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 27-MAR-2024, entry version 261. DE RecName: Full=CREB-binding protein; DE AltName: Full=Histone lysine acetyltransferase CREBBP; DE EC=2.3.1.48 {ECO:0000269|PubMed:21131905, 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 {ECO:0000312|HGNC:HGNC:2348}; 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 FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=21131905; DOI=10.1038/emboj.2010.318; RA Jin Q., Yu L.R., Wang L., Zhang Z., Kasper L.H., Lee J.E., Wang C., RA Brindle P.K., Dent S.Y., Ge K.; RT "Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-mediated RT H3K18/27ac in nuclear receptor transactivation."; RL EMBO J. 30:249-262(2011). RN [49] 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 [50] 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 [51] 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 [52] 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 [53] 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 [54] 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 [55] 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 [56] RP SUBCELLULAR LOCATION. RX PubMed=25593309; DOI=10.1101/gad.252189.114; RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W., RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.; RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of RT transcription-associated DNA damage that promotes homologous RT recombination."; RL Genes Dev. 29:197-211(2015). RN [57] 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 [58] 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 [59] 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 [60] 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 [61] RP FUNCTION, CATALYTIC ACTIVITY, AND ACETYLATION. RX PubMed=35675826; DOI=10.1016/j.cmet.2022.05.005; RA Zhou N., Qi H., Liu J., Zhang G., Liu J., Liu N., Zhu M., Zhao X., Song C., RA Zhou Z., Gong J., Li R., Bai X., Jin Y., Song Y., Yin Y.; RT "Deubiquitinase OTUD3 regulates metabolism homeostasis in response to RT nutritional stresses."; RL Cell Metab. 34:1023-1041.e8(2022). RN [62] 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 [63] 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 [64] 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 [65] 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 [66] {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 [67] 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; LYS-1170; 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 [68] 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 [69] {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 [70] 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 [71] 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 [72] 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 [73] 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 [74] 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 [75] 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 [76] 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 [77] 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 [78] 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:21131905, PubMed:24616510). Mediates CC acetylation of histone H3 at 'Lys-18' and 'Lys-27' (H3K18ac and CC H3K27ac, respectively) (PubMed:21131905). Also acetylates non-histone CC proteins, like DDX21, FBL, IRF2, MAFG, NCOA3, POLR1E/PAF53 and FOXO1 CC (PubMed:10490106, PubMed:11154691, PubMed:12738767, PubMed:12929931, CC PubMed:9707565, PubMed:24207024, PubMed:28790157, PubMed:30540930, CC PubMed:35675826). 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-BMAL1 and CLOCK-BMAL1 heterodimers CC (PubMed:14645221). Acetylates PCNA; acetylation promotes removal of CC chromatin-bound PCNA and its degradation during nucleotide excision CC repair (NER) (PubMed:24939902). Acetylates POLR1E/PAF53, leading to CC decreased association of RNA polymerase I with the rDNA promoter region CC and coding region (PubMed:24207024). Acetylates DDX21, thereby CC inhibiting DDX21 helicase activity (PubMed:28790157). Acetylates FBL, CC preventing methylation of 'Gln-105' of histone H2A (H2AQ104me) CC (PubMed:30540930). Functions as a transcriptional coactivator for SMAD4 CC in the TGF-beta signaling pathway (PubMed:25514493). CC {ECO:0000269|PubMed:10490106, ECO:0000269|PubMed:11154691, CC ECO:0000269|PubMed:12738767, ECO:0000269|PubMed:12929931, CC ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:21131905, 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:35675826, 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:21131905, ECO:0000269|PubMed:24616510}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; CC Evidence={ECO:0000269|PubMed:21131905, 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, ECO:0000269|PubMed:35675826}; 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 ECO:0000269|PubMed:35675826}; 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 BMAL1. Interacts with ASF1A and ASF1B; CC this promotes histone acetylation. Interacts with acetylated TP53/p53 CC 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). Interacts with MSX1; CC the interaction may inhibit MSX1 autoinactivation (By similarity). CC Interacts with ACSS2 (By similarity). {ECO:0000250|UniProtKB:P45481, 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=3; 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 {ECO:0000269|PubMed:12929931}. Nucleus CC {ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:15488321, CC ECO:0000269|PubMed:25593309}. Note=Recruited to nuclear bodies by CC SS18L1/CREST (PubMed:15488321). In the presence of ALX1 relocalizes CC from the cytoplasm to the nucleus (PubMed:12929931). CC {ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:15488321}. 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 (PubMed:24616510). CC Autoacetylation is induced by glucose and fatty acids CC (PubMed:35675826). {ECO:0000269|PubMed:24616510, CC ECO:0000269|PubMed:35675826}. 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="https://atlasgeneticsoncology.org/gene/42/crebbp"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=P300/CBP entry; CC URL="https://en.wikipedia.org/wiki/P300/CBP"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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; 7RLE; X-ray; 2.50 A; B/D=57-80. 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 PDB; 7WX2; X-ray; 1.24 A; A=1081-1197. DR PDB; 7XH6; X-ray; 1.75 A; A/B=1081-1197. DR PDB; 7XHE; X-ray; 1.59 A; A/B=1081-1197. DR PDB; 7XI0; X-ray; 1.62 A; A/B=1081-1197. DR PDB; 7XIJ; X-ray; 1.82 A; A=1081-1197. DR PDB; 7XM7; X-ray; 2.36 A; A/B/C/D=1081-1197. DR PDB; 7XNE; X-ray; 2.17 A; A/B=1081-1197. DR PDB; 7XNG; X-ray; 2.35 A; A/B=1081-1197. DR PDB; 8HAL; EM; 4.40 A; K=1084-1873. DR PDB; 8HAM; EM; 4.50 A; K=1084-1873. DR PDB; 8HAN; EM; 4.20 A; K=1084-1873. 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; 7RLE; -. DR PDBsum; 7TB3; -. DR PDBsum; 7TBH; -. DR PDBsum; 7WX2; -. DR PDBsum; 7XH6; -. DR PDBsum; 7XHE; -. DR PDBsum; 7XI0; -. DR PDBsum; 7XIJ; -. DR PDBsum; 7XM7; -. DR PDBsum; 7XNE; -. DR PDBsum; 7XNG; -. DR PDBsum; 8HAL; -. DR PDBsum; 8HAM; -. DR PDBsum; 8HAN; -. DR AlphaFoldDB; Q92793; -. DR BMRB; Q92793; -. DR EMDB; EMD-25791; -. DR EMDB; EMD-25799; -. DR EMDB; EMD-34595; -. DR EMDB; EMD-34596; -. DR EMDB; EMD-34597; -. DR SMR; Q92793; -. DR BioGRID; 107777; 517. 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 DrugBank; DB02587; Colforsin. DR GuidetoPHARMACOLOGY; 2734; -. DR GlyCosmos; Q92793; 12 sites, 1 glycan. DR GlyGen; Q92793; 17 sites, 1 O-linked glycan (17 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; 9606-ENSP00000262367; -. DR PeptideAtlas; Q92793; -. DR ProteomicsDB; 62237; -. DR ProteomicsDB; 75472; -. [Q92793-1] DR Pumba; Q92793; -. DR Antibodypedia; 3781; 864 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 AGR; HGNC:2348; -. 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; CQVIVAH; -. DR OrthoDB; 5490807at2759; -. 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 Reactome; R-HSA-9768919; NPAS4 regulates expression of target genes. DR Reactome; R-HSA-9793380; Formation of paraxial mesoderm. DR Reactome; R-HSA-9818026; NFE2L2 regulating inflammation associated genes. DR Reactome; R-HSA-9818027; NFE2L2 regulating anti-oxidant/detoxification enzymes. DR Reactome; R-HSA-9818028; NFE2L2 regulates pentose phosphate pathway genes. DR Reactome; R-HSA-9818030; NFE2L2 regulating tumorigenic genes. DR Reactome; R-HSA-9818032; NFE2L2 regulating MDR associated enzymes. DR Reactome; R-HSA-9818035; NFE2L2 regulating ER-stress associated genes. DR Reactome; R-HSA-9818749; Regulation of NFE2L2 gene expression. DR Reactome; R-HSA-9819196; Zygotic genome activation (ZGA). DR SignaLink; Q92793; -. DR SIGNOR; Q92793; -. DR BioGRID-ORCS; 1387; 137 hits in 1212 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 207 other cell types or tissues. DR ExpressionAtlas; Q92793; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central. DR GO; GO:0016604; C:nuclear body; IDA:HPA. 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:0043993; F:histone H3K18 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0044017; F:histone H3K27 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:0031669; P:cellular response to nutrient levels; IDA:UniProt. 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:0042592; P:homeostatic process; NAS:UniProtKB. DR GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; IDA:UniProtKB. DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0038061; P:non-canonical NF-kappaB signal transduction; IDA:UniProt. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:UniProt. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:HGNC-UCL. 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:0006355; P:regulation of DNA-templated transcription; TAS:UniProtKB. DR GO; GO:0008589; P:regulation of smoothened signaling pathway; TAS:BHF-UCL. 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; cd05495; Bromo_cbp_like; 1. DR CDD; cd20910; NCBD_CREBBP-p300_like; 1. DR CDD; cd15557; PHD_CBP_p300; 1. DR CDD; cd15802; RING_CBP-p300; 1. DR CDD; cd02337; ZZ_CBP; 1. DR DisProt; DP02004; -. DR Gene3D; 2.10.110.40; -; 1. DR Gene3D; 3.30.60.90; -; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 1. DR Gene3D; 1.10.246.20; Coactivator CBP, KIX domain; 1. DR Gene3D; 1.10.1630.10; Nuclear receptor coactivator, CREB-bp-like, interlocking domain; 1. DR Gene3D; 1.20.1020.10; TAZ domain; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR IDEAL; 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; CBP/P300-RELATED; 1. DR PANTHER; PTHR13808:SF34; CREB-BINDING PROTEIN; 1. DR Pfam; PF00439; Bromodomain; 1. DR Pfam; PF09030; Creb_binding; 1. DR Pfam; PF08214; HAT_KAT11; 1. DR Pfam; PF02172; KIX; 1. DR Pfam; PF06001; RING_CBP-p300; 1. DR Pfam; PF02135; zf-TAZ; 2. DR Pfam; PF00569; ZZ; 1. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 1. DR SMART; SM01250; KAT11; 1. DR SMART; SM00551; ZnF_TAZ; 2. DR SMART; SM00291; ZnF_ZZ; 1. DR SUPFAM; SSF47370; Bromodomain; 1. DR SUPFAM; SSF47040; Kix domain of CBP (creb binding protein); 1. DR SUPFAM; SSF69125; Nuclear receptor coactivator interlocking domain; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR SUPFAM; SSF57933; TAZ domain; 2. DR PROSITE; PS00633; BROMODOMAIN_1; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 1. DR PROSITE; PS51727; CBP_P300_HAT; 1. DR PROSITE; PS50952; KIX; 1. DR PROSITE; PS50134; ZF_TAZ; 2. DR PROSITE; PS01357; ZF_ZZ_1; 1. DR PROSITE; PS50135; ZF_ZZ_2; 1. DR Genevisible; Q92793; HS. 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; dbSNP:rs2052153254)" 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; dbSNP:rs2051858361)" 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 63..66 FT /evidence="ECO:0007829|PDB:7RLE" 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 //