CBP_HUMAN
ID CBP_HUMAN Reviewed; 2442 AA.
AC Q92793; D3DUC9; O00147; Q16376; Q4LE28;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 252.
DE RecName: Full=CREB-binding protein;
DE AltName: Full=Histone lysine acetyltransferase CREBBP;
DE EC=2.3.1.48 {ECO:0000269|PubMed:24616510};
DE AltName: Full=Protein-lysine acetyltransferase CREBBP;
DE EC=2.3.1.- {ECO:0000269|PubMed:11154691, ECO:0000269|PubMed:12738767, ECO:0000269|PubMed:24207024, ECO:0000269|PubMed:24939902, ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:30540930};
GN Name=CREBBP; Synonyms=CBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9238046; DOI=10.1073/pnas.94.16.8732;
RA Sobulo O.M., Borrow J., Tomek R., Reshimi S., Harden A., Schlegelberger B.,
RA Housman D., Doggett N.A., Rowley J.D., Zeleznik-Le N.J.;
RT "MLL is fused to CBP, a histone acetyltransferase, in therapy-related acute
RT myeloid leukemia with a t(11;16)(q23;p13.3).";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8732-8737(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9177780; DOI=10.1006/geno.1997.4699;
RA Giles R.H., Petrij F., Dauwerse H.G., den Hollander A.I., Lushnikova T.,
RA van Ommen G.J.B., Goodman R.H., Deaven L.L., Doggett N.A., Peters D.J.M.,
RA Breuning M.H.;
RT "Construction of a 1.2-Mb contig surrounding, and molecular analysis of,
RT the human CREB-binding protein (CBP/CREBBP) gene on chromosome 16p13.3.";
RL Genomics 42:96-114(1997).
RN [3]
RP SEQUENCE REVISION TO 1724-1725; 1789 AND 1812.
RA Petrij F., den Hollander A.I., Chrivia J.C.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT encoding large proteins by the ORF trap cloning method.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-405, AND CHROMOSOMAL TRANSLOCATION WITH
RP KAT6A.
RX PubMed=8782817; DOI=10.1038/ng0996-33;
RA Borrow J., Stanton V.P. Jr., Andresen J.M., Becher R., Behm F.G.,
RA Chaganti R.S.K., Civin C.I., Disteche C., Dube I., Frischauf A.M.,
RA Horsman D., Mitelman F., Volinia S., Watmore A.E., Housman D.E.;
RT "The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a
RT putative acetyltransferase to the CREB-binding protein.";
RL Nat. Genet. 14:33-41(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-83, AND CHROMOSOMAL TRANSLOCATION WITH
RP KAT6B.
RX PubMed=11157802; DOI=10.1093/hmg/10.4.395;
RA Panagopoulos I., Fioretos T., Isaksson M., Samuelsson U., Billstroem R.,
RA Stroembeck B., Mitelman F., Johansson B.;
RT "Fusion of the MORF and CBP genes in acute myeloid leukemia with the
RT t(10;16)(q22;p13).";
RL Hum. Mol. Genet. 10:395-404(2001).
RN [8]
RP INTERACTION WITH PCAF.
RX PubMed=8684459; DOI=10.1038/382319a0;
RA Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y.;
RT "A p300/CBP-associated factor that competes with the adenoviral oncoprotein
RT E1A.";
RL Nature 382:319-324(1996).
RN [9]
RP INTERACTION WITH HIF1A AND EP300.
RX PubMed=8917528; DOI=10.1073/pnas.93.23.12969;
RA Arany Z., Huang L.E., Eckner R., Bhattacharya S., Jiang C., Goldberg M.A.,
RA Bunn H.F., Livingston D.M.;
RT "An essential role for p300/CBP in the cellular response to hypoxia.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:12969-12973(1996).
RN [10]
RP INTERACTION WITH DHX9.
RX PubMed=9323138; DOI=10.1016/s0092-8674(00)80376-1;
RA Nakajima T., Uchida C., Anderson S.F., Lee C.-G., Hurwitz J., Parvin J.D.,
RA Montminy M.;
RT "RNA helicase A mediates association of CBP with RNA polymerase II.";
RL Cell 90:1107-1112(1997).
RN [11]
RP INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION).
RX PubMed=9528808; DOI=10.1128/mcb.18.4.2392;
RA Bex F., Yin M.-J., Burny A., Gaynor R.B.;
RT "Differential transcriptional activation by human T-cell leukemia virus
RT type 1 Tax mutants is mediated by distinct interactions with CREB binding
RT protein and p300.";
RL Mol. Cell. Biol. 18:2392-2405(1998).
RN [12]
RP INTERACTION WITH KLF1, AND FUNCTION.
RX PubMed=9707565; DOI=10.1073/pnas.95.17.9855;
RA Zhang W., Bieker J.J.;
RT "Acetylation and modulation of erythroid Krueppel-like factor (EKLF)
RT activity by interaction with histone acetyltransferases.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9855-9860(1998).
RN [13]
RP INTERACTION WITH SRCAP.
RX PubMed=10347196; DOI=10.1074/jbc.274.23.16370;
RA Johnston H., Kneer J., Chackalaparampil I., Yaciuk P., Chrivia J.;
RT "Identification of a novel SNF2/SWI2 protein family member, SRCAP, which
RT interacts with CREB-binding protein.";
RL J. Biol. Chem. 274:16370-16376(1999).
RN [14]
RP INTERACTION WITH PML.
RX PubMed=10077561; DOI=10.1073/pnas.96.6.2627;
RA Doucas V., Tini M., Egan D.A., Evans R.M.;
RT "Modulation of CREB binding protein function by the promyelocytic (PML)
RT oncoprotein suggests a role for nuclear bodies in hormone signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2627-2632(1999).
RN [15]
RP ACETYLATION OF NCOA3.
RX PubMed=10490106; DOI=10.1016/s0092-8674(00)80054-9;
RA Chen H., Lin R.J., Xie W., Wilpitz D., Evans R.M.;
RT "Regulation of hormone-induced histone hyperacetylation and gene activation
RT via acetylation of an acetylase.";
RL Cell 98:675-686(1999).
RN [16]
RP INTERACTION WITH CITED1.
RX PubMed=10722728; DOI=10.1074/jbc.275.12.8825;
RA Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S., Roberts A.B.,
RA Isselbacher K.J., Shioda T.;
RT "The MSG1 non-DNA-binding transactivator binds to the p300/CBP
RT coactivators, enhancing their functional link to the Smad transcription
RT factors.";
RL J. Biol. Chem. 275:8825-8834(2000).
RN [17]
RP INTERACTION WITH NCOA6.
RX PubMed=10866662; DOI=10.1128/mcb.20.14.5048-5063.2000;
RA Mahajan M.A., Samuels H.H.;
RT "A new family of nuclear receptor coregulators that integrates nuclear
RT receptor signaling through CBP.";
RL Mol. Cell. Biol. 20:5048-5063(2000).
RN [18]
RP INTERACTION WITH MAFG, AND FUNCTION IN ACETYLATION OF MAFG.
RX PubMed=11154691; DOI=10.1074/jbc.m007846200;
RA Hung H.-L., Kim A.Y., Hong W., Rakowski C., Blobel G.A.;
RT "Stimulation of NF-E2 DNA binding by CREB-binding protein (CBP)-mediated
RT acetylation.";
RL J. Biol. Chem. 276:10715-10721(2001).
RN [19]
RP INTERACTION WITH NFATC4.
RX PubMed=11514544; DOI=10.1074/jbc.m102961200;
RA Yang T.T.C., Davis R.J., Chow C.-W.;
RT "Requirement of two NFATc4 transactivation domains for CBP potentiation.";
RL J. Biol. Chem. 276:39569-39576(2001).
RN [20]
RP INTERACTION WITH MECOM.
RX PubMed=11568182; DOI=10.1074/jbc.m106733200;
RA Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G.;
RT "Interaction of EVI1 with cAMP-responsive element-binding protein-binding
RT protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible
RT acetylation of EVI1 and in co-localization in nuclear speckles.";
RL J. Biol. Chem. 276:44936-44943(2001).
RN [21]
RP INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION).
RX PubMed=11463834; DOI=10.1128/mcb.21.16.5520-5530.2001;
RA Scoggin K.E.S., Ulloa A., Nyborg J.K.;
RT "The oncoprotein Tax binds the SRC-1-interacting domain of CBP/p300 to
RT mediate transcriptional activation.";
RL Mol. Cell. Biol. 21:5520-5530(2001).
RN [22]
RP INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P30II (MICROBIAL INFECTION).
RX PubMed=11559821; DOI=10.1128/jvi.75.20.9885-9895.2001;
RA Zhang W., Nisbet J.W., Albrecht B., Ding W., Kashanchi F., Bartoe J.T.,
RA Lairmore M.D.;
RT "Human T-lymphotropic virus type 1 p30(II) regulates gene transcription by
RT binding CREB binding protein/p300.";
RL J. Virol. 75:9885-9895(2001).
RN [23]
RP INTERACTION WITH TRERF1.
RX PubMed=11349124; DOI=10.1074/jbc.m100113200;
RA Gizard F., Lavallee B., DeWitte F., Hum D.W.;
RT "A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate
RT human CYP11A1 gene expression.";
RL J. Biol. Chem. 276:33881-33892(2001).
RN [24]
RP INTERACTION WITH PELP1.
RX PubMed=11481323; DOI=10.1074/jbc.m103783200;
RA Vadlamudi R.K., Wang R.-A., Mazumdar A., Kim Y.-S., Shin J., Sahin A.,
RA Kumar R.;
RT "Molecular cloning and characterization of PELP1, a novel human coregulator
RT of estrogen receptor alpha.";
RL J. Biol. Chem. 276:38272-38279(2001).
RN [25]
RP INTERACTION WITH HHV-8 PROTEIN VIRF1 (MICROBIAL INFECTION).
RX PubMed=11314014; DOI=10.1038/sj.onc.1204163;
RA Lin R., Genin P., Mamane Y., Sgarbanti M., Battistini A.,
RA Harrington W.J. Jr., Barber G.N., Hiscott J.;
RT "HHV-8 encoded vIRF-1 represses the interferon antiviral response by
RT blocking IRF-3 recruitment of the CBP/p300 coactivators.";
RL Oncogene 20:800-811(2001).
RN [26]
RP INTERACTION WITH SPIB.
RX PubMed=11864910;
RA Yamamoto H., Kihara-Negishi F., Yamada T., Suzuki M., Nakano T., Oikawa T.;
RT "Interaction between the hematopoietic Ets transcription factor Spi-B and
RT the coactivator CREB-binding protein associated with negative cross-talk
RT with c-Myb.";
RL Cell Growth Differ. 13:69-75(2002).
RN [27]
RP INTERACTION WITH CITED4.
RX PubMed=11744733; DOI=10.1074/jbc.m110850200;
RA Braganca J., Swingler T., Marques F.I.R., Jones T., Eloranta J.J.,
RA Hurst H.C., Shioda T., Bhattacharya S.;
RT "Human CREB-binding protein/p300-interacting transactivator with ED-rich
RT tail (CITED) 4, a new member of the CITED family, functions as a co-
RT activator for transcription factor AP-2.";
RL J. Biol. Chem. 277:8559-8565(2002).
RN [28]
RP IDENTIFICATION IN A COMPLEX WITH NCOA2; NCOA3; IKKA; IKKB AND IKBKG.
RX PubMed=11971985; DOI=10.1128/mcb.22.10.3549-3561.2002;
RA Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J.,
RA O'Malley B.W.;
RT "Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by
RT I kappa B kinase.";
RL Mol. Cell. Biol. 22:3549-3561(2002).
RN [29]
RP INTERACTION WITH IRF2, AND FUNCTION IN ACETYLATION OF IRF2.
RX PubMed=12738767; DOI=10.1074/jbc.m213037200;
RA Masumi A., Yamakawa Y., Fukazawa H., Ozato K., Komuro K.;
RT "Interferon regulatory factor-2 regulates cell growth through its
RT acetylation.";
RL J. Biol. Chem. 278:25401-25407(2003).
RN [30]
RP INTERACTION WITH N4BP2.
RX PubMed=12730195; DOI=10.1074/jbc.m303518200;
RA Watanabe N., Wachi S., Fujita T.;
RT "Identification and characterization of BCL-3-binding protein: implications
RT for transcription and DNA repair or recombination.";
RL J. Biol. Chem. 278:26102-26110(2003).
RN [31]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12929931; DOI=10.1359/jbmr.2003.18.8.1419;
RA Iioka T., Furukawa K., Yamaguchi A., Shindo H., Yamashita S., Tsukazaki T.;
RT "P300/CBP acts as a coactivator to cartilage homeoprotein-1 (Cart1),
RT paired-like homeoprotein, through acetylation of the conserved lysine
RT residue adjacent to the homeodomain.";
RL J. Bone Miner. Res. 18:1419-1429(2003).
RN [32]
RP FUNCTION, AND INTERACTION WITH NPAS2 AND CLOCK.
RX PubMed=14645221; DOI=10.1074/jbc.m311973200;
RA Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M.,
RA Chakravarti D., FitzGerald G.A., McNamara P.;
RT "Histone acetyltransferase-dependent chromatin remodeling and the vascular
RT clock.";
RL J. Biol. Chem. 279:7091-7097(2004).
RN [33]
RP INTERACTION WITH ELF3.
RX PubMed=15075319; DOI=10.1074/jbc.m401356200;
RA Wang H., Fang R., Cho J.-Y., Libermann T.A., Oettgen P.;
RT "Positive and negative modulation of the transcriptional activity of the
RT ETS factor ESE-1 through interaction with p300, CREB-binding protein, and
RT Ku 70/86.";
RL J. Biol. Chem. 279:25241-25250(2004).
RN [34]
RP INTERACTION WITH MLLT7.
RX PubMed=15126506; DOI=10.1074/jbc.m401138200;
RA van der Horst A., Tertoolen L.G.J., de Vries-Smits L.M.M., Frye R.A.,
RA Medema R.H., Burgering B.M.T.;
RT "FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity
RT protein hSir2(SIRT1).";
RL J. Biol. Chem. 279:28873-28879(2004).
RN [35]
RP SUBCELLULAR LOCATION.
RX PubMed=15488321; DOI=10.1016/j.neulet.2004.08.062;
RA Pradhan A., Liu Y.;
RT "The calcium-responsive transactivator recruits CREB binding protein to
RT nuclear bodies.";
RL Neurosci. Lett. 370:191-195(2004).
RN [36]
RP INTERACTION WITH FOXO1.
RX PubMed=15220471; DOI=10.1073/pnas.0400593101;
RA Daitoku H., Hatta M., Matsuzaki H., Aratani S., Ohshima T., Miyagishi M.,
RA Nakajima T., Fukamizu A.;
RT "Silent information regulator 2 potentiates Foxo1-mediated transcription
RT through its deacetylase activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10042-10047(2004).
RN [37]
RP INTERACTION WITH SS18L1/CREST.
RX PubMed=14716005; DOI=10.1126/science.1089845;
RA Aizawa H., Hu S.-C., Bobb K., Balakrishnan K., Ince G., Gurevich I.,
RA Cowan M., Ghosh A.;
RT "Dendrite development regulated by CREST, a calcium-regulated
RT transcriptional activator.";
RL Science 303:197-202(2004).
RN [38]
RP PHOSPHORYLATION AT SER-1382 AND SER-1386 BY CHUK/IKKA.
RX PubMed=17434128; DOI=10.1016/j.molcel.2007.02.019;
RA Huang W.C., Ju T.K., Hung M.C., Chen C.C.;
RT "Phosphorylation of CBP by IKKalpha promotes cell growth by switching the
RT binding preference of CBP from p53 to NF-kappaB.";
RL Mol. Cell 26:75-87(2007).
RN [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1030, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [40]
RP INTERACTION WITH MTDH.
RX PubMed=18316612; DOI=10.1158/0008-5472.can-07-6164;
RA Sarkar D., Park E.S., Emdad L., Lee S.-G., Su Z.-Z., Fisher P.B.;
RT "Molecular basis of nuclear factor-kappaB activation by astrocyte elevated
RT gene-1.";
RL Cancer Res. 68:1478-1484(2008).
RN [41]
RP INTERACTION WITH HUMAN T-CELL LEUKEMIA VIRUS 1/HTLV-1 PROTEIN HBZ.
RX PubMed=18599479; DOI=10.1074/jbc.m803116200;
RA Clerc I., Polakowski N., Andre-Arpin C., Cook P., Barbeau B., Mesnard J.M.,
RA Lemasson I.;
RT "An interaction between the human T cell leukemia virus type 1 basic
RT leucine zipper factor (HBZ) and the KIX domain of p300/CBP contributes to
RT the down-regulation of tax-dependent viral transcription by HBZ.";
RL J. Biol. Chem. 283:23903-23913(2008).
RN [42]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-2063; SER-2076 AND
RP SER-2079, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [43]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [44]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2063, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [45]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1014; LYS-1216; LYS-1583;
RP LYS-1591; LYS-1592; LYS-1595; LYS-1597; LYS-1741 AND LYS-1744, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [46]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [47]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [48]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [49]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1076; SER-1763 AND SER-2063,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [50]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24207024; DOI=10.1016/j.molcel.2013.10.010;
RA Chen S., Seiler J., Santiago-Reichelt M., Felbel K., Grummt I., Voit R.;
RT "Repression of RNA polymerase I upon stress is caused by inhibition of RNA-
RT dependent deacetylation of PAF53 by SIRT7.";
RL Mol. Cell 52:303-313(2013).
RN [51]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [52]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-220, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [53]
RP FUNCTION AS ACETYLTRANSFERASE OF PCNA, AND INTERACTION WITH PCNA.
RX PubMed=24939902; DOI=10.1093/nar/gku533;
RA Cazzalini O., Sommatis S., Tillhon M., Dutto I., Bachi A., Rapp A.,
RA Nardo T., Scovassi A.I., Necchi D., Cardoso M.C., Stivala L.A.,
RA Prosperi E.;
RT "CBP and p300 acetylate PCNA to link its degradation with nucleotide
RT excision repair synthesis.";
RL Nucleic Acids Res. 42:8433-8448(2014).
RN [54]
RP FUNCTION, AND INTERACTION WITH SMAD4.
RX PubMed=25514493; DOI=10.1016/j.bbagrm.2014.12.008;
RA Yang Y., Cui J., Xue F., Zhang C., Mei Z., Wang Y., Bi M., Shan D.,
RA Meredith A., Li H., Xu Z.Q.;
RT "Pokemon (FBI-1) interacts with Smad4 to repress TGF-beta-induced
RT transcriptional responses.";
RL Biochim. Biophys. Acta 1849:270-281(2015).
RN [55]
RP INTERACTION WITH DUX4.
RX PubMed=26951377; DOI=10.1093/nar/gkw141;
RA Choi S.H., Gearhart M.D., Cui Z., Bosnakovski D., Kim M., Schennum N.,
RA Kyba M.;
RT "DUX4 recruits p300/CBP through its C-terminus and induces global H3K27
RT acetylation changes.";
RL Nucleic Acids Res. 44:5161-5173(2016).
RN [56]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28790157; DOI=10.1101/gad.300624.117;
RA Song C., Hotz-Wagenblatt A., Voit R., Grummt I.;
RT "SIRT7 and the DEAD-box helicase DDX21 cooperate to resolve genomic R loops
RT and safeguard genome stability.";
RL Genes Dev. 31:1370-1381(2017).
RN [57]
RP INTERACTION WITH DDX3X.
RX PubMed=28128295; DOI=10.1038/srep41452;
RA Tsai T.Y., Wang W.T., Li H.K., Chen W.J., Tsai Y.H., Chao C.H.,
RA Wu Lee Y.H.;
RT "RNA helicase DDX3 maintains lipid homeostasis through upregulation of the
RT microsomal triglyceride transfer protein by interacting with HNF4 and
RT SHP.";
RL Sci. Rep. 7:41452-41452(2017).
RN [58]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30540930; DOI=10.1016/j.celrep.2018.11.051;
RA Iyer-Bierhoff A., Krogh N., Tessarz P., Ruppert T., Nielsen H., Grummt I.;
RT "SIRT7-dependent deacetylation of fibrillarin controls histone H2A
RT methylation and rRNA synthesis during the cell cycle.";
RL Cell Rep. 25:2946-2954(2018).
RN [59]
RP STRUCTURE BY NMR OF 345-439 IN COMPLEX WITH 776-826 OF HIF1A.
RX PubMed=11959977; DOI=10.1073/pnas.082121399;
RA Dames S.A., Martinez-Yamout M., De Guzman R.N., Dyson H.J., Wright P.E.;
RT "Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic
RT response.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5271-5276(2002).
RN [60]
RP CHROMOSOMAL TRANSLOCATION WITH KAT6A.
RX PubMed=11742995; DOI=10.1093/emboj/20.24.7184;
RA Kitabayashi I., Aikawa Y., Nguyen L.A., Yokoyama A., Ohki M.;
RT "Activation of AML1-mediated transcription by MOZ and inhibition by the
RT MOZ-CBP fusion protein.";
RL EMBO J. 20:7184-7196(2001).
RN [61]
RP STRUCTURE BY NMR OF 589-679 IN COMPLEX WITH HIV-1 TAT (MICROBIAL
RP INFECTION).
RX PubMed=14744133; DOI=10.1021/bi035612l;
RA Vendel A.C., Lumb K.J.;
RT "NMR mapping of the HIV-1 Tat interaction surface of the KIX domain of the
RT human coactivator CBP.";
RL Biochemistry 43:904-908(2004).
RN [62]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1081-1197.
RX PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
RA Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
RA Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
RA Gingras A.C., Arrowsmith C.H., Knapp S.;
RT "Histone recognition and large-scale structural analysis of the human
RT bromodomain family.";
RL Cell 149:214-231(2012).
RN [63] {ECO:0007744|PDB:2LXS, ECO:0007744|PDB:2LXT}
RP STRUCTURE BY NMR OF 587-673 IN COMPLEX WITH KMT2A AND CREB1.
RX PubMed=23651431; DOI=10.1021/cb4002188;
RA Bruschweiler S., Konrat R., Tollinger M.;
RT "Allosteric communication in the KIX domain proceeds through dynamic
RT repacking of the hydrophobic core.";
RL ACS Chem. Biol. 8:1600-1610(2013).
RN [64]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 1082-1197, FUNCTION, INTERACTION
RP WITH ASF1A; ASF1B; ACETYLATED HISTONES AND TP53, MUTAGENESIS OF ASP-1116;
RP PHE-1126; ASN-1162; TRP-1165; SER-1179; LYS-1180 AND GLU-1183,
RP CHARACTERIZATION OF VARIANT RSTS1 CYS-1175, CATALYTIC ACTIVITY, AND
RP AUTOACETYLATION.
RX PubMed=24616510; DOI=10.1073/pnas.1319122111;
RA Das C., Roy S., Namjoshi S., Malarkey C.S., Jones D.N., Kutateladze T.G.,
RA Churchill M.E., Tyler J.K.;
RT "Binding of the histone chaperone ASF1 to the CBP bromodomain promotes
RT histone acetylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E1072-E1081(2014).
RN [65]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 1080-1316 IN COMPLEX WITH ZINC.
RX PubMed=24361270; DOI=10.1016/j.str.2013.10.021;
RA Plotnikov A.N., Yang S., Zhou T.J., Rusinova E., Frasca A., Zhou M.M.;
RT "Structural insights into acetylated-histone H4 recognition by the
RT bromodomain-PHD finger module of human transcriptional coactivator CBP.";
RL Structure 22:353-360(2014).
RN [66] {ECO:0007744|PDB:5JEM}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2065-2111 IN COMPLEX WITH IRF3.
RX PubMed=27302953; DOI=10.1073/pnas.1603269113;
RA Zhao B., Shu C., Gao X., Sankaran B., Du F., Shelton C.L., Herr A.B.,
RA Ji J.Y., Li P.;
RT "Structural basis for concerted recruitment and activation of IRF-3 by
RT innate immune adaptor proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E3403-E3412(2016).
RN [67]
RP VARIANT RSTS1 PRO-1378.
RX PubMed=11331617; DOI=10.1093/hmg/10.10.1071;
RA Murata T., Kurokawa R., Krones A., Tatsumi K., Ishii M., Taki T.,
RA Masuno M., Ohashi H., Yanagisawa M., Rosenfeld M.G., Glass C.K.,
RA Hayashi Y.;
RT "Defect of histone acetyltransferase activity of the nuclear
RT transcriptional coactivator CBP in Rubinstein-Taybi syndrome.";
RL Hum. Mol. Genet. 10:1071-1076(2001).
RN [68]
RP VARIANT RSTS1 CYS-1175.
RX PubMed=12114483; DOI=10.1136/jmg.39.7.496;
RA Bartsch O., Locher K., Meinecke P., Kress W., Seemanova E., Wagner A.,
RA Ostermann K., Roedel G.;
RT "Molecular studies in 10 cases of Rubinstein-Taybi syndrome, including a
RT mild variant showing a missense mutation in codon 1175 of CREBBP.";
RL J. Med. Genet. 39:496-501(2002).
RN [69]
RP VARIANTS RSTS1 LYS-1278 AND HIS-1664, AND CHARACTERIZATION OF VARIANTS
RP RSTS1 LYS-1278 AND HIS-1664.
RX PubMed=12566391; DOI=10.1093/hmg/ddg039;
RA Kalkhoven E., Roelfsema J.H., Teunissen H., den Boer A., Ariyuerek Y.,
RA Zantema A., Breuning M.H., Hennekam R.C.M., Peters D.J.M.;
RT "Loss of CBP acetyltransferase activity by PHD finger mutations in
RT Rubinstein-Taybi syndrome.";
RL Hum. Mol. Genet. 12:441-450(2003).
RN [70]
RP VARIANTS RSTS1 LYS-1278; ILE-1447; HIS-1450; ARG-1470 AND HIS-1664.
RX PubMed=15706485; DOI=10.1086/429130;
RA Roelfsema J.H., White S.J., Ariyuerek Y., Bartholdi D., Niedrist D.,
RA Papadia F., Bacino C.A., den Dunnen J.T., van Ommen G.-J.B., Breuning M.H.,
RA Hennekam R.C., Peters D.J.M.;
RT "Genetic heterogeneity in Rubinstein-Taybi syndrome: mutations in both the
RT CBP and EP300 genes cause disease.";
RL Am. J. Hum. Genet. 76:572-580(2005).
RN [71]
RP VARIANT RSTS1 ALA-910.
RX PubMed=20684013; DOI=10.1002/ajmg.a.33598;
RA Bartsch O., Kress W., Kempf O., Lechno S., Haaf T., Zechner U.;
RT "Inheritance and variable expression in Rubinstein-Taybi syndrome.";
RL Am. J. Med. Genet. A 152A:2254-2261(2010).
RN [72]
RP VARIANTS HIS-503; THR-532 AND ASN-546, AND VARIANTS RSTS1 PHE-650; THR-789;
RP CYS-1175; ALA-1278; PRO-1378; TYR-1406; PRO-1415; THR-1475; PHE-1503;
RP PRO-1507 AND ASN-1543.
RX PubMed=25388907; DOI=10.1111/cge.12537;
RA Spena S., Milani D., Rusconi D., Negri G., Colapietro P., Elcioglu N.,
RA Bedeschi F., Pilotta A., Spaccini L., Ficcadenti A., Magnani C.,
RA Scarano G., Selicorni A., Larizza L., Gervasini C.;
RT "Insights into genotype-phenotype correlations from CREBBP point mutation
RT screening in a cohort of 46 Rubinstein-Taybi syndrome patients.";
RL Clin. Genet. 88:431-440(2015).
RN [73]
RP VARIANTS MKHK1 ARG-1710; ARG-1747; PRO-1786; PHE-1819; TRP-1826; TYR-1838;
RP GLN-1867; TRP-1867; TRP-1868 AND VAL-1872, AND INVOLVEMENT IN MKHK1.
RX PubMed=27311832; DOI=10.1002/ajmg.a.37800;
RG DDD Study;
RA Menke L.A., van Belzen M.J., Alders M., Cristofoli F., Ehmke N.,
RA Fergelot P., Foster A., Gerkes E.H., Hoffer M.J., Horn D., Kant S.G.,
RA Lacombe D., Leon E., Maas S.M., Melis D., Muto V., Park S.M., Peeters H.,
RA Peters D.J., Pfundt R., van Ravenswaaij-Arts C.M., Tartaglia M.,
RA Hennekam R.C.;
RT "CREBBP mutations in individuals without Rubinstein-Taybi syndrome
RT phenotype.";
RL Am. J. Med. Genet. A 170:2681-2693(2016).
RN [74]
RP VARIANTS MKHK1 ASP-1719; VAL-1782; ASP-1829; 1865-MET-ARG-1866 DELINS ILE;
RP GLN-1867; GLN-1868; TRP-1868; PRO-1870 AND VAL-1872, AND INVOLVEMENT IN
RP MKHK1.
RX PubMed=29460469; DOI=10.1002/ajmg.a.38626;
RG DDD study;
RA Menke L.A., Gardeitchik T., Hammond P., Heimdal K.R., Houge G.,
RA Hufnagel S.B., Ji J., Johansson S., Kant S.G., Kinning E., Leon E.L.,
RA Newbury-Ecob R., Paolacci S., Pfundt R., Ragge N.K., Rinne T.,
RA Ruivenkamp C., Saitta S.C., Sun Y., Tartaglia M., Terhal P.A.,
RA van Essen A.J., Vigeland M.D., Xiao B., Hennekam R.C.;
RT "Further delineation of an entity caused by CREBBP and EP300 mutations but
RT not resembling Rubinstein-Taybi syndrome.";
RL Am. J. Med. Genet. A 176:862-876(2018).
RN [75]
RP VARIANT MKHK1 LYS-1724.
RX PubMed=30737887; DOI=10.1002/ajmg.a.61052;
RA Angius A., Uva P., Oppo M., Persico I., Onano S., Olla S., Pes V.,
RA Perria C., Cuccuru G., Atzeni R., Serra G., Cucca F., Sotgiu S.,
RA Hennekam R.C., Crisponi L.;
RT "Confirmation of a new phenotype in an individual with a variant in the
RT last part of exon 30 of CREBBP.";
RL Am. J. Med. Genet. A 179:634-638(2019).
CC -!- FUNCTION: Acetylates histones, giving a specific tag for
CC transcriptional activation (PubMed:24616510). Also acetylates non-
CC histone proteins, like DDX21, FBL, IRF2, MAFG, NCOA3, POLR1E/PAF53 and
CC FOXO1 (PubMed:10490106, PubMed:11154691, PubMed:12738767,
CC PubMed:12929931, PubMed:9707565, PubMed:24207024, PubMed:28790157,
CC PubMed:30540930). Binds specifically to phosphorylated CREB and
CC enhances its transcriptional activity toward cAMP-responsive genes.
CC Acts as a coactivator of ALX1. Acts as a circadian transcriptional
CC coactivator which enhances the activity of the circadian
CC transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1
CC heterodimers (PubMed:14645221). Acetylates PCNA; acetylation promotes
CC removal of chromatin-bound PCNA and its degradation during nucleotide
CC excision repair (NER) (PubMed:24939902). Acetylates POLR1E/PAF53,
CC leading to decreased association of RNA polymerase I with the rDNA
CC promoter region and coding region (PubMed:24207024). Acetylates DDX21,
CC thereby inhibiting DDX21 helicase activity (PubMed:28790157).
CC Acetylates FBL, preventing methylation of 'Gln-105' of histone H2A
CC (H2AQ104me) (PubMed:30540930). Functions as a transcriptional
CC coactivator for SMAD4 in the TGF-beta signaling pathway
CC (PubMed:25514493). {ECO:0000269|PubMed:10490106,
CC ECO:0000269|PubMed:11154691, ECO:0000269|PubMed:12738767,
CC ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:14645221,
CC ECO:0000269|PubMed:24207024, ECO:0000269|PubMed:24616510,
CC ECO:0000269|PubMed:24939902, ECO:0000269|PubMed:25514493,
CC ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:30540930,
CC ECO:0000269|PubMed:9707565}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845,
CC Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000269|PubMed:24616510};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC Evidence={ECO:0000269|PubMed:24616510};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC Evidence={ECO:0000269|PubMed:11154691, ECO:0000269|PubMed:12738767,
CC ECO:0000269|PubMed:24207024, ECO:0000269|PubMed:24939902,
CC ECO:0000269|PubMed:30540930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC Evidence={ECO:0000269|PubMed:11154691, ECO:0000269|PubMed:12738767,
CC ECO:0000269|PubMed:24207024, ECO:0000269|PubMed:24939902,
CC ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:30540930};
CC -!- SUBUNIT: Found in a complex containing NCOA2; NCOA3; IKKA; IKKB and
CC IKBKG. Probably part of a complex with HIF1A and EP300. Interacts with
CC GATA1; the interaction results in acetylation and enhancement of
CC transcriptional activity of GATA1. Interacts with MAF AND ZCCHC12.
CC Interacts with DAXX; the interaction is dependent on CBP sumoylation
CC and results in suppression of the transcriptional activity via
CC recruitment of HDAC2 to DAXX (By similarity). Interacts with
CC phosphorylated CREB1. Interacts with CITED4 (C-terminal region).
CC Interacts (via the TAZ-type 1 domain) with HIF1A. Interacts with SRCAP,
CC CARM1, ELF3, MLLT7/FOXO4, N4BP2, NCOA1, NCOA3, NCOA6, PCAF, DDX5,
CC DDX17, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB and TRERF1. Interacts with
CC KLF1; the interaction results in acetylation of KLF1 and enhancement of
CC its transcriptional activity. Interacts with MTDH. Interacts with
CC NFATC4. Interacts with MAFG; the interaction acetylates MAFG in the
CC basic region and stimulates NFE2 transcriptional activity through
CC increasing its DNA-binding activity. Interacts with IRF2; the
CC interaction acetylates IRF2 and regulates its activity on the H4
CC promoter. Interacts with IRF3 (when phosphorylated); forming the dsRNA-
CC activated factor 1 (DRAF1), a complex which activates the transcription
CC of the type I interferon genes (PubMed:27302953). Interacts (via N-
CC terminus) with SS18L1/CREST (via C-terminus). Interacts with MECOM.
CC Interacts with CITED1 (via C-terminus). Interacts with FOXO1; the
CC interaction acetylates FOXO1 and inhibits its transcriptional activity.
CC Interacts with NPAS2, CLOCK and ARNTL/BMAL1. Interacts with ASF1A and
CC ASF1B; this promotes histone acetylation. Interacts with acetylated
CC TP53/p53 and with the acetylated histones H3 and H4. Interacts (via
CC transactivation domain and C-terminus) with PCNA; the interaction
CC occurs on chromatin in UV-irradiated damaged cells (PubMed:24939902).
CC Interacts with DHX9 (via N-terminus); this interaction mediates
CC association with RNA polymerase II holoenzyme and stimulates CREB-
CC dependent transcriptional activation (PubMed:9323138). Interacts with
CC SMAD4; negatively regulated by ZBTB7A (PubMed:25514493). Interacts with
CC DUX4 (via C-terminus) (PubMed:26951377). Forms a complex with KMT2A and
CC CREB1 (PubMed:23651431). Interacts with DDX3X; this interaction may
CC facilitate HNF4A acetylation (PubMed:28128295). {ECO:0000250,
CC ECO:0000269|PubMed:10077561, ECO:0000269|PubMed:10347196,
CC ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:10866662,
CC ECO:0000269|PubMed:11154691, ECO:0000269|PubMed:11349124,
CC ECO:0000269|PubMed:11481323, ECO:0000269|PubMed:11514544,
CC ECO:0000269|PubMed:11568182, ECO:0000269|PubMed:11744733,
CC ECO:0000269|PubMed:11864910, ECO:0000269|PubMed:11959977,
CC ECO:0000269|PubMed:11971985, ECO:0000269|PubMed:12730195,
CC ECO:0000269|PubMed:12738767, ECO:0000269|PubMed:14645221,
CC ECO:0000269|PubMed:14716005, ECO:0000269|PubMed:15075319,
CC ECO:0000269|PubMed:15126506, ECO:0000269|PubMed:15220471,
CC ECO:0000269|PubMed:18316612, ECO:0000269|PubMed:23651431,
CC ECO:0000269|PubMed:24616510, ECO:0000269|PubMed:24939902,
CC ECO:0000269|PubMed:25514493, ECO:0000269|PubMed:26951377,
CC ECO:0000269|PubMed:27302953, ECO:0000269|PubMed:28128295,
CC ECO:0000269|PubMed:8684459, ECO:0000269|PubMed:8917528,
CC ECO:0000269|PubMed:9323138, ECO:0000269|PubMed:9707565}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 Tax, p30II and
CC HBZ. {ECO:0000269|PubMed:11463834, ECO:0000269|PubMed:11559821,
CC ECO:0000269|PubMed:9528808}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human herpes virus 8/HHV-
CC 8 protein vIRF-1; this interaction inhibits CREBBP binding to IRF3.
CC {ECO:0000269|PubMed:11314014}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat.
CC {ECO:0000269|PubMed:14744133}.
CC -!- INTERACTION:
CC Q92793; P31749: AKT1; NbExp=3; IntAct=EBI-81215, EBI-296087;
CC Q92793; P10275: AR; NbExp=3; IntAct=EBI-81215, EBI-608057;
CC Q92793; P61201: COPS2; NbExp=3; IntAct=EBI-81215, EBI-1050386;
CC Q92793; P16220: CREB1; NbExp=2; IntAct=EBI-81215, EBI-711855;
CC Q92793; P35222: CTNNB1; NbExp=2; IntAct=EBI-81215, EBI-491549;
CC Q92793; Q9UER7: DAXX; NbExp=2; IntAct=EBI-81215, EBI-77321;
CC Q92793; Q12778: FOXO1; NbExp=3; IntAct=EBI-81215, EBI-1108782;
CC Q92793; O43524: FOXO3; NbExp=3; IntAct=EBI-81215, EBI-1644164;
CC Q92793; P23769: GATA2; NbExp=2; IntAct=EBI-81215, EBI-2806671;
CC Q92793; P62805: H4C9; NbExp=6; IntAct=EBI-81215, EBI-302023;
CC Q92793; Q16665: HIF1A; NbExp=2; IntAct=EBI-81215, EBI-447269;
CC Q92793; P42858: HTT; NbExp=2; IntAct=EBI-81215, EBI-466029;
CC Q92793; P48551: IFNAR2; NbExp=4; IntAct=EBI-81215, EBI-958408;
CC Q92793; Q14653: IRF3; NbExp=12; IntAct=EBI-81215, EBI-2650369;
CC Q92793; Q13568: IRF5; NbExp=3; IntAct=EBI-81215, EBI-3931258;
CC Q92793; Q92831: KAT2B; NbExp=4; IntAct=EBI-81215, EBI-477430;
CC Q92793; Q13351: KLF1; NbExp=2; IntAct=EBI-81215, EBI-8284732;
CC Q92793; Q86UE4: MTDH; NbExp=2; IntAct=EBI-81215, EBI-1046588;
CC Q92793; P55209: NAP1L1; NbExp=3; IntAct=EBI-81215, EBI-356392;
CC Q92793; Q14686: NCOA6; NbExp=2; IntAct=EBI-81215, EBI-78670;
CC Q92793; Q04206: RELA; NbExp=6; IntAct=EBI-81215, EBI-73886;
CC Q92793; P36956-1: SREBF1; NbExp=3; IntAct=EBI-81215, EBI-948328;
CC Q92793; P36956-3: SREBF1; NbExp=2; IntAct=EBI-81215, EBI-948338;
CC Q92793; Q12772: SREBF2; NbExp=2; IntAct=EBI-81215, EBI-465059;
CC Q92793; Q9UL17: TBX21; NbExp=4; IntAct=EBI-81215, EBI-3922312;
CC Q92793; P04637: TP53; NbExp=17; IntAct=EBI-81215, EBI-366083;
CC Q92793; P0DTC9: N; Xeno; NbExp=2; IntAct=EBI-81215, EBI-25475856;
CC Q92793; P04608: tat; Xeno; NbExp=2; IntAct=EBI-81215, EBI-6164389;
CC Q92793; P03070; Xeno; NbExp=2; IntAct=EBI-81215, EBI-617698;
CC Q92793; P03255; Xeno; NbExp=3; IntAct=EBI-81215, EBI-2603114;
CC Q92793; P03259; Xeno; NbExp=5; IntAct=EBI-81215, EBI-6947456;
CC Q92793; P03259-2; Xeno; NbExp=3; IntAct=EBI-81215, EBI-7225021;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Recruited to nuclear
CC bodies by SS18L1/CREST. In the presence of ALX1 relocalizes from the
CC cytoplasm to the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92793-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92793-2; Sequence=VSP_045700;
CC -!- DOMAIN: The KIX domain mediates binding to HIV-1 Tat.
CC -!- PTM: Methylation of the KIX domain by CARM1 blocks association with
CC CREB. This results in the blockade of CREB signaling, and in activation
CC of apoptotic response (By similarity). {ECO:0000250|UniProtKB:P45481}.
CC -!- PTM: Phosphorylated by CHUK/IKKA at Ser-1382 and Ser-1386; these
CC phosphorylations promote cell growth by switching the binding
CC preference of CREBBP from TP53 to NF-kappa-B.
CC {ECO:0000269|PubMed:17434128}.
CC -!- PTM: Sumoylation negatively regulates transcriptional activity via the
CC recruitment of DAAX. {ECO:0000250|UniProtKB:P45481}.
CC -!- PTM: Autoacetylation is required for binding to protein substrates,
CC such as acetylated histones and acetylated TP53/p53.
CC {ECO:0000269|PubMed:24616510}.
CC -!- DISEASE: Note=Chromosomal aberrations involving CREBBP may be a cause
CC of acute myeloid leukemias. Translocation t(8;16)(p11;p13) with KAT6A;
CC translocation t(11;16)(q23;p13.3) with KMT2A/MLL1; translocation
CC t(10;16)(q22;p13) with KAT6B. KAT6A-CREBBP may induce leukemia by
CC inhibiting RUNX1-mediated transcription.
CC -!- DISEASE: Rubinstein-Taybi syndrome 1 (RSTS1) [MIM:180849]: A disorder
CC characterized by craniofacial abnormalities, postnatal growth
CC deficiency, broad thumbs, broad big toes, intellectual disability and a
CC propensity for development of malignancies.
CC {ECO:0000269|PubMed:11331617, ECO:0000269|PubMed:12114483,
CC ECO:0000269|PubMed:12566391, ECO:0000269|PubMed:15706485,
CC ECO:0000269|PubMed:20684013, ECO:0000269|PubMed:24616510,
CC ECO:0000269|PubMed:25388907}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Menke-Hennekam syndrome 1 (MKHK1) [MIM:618332]: A form of
CC Menke-Hennekam syndrome, a congenital autosomal dominant disease
CC characterized by developmental delay, growth retardation, and
CC craniofacial dysmorphism. Patients have intellectual disability of
CC variable severity, speech delay, autistic behavior, short stature and
CC microcephaly. Main facial characteristics include short palpebral
CC fissures, telecanthi, depressed nasal ridge, short nose, anteverted
CC nares, short columella and long philtrum. {ECO:0000269|PubMed:27311832,
CC ECO:0000269|PubMed:29460469, ECO:0000269|PubMed:30737887}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE06125.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CBPID42.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=P300/CBP entry;
CC URL="https://en.wikipedia.org/wiki/P300/CBP";
CC ---------------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
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DR EMBL; U85962; AAC51331.2; -; mRNA.
DR EMBL; U89354; AAC51339.1; -; mRNA.
DR EMBL; U89355; AAC51340.1; -; mRNA.
DR EMBL; U47741; AAC51770.1; -; mRNA.
DR EMBL; AB210043; BAE06125.1; ALT_INIT; mRNA.
DR EMBL; CH471112; EAW85335.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85336.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85337.1; -; Genomic_DNA.
DR CCDS; CCDS10509.1; -. [Q92793-1]
DR CCDS; CCDS45399.1; -. [Q92793-2]
DR PIR; S39162; S39162.
DR RefSeq; NP_001073315.1; NM_001079846.1. [Q92793-2]
DR RefSeq; NP_004371.2; NM_004380.2. [Q92793-1]
DR PDB; 1JSP; NMR; -; B=1081-1197.
DR PDB; 1LIQ; NMR; -; A=376-402.
DR PDB; 1RDT; X-ray; 2.40 A; E=58-80.
DR PDB; 1WO3; NMR; -; A=387-398.
DR PDB; 1WO4; NMR; -; A=387-398.
DR PDB; 1WO5; NMR; -; A=387-398.
DR PDB; 1WO6; NMR; -; A=376-400.
DR PDB; 1WO7; NMR; -; A=376-400.
DR PDB; 1ZOQ; X-ray; 2.37 A; C/D=2065-2111.
DR PDB; 2D82; NMR; -; A=1081-1197.
DR PDB; 2KJE; NMR; -; A=1763-1854.
DR PDB; 2KWF; NMR; -; A=587-673.
DR PDB; 2L84; NMR; -; A=1081-1197.
DR PDB; 2L85; NMR; -; A=1081-1197.
DR PDB; 2LXS; NMR; -; A=587-673.
DR PDB; 2LXT; NMR; -; A=587-673.
DR PDB; 2N1A; NMR; -; B=1699-1751.
DR PDB; 2RNY; NMR; -; A=1081-1197.
DR PDB; 3DWY; X-ray; 1.98 A; A/B=1081-1197.
DR PDB; 3P1C; X-ray; 1.82 A; A/B=1081-1197.
DR PDB; 3P1D; X-ray; 1.86 A; A/B=1081-1197.
DR PDB; 3P1E; X-ray; 1.80 A; A/B=1081-1197.
DR PDB; 3P1F; X-ray; 1.63 A; A/B=1081-1197.
DR PDB; 3SVH; X-ray; 1.80 A; A/B=1081-1197.
DR PDB; 4A9K; X-ray; 1.81 A; A/B=1081-1197.
DR PDB; 4N3W; X-ray; 1.90 A; A=1080-1316.
DR PDB; 4N4F; X-ray; 1.83 A; A=1080-1316.
DR PDB; 4NR4; X-ray; 1.69 A; A/B=1081-1197.
DR PDB; 4NR5; X-ray; 1.66 A; A=1081-1197.
DR PDB; 4NR6; X-ray; 1.66 A; A=1081-1197.
DR PDB; 4NR7; X-ray; 1.20 A; A=1081-1197.
DR PDB; 4NYV; X-ray; 1.83 A; A/B/C/D=1081-1197.
DR PDB; 4NYW; X-ray; 1.43 A; A=1081-1197.
DR PDB; 4NYX; X-ray; 1.10 A; A=1081-1197.
DR PDB; 4OUF; X-ray; 1.40 A; A/B=1082-1197.
DR PDB; 4TQN; X-ray; 1.70 A; A=1081-1197.
DR PDB; 4TS8; X-ray; 2.00 A; A=1081-1197.
DR PDB; 4WHU; X-ray; 2.11 A; A=1081-1197.
DR PDB; 4YK0; X-ray; 1.65 A; A/B/C/D=1083-1196.
DR PDB; 5CGP; X-ray; 1.96 A; A=1081-1197.
DR PDB; 5DBM; X-ray; 1.86 A; A/B/C=1082-1197.
DR PDB; 5EIC; X-ray; 1.50 A; A/B=1081-1197.
DR PDB; 5ENG; X-ray; 1.30 A; A=1081-1197.
DR PDB; 5EP7; X-ray; 1.20 A; A=1081-1197.
DR PDB; 5GH9; X-ray; 1.45 A; A=1081-1196.
DR PDB; 5H85; X-ray; 1.70 A; A=1081-1197.
DR PDB; 5I83; X-ray; 1.35 A; A=1082-1197.
DR PDB; 5I86; X-ray; 1.05 A; A/B=1082-1197.
DR PDB; 5I89; X-ray; 1.07 A; A=1082-1197.
DR PDB; 5I8B; X-ray; 1.52 A; A=1081-1312.
DR PDB; 5I8G; X-ray; 1.41 A; A=1081-1312.
DR PDB; 5J0D; X-ray; 1.05 A; A=1081-1197.
DR PDB; 5JEM; X-ray; 2.50 A; C/D/F/H=2065-2111.
DR PDB; 5KTU; X-ray; 1.38 A; A/B=1082-1197.
DR PDB; 5KTW; X-ray; 1.09 A; A/B/C=1085-1194.
DR PDB; 5KTX; X-ray; 1.27 A; A=1085-1194.
DR PDB; 5LPJ; X-ray; 1.65 A; A=1081-1197.
DR PDB; 5LPL; X-ray; 1.65 A; A=1081-1197.
DR PDB; 5MME; X-ray; 1.35 A; A/B=1081-1197.
DR PDB; 5MMG; X-ray; 1.23 A; A=1081-1197.
DR PDB; 5MPK; X-ray; 1.90 A; A/B=1081-1197.
DR PDB; 5MPN; X-ray; 1.23 A; A=1081-1197.
DR PDB; 5MPZ; X-ray; 1.40 A; A=1081-1197.
DR PDB; 5MQE; X-ray; 1.65 A; A/B=1081-1197.
DR PDB; 5MQG; X-ray; 1.35 A; A/B=1081-1197.
DR PDB; 5MQK; X-ray; 1.53 A; A/B=1081-1197.
DR PDB; 5NLK; X-ray; 1.80 A; A=1081-1197.
DR PDB; 5NRW; X-ray; 1.70 A; A=1081-1197.
DR PDB; 5NU3; X-ray; 1.75 A; A=1081-1197.
DR PDB; 5OWK; X-ray; 1.25 A; A=1081-1197.
DR PDB; 5SVH; X-ray; 2.05 A; A=587-673.
DR PDB; 5TB6; X-ray; 1.79 A; A=1081-1197.
DR PDB; 5W0E; X-ray; 1.41 A; A=1082-1197.
DR PDB; 5W0F; X-ray; 1.60 A; A=1082-1197.
DR PDB; 5W0L; X-ray; 1.55 A; A/B=1082-1197.
DR PDB; 5W0Q; X-ray; 1.70 A; A=1082-1197.
DR PDB; 5XXH; X-ray; 1.62 A; A=1081-1197.
DR PDB; 6ALB; X-ray; 2.05 A; A=1081-1312.
DR PDB; 6ALC; X-ray; 1.39 A; A/B=1085-1196.
DR PDB; 6AXQ; X-ray; 1.30 A; A/B/C/D=1085-1196.
DR PDB; 6AY3; X-ray; 1.39 A; A/B=1083-1197.
DR PDB; 6AY5; X-ray; 1.44 A; A=1083-1197.
DR PDB; 6DMK; X-ray; 1.66 A; A=1083-1195.
DR PDB; 6ES5; NMR; -; B=2061-2105.
DR PDB; 6ES6; NMR; -; B=2061-2108.
DR PDB; 6ES7; NMR; -; B=2061-2109.
DR PDB; 6FQO; X-ray; 1.35 A; A/B=1081-1197.
DR PDB; 6FQT; X-ray; 1.80 A; A=1081-1197.
DR PDB; 6FQU; X-ray; 1.43 A; A=1081-1197.
DR PDB; 6FR0; X-ray; 1.50 A; A/B=1081-1197.
DR PDB; 6FRF; X-ray; 2.10 A; A/B/C/D=1081-1197.
DR PDB; 6LQX; X-ray; 2.46 A; A/B/C/D=1082-1196.
DR PDB; 6M64; X-ray; 1.45 A; B/D/F=1951-1973.
DR PDB; 6QST; X-ray; 2.10 A; A/B/C/D=1081-1197.
DR PDB; 6SQE; X-ray; 1.51 A; A=1081-1197.
DR PDB; 6SQF; X-ray; 2.01 A; A=1081-1197.
DR PDB; 6SQM; X-ray; 1.80 A; A/B/C=1081-1197.
DR PDB; 6SXX; X-ray; 2.01 A; A/B=1081-1197.
DR PDB; 6YIJ; X-ray; 2.20 A; A/B/C/D/E/F/G=1081-1197.
DR PDB; 6YIK; X-ray; 1.70 A; A/B/C=1081-1197.
DR PDB; 6YIL; X-ray; 1.22 A; A=1081-1197.
DR PDB; 6YIM; X-ray; 1.23 A; A=1081-1197.
DR PDB; 7CO1; X-ray; 3.30 A; B/D/F=1951-1973.
DR PDB; 7EVJ; X-ray; 2.57 A; A=1081-1197.
DR PDB; 7JFL; X-ray; 1.68 A; C/D=2065-2111.
DR PDB; 7JFM; X-ray; 2.23 A; C/D=2065-2111.
DR PDB; 7JUO; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1082-1197.
DR PDB; 7KPY; X-ray; 1.70 A; A/B=1082-1197.
DR PDB; 7TB3; EM; 2.57 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=587-668.
DR PDB; 7TBH; EM; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=587-668.
DR PDBsum; 1JSP; -.
DR PDBsum; 1LIQ; -.
DR PDBsum; 1RDT; -.
DR PDBsum; 1WO3; -.
DR PDBsum; 1WO4; -.
DR PDBsum; 1WO5; -.
DR PDBsum; 1WO6; -.
DR PDBsum; 1WO7; -.
DR PDBsum; 1ZOQ; -.
DR PDBsum; 2D82; -.
DR PDBsum; 2KJE; -.
DR PDBsum; 2KWF; -.
DR PDBsum; 2L84; -.
DR PDBsum; 2L85; -.
DR PDBsum; 2LXS; -.
DR PDBsum; 2LXT; -.
DR PDBsum; 2N1A; -.
DR PDBsum; 2RNY; -.
DR PDBsum; 3DWY; -.
DR PDBsum; 3P1C; -.
DR PDBsum; 3P1D; -.
DR PDBsum; 3P1E; -.
DR PDBsum; 3P1F; -.
DR PDBsum; 3SVH; -.
DR PDBsum; 4A9K; -.
DR PDBsum; 4N3W; -.
DR PDBsum; 4N4F; -.
DR PDBsum; 4NR4; -.
DR PDBsum; 4NR5; -.
DR PDBsum; 4NR6; -.
DR PDBsum; 4NR7; -.
DR PDBsum; 4NYV; -.
DR PDBsum; 4NYW; -.
DR PDBsum; 4NYX; -.
DR PDBsum; 4OUF; -.
DR PDBsum; 4TQN; -.
DR PDBsum; 4TS8; -.
DR PDBsum; 4WHU; -.
DR PDBsum; 4YK0; -.
DR PDBsum; 5CGP; -.
DR PDBsum; 5DBM; -.
DR PDBsum; 5EIC; -.
DR PDBsum; 5ENG; -.
DR PDBsum; 5EP7; -.
DR PDBsum; 5GH9; -.
DR PDBsum; 5H85; -.
DR PDBsum; 5I83; -.
DR PDBsum; 5I86; -.
DR PDBsum; 5I89; -.
DR PDBsum; 5I8B; -.
DR PDBsum; 5I8G; -.
DR PDBsum; 5J0D; -.
DR PDBsum; 5JEM; -.
DR PDBsum; 5KTU; -.
DR PDBsum; 5KTW; -.
DR PDBsum; 5KTX; -.
DR PDBsum; 5LPJ; -.
DR PDBsum; 5LPL; -.
DR PDBsum; 5MME; -.
DR PDBsum; 5MMG; -.
DR PDBsum; 5MPK; -.
DR PDBsum; 5MPN; -.
DR PDBsum; 5MPZ; -.
DR PDBsum; 5MQE; -.
DR PDBsum; 5MQG; -.
DR PDBsum; 5MQK; -.
DR PDBsum; 5NLK; -.
DR PDBsum; 5NRW; -.
DR PDBsum; 5NU3; -.
DR PDBsum; 5OWK; -.
DR PDBsum; 5SVH; -.
DR PDBsum; 5TB6; -.
DR PDBsum; 5W0E; -.
DR PDBsum; 5W0F; -.
DR PDBsum; 5W0L; -.
DR PDBsum; 5W0Q; -.
DR PDBsum; 5XXH; -.
DR PDBsum; 6ALB; -.
DR PDBsum; 6ALC; -.
DR PDBsum; 6AXQ; -.
DR PDBsum; 6AY3; -.
DR PDBsum; 6AY5; -.
DR PDBsum; 6DMK; -.
DR PDBsum; 6ES5; -.
DR PDBsum; 6ES6; -.
DR PDBsum; 6ES7; -.
DR PDBsum; 6FQO; -.
DR PDBsum; 6FQT; -.
DR PDBsum; 6FQU; -.
DR PDBsum; 6FR0; -.
DR PDBsum; 6FRF; -.
DR PDBsum; 6LQX; -.
DR PDBsum; 6M64; -.
DR PDBsum; 6QST; -.
DR PDBsum; 6SQE; -.
DR PDBsum; 6SQF; -.
DR PDBsum; 6SQM; -.
DR PDBsum; 6SXX; -.
DR PDBsum; 6YIJ; -.
DR PDBsum; 6YIK; -.
DR PDBsum; 6YIL; -.
DR PDBsum; 6YIM; -.
DR PDBsum; 7CO1; -.
DR PDBsum; 7EVJ; -.
DR PDBsum; 7JFL; -.
DR PDBsum; 7JFM; -.
DR PDBsum; 7JUO; -.
DR PDBsum; 7KPY; -.
DR PDBsum; 7TB3; -.
DR PDBsum; 7TBH; -.
DR AlphaFoldDB; Q92793; -.
DR BMRB; Q92793; -.
DR SMR; Q92793; -.
DR BioGRID; 107777; 486.
DR CORUM; Q92793; -.
DR DIP; DIP-952N; -.
DR ELM; Q92793; -.
DR IntAct; Q92793; 125.
DR MINT; Q92793; -.
DR STRING; 9606.ENSP00000262367; -.
DR BindingDB; Q92793; -.
DR ChEMBL; CHEMBL5747; -.
DR DrugBank; DB08655; 9-ACETYL-2,3,4,9-TETRAHYDRO-1H-CARBAZOL-1-ONE.
DR GuidetoPHARMACOLOGY; 2734; -.
DR GlyGen; Q92793; 12 sites, 1 O-linked glycan (12 sites).
DR iPTMnet; Q92793; -.
DR PhosphoSitePlus; Q92793; -.
DR BioMuta; CREBBP; -.
DR DMDM; 116241283; -.
DR EPD; Q92793; -.
DR jPOST; Q92793; -.
DR MassIVE; Q92793; -.
DR MaxQB; Q92793; -.
DR PaxDb; Q92793; -.
DR PeptideAtlas; Q92793; -.
DR PRIDE; Q92793; -.
DR ProteomicsDB; 62237; -.
DR ProteomicsDB; 75472; -. [Q92793-1]
DR Antibodypedia; 3781; 765 antibodies from 41 providers.
DR DNASU; 1387; -.
DR Ensembl; ENST00000262367.10; ENSP00000262367.5; ENSG00000005339.15. [Q92793-1]
DR Ensembl; ENST00000382070.7; ENSP00000371502.3; ENSG00000005339.15. [Q92793-2]
DR GeneID; 1387; -.
DR KEGG; hsa:1387; -.
DR MANE-Select; ENST00000262367.10; ENSP00000262367.5; NM_004380.3; NP_004371.2.
DR UCSC; uc002cvv.4; human. [Q92793-1]
DR CTD; 1387; -.
DR DisGeNET; 1387; -.
DR GeneCards; CREBBP; -.
DR GeneReviews; CREBBP; -.
DR HGNC; HGNC:2348; CREBBP.
DR HPA; ENSG00000005339; Low tissue specificity.
DR MalaCards; CREBBP; -.
DR MIM; 180849; phenotype.
DR MIM; 600140; gene.
DR MIM; 618332; phenotype.
DR neXtProt; NX_Q92793; -.
DR OpenTargets; ENSG00000005339; -.
DR Orphanet; 370026; Acute myeloid leukemia with t(8;16)(p11;p13) translocation.
DR Orphanet; 592574; Menke-Hennekam syndrome.
DR Orphanet; 353281; Rubinstein-Taybi syndrome due to 16p13.3 microdeletion.
DR Orphanet; 353277; Rubinstein-Taybi syndrome due to CREBBP mutations.
DR PharmGKB; PA26866; -.
DR VEuPathDB; HostDB:ENSG00000005339; -.
DR eggNOG; KOG1778; Eukaryota.
DR GeneTree; ENSGT00940000155364; -.
DR HOGENOM; CLU_000162_2_0_1; -.
DR InParanoid; Q92793; -.
DR OMA; XTISKDQ; -.
DR OrthoDB; 236283at2759; -.
DR PhylomeDB; Q92793; -.
DR TreeFam; TF101097; -.
DR BRENDA; 2.3.1.48; 2681.
DR PathwayCommons; Q92793; -.
DR Reactome; R-HSA-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR Reactome; R-HSA-1368082; RORA activates gene expression.
DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-210744; Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR Reactome; R-HSA-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-3371568; Attenuation phase.
DR Reactome; R-HSA-350054; Notch-HLH transcription pathway.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR Reactome; R-HSA-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR Reactome; R-HSA-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
DR Reactome; R-HSA-8941856; RUNX3 regulates NOTCH signaling.
DR Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-9013695; NOTCH4 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-918233; TRAF3-dependent IRF activation pathway.
DR Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
DR Reactome; R-HSA-9614657; FOXO-mediated transcription of cell death genes.
DR Reactome; R-HSA-9617629; Regulation of FOXO transcriptional activity by acetylation.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR Reactome; R-HSA-9707616; Heme signaling.
DR Reactome; R-HSA-9759194; Nuclear events mediated by NFE2L2.
DR SignaLink; Q92793; -.
DR SIGNOR; Q92793; -.
DR BioGRID-ORCS; 1387; 115 hits in 1117 CRISPR screens.
DR ChiTaRS; CREBBP; human.
DR EvolutionaryTrace; Q92793; -.
DR GeneWiki; CREB-binding_protein; -.
DR GenomeRNAi; 1387; -.
DR Pharos; Q92793; Tchem.
DR PRO; PR:Q92793; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q92793; protein.
DR Bgee; ENSG00000005339; Expressed in sural nerve and 206 other tissues.
DR ExpressionAtlas; Q92793; baseline and differential.
DR Genevisible; Q92793; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043426; F:MRF binding; IDA:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR GO; GO:0034212; F:peptide N-acetyltransferase activity; TAS:Reactome.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
DR GO; GO:0042733; P:embryonic digit morphogenesis; TAS:BHF-UCL.
DR GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
DR GO; GO:1990258; P:histone glutamine methylation; IDA:UniProtKB.
DR GO; GO:0042592; P:homeostatic process; NAS:UniProtKB.
DR GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:HGNC-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006473; P:protein acetylation; IDA:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; TAS:BHF-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; TAS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
DR CDD; cd15802; RING_CBP-p300; 1.
DR DisProt; DP02004; -.
DR Gene3D; 1.10.1630.10; -; 1.
DR Gene3D; 1.10.246.20; -; 1.
DR Gene3D; 1.20.1020.10; -; 2.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 2.10.110.40; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR IDEAL; IID00092; -.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR003101; KIX_dom.
DR InterPro; IPR036529; KIX_dom_sf.
DR InterPro; IPR009110; Nuc_rcpt_coact.
DR InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
DR InterPro; IPR037073; Nuc_rcpt_coact_CREBbp_sf.
DR InterPro; IPR010303; RING_CBP-p300.
DR InterPro; IPR038547; RING_CBP-p300_sf.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; PTHR13808; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF09030; Creb_binding; 1.
DR Pfam; PF06001; DUF902; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF02172; KIX; 1.
DR Pfam; PF02135; zf-TAZ; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47040; SSF47040; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57933; SSF57933; 2.
DR SUPFAM; SSF69125; SSF69125; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS50952; KIX; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Acyltransferase;
KW Alternative splicing; Biological rhythms; Bromodomain;
KW Chromosomal rearrangement; Cytoplasm; Disease variant;
KW Host-virus interaction; Intellectual disability; Isopeptide bond;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Transferase;
KW Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..2442
FT /note="CREB-binding protein"
FT /id="PRO_0000211190"
FT DOMAIN 587..666
FT /note="KIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00311"
FT DOMAIN 1103..1175
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 1323..1700
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01065"
FT ZN_FING 347..433
FT /note="TAZ-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT ZN_FING 1702..1750
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1765..1846
FT /note="TAZ-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..410
FT /note="Interaction with SRCAP"
FT /evidence="ECO:0000269|PubMed:10347196"
FT REGION 266..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1170
FT /note="Interaction with histone"
FT /evidence="ECO:0000269|PubMed:24361270"
FT REGION 1162..1180
FT /note="Interaction with ASF1A"
FT /evidence="ECO:0000269|PubMed:24616510"
FT REGION 1433..1435
FT /note="Interaction with histone"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT REGION 1460..1891
FT /note="Interaction with TRERF1"
FT /evidence="ECO:0000269|PubMed:11349124"
FT REGION 1556..1615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1874..1959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1977..2028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2112..2263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2294..2433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..862
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..887
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1065
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1556..1571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1588..1602
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1883..1916
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1921..1939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1940..1954
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1977..2008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2112..2145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2160..2186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2193..2220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2239..2263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2294..2350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2351..2378
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2395..2429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1434..1436
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1446..1447
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1493
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1498
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1502
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1707
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1710
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1720
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1723
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1729
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1732
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1738
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1740
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT SITE 29..30
FT /note="Breakpoint for translocation to form KAT6B-CREBBP"
FT SITE 266..267
FT /note="Breakpoint for translocation to form KAT6A-CREBBP"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 220
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 601
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 625
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 657
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P45481"
FT MOD_RES 1014
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1030
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 1076
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1216
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1382
FT /note="Phosphoserine; by IKKA"
FT /evidence="ECO:0000269|PubMed:17434128"
FT MOD_RES 1386
FT /note="Phosphoserine; by IKKA"
FT /evidence="ECO:0000269|PubMed:17434128"
FT MOD_RES 1583
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1591
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1592
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1595
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1597
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1741
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1744
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1763
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2063
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 2076
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2079
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P45481"
FT CROSSLNK 998
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P45481"
FT CROSSLNK 1033
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P45481"
FT CROSSLNK 1056
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P45481"
FT VAR_SEQ 406..444
FT /note="VAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQT -> A (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045700"
FT VARIANT 503
FT /note="Q -> H (in dbSNP:rs748447855)"
FT /evidence="ECO:0000269|PubMed:25388907"
FT /id="VAR_072912"
FT VARIANT 532
FT /note="P -> T (in dbSNP:rs902901184)"
FT /evidence="ECO:0000269|PubMed:25388907"
FT /id="VAR_072913"
FT VARIANT 546
FT /note="I -> N"
FT /evidence="ECO:0000269|PubMed:25388907"
FT /id="VAR_072914"
FT VARIANT 650
FT /note="Y -> F (in RSTS1)"
FT /evidence="ECO:0000269|PubMed:25388907"
FT /id="VAR_072915"
FT VARIANT 789
FT /note="A -> T (in RSTS1; dbSNP:rs746728741)"
FT /evidence="ECO:0000269|PubMed:25388907"
FT /id="VAR_072916"
FT VARIANT 910
FT /note="T -> A (in RSTS1; incomplete; dbSNP:rs143247685)"
FT /evidence="ECO:0000269|PubMed:20684013"
FT /id="VAR_072917"
FT VARIANT 1175
FT /note="Y -> C (in RSTS1; mild form; impairs binding to
FT ASF1A and acetylated histone H3; dbSNP:rs28937315)"
FT /evidence="ECO:0000269|PubMed:12114483,
FT ECO:0000269|PubMed:24616510, ECO:0000269|PubMed:25388907"
FT /id="VAR_037305"
FT VARIANT 1278
FT /note="E -> A (in RSTS1)"
FT /evidence="ECO:0000269|PubMed:25388907"
FT /id="VAR_072918"
FT VARIANT 1278
FT /note="E -> K (in RSTS1; abolishes acetyltransferase
FT activity; dbSNP:rs267606752)"
FT /evidence="ECO:0000269|PubMed:12566391,
FT ECO:0000269|PubMed:15706485"
FT /id="VAR_035080"
FT VARIANT 1378
FT /note="R -> P (in RSTS1; abolishes acetyltransferase
FT activity and the ability of transactivate CREB;
FT dbSNP:rs121434626)"
FT /evidence="ECO:0000269|PubMed:11331617,
FT ECO:0000269|PubMed:25388907"
FT /id="VAR_015578"
FT VARIANT 1406
FT /note="D -> Y (in RSTS1)"
FT /evidence="ECO:0000269|PubMed:25388907"
FT /id="VAR_072919"
FT VARIANT 1414
FT /note="V -> I (in dbSNP:rs130015)"
FT /id="VAR_027953"
FT VARIANT 1415
FT /note="Q -> P (in RSTS1)"
FT /evidence="ECO:0000269|PubMed:25388907"
FT /id="VAR_072920"
FT VARIANT 1447
FT /note="T -> I (in RSTS1)"
FT /evidence="ECO:0000269|PubMed:15706485"
FT /id="VAR_035081"
FT VARIANT 1450
FT /note="Y -> H (in RSTS1; dbSNP:rs1555473499)"
FT /evidence="ECO:0000269|PubMed:15706485"
FT /id="VAR_035082"
FT VARIANT 1470
FT /note="H -> R (in RSTS1; dbSNP:rs797044860)"
FT /evidence="ECO:0000269|PubMed:15706485"
FT /id="VAR_035083"
FT VARIANT 1475
FT /note="P -> T (in RSTS1)"
FT /evidence="ECO:0000269|PubMed:25388907"
FT /id="VAR_072921"
FT VARIANT 1503
FT /note="Y -> F (in RSTS1)"
FT /evidence="ECO:0000269|PubMed:25388907"
FT /id="VAR_072922"
FT VARIANT 1507
FT /note="L -> P (in RSTS1; dbSNP:rs1057520191)"
FT /evidence="ECO:0000269|PubMed:25388907"
FT /id="VAR_072923"
FT VARIANT 1543
FT /note="D -> N (in RSTS1)"
FT /evidence="ECO:0000269|PubMed:25388907"
FT /id="VAR_072924"
FT VARIANT 1664
FT /note="R -> H (in RSTS1; abolishes acetyltransferase
FT activity; dbSNP:rs1596791996)"
FT /evidence="ECO:0000269|PubMed:12566391,
FT ECO:0000269|PubMed:15706485"
FT /id="VAR_035084"
FT VARIANT 1710
FT /note="C -> R (in MKHK1; dbSNP:rs1567265203)"
FT /evidence="ECO:0000269|PubMed:27311832"
FT /id="VAR_078557"
FT VARIANT 1719
FT /note="H -> D (in MKHK1)"
FT /evidence="ECO:0000269|PubMed:29460469"
FT /id="VAR_081979"
FT VARIANT 1724
FT /note="E -> K (in MKHK1; dbSNP:rs1567265131)"
FT /evidence="ECO:0000269|PubMed:30737887"
FT /id="VAR_081980"
FT VARIANT 1747
FT /note="L -> R (in MKHK1)"
FT /evidence="ECO:0000269|PubMed:27311832"
FT /id="VAR_078558"
FT VARIANT 1782
FT /note="A -> V (in MKHK1)"
FT /evidence="ECO:0000269|PubMed:29460469"
FT /id="VAR_081981"
FT VARIANT 1786
FT /note="R -> P (in MKHK1)"
FT /evidence="ECO:0000269|PubMed:27311832"
FT /id="VAR_078559"
FT VARIANT 1819
FT /note="C -> F (in MKHK1)"
FT /evidence="ECO:0000269|PubMed:27311832"
FT /id="VAR_078560"
FT VARIANT 1826
FT /note="C -> W (in MKHK1)"
FT /evidence="ECO:0000269|PubMed:27311832"
FT /id="VAR_078561"
FT VARIANT 1829
FT /note="H -> D (in MKHK1)"
FT /evidence="ECO:0000269|PubMed:29460469"
FT /id="VAR_081982"
FT VARIANT 1838
FT /note="C -> Y (in MKHK1)"
FT /evidence="ECO:0000269|PubMed:27311832"
FT /id="VAR_078562"
FT VARIANT 1865..1866
FT /note="MR -> I (in MKHK1)"
FT /evidence="ECO:0000269|PubMed:29460469"
FT /id="VAR_081983"
FT VARIANT 1867
FT /note="R -> Q (in MKHK1; dbSNP:rs1131691326)"
FT /evidence="ECO:0000269|PubMed:27311832,
FT ECO:0000269|PubMed:29460469"
FT /id="VAR_078563"
FT VARIANT 1867
FT /note="R -> W (in MKHK1)"
FT /evidence="ECO:0000269|PubMed:27311832"
FT /id="VAR_078564"
FT VARIANT 1868
FT /note="R -> Q (in MKHK1; dbSNP:rs1567263168)"
FT /evidence="ECO:0000269|PubMed:29460469"
FT /id="VAR_081984"
FT VARIANT 1868
FT /note="R -> W (in MKHK1; dbSNP:rs886039491)"
FT /evidence="ECO:0000269|PubMed:27311832,
FT ECO:0000269|PubMed:29460469"
FT /id="VAR_078565"
FT VARIANT 1870
FT /note="A -> P (in MKHK1)"
FT /evidence="ECO:0000269|PubMed:29460469"
FT /id="VAR_081985"
FT VARIANT 1872
FT /note="M -> V (in MKHK1; dbSNP:rs797045037)"
FT /evidence="ECO:0000269|PubMed:27311832,
FT ECO:0000269|PubMed:29460469"
FT /id="VAR_078566"
FT MUTAGEN 1116
FT /note="D->R: Impairs binding to acetylated histones."
FT /evidence="ECO:0000269|PubMed:24616510"
FT MUTAGEN 1126
FT /note="F->A: Impairs binding to acetylated histones."
FT /evidence="ECO:0000269|PubMed:24616510"
FT MUTAGEN 1162
FT /note="N->E,R: Abolishes interaction with ASF1A."
FT /evidence="ECO:0000269|PubMed:24616510"
FT MUTAGEN 1165
FT /note="W->A: Abolishes interaction with ASF1A."
FT /evidence="ECO:0000269|PubMed:24616510"
FT MUTAGEN 1170
FT /note="K->E: Impairs binding to acetylated histones."
FT /evidence="ECO:0000269|PubMed:24616510"
FT MUTAGEN 1179
FT /note="S->I: Impairs interaction with ASF1A."
FT /evidence="ECO:0000269|PubMed:24616510"
FT MUTAGEN 1180
FT /note="K->E: Abolishes interaction with ASF1A."
FT /evidence="ECO:0000269|PubMed:24616510"
FT MUTAGEN 1183
FT /note="E->R: Abolishes interaction with ASF1A."
FT /evidence="ECO:0000269|PubMed:24616510"
FT CONFLICT 1511..1513
FT /note="FAE -> NSG (in Ref. 2; AAC51340)"
FT /evidence="ECO:0000305"
FT CONFLICT 1724..1725
FT /note="ED -> VV (in Ref. 2; AAC51340)"
FT /evidence="ECO:0000305"
FT CONFLICT 1770
FT /note="L -> V (in Ref. 1; AAC51770)"
FT /evidence="ECO:0000305"
FT CONFLICT 1789
FT /note="N -> F (in Ref. 2; AAC51340)"
FT /evidence="ECO:0000305"
FT CONFLICT 1812
FT /note="T -> P (in Ref. 2; AAC51340)"
FT /evidence="ECO:0000305"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:1RDT"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:1LIQ"
FT TURN 383..388
FT /evidence="ECO:0007829|PDB:1LIQ"
FT HELIX 391..395
FT /evidence="ECO:0007829|PDB:1LIQ"
FT HELIX 592..595
FT /evidence="ECO:0007829|PDB:5SVH"
FT HELIX 598..612
FT /evidence="ECO:0007829|PDB:5SVH"
FT HELIX 618..622
FT /evidence="ECO:0007829|PDB:5SVH"
FT HELIX 624..641
FT /evidence="ECO:0007829|PDB:5SVH"
FT HELIX 647..670
FT /evidence="ECO:0007829|PDB:5SVH"
FT HELIX 1087..1102
FT /evidence="ECO:0007829|PDB:5I86"
FT TURN 1105..1108
FT /evidence="ECO:0007829|PDB:5I86"
FT HELIX 1109..1111
FT /evidence="ECO:0007829|PDB:5I86"
FT HELIX 1117..1120
FT /evidence="ECO:0007829|PDB:5I86"
FT HELIX 1125..1128
FT /evidence="ECO:0007829|PDB:5I86"
FT HELIX 1135..1143
FT /evidence="ECO:0007829|PDB:5I86"
FT STRAND 1146..1149
FT /evidence="ECO:0007829|PDB:2L85"
FT HELIX 1150..1167
FT /evidence="ECO:0007829|PDB:5I86"
FT TURN 1169..1171
FT /evidence="ECO:0007829|PDB:1JSP"
FT HELIX 1173..1195
FT /evidence="ECO:0007829|PDB:5I86"
FT STRAND 1214..1218
FT /evidence="ECO:0007829|PDB:5I8G"
FT STRAND 1226..1230
FT /evidence="ECO:0007829|PDB:5I8G"
FT TURN 1231..1233
FT /evidence="ECO:0007829|PDB:5I8G"
FT STRAND 1234..1237
FT /evidence="ECO:0007829|PDB:5I8G"
FT TURN 1238..1240
FT /evidence="ECO:0007829|PDB:5I8G"
FT STRAND 1266..1272
FT /evidence="ECO:0007829|PDB:5I8G"
FT STRAND 1280..1282
FT /evidence="ECO:0007829|PDB:5I8G"
FT TURN 1284..1286
FT /evidence="ECO:0007829|PDB:5I8G"
FT STRAND 1289..1291
FT /evidence="ECO:0007829|PDB:5I8G"
FT HELIX 1292..1295
FT /evidence="ECO:0007829|PDB:5I8G"
FT TURN 1309..1311
FT /evidence="ECO:0007829|PDB:5I8G"
FT TURN 1708..1710
FT /evidence="ECO:0007829|PDB:2N1A"
FT STRAND 1718..1721
FT /evidence="ECO:0007829|PDB:2N1A"
FT STRAND 1725..1728
FT /evidence="ECO:0007829|PDB:2N1A"
FT HELIX 1730..1736
FT /evidence="ECO:0007829|PDB:2N1A"
FT STRAND 1742..1744
FT /evidence="ECO:0007829|PDB:2N1A"
FT HELIX 1765..1784
FT /evidence="ECO:0007829|PDB:2KJE"
FT HELIX 1793..1805
FT /evidence="ECO:0007829|PDB:2KJE"
FT TURN 1811..1815
FT /evidence="ECO:0007829|PDB:2KJE"
FT HELIX 1817..1832
FT /evidence="ECO:0007829|PDB:2KJE"
FT HELIX 1841..1853
FT /evidence="ECO:0007829|PDB:2KJE"
FT HELIX 1953..1967
FT /evidence="ECO:0007829|PDB:6M64"
FT TURN 2063..2065
FT /evidence="ECO:0007829|PDB:6ES5"
FT HELIX 2068..2070
FT /evidence="ECO:0007829|PDB:7JFM"
FT HELIX 2071..2073
FT /evidence="ECO:0007829|PDB:7JFL"
FT HELIX 2080..2092
FT /evidence="ECO:0007829|PDB:7JFL"
FT HELIX 2094..2103
FT /evidence="ECO:0007829|PDB:7JFL"
FT TURN 2104..2106
FT /evidence="ECO:0007829|PDB:1ZOQ"
SQ 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
