817; DOI=10.1038/ng0996-33;
Borrow J., Stanton V.P. Jr., Andresen J.M., Becher R., Behm F.G.,
Chaganti R.S.K., Civin C.I., Disteche C., Dube I., Frischauf A.M.,
Horsman D., Mitelman F., Volinia S., Watmore A.E., Housman D.E.;
"The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a
putative acetyltransferase to the CREB-binding protein.";
Nat. Genet. 14:33-41(1996).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-83, AND CHROMOSOMAL TRANSLOCATION WITH
KAT6B.
PubMed=11157802; DOI=10.1093/hmg/10.4.395;
Panagopoulos I., Fioretos T., Isaksson M., Samuelsson U.,
Billstroem R., Stroembeck B., Mitelman F., Johansson B.;
"Fusion of the MORF and CBP genes in acute myeloid leukemia with the
t(10;16)(q22;p13).";
Hum. Mol. Genet. 10:395-404(2001).
[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 EP300.
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 DHX9.
PubMed=9323138; DOI=10.1016/S0092-8674(00)80376-1;
Nakajima T., Uchida C., Anderson S.F., Lee C.-G., Hurwitz J.,
Parvin J.D., Montminy M.;
"RNA helicase A mediates association of CBP with RNA polymerase II.";
Cell 90:1107-1112(1997).
[11]
INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION).
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).
[12]
INTERACTION WITH KLF1, AND FUNCTION.
PubMed=9707565; DOI=10.1073/pnas.95.17.9855;
Zhang W., Bieker J.J.;
"Acetylation and modulation of erythroid Krueppel-like factor (EKLF)
activity by interaction with histone acetyltransferases.";
Proc. Natl. Acad. Sci. U.S.A. 95:9855-9860(1998).
[13]
INTERACTION WITH SRCAP.
PubMed=10347196; DOI=10.1074/jbc.274.23.16370;
Johnston H., Kneer J., Chackalaparampil I., Yaciuk P., Chrivia J.;
"Identification of a novel SNF2/SWI2 protein family member, SRCAP,
which interacts with CREB-binding protein.";
J. Biol. Chem. 274:16370-16376(1999).
[14]
INTERACTION WITH PML.
PubMed=10077561; DOI=10.1073/pnas.96.6.2627;
Doucas V., Tini M., Egan D.A., Evans R.M.;
"Modulation of CREB binding protein function by the promyelocytic
(PML) oncoprotein suggests a role for nuclear bodies in hormone
signaling.";
Proc. Natl. Acad. Sci. U.S.A. 96:2627-2632(1999).
[15]
ACETYLATION OF NCOA3.
PubMed=10490106; DOI=10.1016/S0092-8674(00)80054-9;
Chen H., Lin R.J., Xie W., Wilpitz D., Evans R.M.;
"Regulation of hormone-induced histone hyperacetylation and gene
activation via acetylation of an acetylase.";
Cell 98:675-686(1999).
[16]
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).
[17]
INTERACTION WITH NCOA6.
PubMed=10866662; DOI=10.1128/MCB.20.14.5048-5063.2000;
Mahajan M.A., Samuels H.H.;
"A new family of nuclear receptor coregulators that integrates nuclear
receptor signaling through CBP.";
Mol. Cell. Biol. 20:5048-5063(2000).
[18]
INTERACTION WITH MAFG, AND FUNCTION IN ACETYLATION OF MAFG.
PubMed=11154691; DOI=10.1074/jbc.M007846200;
Hung H.-L., Kim A.Y., Hong W., Rakowski C., Blobel G.A.;
"Stimulation of NF-E2 DNA binding by CREB-binding protein (CBP)-
mediated acetylation.";
J. Biol. Chem. 276:10715-10721(2001).
[19]
INTERACTION WITH NFATC4.
PubMed=11514544; DOI=10.1074/jbc.M102961200;
Yang T.T.C., Davis R.J., Chow C.-W.;
"Requirement of two NFATc4 transactivation domains for CBP
potentiation.";
J. Biol. Chem. 276:39569-39576(2001).
[20]
INTERACTION WITH MECOM.
PubMed=11568182; DOI=10.1074/jbc.M106733200;
Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G.;
"Interaction of EVI1 with cAMP-responsive element-binding protein-
binding protein (CBP) and p300/CBP-associated factor (P/CAF) results
in reversible acetylation of EVI1 and in co-localization in nuclear
speckles.";
J. Biol. Chem. 276:44936-44943(2001).
[21]
INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION).
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).
[22]
INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P30II (MICROBIAL INFECTION).
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).
[23]
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).
[24]
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).
[25]
INTERACTION WITH HHV-8 PROTEIN VIRF1 (MICROBIAL INFECTION).
PubMed=11314014; DOI=10.1038/sj.onc.1204163;
Lin R., Genin P., Mamane Y., Sgarbanti M., Battistini A.,
Harrington W.J. Jr., Barber G.N., Hiscott J.;
"HHV-8 encoded vIRF-1 represses the interferon antiviral response by
blocking IRF-3 recruitment of the CBP/p300 coactivators.";
Oncogene 20:800-811(2001).
[26]
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).
[27]
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).
[28]
IDENTIFICATION IN A COMPLEX WITH NCOA2; NCOA3; IKKA; IKKB AND IKBKG.
PubMed=11971985; DOI=10.1128/MCB.22.10.3549-3561.2002;
Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J.,
O'Malley B.W.;
"Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator
activity by I kappa B kinase.";
Mol. Cell. Biol. 22:3549-3561(2002).
[29]
INTERACTION WITH IRF2, AND FUNCTION IN ACETYLATION OF IRF2.
PubMed=12738767; DOI=10.1074/jbc.M213037200;
Masumi A., Yamakawa Y., Fukazawa H., Ozato K., Komuro K.;
"Interferon regulatory factor-2 regulates cell growth through its
acetylation.";
J. Biol. Chem. 278:25401-25407(2003).
[30]
INTERACTION WITH N4BP2.
PubMed=12730195; DOI=10.1074/jbc.M303518200;
Watanabe N., Wachi S., Fujita T.;
"Identification and characterization of BCL-3-binding protein:
implications for transcription and DNA repair or recombination.";
J. Biol. Chem. 278:26102-26110(2003).
[31]
FUNCTION, AND SUBCELLULAR LOCATION.
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).
[32]
FUNCTION, AND INTERACTION WITH NPAS2 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).
[33]
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).
[34]
INTERACTION WITH MLLT7.
PubMed=15126506; DOI=10.1074/jbc.M401138200;
van der Horst A., Tertoolen L.G.J., de Vries-Smits L.M.M., Frye R.A.,
Medema R.H., Burgering B.M.T.;
"FOXO4 is acetylated upon peroxide stress and deacetylated by the
longevity protein hSir2(SIRT1).";
J. Biol. Chem. 279:28873-28879(2004).
[35]
SUBCELLULAR LOCATION.
PubMed=15488321; DOI=10.1016/j.neulet.2004.08.062;
Pradhan A., Liu Y.;
"The calcium-responsive transactivator recruits CREB binding protein
to nuclear bodies.";
Neurosci. Lett. 370:191-195(2004).
[36]
INTERACTION WITH FOXO1.
PubMed=15220471; DOI=10.1073/pnas.0400593101;
Daitoku H., Hatta M., Matsuzaki H., Aratani S., Ohshima T.,
Miyagishi M., Nakajima T., Fukamizu A.;
"Silent information regulator 2 potentiates Foxo1-mediated
transcription through its deacetylase activity.";
Proc. Natl. Acad. Sci. U.S.A. 101:10042-10047(2004).
[37]
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).
[38]
PHOSPHORYLATION AT SER-1382 AND SER-1386 BY CHUK/IKKA.
PubMed=17434128; DOI=10.1016/j.molcel.2007.02.019;
Huang W.C., Ju T.K., Hung M.C., Chen C.C.;
"Phosphorylation of CBP by IKKalpha promotes cell growth by switching
the binding preference of CBP from p53 to NF-kappaB.";
Mol. Cell 26:75-87(2007).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1030, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[40]
INTERACTION WITH MTDH.
PubMed=18316612; DOI=10.1158/0008-5472.CAN-07-6164;
Sarkar D., Park E.S., Emdad L., Lee S.-G., Su Z.-Z., Fisher P.B.;
"Molecular basis of nuclear factor-kappaB activation by astrocyte
elevated gene-1.";
Cancer Res. 68:1478-1484(2008).
[41]
INTERACTION WITH HUMAN T-CELL LEUKEMIA VIRUS 1/HTLV-1 PROTEIN HBZ.
PubMed=18599479; DOI=10.1074/jbc.M803116200;
Clerc I., Polakowski N., Andre-Arpin C., Cook P., Barbeau B.,
Mesnard J.M., Lemasson I.;
"An interaction between the human T cell leukemia virus type 1 basic
leucine zipper factor (HBZ) and the KIX domain of p300/CBP contributes
to the down-regulation of tax-dependent viral transcription by HBZ.";
J. Biol. Chem. 283:23903-23913(2008).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-2063; SER-2076
AND SER-2079, AND 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).
[43]
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).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2063, AND 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).
[45]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1014; LYS-1216; LYS-1583;
LYS-1591; LYS-1592; LYS-1595; LYS-1597; LYS-1741 AND LYS-1744, 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).
[46]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[47]
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).
[48]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[49]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1076; SER-1763 AND
SER-2063, 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).
[50]
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).
[51]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-220, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[52]
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).
[53]
FUNCTION, AND INTERACTION WITH SMAD4.
PubMed=25514493; DOI=10.1016/j.bbagrm.2014.12.008;
Yang Y., Cui J., Xue F., Zhang C., Mei Z., Wang Y., Bi M., Shan D.,
Meredith A., Li H., Xu Z.Q.;
"Pokemon (FBI-1) interacts with Smad4 to repress TGF-beta-induced
transcriptional responses.";
Biochim. Biophys. Acta 1849:270-281(2015).
[54]
STRUCTURE BY NMR OF 345-439 IN COMPLEX WITH 776-826 OF HIF1A.
PubMed=11959977; DOI=10.1073/pnas.082121399;
Dames S.A., Martinez-Yamout M., De Guzman R.N., Dyson H.J.,
Wright P.E.;
"Structural basis for Hif-1 alpha /CBP recognition in the cellular
hypoxic response.";
Proc. Natl. Acad. Sci. U.S.A. 99:5271-5276(2002).
[55]
CHROMOSOMAL TRANSLOCATION WITH KAT6A.
PubMed=11742995; DOI=10.1093/emboj/20.24.7184;
Kitabayashi I., Aikawa Y., Nguyen L.A., Yokoyama A., Ohki M.;
"Activation of AML1-mediated transcription by MOZ and inhibition by
the MOZ-CBP fusion protein.";
EMBO J. 20:7184-7196(2001).
[56]
STRUCTURE BY NMR OF 589-679 IN COMPLEX WITH HIV-1 TAT (MICROBIAL
INFECTION).
PubMed=14744133; DOI=10.1021/bi035612l;
Vendel A.C., Lumb K.J.;
"NMR mapping of the HIV-1 Tat interaction surface of the KIX domain of
the human coactivator CBP.";
Biochemistry 43:904-908(2004).
[57]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1081-1197.
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).
[58]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 1082-1197, FUNCTION,
INTERACTION WITH ASF1A; ASF1B; ACETYLATED HISTONES AND TP53,
MUTAGENESIS OF ASP-1116; PHE-1126; ASN-1162; TRP-1165; SER-1179;
LYS-1180 AND GLU-1183, CHARACTERIZATION OF VARIANT RSTS1 CYS-1175,
CATALYTIC ACTIVITY, AND AUTOACETYLATION.
PubMed=24616510; DOI=10.1073/pnas.1319122111;
Das C., Roy S., Namjoshi S., Malarkey C.S., Jones D.N.,
Kutateladze T.G., Churchill M.E., Tyler J.K.;
"Binding of the histone chaperone ASF1 to the CBP bromodomain promotes
histone acetylation.";
Proc. Natl. Acad. Sci. U.S.A. 111:E1072-E1081(2014).
[59]
X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 1080-1316 IN COMPLEX WITH
ZINC.
PubMed=24361270; DOI=10.1016/j.str.2013.10.021;
Plotnikov A.N., Yang S., Zhou T.J., Rusinova E., Frasca A., Zhou M.M.;
"Structural insights into acetylated-histone H4 recognition by the
bromodomain-PHD finger module of human transcriptional coactivator
CBP.";
Structure 22:353-360(2014).
[60]
VARIANT RSTS1 PRO-1378.
PubMed=11331617; DOI=10.1093/hmg/10.10.1071;
Murata T., Kurokawa R., Krones A., Tatsumi K., Ishii M., Taki T.,
Masuno M., Ohashi H., Yanagisawa M., Rosenfeld M.G., Glass C.K.,
Hayashi Y.;
"Defect of histone acetyltransferase activity of the nuclear
transcriptional coactivator CBP in Rubinstein-Taybi syndrome.";
Hum. Mol. Genet. 10:1071-1076(2001).
[61]
VARIANT RSTS1 CYS-1175.
PubMed=12114483; DOI=10.1136/jmg.39.7.496;
Bartsch O., Locher K., Meinecke P., Kress W., Seemanova E., Wagner A.,
Ostermann K., Roedel G.;
"Molecular studies in 10 cases of Rubinstein-Taybi syndrome, including
a mild variant showing a missense mutation in codon 1175 of CREBBP.";
J. Med. Genet. 39:496-501(2002).
[62]
VARIANTS RSTS1 LYS-1278 AND HIS-1664, AND CHARACTERIZATION OF VARIANTS
RSTS1 LYS-1278 AND HIS-1664.
PubMed=12566391; DOI=10.1093/hmg/ddg039;
Kalkhoven E., Roelfsema J.H., Teunissen H., den Boer A., Ariyuerek Y.,
Zantema A., Breuning M.H., Hennekam R.C.M., Peters D.J.M.;
"Loss of CBP acetyltransferase activity by PHD finger mutations in
Rubinstein-Taybi syndrome.";
Hum. Mol. Genet. 12:441-450(2003).
[63]
VARIANTS RSTS1 LYS-1278; ILE-1447; HIS-1450; ARG-1470 AND HIS-1664.
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).
[64]
VARIANT RSTS1 ALA-910.
PubMed=20684013; DOI=10.1002/ajmg.a.33598;
Bartsch O., Kress W., Kempf O., Lechno S., Haaf T., Zechner U.;
"Inheritance and variable expression in Rubinstein-Taybi syndrome.";
Am. J. Med. Genet. A 152A:2254-2261(2010).
[65]
VARIANTS HIS-503; THR-532 AND ASN-546, AND VARIANTS RSTS1 PHE-650;
THR-789; CYS-1175; ALA-1278; PRO-1378; TYR-1406; PRO-1415; THR-1475;
PHE-1503; PRO-1507 AND ASN-1543.
PubMed=25388907; DOI=10.1111/cge.12537;
Spena S., Milani D., Rusconi D., Negri G., Colapietro P., Elcioglu N.,
Bedeschi F., Pilotta A., Spaccini L., Ficcadenti A., Magnani C.,
Scarano G., Selicorni A., Larizza L., Gervasini C.;
"Insights into genotype-phenotype correlations from CREBBP point
mutation screening in a cohort of 46 Rubinstein-Taybi syndrome
patients.";
Clin. Genet. 88:431-440(2015).
[66]
INVOLVEMENT IN RUBINSTEIN-TAYBI-LIKE SYNDROME, AND VARIANTS ARG-1710;
ARG-1747; PRO-1786; PHE-1819; TRP-1826; TYR-1838; GLN-1867; TRP-1867;
TRP-1868 AND VAL-1872.
PubMed=27311832; DOI=10.1002/ajmg.a.37800;
DDD Study;
Menke L.A., van Belzen M.J., Alders M., Cristofoli F., Ehmke N.,
Fergelot P., Foster A., Gerkes E.H., Hoffer M.J., Horn D., Kant S.G.,
Lacombe D., Leon E., Maas S.M., Melis D., Muto V., Park S.M.,
Peeters H., Peters D.J., Pfundt R., van Ravenswaaij-Arts C.M.,
Tartaglia M., Hennekam R.C.;
"CREBBP mutations in individuals without Rubinstein-Taybi syndrome
phenotype.";
Am. J. Med. Genet. A 170:2681-2693(2016).
-!- FUNCTION: Acetylates histones, giving a specific tag for
transcriptional activation. Also acetylates non-histone proteins,
like NCOA3 and FOXO1. Binds specifically to phosphorylated CREB
and enhances its transcriptional activity toward cAMP-responsive
genes. Acts as a coactivator of ALX1. Acts as a circadian
transcriptional coactivator which enhances the activity of the
circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-
ARNTL/BMAL1 heterodimers. Acetylates PCNA; acetylation promotes
removal of chromatin-bound PCNA and its degradation during
nucleotide excision repair (NER) (PubMed:24939902). Functions as a
transcriptional coactivator for SMAD4 in the TGF-beta signaling
pathway (PubMed:25514493). {ECO:0000269|PubMed:11154691,
ECO:0000269|PubMed:12738767, ECO:0000269|PubMed:12929931,
ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:24939902,
ECO:0000269|PubMed:25514493, ECO:0000269|PubMed:9707565}.
-!- CATALYTIC ACTIVITY:
Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-
acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-
COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378,
ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
ChEBI:CHEBI:61930; EC=2.3.1.48;
Evidence={ECO:0000269|PubMed:24616510};
-!- SUBUNIT: Found in a complex containing NCOA2; NCOA3; IKKA; IKKB
and IKBKG. Probably part of a complex with HIF1A and EP300.
Interacts with GATA1; the interaction results in acetylation and
enhancement of transcriptional activity of GATA1. Interacts with
MAF AND ZCCHC12. Interacts with DAXX; the interaction is dependent
on CBP sumoylation and results in suppression of the
transcriptional activity via recruitment of HDAC2 to DAXX (By
similarity). Interacts with phosphorylated CREB1. Interacts with
CITED4 (C-terminal region). Interacts (via the TAZ-type 1 domain)
with HIF1A. Interacts with SRCAP, CARM1, ELF3, MLLT7/FOXO4, N4BP2,
NCOA1, NCOA3, NCOA6, PCAF, DDX5, DDX17, PELP1, PML, SMAD1, SMAD2,
SMAD3, SPIB and TRERF1. Interacts with KLF1; the interaction
results in acetylation of KLF1 and enhancement of its
transcriptional activity. Interacts with MTDH. Interacts with
NFATC4. Interacts with MAFG; the interaction acetylates MAFG in
the basic region and stimulates NFE2 transcriptional activity
through increasing its DNA-binding activity. Interacts with IRF2;
the interaction acetylates IRF2 and regulates its activity on the
H4 promoter. Interacts (via N-terminus) with SS18L1/CREST (via C-
terminus). Interacts with MECOM. Interacts with CITED1 (via C-
terminus). Interacts with FOXO1; the interaction acetylates FOXO1
and inhibits its transcriptional activity. Interacts with NPAS2,
CLOCK and ARNTL/BMAL1. Interacts with ASF1A and ASF1B; this
promotes histone acetylation. Interacts with acetylated TP53/p53
and with the acetylated histones H3 and H4. Interacts (via
transactivation domain and C-terminus) with PCNA; the interaction
occurs on chromatin in UV-irradiated damaged cells
(PubMed:24939902). Interacts with DHX9 (via N-terminus); this
interaction mediates association with RNA polymerase II holoenzyme
and stimulates CREB-dependent transcriptional activation
(PubMed:9323138). Interacts with SMAD4; negatively regulated by
ZBTB7A (PubMed:25514493). {ECO:0000250,
ECO:0000269|PubMed:10077561, ECO:0000269|PubMed:10347196,
ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:10866662,
ECO:0000269|PubMed:11154691, ECO:0000269|PubMed:11349124,
ECO:0000269|PubMed:11481323, ECO:0000269|PubMed:11514544,
ECO:0000269|PubMed:11568182, ECO:0000269|PubMed:11744733,
ECO:0000269|PubMed:11864910, ECO:0000269|PubMed:11959977,
ECO:0000269|PubMed:11971985, ECO:0000269|PubMed:12730195,
ECO:0000269|PubMed:12738767, ECO:0000269|PubMed:14645221,
ECO:0000269|PubMed:14716005, ECO:0000269|PubMed:15075319,
ECO:0000269|PubMed:15126506, ECO:0000269|PubMed:15220471,
ECO:0000269|PubMed:18316612, ECO:0000269|PubMed:24616510,
ECO:0000269|PubMed:24939902, ECO:0000269|PubMed:25514493,
ECO:0000269|PubMed:8684459, ECO:0000269|PubMed:8917528,
ECO:0000269|PubMed:9323138, ECO:0000269|PubMed:9707565}.
-!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 Tax, p30II
and HBZ. {ECO:0000269|PubMed:11463834,
ECO:0000269|PubMed:11559821, ECO:0000269|PubMed:9528808}.
-!- SUBUNIT: (Microbial infection) Interacts with human herpes virus
8/HHV-8 protein vIRF-1; this interaction inhibits CREBBP binding
to IRF3. {ECO:0000269|PubMed:11314014}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat.
{ECO:0000269|PubMed:14744133}.
-!- INTERACTION:
P03070:- (xeno); NbExp=2; IntAct=EBI-81215, EBI-617698;
P03255:- (xeno); NbExp=3; IntAct=EBI-81215, EBI-2603114;
P03259:- (xeno); NbExp=5; IntAct=EBI-81215, EBI-6947456;
P03259-2:- (xeno); NbExp=3; IntAct=EBI-81215, EBI-7225021;
P31749:AKT1; NbExp=3; IntAct=EBI-81215, EBI-296087;
P10275:AR; NbExp=2; IntAct=EBI-81215, EBI-608057;
P61201:COPS2; NbExp=3; IntAct=EBI-81215, EBI-1050386;
P16220:CREB1; NbExp=3; IntAct=EBI-81215, EBI-711855;
P35222:CTNNB1; NbExp=2; IntAct=EBI-81215, EBI-491549;
Q9UER7:DAXX; NbExp=2; IntAct=EBI-81215, EBI-77321;
Q12778:FOXO1; NbExp=3; IntAct=EBI-81215, EBI-1108782;
O43524:FOXO3; NbExp=3; IntAct=EBI-81215, EBI-1644164;
Q16665:HIF1A; NbExp=2; IntAct=EBI-81215, EBI-447269;
P62805:HIST2H4B; NbExp=6; IntAct=EBI-81215, EBI-302023;
P42858:HTT; NbExp=2; IntAct=EBI-81215, EBI-466029;
P48551:IFNAR2; NbExp=4; IntAct=EBI-81215, EBI-958408;
O14920:IKBKB; NbExp=2; IntAct=EBI-81215, EBI-81266;
Q14653:IRF3; NbExp=10; IntAct=EBI-81215, EBI-2650369;
Q13568:IRF5; NbExp=3; IntAct=EBI-81215, EBI-3931258;
Q92831:KAT2B; NbExp=4; IntAct=EBI-81215, EBI-477430;
Q13351:KLF1; NbExp=2; IntAct=EBI-81215, EBI-8284732;
Q86UE4:MTDH; NbExp=2; IntAct=EBI-81215, EBI-1046588;
P55209:NAP1L1; NbExp=3; IntAct=EBI-81215, EBI-356392;
Q14686:NCOA6; NbExp=2; IntAct=EBI-81215, EBI-78670;
Q04206:RELA; NbExp=5; IntAct=EBI-81215, EBI-73886;
O95863:SNAI1; NbExp=9; IntAct=EBI-81215, EBI-1045459;
P36956-1:SREBF1; NbExp=3; IntAct=EBI-81215, EBI-948328;
P36956-3:SREBF1; NbExp=2; IntAct=EBI-81215, EBI-948338;
Q12772:SREBF2; NbExp=2; IntAct=EBI-81215, EBI-465059;
P04608:tat (xeno); NbExp=2; IntAct=EBI-81215, EBI-6164389;
Q9UL17:TBX21; NbExp=4; IntAct=EBI-81215, EBI-3922312;
P04637:TP53; NbExp=11; IntAct=EBI-81215, EBI-366083;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Recruited to
nuclear bodies by SS18L1/CREST. In the presence of ALX1
relocalizes from the cytoplasm to the nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q92793-1; Sequence=Displayed;
Name=2;
IsoId=Q92793-2; Sequence=VSP_045700;
Note=No experimental confirmation available.;
-!- DOMAIN: The KIX domain mediates binding to HIV-1 Tat.
-!- PTM: Methylation of the KIX domain by CARM1 blocks association
with CREB. This results in the blockade of CREB signaling, and in
activation of apoptotic response (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated by CHUK/IKKA at Ser-1382 and Ser-1386; these
phosphorylations promote cell growth by switching the binding
preference of CREBBP from TP53 to NF-kappa-B.
{ECO:0000269|PubMed:17434128}.
-!- PTM: Sumoylation negatively regulates transcriptional activity via
the recruitment of DAAX. {ECO:0000250}.
-!- PTM: Autoacetylation is required for binding to protein
substrates, such as acetylated histones and acetylated TP53/p53.
{ECO:0000269|PubMed:24616510}.
-!- DISEASE: Note=Chromosomal aberrations involving CREBBP may be a
cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13)
with KAT6A; translocation t(11;16)(q23;p13.3) with KMT2A/MLL1;
translocation t(10;16)(q22;p13) with KAT6B. KAT6A-CREBBP may
induce leukemia by inhibiting RUNX1-mediated transcription.
-!- DISEASE: Rubinstein-Taybi syndrome 1 (RSTS1) [MIM:180849]: A
disorder characterized by craniofacial abnormalities, postnatal
growth deficiency, broad thumbs, broad big toes, mental
retardation and a propensity for development of malignancies.
{ECO:0000269|PubMed:11331617, ECO:0000269|PubMed:12114483,
ECO:0000269|PubMed:12566391, ECO:0000269|PubMed:15706485,
ECO:0000269|PubMed:20684013, ECO:0000269|PubMed:24616510,
ECO:0000269|PubMed:25388907}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=De novo missense mutations in the last part of exon
30 or beginning of exon 31 are associated with growth retardation,
craniofacial dysmorphism and additional Rubinstein-Taybi-like
features. No patients have broad thumbs. Patients have
intellectual disability of variable severity, a marked speech
delay, short stature and microcephaly. Main facial characteristics
include short palpebral fissures, telecanthi, depressed nasal
ridge, short nose, anteverted nares, short columella and long
philtrum. {ECO:0000269|PubMed:27311832}.
-!- SEQUENCE CAUTION:
Sequence=BAE06125.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CBPID42.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=P300/CBP entry;
URL="https://en.wikipedia.org/wiki/P300/CBP";
-----------------------------------------------------------------------
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EMBL; U85962; AAC51331.2; -; mRNA.
EMBL; U89354; AAC51339.1; -; mRNA.
EMBL; U89355; AAC51340.1; -; mRNA.
EMBL; U47741; AAC51770.1; -; mRNA.
EMBL; AB210043; BAE06125.1; ALT_INIT; mRNA.
EMBL; CH471112; EAW85335.1; -; Genomic_DNA.
EMBL; CH471112; EAW85336.1; -; Genomic_DNA.
EMBL; CH471112; EAW85337.1; -; Genomic_DNA.
CCDS; CCDS10509.1; -. [Q92793-1]
CCDS; CCDS45399.1; -. [Q92793-2]
PIR; S39162; S39162.
RefSeq; NP_001073315.1; NM_001079846.1. [Q92793-2]
RefSeq; NP_004371.2; NM_004380.2. [Q92793-1]
UniGene; Hs.459759; -.
PDB; 1JSP; NMR; -; B=1081-1197.
PDB; 1LIQ; NMR; -; A=376-402.
PDB; 1RDT; X-ray; 2.40 A; E=58-80.
PDB; 1WO3; NMR; -; A=387-398.
PDB; 1WO4; NMR; -; A=387-398.
PDB; 1WO5; NMR; -; A=387-398.
PDB; 1WO6; NMR; -; A=376-400.
PDB; 1WO7; NMR; -; A=376-400.
PDB; 1ZOQ; X-ray; 2.37 A; C/D=2065-2111.
PDB; 2D82; NMR; -; A=1081-1197.
PDB; 2KJE; NMR; -; A=1763-1854.
PDB; 2KWF; NMR; -; A=587-673.
PDB; 2L84; NMR; -; A=1081-1197.
PDB; 2L85; NMR; -; A=1081-1197.
PDB; 2LXS; NMR; -; A=587-673.
PDB; 2LXT; NMR; -; A=587-673.
PDB; 2N1A; NMR; -; B=1699-1751.
PDB; 2RNY; NMR; -; A=1081-1197.
PDB; 3DWY; X-ray; 1.98 A; A/B=1081-1197.
PDB; 3P1C; X-ray; 1.82 A; A/B=1081-1197.
PDB; 3P1D; X-ray; 1.86 A; A/B=1081-1197.
PDB; 3P1E; X-ray; 1.80 A; A/B=1081-1197.
PDB; 3P1F; X-ray; 1.63 A; A/B=1081-1197.
PDB; 3SVH; X-ray; 1.80 A; A/B=1081-1197.
PDB; 4A9K; X-ray; 1.81 A; A/B=1081-1197.
PDB; 4N3W; X-ray; 1.90 A; A=1080-1316.
PDB; 4N4F; X-ray; 1.83 A; A=1080-1316.
PDB; 4NR4; X-ray; 1.69 A; A/B=1081-1197.
PDB; 4NR5; X-ray; 1.66 A; A=1081-1197.
PDB; 4NR6; X-ray; 1.66 A; A=1081-1197.
PDB; 4NR7; X-ray; 1.20 A; A=1081-1197.
PDB; 4NYV; X-ray; 1.83 A; A/B/C/D=1081-1197.
PDB; 4NYW; X-ray; 1.43 A; A=1081-1197.
PDB; 4NYX; X-ray; 1.10 A; A=1081-1197.
PDB; 4OUF; X-ray; 1.40 A; A/B=1082-1197.
PDB; 4TQN; X-ray; 1.70 A; A=1081-1197.
PDB; 4TS8; X-ray; 2.00 A; A=1081-1197.
PDB; 4WHU; X-ray; 2.11 A; A=1081-1197.
PDB; 4YK0; X-ray; 1.65 A; A/B/C/D=1083-1196.
PDB; 5CGP; X-ray; 1.96 A; A=1081-1197.
PDB; 5DBM; X-ray; 1.86 A; A/B/C=1082-1197.
PDB; 5EIC; X-ray; 1.50 A; A/B=1081-1197.
PDB; 5ENG; X-ray; 1.30 A; A=1081-1197.
PDB; 5EP7; X-ray; 1.20 A; A=1081-1197.
PDB; 5GH9; X-ray; 1.45 A; A=1081-1196.
PDB; 5H85; X-ray; 1.70 A; A=1081-1197.
PDB; 5I83; X-ray; 1.35 A; A=1082-1197.
PDB; 5I86; X-ray; 1.05 A; A/B=1082-1197.
PDB; 5I89; X-ray; 1.07 A; A=1082-1197.
PDB; 5I8B; X-ray; 1.52 A; A=1081-1312.
PDB; 5I8G; X-ray; 1.41 A; A=1081-1312.
PDB; 5J0D; X-ray; 1.05 A; A=1081-1197.
PDB; 5JEM; X-ray; 2.50 A; C/D/F/H=2065-2111.
PDB; 5KTU; X-ray; 1.38 A; A/B=1082-1197.
PDB; 5KTW; X-ray; 1.09 A; A/B/C=1085-1194.
PDB; 5KTX; X-ray; 1.27 A; A=1085-1194.
PDB; 5LPJ; X-ray; 1.65 A; A=1081-1197.
PDB; 5LPL; X-ray; 1.65 A; A=1081-1197.
PDB; 5MME; X-ray; 1.35 A; A/B=1081-1197.
PDB; 5MMG; X-ray; 1.23 A; A=1081-1197.
PDB; 5MPK; X-ray; 1.90 A; A/B=1081-1197.
PDB; 5MPN; X-ray; 1.23 A; A=1081-1197.
PDB; 5MPZ; X-ray; 1.40 A; A=1081-1197.
PDB; 5MQE; X-ray; 1.65 A; A/B=1081-1197.
PDB; 5MQG; X-ray; 1.35 A; A/B=1081-1197.
PDB; 5MQK; X-ray; 1.53 A; A/B=1081-1197.
PDB; 5NLK; X-ray; 1.80 A; A=1081-1197.
PDB; 5NRW; X-ray; 1.70 A; A=1081-1197.
PDB; 5NU3; X-ray; 1.75 A; A=1081-1197.
PDB; 5OWK; X-ray; 1.25 A; A=1081-1197.
PDB; 5SVH; X-ray; 2.05 A; A=587-673.
PDB; 5TB6; X-ray; 1.79 A; A=1081-1197.
PDB; 5W0E; X-ray; 1.41 A; A=1082-1197.
PDB; 5W0F; X-ray; 1.60 A; A=1082-1197.
PDB; 5W0L; X-ray; 1.55 A; A/B=1082-1197.
PDB; 5W0Q; X-ray; 1.70 A; A=1082-1197.
PDB; 5XXH; X-ray; 1.62 A; A=1081-1197.
PDB; 6ALB; X-ray; 2.05 A; A=1081-1312.
PDB; 6ALC; X-ray; 1.39 A; A/B=1085-1196.
PDB; 6AXQ; X-ray; 1.30 A; A/B/C/D=1085-1196.
PDB; 6AY3; X-ray; 1.39 A; A/B=1083-1197.
PDB; 6AY5; X-ray; 1.44 A; A=1083-1197.
PDB; 6FQO; X-ray; 1.35 A; A/B=1081-1197.
PDB; 6FQU; X-ray; 1.43 A; A=1081-1197.
PDB; 6FR0; X-ray; 1.50 A; A/B=1081-1197.
PDB; 6FRF; X-ray; 2.10 A; A/B/C/D=1081-1197.
PDBsum; 1JSP; -.
PDBsum; 1LIQ; -.
PDBsum; 1RDT; -.
PDBsum; 1WO3; -.
PDBsum; 1WO4; -.
PDBsum; 1WO5; -.
PDBsum; 1WO6; -.
PDBsum; 1WO7; -.
PDBsum; 1ZOQ; -.
PDBsum; 2D82; -.
PDBsum; 2KJE; -.
PDBsum; 2KWF; -.
PDBsum; 2L84; -.
PDBsum; 2L85; -.
PDBsum; 2LXS; -.
PDBsum; 2LXT; -.
PDBsum; 2N1A; -.
PDBsum; 2RNY; -.
PDBsum; 3DWY; -.
PDBsum; 3P1C; -.
PDBsum; 3P1D; -.
PDBsum; 3P1E; -.
PDBsum; 3P1F; -.
PDBsum; 3SVH; -.
PDBsum; 4A9K; -.
PDBsum; 4N3W; -.
PDBsum; 4N4F; -.
PDBsum; 4NR4; -.
PDBsum; 4NR5; -.
PDBsum; 4NR6; -.
PDBsum; 4NR7; -.
PDBsum; 4NYV; -.
PDBsum; 4NYW; -.
PDBsum; 4NYX; -.
PDBsum; 4OUF; -.
PDBsum; 4TQN; -.
PDBsum; 4TS8; -.
PDBsum; 4WHU; -.
PDBsum; 4YK0; -.
PDBsum; 5CGP; -.
PDBsum; 5DBM; -.
PDBsum; 5EIC; -.
PDBsum; 5ENG; -.
PDBsum; 5EP7; -.
PDBsum; 5GH9; -.
PDBsum; 5H85; -.
PDBsum; 5I83; -.
PDBsum; 5I86; -.
PDBsum; 5I89; -.
PDBsum; 5I8B; -.
PDBsum; 5I8G; -.
PDBsum; 5J0D; -.
PDBsum; 5JEM; -.
PDBsum; 5KTU; -.
PDBsum; 5KTW; -.
PDBsum; 5KTX; -.
PDBsum; 5LPJ; -.
PDBsum; 5LPL; -.
PDBsum; 5MME; -.
PDBsum; 5MMG; -.
PDBsum; 5MPK; -.
PDBsum; 5MPN; -.
PDBsum; 5MPZ; -.
PDBsum; 5MQE; -.
PDBsum; 5MQG; -.
PDBsum; 5MQK; -.
PDBsum; 5NLK; -.
PDBsum; 5NRW; -.
PDBsum; 5NU3; -.
PDBsum; 5OWK; -.
PDBsum; 5SVH; -.
PDBsum; 5TB6; -.
PDBsum; 5W0E; -.
PDBsum; 5W0F; -.
PDBsum; 5W0L; -.
PDBsum; 5W0Q; -.
PDBsum; 5XXH; -.
PDBsum; 6ALB; -.
PDBsum; 6ALC; -.
PDBsum; 6AXQ; -.
PDBsum; 6AY3; -.
PDBsum; 6AY5; -.
PDBsum; 6FQO; -.
PDBsum; 6FQU; -.
PDBsum; 6FR0; -.
PDBsum; 6FRF; -.
ProteinModelPortal; Q92793; -.
SMR; Q92793; -.
BioGrid; 107777; 331.
CORUM; Q92793; -.
DIP; DIP-952N; -.
ELM; Q92793; -.
IntAct; Q92793; 85.
MINT; Q92793; -.
STRING; 9606.ENSP00000262367; -.
BindingDB; Q92793; -.
ChEMBL; CHEMBL5747; -.
GuidetoPHARMACOLOGY; 2734; -.
iPTMnet; Q92793; -.
PhosphoSitePlus; Q92793; -.
BioMuta; CREBBP; -.
DMDM; 116241283; -.
EPD; Q92793; -.
MaxQB; Q92793; -.
PaxDb; Q92793; -.
PeptideAtlas; Q92793; -.
PRIDE; Q92793; -.
ProteomicsDB; 75472; -.
Ensembl; ENST00000262367; ENSP00000262367; ENSG00000005339. [Q92793-1]
Ensembl; ENST00000382070; ENSP00000371502; ENSG00000005339. [Q92793-2]
GeneID; 1387; -.
KEGG; hsa:1387; -.
UCSC; uc002cvv.4; human. [Q92793-1]
CTD; 1387; -.
DisGeNET; 1387; -.
EuPathDB; HostDB:ENSG00000005339.13; -.
GeneCards; CREBBP; -.
GeneReviews; CREBBP; -.
HGNC; HGNC:2348; CREBBP.
HPA; CAB004212; -.
HPA; HPA055861; -.
MalaCards; CREBBP; -.
MIM; 180849; phenotype.
MIM; 600140; gene.
neXtProt; NX_Q92793; -.
OpenTargets; ENSG00000005339; -.
Orphanet; 370026; Acute myeloid leukemia with t(8;16)(p11;p13) translocation.
Orphanet; 353281; Rubinstein-Taybi syndrome due to 16p13.3 microdeletion.
Orphanet; 353277; Rubinstein-Taybi syndrome due to CREBBP mutations.
PharmGKB; PA26866; -.
eggNOG; KOG1778; Eukaryota.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00940000155364; -.
HOGENOM; HOG000111353; -.
HOVERGEN; HBG000185; -.
InParanoid; Q92793; -.
KO; K04498; -.
OMA; RPPNGPM; -.
OrthoDB; EOG091G0L04; -.
PhylomeDB; Q92793; -.
TreeFam; TF101097; -.
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-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-210744; Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
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-350054; Notch-HLH transcription pathway.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
Reactome; R-HSA-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
Reactome; R-HSA-400253; Circadian Clock.
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-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
Reactome; R-HSA-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
Reactome; R-HSA-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
Reactome; R-HSA-8941856; RUNX3 regulates NOTCH signaling.
Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-9013695; NOTCH4 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
Reactome; R-HSA-918233; TRAF3-dependent IRF activation pathway.
Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
SignaLink; Q92793; -.
SIGNOR; Q92793; -.
ChiTaRS; CREBBP; human.
EvolutionaryTrace; Q92793; -.
GeneWiki; CREB-binding_protein; -.
GenomeRNAi; 1387; -.
PRO; PR:Q92793; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000005339; Expressed in 241 organ(s), highest expression level in testis.
CleanEx; HS_CREBBP; -.
ExpressionAtlas; Q92793; baseline and differential.
Genevisible; Q92793; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0000123; C:histone acetyltransferase complex; IEA:InterPro.
GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
GO; GO:0043426; F:MRF binding; IDA:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
GO; GO:0034212; F:peptide N-acetyltransferase activity; TAS:Reactome.
GO; GO:0001078; F:proximal promoter DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:BHF-UCL.
GO; GO:0000987; F:proximal promoter sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; TAS:BHF-UCL.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
GO; GO:0042733; P:embryonic digit morphogenesis; TAS:BHF-UCL.
GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
GO; GO:0042592; P:homeostatic process; NAS:UniProtKB.
GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; TAS:Reactome.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; TAS:Reactome.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP: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:0065003; P:protein-containing complex assembly; TAS:ProtInc.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0045637; P:regulation of myeloid cell differentiation; TAS:Reactome.
GO; GO:0008589; P:regulation of smoothened signaling pathway; TAS:BHF-UCL.
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:HGNC.
GO; GO:0001666; P:response to hypoxia; TAS:UniProtKB.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; 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; -; 2.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 2.10.110.40; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR031162; CBP_P300_HAT.
InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
InterPro; IPR003101; KIX_dom.
InterPro; IPR036529; KIX_dom_sf.
InterPro; IPR009110; Nuc_rcpt_coact.
InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
InterPro; IPR037073; Nuc_rcpt_coact_CREBbp_sf.
InterPro; IPR010303; RING_CBP-p300.
InterPro; IPR038547; RING_CBP-p300_sf.
InterPro; IPR035898; TAZ_dom_sf.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; Activator; Acyltransferase;
Alternative splicing; Biological rhythms; Bromodomain;
Chromosomal rearrangement; Complete proteome; Cytoplasm;
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:22814378}.
CHAIN 2 2442 CREB-binding protein.
/FTId=PRO_0000211190.
DOMAIN 587 666 KIX. {ECO:0000255|PROSITE-
ProRule:PRU00311}.
DOMAIN 1103 1175 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 1323 1700 CBP/p300-type HAT. {ECO:0000255|PROSITE-
ProRule:PRU01065}.
ZN_FING 347 433 TAZ-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00203}.
ZN_FING 1701 1744 ZZ-type. {ECO:0000255|PROSITE-
ProRule:PRU00228}.
ZN_FING 1765 1846 TAZ-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00203}.
REGION 227 410 Interaction with SRCAP.
{ECO:0000269|PubMed:10347196}.
REGION 1124 1170 Interaction with histone.
{ECO:0000269|PubMed:24361270}.
REGION 1162 1180 Interaction with ASF1A.
{ECO:0000269|PubMed:24616510}.
REGION 1433 1435 Interaction with histone.
{ECO:0000250|UniProtKB:Q09472}.
REGION 1434 1436 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q09472}.
REGION 1446 1447 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q09472}.
REGION 1460 1891 Interaction with TRERF1.
{ECO:0000269|PubMed:11349124}.
COMPBIAS 1061 1064 Poly-Glu.
COMPBIAS 1199 1487 Cys/His-rich.
COMPBIAS 1555 1562 Poly-Glu.
COMPBIAS 1943 1948 Poly-Pro.
COMPBIAS 1967 1970 Poly-Gln.
COMPBIAS 2081 2085 Poly-Gln.
COMPBIAS 2199 2216 Poly-Gln.
COMPBIAS 2245 2248 Poly-Gln.
COMPBIAS 2297 2300 Poly-Gln.
METAL 363 363 Zinc 1. {ECO:0000250}.
METAL 367 367 Zinc 1. {ECO:0000250}.
METAL 380 380 Zinc 1. {ECO:0000250}.
METAL 385 385 Zinc 1. {ECO:0000250}.
METAL 394 394 Zinc 2. {ECO:0000250}.
METAL 398 398 Zinc 2. {ECO:0000250}.
METAL 404 404 Zinc 2. {ECO:0000250}.
METAL 409 409 Zinc 2. {ECO:0000250}.
METAL 418 418 Zinc 3. {ECO:0000250}.
METAL 422 422 Zinc 3. {ECO:0000250}.
METAL 427 427 Zinc 3. {ECO:0000250}.
METAL 430 430 Zinc 3. {ECO:0000250}.
BINDING 1493 1493 Acetyl-CoA; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q09472}.
BINDING 1498 1498 Acetyl-CoA.
{ECO:0000250|UniProtKB:Q09472}.
BINDING 1502 1502 Acetyl-CoA.
{ECO:0000250|UniProtKB:Q09472}.
SITE 29 30 Breakpoint for translocation to form
KAT6B-CREBBP.
SITE 266 267 Breakpoint for translocation to form
KAT6A-CREBBP.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 121 121 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 220 220 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 601 601 Omega-N-methylated arginine.
{ECO:0000250}.
MOD_RES 625 625 Omega-N-methylated arginine.
{ECO:0000250}.
MOD_RES 657 657 N6-acetyllysine.
{ECO:0000250|UniProtKB:P45481}.
MOD_RES 1014 1014 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1030 1030 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 1076 1076 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1216 1216 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1382 1382 Phosphoserine; by IKKA.
{ECO:0000269|PubMed:17434128}.
MOD_RES 1386 1386 Phosphoserine; by IKKA.
{ECO:0000269|PubMed:17434128}.
MOD_RES 1583 1583 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1591 1591 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1592 1592 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1595 1595 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1597 1597 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1741 1741 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1744 1744 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1763 1763 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2063 2063 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 2076 2076 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2079 2079 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2351 2351 Phosphoserine.
{ECO:0000250|UniProtKB:P45481}.
CROSSLNK 998 998 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P45481}.
CROSSLNK 1033 1033 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P45481}.
CROSSLNK 1056 1056 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P45481}.
VAR_SEQ 406 444 VAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQT
-> A (in isoform 2). {ECO:0000303|Ref.4}.
/FTId=VSP_045700.
VARIANT 503 503 Q -> H (in dbSNP:rs748447855).
{ECO:0000269|PubMed:25388907}.
/FTId=VAR_072912.
VARIANT 532 532 P -> T (in dbSNP:rs902901184).
{ECO:0000269|PubMed:25388907}.
/FTId=VAR_072913.
VARIANT 546 546 I -> N. {ECO:0000269|PubMed:25388907}.
/FTId=VAR_072914.
VARIANT 650 650 Y -> F (in RSTS1).
{ECO:0000269|PubMed:25388907}.
/FTId=VAR_072915.
VARIANT 789 789 A -> T (in RSTS1; dbSNP:rs746728741).
{ECO:0000269|PubMed:25388907}.
/FTId=VAR_072916.
VARIANT 910 910 T -> A (in RSTS1; incomplete;
dbSNP:rs143247685).
{ECO:0000269|PubMed:20684013}.
/FTId=VAR_072917.
VARIANT 1175 1175 Y -> C (in RSTS1; mild form; impairs
binding to ASF1A and acetylated histone
H3; dbSNP:rs28937315).
{ECO:0000269|PubMed:12114483,
ECO:0000269|PubMed:24616510,
ECO:0000269|PubMed:25388907}.
/FTId=VAR_037305.
VARIANT 1278 1278 E -> A (in RSTS1).
{ECO:0000269|PubMed:25388907}.
/FTId=VAR_072918.
VARIANT 1278 1278 E -> K (in RSTS1; abolishes
acetyltransferase activity;
dbSNP:rs267606752).
{ECO:0000269|PubMed:12566391,
ECO:0000269|PubMed:15706485}.
/FTId=VAR_035080.
VARIANT 1378 1378 R -> P (in RSTS1; abolishes
acetyltransferase activity and the
ability of transactivate CREB;
dbSNP:rs121434626).
{ECO:0000269|PubMed:11331617,
ECO:0000269|PubMed:25388907}.
/FTId=VAR_015578.
VARIANT 1406 1406 D -> Y (in RSTS1).
{ECO:0000269|PubMed:25388907}.
/FTId=VAR_072919.
VARIANT 1414 1414 V -> I (in dbSNP:rs130015).
/FTId=VAR_027953.
VARIANT 1415 1415 Q -> P (in RSTS1).
{ECO:0000269|PubMed:25388907}.
/FTId=VAR_072920.
VARIANT 1447 1447 T -> I (in RSTS1).
{ECO:0000269|PubMed:15706485}.
/FTId=VAR_035081.
VARIANT 1450 1450 Y -> H (in RSTS1).
{ECO:0000269|PubMed:15706485}.
/FTId=VAR_035082.
VARIANT 1470 1470 H -> R (in RSTS1; dbSNP:rs797044860).
{ECO:0000269|PubMed:15706485}.
/FTId=VAR_035083.
VARIANT 1475 1475 P -> T (in RSTS1).
{ECO:0000269|PubMed:25388907}.
/FTId=VAR_072921.
VARIANT 1503 1503 Y -> F (in RSTS1).
{ECO:0000269|PubMed:25388907}.
/FTId=VAR_072922.
VARIANT 1507 1507 L -> P (in RSTS1; dbSNP:rs1057520191).
{ECO:0000269|PubMed:25388907}.
/FTId=VAR_072923.
VARIANT 1543 1543 D -> N (in RSTS1).
{ECO:0000269|PubMed:25388907}.
/FTId=VAR_072924.
VARIANT 1664 1664 R -> H (in RSTS1; abolishes
acetyltransferase activity).
{ECO:0000269|PubMed:12566391,
ECO:0000269|PubMed:15706485}.
/FTId=VAR_035084.
VARIANT 1710 1710 C -> R (probable disease-associated
mutation found in patient with growth
retardation, craniofacial dysmorphism and
additional Rubinstein-Taybi-like
features; de novo mutation).
{ECO:0000269|PubMed:27311832}.
/FTId=VAR_078557.
VARIANT 1747 1747 L -> R (probable disease-associated
mutation found in patient with growth
retardation, craniofacial dysmorphism and
additional Rubinstein-Taybi-like
features; de novo mutation).
{ECO:0000269|PubMed:27311832}.
/FTId=VAR_078558.
VARIANT 1786 1786 R -> P (probable disease-associated
mutation found in patient with growth
retardation, craniofacial dysmorphism and
additional Rubinstein-Taybi-like
features; de novo mutation).
{ECO:0000269|PubMed:27311832}.
/FTId=VAR_078559.
VARIANT 1819 1819 C -> F (probable disease-associated
mutation found in patient with growth
retardation, craniofacial dysmorphism and
additional Rubinstein-Taybi-like
features; de novo mutation).
{ECO:0000269|PubMed:27311832}.
/FTId=VAR_078560.
VARIANT 1826 1826 C -> W (probable disease-associated
mutation found in patient with growth
retardation, craniofacial dysmorphism and
additional Rubinstein-Taybi-like
features; de novo mutation).
{ECO:0000269|PubMed:27311832}.
/FTId=VAR_078561.
VARIANT 1838 1838 C -> Y (probable disease-associated
mutation found in patient with growth
retardation, craniofacial dysmorphism and
additional Rubinstein-Taybi-like
features; de novo mutation).
{ECO:0000269|PubMed:27311832}.
/FTId=VAR_078562.
VARIANT 1867 1867 R -> Q (probable disease-associated
mutation found in patient with growth
retardation, craniofacial dysmorphism and
additional Rubinstein-Taybi-like
features; de novo mutation;
dbSNP:rs1131691326).
{ECO:0000269|PubMed:27311832}.
/FTId=VAR_078563.
VARIANT 1867 1867 R -> W (probable disease-associated
mutation found in patient with growth
retardation, craniofacial dysmorphism and
additional Rubinstein-Taybi-like
features; de novo mutation).
{ECO:0000269|PubMed:27311832}.
/FTId=VAR_078564.
VARIANT 1868 1868 R -> W (probable disease-associated
mutation found in patient with growth
retardation, craniofacial dysmorphism and
additional Rubinstein-Taybi-like
features; de novo mutation;
dbSNP:rs886039491).
{ECO:0000269|PubMed:27311832}.
/FTId=VAR_078565.
VARIANT 1872 1872 M -> V (probable disease-associated
mutation found in patient with growth
retardation, craniofacial dysmorphism and
additional Rubinstein-Taybi-like
features; de novo mutation;
dbSNP:rs797045037).
{ECO:0000269|PubMed:27311832}.
/FTId=VAR_078566.
MUTAGEN 1116 1116 D->R: Impairs binding to acetylated
histones. {ECO:0000269|PubMed:24616510}.
MUTAGEN 1126 1126 F->A: Impairs binding to acetylated
histones. {ECO:0000269|PubMed:24616510}.
MUTAGEN 1162 1162 N->E,R: Abolishes interaction with ASF1A.
{ECO:0000269|PubMed:24616510}.
MUTAGEN 1165 1165 W->A: Abolishes interaction with ASF1A.
{ECO:0000269|PubMed:24616510}.
MUTAGEN 1170 1170 K->E: Impairs binding to acetylated
histones. {ECO:0000269|PubMed:24616510}.
MUTAGEN 1179 1179 S->I: Impairs interaction with ASF1A.
{ECO:0000269|PubMed:24616510}.
MUTAGEN 1180 1180 K->E: Abolishes interaction with ASF1A.
{ECO:0000269|PubMed:24616510}.
MUTAGEN 1183 1183 E->R: Abolishes interaction with ASF1A.
{ECO:0000269|PubMed:24616510}.
CONFLICT 1511 1513 FAE -> NSG (in Ref. 2; AAC51340).
{ECO:0000305}.
CONFLICT 1724 1725 ED -> VV (in Ref. 2; AAC51340).
{ECO:0000305}.
CONFLICT 1770 1770 L -> V (in Ref. 1; AAC51770).
{ECO:0000305}.
CONFLICT 1789 1789 N -> F (in Ref. 2; AAC51340).
{ECO:0000305}.
CONFLICT 1812 1812 T -> P (in Ref. 2; AAC51340).
{ECO:0000305}.
HELIX 69 73 {ECO:0000244|PDB:1RDT}.
HELIX 377 379 {ECO:0000244|PDB:1LIQ}.
TURN 383 388 {ECO:0000244|PDB:1LIQ}.
HELIX 391 395 {ECO:0000244|PDB:1LIQ}.
HELIX 592 595 {ECO:0000244|PDB:5SVH}.
HELIX 598 612 {ECO:0000244|PDB:5SVH}.
HELIX 618 622 {ECO:0000244|PDB:5SVH}.
HELIX 624 641 {ECO:0000244|PDB:5SVH}.
HELIX 647 670 {ECO:0000244|PDB:5SVH}.
HELIX 1087 1102 {ECO:0000244|PDB:5I86}.
TURN 1105 1108 {ECO:0000244|PDB:5I86}.
HELIX 1109 1111 {ECO:0000244|PDB:5I86}.
HELIX 1117 1120 {ECO:0000244|PDB:5I86}.
HELIX 1125 1128 {ECO:0000244|PDB:5I86}.
HELIX 1135 1143 {ECO:0000244|PDB:5I86}.
STRAND 1146 1149 {ECO:0000244|PDB:2L85}.
HELIX 1150 1167 {ECO:0000244|PDB:5I86}.
TURN 1169 1171 {ECO:0000244|PDB:1JSP}.
HELIX 1173 1195 {ECO:0000244|PDB:5I86}.
STRAND 1214 1218 {ECO:0000244|PDB:5I8G}.
STRAND 1226 1230 {ECO:0000244|PDB:5I8G}.
TURN 1231 1233 {ECO:0000244|PDB:5I8G}.
STRAND 1234 1237 {ECO:0000244|PDB:5I8G}.
TURN 1238 1240 {ECO:0000244|PDB:5I8G}.
STRAND 1266 1272 {ECO:0000244|PDB:5I8G}.
STRAND 1280 1282 {ECO:0000244|PDB:5I8G}.
TURN 1284 1286 {ECO:0000244|PDB:5I8G}.
STRAND 1289 1291 {ECO:0000244|PDB:5I8G}.
HELIX 1292 1295 {ECO:0000244|PDB:5I8G}.
TURN 1309 1311 {ECO:0000244|PDB:5I8G}.
TURN 1708 1710 {ECO:0000244|PDB:2N1A}.
STRAND 1718 1721 {ECO:0000244|PDB:2N1A}.
STRAND 1725 1728 {ECO:0000244|PDB:2N1A}.
HELIX 1730 1736 {ECO:0000244|PDB:2N1A}.
STRAND 1742 1744 {ECO:0000244|PDB:2N1A}.
HELIX 1765 1784 {ECO:0000244|PDB:2KJE}.
HELIX 1793 1805 {ECO:0000244|PDB:2KJE}.
TURN 1811 1815 {ECO:0000244|PDB:2KJE}.
HELIX 1817 1832 {ECO:0000244|PDB:2KJE}.
HELIX 1841 1853 {ECO:0000244|PDB:2KJE}.
HELIX 2066 2072 {ECO:0000244|PDB:1ZOQ}.
HELIX 2080 2091 {ECO:0000244|PDB:1ZOQ}.
HELIX 2094 2103 {ECO:0000244|PDB:1ZOQ}.
TURN 2104 2106 {ECO:0000244|PDB:1ZOQ}.
SEQUENCE 2442 AA; 265351 MW; 3BEA9B8558BA1A5E CRC64;
MAENLLDGPP NPKRAKLSSP GFSANDSTDF GSLFDLENDL PDELIPNGGE LGLLNSGNLV
PDAASKHKQL SELLRGGSGS SINPGIGNVS ASSPVQQGLG GQAQGQPNSA NMASLSAMGK
SPLSQGDSSA PSLPKQAAST SGPTPAASQA LNPQAQKQVG LATSSPATSQ TGPGICMNAN
FNQTHPGLLN SNSGHSLINQ ASQGQAQVMN GSLGAAGRGR GAGMPYPTPA MQGASSSVLA
ETLTQVSPQM TGHAGLNTAQ AGGMAKMGIT GNTSPFGQPF SQAGGQPMGA TGVNPQLASK
QSMVNSLPTF PTDIKNTSVT NVPNMSQMQT SVGIVPTQAI ATGPTADPEK RKLIQQQLVL
LLHAHKCQRR EQANGEVRAC SLPHCRTMKN VLNHMTHCQA GKACQVAHCA SSRQIISHWK
NCTRHDCPVC LPLKNASDKR NQQTILGSPA SGIQNTIGSV GTGQQNATSL SNPNPIDPSS
MQRAYAALGL PYMNQPQTQL QPQVPGQQPA QPQTHQQMRT LNPLGNNPMN IPAGGITTDQ
QPPNLISESA LPTSLGATNP LMNDGSNSGN IGTLSTIPTA APPSSTGVRK GWHEHVTQDL
RSHLVHKLVQ AIFPTPDPAA LKDRRMENLV AYAKKVEGDM YESANSRDEY YHLLAEKIYK
IQKELEEKRR SRLHKQGILG NQPALPAPGA QPPVIPQAQP VRPPNGPLSL PVNRMQVSQG
MNSFNPMSLG NVQLPQAPMG PRAASPMNHS VQMNSMGSVP GMAISPSRMP QPPNMMGAHT
NNMMAQAPAQ SQFLPQNQFP SSSGAMSVGM GQPPAQTGVS QGQVPGAALP NPLNMLGPQA
SQLPCPPVTQ SPLHPTPPPA STAAGMPSLQ HTTPPGMTPP QPAAPTQPST PVSSSGQTPT
PTPGSVPSAT QTQSTPTVQA AAQAQVTPQP QTPVQPPSVA TPQSSQQQPT PVHAQPPGTP
LSQAAASIDN RVPTPSSVAS AETNSQQPGP DVPVLEMKTE TQAEDTEPDP GESKGEPRSE
MMEEDLQGAS QVKEETDIAE QKSEPMEVDE KKPEVKVEVK EEEESSSNGT ASQSTSPSQP
RKKIFKPEEL RQALMPTLEA LYRQDPESLP FRQPVDPQLL GIPDYFDIVK NPMDLSTIKR
KLDTGQYQEP WQYVDDVWLM FNNAWLYNRK TSRVYKFCSK LAEVFEQEID PVMQSLGYCC
GRKYEFSPQT LCCYGKQLCT IPRDAAYYSY QNRYHFCEKC FTEIQGENVT LGDDPSQPQT
TISKDQFEKK KNDTLDPEPF VDCKECGRKM HQICVLHYDI IWPSGFVCDN CLKKTGRPRK
ENKFSAKRLQ TTRLGNHLED RVNKFLRRQN HPEAGEVFVR VVASSDKTVE VKPGMKSRFV
DSGEMSESFP YRTKALFAFE EIDGVDVCFF GMHVQEYGSD CPPPNTRRVY ISYLDSIHFF
RPRCLRTAVY HEILIGYLEY VKKLGYVTGH IWACPPSEGD DYIFHCHPPD QKIPKPKRLQ
EWYKKMLDKA FAERIIHDYK DIFKQATEDR LTSAKELPYF EGDFWPNVLE ESIKELEQEE
EERKKEESTA ASETTEGSQG DSKNAKKKNN KKTNKNKSSI SRANKKKPSM PNVSNDLSQK
LYATMEKHKE VFFVIHLHAG PVINTLPPIV DPDPLLSCDL MDGRDAFLTL ARDKHWEFSS
LRRSKWSTLC MLVELHTQGQ DRFVYTCNEC KHHVETRWHC TVCEDYDLCI NCYNTKSHAH
KMVKWGLGLD DEGSSQGEPQ SKSPQESRRL SIQRCIQSLV HACQCRNANC SLPSCQKMKR
VVQHTKGCKR KTNGGCPVCK QLIALCCYHA KHCQENKCPV PFCLNIKHKL RQQQIQHRLQ
QAQLMRRRMA TMNTRNVPQQ SLPSPTSAPP GTPTQQPSTP QTPQPPAQPQ PSPVSMSPAG
FPSVARTQPP TTVSTGKPTS QVPAPPPPAQ PPPAAVEAAR QIEREAQQQQ HLYRVNINNS
MPPGRTGMGT PGSQMAPVSL NVPRPNQVSG PVMPSMPPGQ WQQAPLPQQQ PMPGLPRPVI
SMQAQAAVAG PRMPSVQPPR SISPSALQDL LRTLKSPSSP QQQQQVLNIL KSNPQLMAAF
IKQRTAKYVA NQPGMQPQPG LQSQPGMQPQ PGMHQQPSLQ NLNAMQAGVP RPGVPPQQQA
MGGLNPQGQA LNIMNPGHNP NMASMNPQYR EMLRRQLLQQ QQQQQQQQQQ QQQQQQGSAG
MAGGMAGHGQ FQQPQGPGGY PPAMQQQQRM QQHLPLQGSS MGQMAAQMGQ LGQMGQPGLG
ADSTPNIQQA LQQRILQQQQ MKQQIGSPGQ PNPMSPQQHM LSGQPQASHL PGQQIATSLS
NQVRSPAPVQ SPRPQSQPPH SSPSPRIQPQ PSPHHVSPQT GSPHPGLAVT MASSIDQGHL
GNPEQSAMLP QLNTPSRSAL SSELSLVGDT TGDTLEKFVE GL


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