CBP_MOUSE
ID CBP_MOUSE Reviewed; 2441 AA.
AC P45481; E9QPH4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 226.
DE RecName: Full=Histone lysine acetyltransferase CREBBP;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q92793};
DE AltName: Full=Protein-lysine acetyltransferase CREBBP;
DE EC=2.3.1.- {ECO:0000269|PubMed:15220471};
GN Name=Crebbp; Synonyms=Cbp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8413673; DOI=10.1038/365855a0;
RA Chrivia J.C., Kwok R.P.S., Lamb N., Hagiwara M., Montminy M.R.,
RA Goodman R.H.;
RT "Phosphorylated CREB binds specifically to the nuclear protein CBP.";
RL Nature 365:855-859(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP INTERACTION WITH NCOA1.
RX PubMed=8616895; DOI=10.1016/s0092-8674(00)81118-6;
RA Kamei Y., Xu L., Heinzel T., Torchia J., Kurokawa R., Gloss B., Lin S.-C.,
RA Heyman R.A., Rose D.W., Glass C.K., Rosenfeld M.G.;
RT "A CBP integrator complex mediates transcriptional activation and AP-1
RT inhibition by nuclear receptors.";
RL Cell 85:403-414(1996).
RN [4]
RP INTERACTION WITH CREB1, AND MUTAGENESIS OF ARG-600.
RX PubMed=8552098; DOI=10.1128/mcb.16.2.694;
RA Parker D., Ferreri K., Nakajima T., LaMorte V.J., Evans R., Koerber S.C.,
RA Hoeger C., Montminy M.R.;
RT "Phosphorylation of CREB at Ser-133 induces complex formation with CREB-
RT binding protein via a direct mechanism.";
RL Mol. Cell. Biol. 16:694-703(1996).
RN [5]
RP INTERACTION WITH NCOA3.
RX PubMed=9192892; DOI=10.1038/42652;
RA Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K.,
RA Rosenfeld M.G.;
RT "The transcriptional co-activator p/CIP binds CBP and mediates nuclear-
RT receptor function.";
RL Nature 387:677-684(1997).
RN [6]
RP FUNCTION, INTERACTION WITH GATA1, AND MUTAGENESIS OF 1690-LYS-CYS-1691.
RX PubMed=10207073; DOI=10.1128/mcb.19.5.3496;
RA Hung H.L., Lau J., Kim A.Y., Weiss M.J., Blobel G.A.;
RT "CREB-Binding protein acetylates hematopoietic transcription factor GATA-1
RT at functionally important sites.";
RL Mol. Cell. Biol. 19:3496-3505(1999).
RN [7]
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 [8]
RP INTERACTION WITH CARM1, METHYLATION AT ARG-600 AND ARG-624, AND FUNCTION.
RX PubMed=11701890; DOI=10.1126/science.1065961;
RA Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M.,
RA Evans R.M.;
RT "A transcriptional switch mediated by cofactor methylation.";
RL Science 294:2507-2511(2001).
RN [9]
RP INTERACTION WITH CITED4.
RX PubMed=12504852; DOI=10.1006/geno.2002.7005;
RA Yahata T., Takedatsu H., Dunwoodie S.L., Braganca J., Swingler T.,
RA Withington S.L., Hur J., Coser K.R., Isselbacher K.J., Bhattacharya S.,
RA Shioda T.;
RT "Cloning of mouse Cited4, a member of the CITED family p300/CBP-binding
RT transcriptional coactivators: induced expression in mammary epithelial
RT cells.";
RL Genomics 80:601-613(2002).
RN [10]
RP INTERACTION WITH MAF.
RX PubMed=11943779; DOI=10.1074/jbc.m201821200;
RA Chen Q., Dowhan D.H., Liang D., Moore D.D., Overbeek P.A.;
RT "CREB-binding protein/p300 co-activation of crystallin gene expression.";
RL J. Biol. Chem. 277:24081-24089(2002).
RN [11]
RP INTERACTION WITH DDX5.
RX PubMed=12527917; DOI=10.1038/sj.onc.1206067;
RA Rossow K.L., Janknecht R.;
RT "Synergism between p68 RNA helicase and the transcriptional coactivators
RT CBP and p300.";
RL Oncogene 22:151-156(2003).
RN [12]
RP FUNCTION IN ACETYLATION OF FOXO1, AND CATALYTIC ACTIVITY.
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 [13]
RP SUMOYLATION AT LYS-999; LYS-1015; LYS-1034 AND LYS-1057, INTERACTION WITH
RP DAXX, FUNCTION, AND MUTAGENESIS OF LYS-999; LYS-1015; LYS-1034; LYS-1043;
RP LYS-1053; LYS-1057 AND LYS-1061.
RX PubMed=16287980; DOI=10.1073/pnas.0504460102;
RA Kuo H.-Y., Chang C.-C., Jeng J.-C., Hu H.-M., Lin D.-Y., Maul G.G.,
RA Kwok R.P.S., Shih H.-M.;
RT "SUMO modification negatively modulates the transcriptional activity of
RT CREB-binding protein via the recruitment of Daxx.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16973-16978(2005).
RN [14]
RP INTERACTION WITH DDX17.
RX PubMed=17226766; DOI=10.1002/jcb.21250;
RA Shin S., Janknecht R.;
RT "Concerted activation of the Mdm2 promoter by p72 RNA helicase and the
RT coactivators p300 and P/CAF.";
RL J. Cell. Biochem. 101:1252-1265(2007).
RN [15]
RP INTERACTION WITH ZCCHC12.
RX PubMed=18160706; DOI=10.1128/mcb.01038-07;
RA Cho G., Lim Y., Zand D., Golden J.A.;
RT "Sizn1 is a novel protein that functions as a transcriptional coactivator
RT of bone morphogenic protein signaling.";
RL Mol. Cell. Biol. 28:1565-1572(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-2064 AND SER-2350,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-656; LYS-1217; LYS-1596; LYS-1598
RP AND LYS-1745, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [18]
RP FUNCTION, AND INTERACTION WITH ARNTL/BMAL1.
RX PubMed=24737000; DOI=10.1371/journal.pbio.1001840;
RA Anafi R.C., Lee Y., Sato T.K., Venkataraman A., Ramanathan C.,
RA Kavakli I.H., Hughes M.E., Baggs J.E., Growe J., Liu A.C., Kim J.,
RA Hogenesch J.B.;
RT "Machine learning helps identify CHRONO as a circadian clock component.";
RL PLoS Biol. 12:E1001840-E1001840(2014).
RN [19]
RP STRUCTURE BY NMR OF 340-439 IN COMPLEX WITH 220-269 OF CITED2 AND ZINC
RP IONS.
RX PubMed=14594809; DOI=10.1074/jbc.m310348200;
RA De Guzman R.N., Martinez-Yamout M.A., Dyson H.J., Wright P.E.;
RT "Interaction of the TAZ1 domain of the CREB-binding protein with the
RT activation domain of CITED2: regulation by competition between
RT intrinsically unstructured ligands for non-identical binding sites.";
RL J. Biol. Chem. 279:3042-3049(2004).
CC -!- FUNCTION: Acetylates histones, giving a specific tag for
CC transcriptional activation (By similarity). Also acetylates non-histone
CC proteins, like DDX21, FBL, IRF2, MAFG, NCOA3, POLR1E/PAF53 and FOXO1
CC (PubMed:10207073, PubMed:11701890, PubMed:16287980, PubMed:15220471).
CC Binds specifically to phosphorylated CREB and enhances its
CC transcriptional activity toward cAMP-responsive genes (By similarity).
CC Acts as a coactivator of ALX1 (By similarity). Acts as a circadian
CC transcriptional coactivator which enhances the activity of the
CC circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-
CC ARNTL/BMAL1 heterodimers (By similarity). Acetylates PCNA; acetylation
CC promotes removal of chromatin-bound PCNA and its degradation during
CC nucleotide excision repair (NER) (PubMed:24737000). Acetylates
CC POLR1E/PAF53, leading to decreased association of RNA polymerase I with
CC the rDNA promoter region and coding region (By similarity). Acetylates
CC DDX21, thereby inhibiting DDX21 helicase activity (By similarity).
CC Acetylates FBL, preventing methylation of 'Gln-105' of histone H2A
CC (H2AQ104me) (By similarity). Functions as a transcriptional coactivator
CC for SMAD4 in the TGF-beta signaling pathway (By similarity).
CC {ECO:0000250|UniProtKB:Q92793, ECO:0000269|PubMed:10207073,
CC ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:15220471,
CC ECO:0000269|PubMed:16287980, ECO:0000269|PubMed:24737000}.
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:0000250|UniProtKB:Q92793};
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:15220471};
CC -!- SUBUNIT: Interacts with DHX9 (via N-terminus); this interaction
CC mediates association with RNA polymerase II holoenzyme and stimulates
CC CREB-dependent transcriptional activation (By similarity). Interacts
CC (via transactivation domain and C-terminus) with PCNA; the interaction
CC occurs on chromatin in UV-irradiated damaged cells (By similarity).
CC Found in a complex containing NCOA2; NCOA3; IKKA; IKKB and IKBKG.
CC Probably part of a complex with HIF1A and EP300. The TAZ-type 1 domain
CC interacts with HIF1A. Interacts with SRCAP, ELF3, MLLT7/FOXO4, N4BP2,
CC NCOA6, PCAF, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB and TRERF1.
CC Interacts with KLF1; the interaction results in acetylation and
CC enhancement of transcriptional activity of KLF1. Interacts with MAFG;
CC the interaction acetylates MAFG in the basic region and stimulates NFE2
CC transcriptional activity through increasing its DNA-binding activity.
CC Interacts with IRF2; the interaction acetylates IRF2 and regulates its
CC activity on the H4 promoter. Interacts with IRF3 (when phosphorylated);
CC forming the dsRNA-activated factor 1 (DRAF1), a complex which activates
CC the transcription of the type I interferon genes (By similarity).
CC Interacts (via N-terminus) with SS18L1/CREST (via C-terminus).
CC Interacts with FOXO1; the interaction acetylates FOXO1 and inhibits its
CC transcriptional activity. Interacts with MECOM and MTDH. Interacts with
CC ASF1A and ASF1B; this promotes histone acetylation. Interacts with
CC acetylated TP53/p53 and with the acetylated histones H3 and H4 (By
CC similarity). Interacts with CITED1 (via C-terminus). Interacts with
CC GATA1; the interaction results in acetylation and enhancement of
CC transcriptional activity of GATA1. Interacts with MAF, CARM1. NCOA3,
CC ZCCHC12, DDX17, DDX5 AND CITED4 (C-terminal region). Interacts with
CC phosphorylated CREB1. Interacts with DAXX; the interaction is dependent
CC on CBP sumoylation and results in suppression of the transcriptional
CC activity via recruitment of HDAC2 to DAXX. Interacts with NPAS2, CLOCK
CC and ARNTL/BMAL1. Interacts with SMAD4; negatively regulated by ZBTB7A
CC (By similarity). Forms a complex with KMT2A and CREB1 (By similarity).
CC Interacts with DDX3X; this interaction may facilitate HNF4A acetylation
CC (By similarity). {ECO:0000250|UniProtKB:Q92793,
CC ECO:0000269|PubMed:10207073, ECO:0000269|PubMed:10722728,
CC ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:11943779,
CC ECO:0000269|PubMed:12504852, ECO:0000269|PubMed:12527917,
CC ECO:0000269|PubMed:14594809, ECO:0000269|PubMed:16287980,
CC ECO:0000269|PubMed:17226766, ECO:0000269|PubMed:18160706,
CC ECO:0000269|PubMed:24737000, ECO:0000269|PubMed:8552098,
CC ECO:0000269|PubMed:8616895, ECO:0000269|PubMed:9192892}.
CC -!- INTERACTION:
CC P45481; Q9WTL8-4: Arntl; NbExp=2; IntAct=EBI-296306, EBI-644568;
CC P45481; Q02248: Ctnnb1; NbExp=3; IntAct=EBI-296306, EBI-397872;
CC P45481; P27577: Ets1; NbExp=3; IntAct=EBI-296306, EBI-4289053;
CC P45481; Q60749: Khdrbs1; NbExp=7; IntAct=EBI-296306, EBI-519077;
CC P45481; Q04207: Rela; NbExp=9; IntAct=EBI-296306, EBI-644400;
CC P45481; Q62318-1: Trim28; NbExp=2; IntAct=EBI-296306, EBI-6876996;
CC P45481; P41182: BCL6; Xeno; NbExp=2; IntAct=EBI-296306, EBI-765407;
CC P45481; O60566: BUB1B; Xeno; NbExp=3; IntAct=EBI-296306, EBI-1001438;
CC P45481; P61201: COPS2; Xeno; NbExp=2; IntAct=EBI-296306, EBI-1050386;
CC P45481; P17844: DDX5; Xeno; NbExp=3; IntAct=EBI-296306, EBI-351962;
CC P45481; P35637: FUS; Xeno; NbExp=4; IntAct=EBI-296306, EBI-400434;
CC P45481; P62805: H4C9; Xeno; NbExp=2; IntAct=EBI-296306, EBI-302023;
CC P45481; Q03164: KMT2A; Xeno; NbExp=7; IntAct=EBI-296306, EBI-591370;
CC P45481; O95863: SNAI1; Xeno; NbExp=7; IntAct=EBI-296306, EBI-1045459;
CC P45481; P04637: TP53; Xeno; NbExp=10; IntAct=EBI-296306, EBI-366083;
CC P45481; P03254; Xeno; NbExp=3; IntAct=EBI-296306, EBI-8599077;
CC P45481; P03255; Xeno; NbExp=2; IntAct=EBI-296306, EBI-2603114;
CC P45481; P88946; Xeno; NbExp=6; IntAct=EBI-296306, EBI-936023;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92793}.
CC Nucleus. Note=Recruited to nuclear bodies by SS18L1/CREST. In the
CC presence of ALX1 relocalizes from the cytoplasm to the nucleus.
CC {ECO:0000250|UniProtKB:Q92793}.
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. {ECO:0000269|PubMed:11701890}.
CC -!- PTM: Phosphorylated by CHUK/IKKA at Ser-1383 and Ser-1387; these
CC phosphorylations promote cell growth by switching the binding
CC preference of CREBBP from TP53 to NF-kappa-B.
CC {ECO:0000250|UniProtKB:Q92793}.
CC -!- PTM: Sumoylation negatively regulates transcriptional activity via the
CC recruitment of DAAX. {ECO:0000269|PubMed:16287980}.
CC -!- PTM: Autoacetylation is required for binding to protein substrates,
CC such as acetylated histones and acetylated TP53/p53.
CC {ECO:0000250|UniProtKB:Q92793}.
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DR EMBL; S66385; AAB28651.1; -; mRNA.
DR EMBL; AC132380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS27915.1; -.
DR PIR; S39161; S39161.
DR PDB; 1F81; NMR; -; A=1764-1850.
DR PDB; 1JJS; NMR; -; A=2067-2112.
DR PDB; 1KBH; NMR; -; B=2059-2117.
DR PDB; 1KDX; NMR; -; A=586-666.
DR PDB; 1L8C; NMR; -; A=345-439.
DR PDB; 1R8U; NMR; -; B=340-439.
DR PDB; 1SB0; NMR; -; A=586-672.
DR PDB; 1TOT; NMR; -; A=1700-1751.
DR PDB; 1U2N; NMR; -; A=340-439.
DR PDB; 2AGH; NMR; -; B=586-672.
DR PDB; 2C52; NMR; -; A=2059-2117.
DR PDB; 2KA4; NMR; -; A=340-439.
DR PDB; 2KA6; NMR; -; A=1764-1855.
DR PDB; 2KKJ; NMR; -; A=2059-2117.
DR PDB; 2L14; NMR; -; A=2059-2117.
DR PDB; 2LQH; NMR; -; A=586-672.
DR PDB; 2LQI; NMR; -; A=586-672.
DR PDB; 2LWW; NMR; -; A=340-439.
DR PDB; 4I9O; X-ray; 2.00 A; A=586-672.
DR PDB; 5HOU; NMR; -; A=340-439.
DR PDB; 5HP0; NMR; -; A=1764-1857.
DR PDB; 5HPD; NMR; -; A=1764-1855.
DR PDB; 5U4K; NMR; -; A=586-672.
DR PDB; 5U7G; X-ray; 2.40 A; A/B=1079-1556.
DR PDB; 5W0I; X-ray; 1.43 A; A=1083-1198.
DR PDB; 6DMX; X-ray; 2.80 A; B/D/G/I=586-672.
DR PDB; 6DNQ; X-ray; 2.35 A; B/D=586-672.
DR PDB; 7LVS; X-ray; 2.02 A; B=340-439.
DR PDBsum; 1F81; -.
DR PDBsum; 1JJS; -.
DR PDBsum; 1KBH; -.
DR PDBsum; 1KDX; -.
DR PDBsum; 1L8C; -.
DR PDBsum; 1R8U; -.
DR PDBsum; 1SB0; -.
DR PDBsum; 1TOT; -.
DR PDBsum; 1U2N; -.
DR PDBsum; 2AGH; -.
DR PDBsum; 2C52; -.
DR PDBsum; 2KA4; -.
DR PDBsum; 2KA6; -.
DR PDBsum; 2KKJ; -.
DR PDBsum; 2L14; -.
DR PDBsum; 2LQH; -.
DR PDBsum; 2LQI; -.
DR PDBsum; 2LWW; -.
DR PDBsum; 4I9O; -.
DR PDBsum; 5HOU; -.
DR PDBsum; 5HP0; -.
DR PDBsum; 5HPD; -.
DR PDBsum; 5U4K; -.
DR PDBsum; 5U7G; -.
DR PDBsum; 5W0I; -.
DR PDBsum; 6DMX; -.
DR PDBsum; 6DNQ; -.
DR PDBsum; 7LVS; -.
DR AlphaFoldDB; P45481; -.
DR BMRB; P45481; -.
DR SASBDB; P45481; -.
DR SMR; P45481; -.
DR CORUM; P45481; -.
DR DIP; DIP-5974N; -.
DR IntAct; P45481; 39.
DR MINT; P45481; -.
DR STRING; 10090.ENSMUSP00000023165; -.
DR iPTMnet; P45481; -.
DR PhosphoSitePlus; P45481; -.
DR SwissPalm; P45481; -.
DR EPD; P45481; -.
DR jPOST; P45481; -.
DR MaxQB; P45481; -.
DR PaxDb; P45481; -.
DR PRIDE; P45481; -.
DR ProteomicsDB; 281475; -.
DR MGI; MGI:1098280; Crebbp.
DR eggNOG; KOG1778; Eukaryota.
DR InParanoid; P45481; -.
DR Reactome; R-MMU-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-MMU-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-MMU-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
DR Reactome; R-MMU-3371568; Attenuation phase.
DR Reactome; R-MMU-350054; Notch-HLH transcription pathway.
DR Reactome; R-MMU-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-MMU-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR Reactome; R-MMU-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
DR Reactome; R-MMU-8941856; RUNX3 regulates NOTCH signaling.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR Reactome; R-MMU-918233; TRAF3-dependent IRF activation pathway.
DR Reactome; R-MMU-933541; TRAF6 mediated IRF7 activation.
DR Reactome; R-MMU-9617629; Regulation of FOXO transcriptional activity by acetylation.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR Reactome; R-MMU-9759194; Nuclear events mediated by NFE2L2.
DR ChiTaRS; Crebbp; mouse.
DR EvolutionaryTrace; P45481; -.
DR PRO; PR:P45481; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P45481; protein.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000940; C:outer kinetochore; IDA:MGI.
DR GO; GO:0016605; C:PML body; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0016407; F:acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008140; F:cAMP response element binding protein binding; IPI:CAFA.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:MGI.
DR GO; GO:0043426; F:MRF binding; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; ISO:MGI.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0001093; F:TFIIB-class transcription factor binding; IPI:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IMP:CAFA.
DR GO; GO:0048148; P:behavioral response to cocaine; ISO:MGI.
DR GO; GO:0008283; P:cell population proliferation; ISO:MGI.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IDA:MGI.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0098586; P:cellular response to virus; IMP:CAFA.
DR GO; GO:0060325; P:face morphogenesis; IMP:ARUK-UCL.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:MGI.
DR GO; GO:0016573; P:histone acetylation; ISS:UniProtKB.
DR GO; GO:1990258; P:histone glutamine methylation; ISS:UniProtKB.
DR GO; GO:0007616; P:long-term memory; ISO:MGI.
DR GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; ISS:UniProtKB.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:CAFA.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0048525; P:negative regulation of viral process; IMP:CAFA.
DR GO; GO:0060355; P:positive regulation of cell adhesion molecule production; ISO:MGI.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IDA:MGI.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; TAS:UniProtKB.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:MGI.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
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; ISO:MGI.
DR GO; GO:0006473; P:protein acetylation; ISO:MGI.
DR GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd15802; RING_CBP-p300; 1.
DR DisProt; DP00348; -.
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; IID50008; -.
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; Biological rhythms;
KW Bromodomain; Cytoplasm; Isopeptide bond; Metal-binding; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT CHAIN 2..2441
FT /note="Histone lysine acetyltransferase CREBBP"
FT /id="PRO_0000211191"
FT DOMAIN 586..665
FT /note="KIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00311"
FT DOMAIN 1104..1176
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 1324..1701
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01065"
FT ZN_FING 346..432
FT /note="TAZ-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT ZN_FING 1703..1751
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1766..1847
FT /note="TAZ-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..409
FT /note="Interaction with SRCAP"
FT /evidence="ECO:0000250"
FT REGION 261..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1171
FT /note="Interaction with histone"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT REGION 1163..1181
FT /note="Interaction with ASF1A"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT REGION 1434..1436
FT /note="Interaction with histone"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT REGION 1557..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1875..1959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2112..2421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..864
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..889
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1589..1603
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1884..1917
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1922..1939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1941..1955
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2112..2146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2169..2265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2276..2349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2350..2377
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2394..2421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 421
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 1435..1437
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1447..1448
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1494
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1499
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1503
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1708
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1711
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1721
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1724
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1730
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1733
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1739
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1741
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 219
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT MOD_RES 600
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000305|PubMed:11701890"
FT MOD_RES 624
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000305|PubMed:11701890"
FT MOD_RES 656
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1015
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT MOD_RES 1077
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT MOD_RES 1217
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1383
FT /note="Phosphoserine; by IKKA"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT MOD_RES 1387
FT /note="Phosphoserine; by IKKA"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT MOD_RES 1584
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT MOD_RES 1592
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT MOD_RES 1593
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT MOD_RES 1596
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1598
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1742
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT MOD_RES 1745
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1764
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT MOD_RES 2064
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2077
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT MOD_RES 2080
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT MOD_RES 2350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 999
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000269|PubMed:16287980"
FT CROSSLNK 1034
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000269|PubMed:16287980"
FT CROSSLNK 1057
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000269|PubMed:16287980"
FT MUTAGEN 600
FT /note="R->N: Abolishes binding to CREB."
FT /evidence="ECO:0000269|PubMed:8552098"
FT MUTAGEN 999
FT /note="K->R: Enhanced transcriptional activity. No
FT sumoylation, loss of recruitment of HDAC2 to DAAX and
FT greatly enhanced transcriptional activity; when associated
FT with R-1034 and R-1057."
FT /evidence="ECO:0000269|PubMed:16287980"
FT MUTAGEN 1015
FT /note="K->R: No change in sumoylation."
FT /evidence="ECO:0000269|PubMed:16287980"
FT MUTAGEN 1034
FT /note="K->R: Enhanced transcriptional activity. No
FT sumoylation, loss of recruitment of HDAC2 to DAAX and
FT greatly enhanced transcriptional activity; when associated
FT with R-999 and R-1057."
FT /evidence="ECO:0000269|PubMed:16287980"
FT MUTAGEN 1043
FT /note="K->R: No change in sumoylation."
FT /evidence="ECO:0000269|PubMed:16287980"
FT MUTAGEN 1053
FT /note="K->R: No change in sumoylation."
FT /evidence="ECO:0000269|PubMed:16287980"
FT MUTAGEN 1057
FT /note="K->R: Enhanced transcriptional activity. No
FT sumoylation, loss of recruitment of HDAC2 to DAAX and
FT greatly enhanced transcriptional activity; when associated
FT with R-999 and R-1034."
FT /evidence="ECO:0000269|PubMed:16287980"
FT MUTAGEN 1061
FT /note="K->R: No change in sumoylation."
FT /evidence="ECO:0000269|PubMed:16287980"
FT MUTAGEN 1087
FT /note="K->R: No change in sumoylation."
FT MUTAGEN 1690..1691
FT /note="LC->KL: Abolishes histone acetyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:10207073"
FT CONFLICT 400
FT /note="G -> P (in Ref. 1; AAB28651)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="I -> V (in Ref. 1; AAB28651)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="S -> T (in Ref. 1; AAB28651)"
FT /evidence="ECO:0000305"
FT CONFLICT 826
FT /note="V -> E (in Ref. 1; AAB28651)"
FT /evidence="ECO:0000305"
FT CONFLICT 978
FT /note="S -> T (in Ref. 1; AAB28651)"
FT /evidence="ECO:0000305"
FT CONFLICT 1159
FT /note="W -> R (in Ref. 1; AAB28651)"
FT /evidence="ECO:0000305"
FT CONFLICT 1239
FT /note="E -> G (in Ref. 1; AAB28651)"
FT /evidence="ECO:0000305"
FT CONFLICT 1417
FT /note="N -> D (in Ref. 1; AAB28651)"
FT /evidence="ECO:0000305"
FT CONFLICT 1429
FT /note="R -> C (in Ref. 1; AAB28651)"
FT /evidence="ECO:0000305"
FT CONFLICT 1466
FT /note="G -> V (in Ref. 1; AAB28651)"
FT /evidence="ECO:0000305"
FT CONFLICT 1470
FT /note="G -> A (in Ref. 1; AAB28651)"
FT /evidence="ECO:0000305"
FT CONFLICT 1850..1851
FT /note="KL -> NV (in Ref. 1; AAB28651)"
FT /evidence="ECO:0000305"
FT CONFLICT 1859
FT /note="R -> C (in Ref. 1; AAB28651)"
FT /evidence="ECO:0000305"
FT CONFLICT 1987
FT /note="A -> D (in Ref. 1; AAB28651)"
FT /evidence="ECO:0000305"
FT CONFLICT 2060
FT /note="P -> N (in Ref. 1; AAB28651)"
FT /evidence="ECO:0000305"
FT CONFLICT 2381
FT /note="S -> T (in Ref. 1; AAB28651)"
FT /evidence="ECO:0000305"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:2KA4"
FT HELIX 347..373
FT /evidence="ECO:0007829|PDB:7LVS"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:1U2N"
FT HELIX 384..394
FT /evidence="ECO:0007829|PDB:7LVS"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:7LVS"
FT HELIX 408..420
FT /evidence="ECO:0007829|PDB:7LVS"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:2LWW"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:7LVS"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:7LVS"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:1R8U"
FT HELIX 590..594
FT /evidence="ECO:0007829|PDB:4I9O"
FT HELIX 597..611
FT /evidence="ECO:0007829|PDB:4I9O"
FT TURN 617..619
FT /evidence="ECO:0007829|PDB:4I9O"
FT HELIX 622..642
FT /evidence="ECO:0007829|PDB:4I9O"
FT HELIX 646..664
FT /evidence="ECO:0007829|PDB:4I9O"
FT TURN 667..671
FT /evidence="ECO:0007829|PDB:1SB0"
FT HELIX 1088..1103
FT /evidence="ECO:0007829|PDB:5W0I"
FT TURN 1106..1109
FT /evidence="ECO:0007829|PDB:5W0I"
FT HELIX 1110..1112
FT /evidence="ECO:0007829|PDB:5W0I"
FT HELIX 1118..1121
FT /evidence="ECO:0007829|PDB:5W0I"
FT HELIX 1126..1129
FT /evidence="ECO:0007829|PDB:5W0I"
FT HELIX 1136..1144
FT /evidence="ECO:0007829|PDB:5W0I"
FT HELIX 1151..1168
FT /evidence="ECO:0007829|PDB:5W0I"
FT HELIX 1174..1197
FT /evidence="ECO:0007829|PDB:5W0I"
FT STRAND 1281..1283
FT /evidence="ECO:0007829|PDB:5U7G"
FT TURN 1285..1287
FT /evidence="ECO:0007829|PDB:5U7G"
FT STRAND 1290..1292
FT /evidence="ECO:0007829|PDB:5U7G"
FT HELIX 1293..1296
FT /evidence="ECO:0007829|PDB:5U7G"
FT TURN 1300..1302
FT /evidence="ECO:0007829|PDB:5U7G"
FT HELIX 1310..1314
FT /evidence="ECO:0007829|PDB:5U7G"
FT HELIX 1334..1350
FT /evidence="ECO:0007829|PDB:5U7G"
FT STRAND 1358..1371
FT /evidence="ECO:0007829|PDB:5U7G"
FT HELIX 1374..1380
FT /evidence="ECO:0007829|PDB:5U7G"
FT TURN 1381..1384
FT /evidence="ECO:0007829|PDB:5U7G"
FT STRAND 1388..1403
FT /evidence="ECO:0007829|PDB:5U7G"
FT STRAND 1406..1418
FT /evidence="ECO:0007829|PDB:5U7G"
FT STRAND 1429..1437
FT /evidence="ECO:0007829|PDB:5U7G"
FT HELIX 1444..1446
FT /evidence="ECO:0007829|PDB:5U7G"
FT HELIX 1447..1465
FT /evidence="ECO:0007829|PDB:5U7G"
FT STRAND 1469..1473
FT /evidence="ECO:0007829|PDB:5U7G"
FT STRAND 1483..1487
FT /evidence="ECO:0007829|PDB:5U7G"
FT HELIX 1497..1513
FT /evidence="ECO:0007829|PDB:5U7G"
FT STRAND 1518..1522
FT /evidence="ECO:0007829|PDB:5U7G"
FT HELIX 1523..1530
FT /evidence="ECO:0007829|PDB:5U7G"
FT HELIX 1535..1537
FT /evidence="ECO:0007829|PDB:5U7G"
FT HELIX 1545..1555
FT /evidence="ECO:0007829|PDB:5U7G"
FT TURN 1709..1711
FT /evidence="ECO:0007829|PDB:1TOT"
FT STRAND 1713..1726
FT /evidence="ECO:0007829|PDB:1TOT"
FT HELIX 1731..1737
FT /evidence="ECO:0007829|PDB:1TOT"
FT STRAND 1741..1746
FT /evidence="ECO:0007829|PDB:1TOT"
FT HELIX 1765..1785
FT /evidence="ECO:0007829|PDB:1F81"
FT HELIX 1794..1808
FT /evidence="ECO:0007829|PDB:1F81"
FT HELIX 1812..1815
FT /evidence="ECO:0007829|PDB:1F81"
FT HELIX 1818..1833
FT /evidence="ECO:0007829|PDB:1F81"
FT STRAND 1840..1843
FT /evidence="ECO:0007829|PDB:5HPD"
FT HELIX 1844..1849
FT /evidence="ECO:0007829|PDB:1F81"
FT STRAND 2061..2064
FT /evidence="ECO:0007829|PDB:1KBH"
FT HELIX 2068..2075
FT /evidence="ECO:0007829|PDB:1JJS"
FT STRAND 2076..2079
FT /evidence="ECO:0007829|PDB:1JJS"
FT HELIX 2088..2091
FT /evidence="ECO:0007829|PDB:1JJS"
FT HELIX 2097..2100
FT /evidence="ECO:0007829|PDB:1JJS"
FT HELIX 2102..2104
FT /evidence="ECO:0007829|PDB:1JJS"
FT STRAND 2106..2108
FT /evidence="ECO:0007829|PDB:1JJS"
SQ SEQUENCE 2441 AA; 265494 MW; D89AF52B7BD33347 CRC64;
MAENLLDGPP NPKRAKLSSP GFSANDNTDF GSLFDLENDL PDELIPNGEL SLLNSGNLVP
DAASKHKQLS ELLRGGSGSS INPGIGNVSA SSPVQQGLGG QAQGQPNSTN MASLGAMGKS
PLNQGDSSTP NLPKQAASTS GPTPPASQAL NPQAQKQVGL VTSSPATSQT GPGICMNANF
NQTHPGLLNS NSGHSLMNQA QQGQAQVMNG SLGAAGRGRG AGMPYPAPAM QGATSSVLAE
TLTQVSPQMA GHAGLNTAQA GGMTKMGMTG TTSPFGQPFS QTGGQQMGAT GVNPQLASKQ
SMVNSLPAFP TDIKNTSVTT VPNMSQLQTS VGIVPTQAIA TGPTADPEKR KLIQQQLVLL
LHAHKCQRRE QANGEVRACS LPHCRTMKNV LNHMTHCQAG KACQVAHCAS SRQIISHWKN
CTRHDCPVCL PLKNASDKRN QQTILGSPAS GIQNTIGSVG AGQQNATSLS NPNPIDPSSM
QRAYAALGLP YMNQPQTQLQ PQVPGQQPAQ PPAHQQMRTL NALGNNPMSI PAGGITTDQQ
PPNLISESAL PTSLGATNPL MNDGSNSGNI GSLSTIPTAA PPSSTGVRKG WHEHVTQDLR
SHLVHKLVQA IFPTPDPAAL KDRRMENLVA YAKKVEGDMY ESANSRDEYY HLLAEKIYKI
QKELEEKRRS RLHKQGILGN QPALPASGAQ PPVIPPAQSV RPPNGPLPLP VNRMQVSQGM
NSFNPMSLGN VQLPQAPMGP RAASPMNHSV QMNSMASVPG MAISPSRMPQ PPNMMGTHAN
NIMAQAPTQN QFLPQNQFPS SSGAMSVNSV GMGQPAAQAG VSQGQVPGAA LPNPLNMLAP
QASQLPCPPV TQSPLHPTPP PASTAAGMPS LQHPTAPGMT PPQPAAPTQP STPVSSGQTP
TPTPGSVPSA AQTQSTPTVQ AAAQAQVTPQ PQTPVQPPSV ATPQSSQQQP TPVHTQPPGT
PLSQAAASID NRVPTPSSVT SAETSSQQPG PDVPMLEMKT EVQTDDAEPE PTESKGEPRS
EMMEEDLQGS SQVKEETDTT EQKSEPMEVE EKKPEVKVEA KEEEENSSND TASQSTSPSQ
PRKKIFKPEE LRQALMPTLE ALYRQDPESL PFRQPVDPQL LGIPDYFDIV KNPMDLSTIK
RKLDTGQYQE PWQYVDDVWL MFNNAWLYNR KTSRVYKFCS KLAEVFEQEI DPVMQSLGYC
CGRKYEFSPQ TLCCYGKQLC TIPRDAAYYS YQNRYHFCEK CFTEIQGENV TLGDDPSQPQ
TTISKDQFEK KKNDTLDPEP FVDCKECGRK MHQICVLHYD IIWPSGFVCD NCLKKTGRPR
KENKFSAKRL QTTRLGNHLE DRVNKFLRRQ NHPEAGEVFV RVVASSDKTV EVKPGMKSRF
VDSGEMSESF PYRTKALFAF EEIDGVDVCF FGMHVQNTAL IAPHQIQGRV YISYLDSIHF
FRPRCLRTAV YHEILIGYLE YVKKLGYVTG HIWACPPSEG DDYIFHCHPP DQKIPKPKRL
QEWYKKMLDK AFAERIINDY KDIFKQANED RLTSAKELPY FEGDFWPNVL EESIKELEQE
EEERKKEEST AASETPEGSQ GDSKNAKKKN NKKTNKNKSS ISRANKKKPS MPNVSNDLSQ
KLYATMEKHK EVFFVIHLHA GPVISTQPPI VDPDPLLSCD LMDGRDAFLT LARDKHWEFS
SLRRSKWSTL CMLVELHTQG QDRFVYTCNE CKHHVETRWH CTVCEDYDLC INCYNTKSHT
HKMVKWGLGL DDEGSSQGEP QSKSPQESRR LSIQRCIQSL VHACQCRNAN CSLPSCQKMK
RVVQHTKGCK RKTNGGCPVC KQLIALCCYH AKHCQENKCP VPFCLNIKHK LRQQQIQHRL
QQAQLMRRRM ATMNTRNVPQ QSLPSPTSAP PGTPTQQPST PQTPQPPAQP QPSPVNMSPA
GFPNVARTQP PTIVSAGKPT NQVPAPPPPA QPPPAAVEAA RQIEREAQQQ QHLYRANINN
GMPPGRAGMG TPGSQMTPVG LNVPRPNQVS GPVMSSMPPG QWQQAPIPQQ QPMPGMPRPV
MSMQAQAAVA GPRMPNVQPP RSISPSALQD LLRTLKSPSS PQQQQQVLNI LKSNPQLMAA
FIKQRTAKYV ANQPGMQPQP GLQSQPGMQP QPGMHQQPSL QNLNAMQAGV PRPGVPPPQP
AMGGLNPQGQ ALNIMNPGHN PNMTNMNPQY REMVRRQLLQ HQQQQQQQQQ QQQQQQNSAS
LAGGMAGHSQ FQQPQGPGGY APAMQQQRMQ QHLPIQGSSM GQMAAPMGQL GQMGQPGLGA
DSTPNIQQAL QQRILQQQQM KQQIGSPGQP NPMSPQQHML SGQPQASHLP GQQIATSLSN
QVRSPAPVQS PRPQSQPPHS SPSPRIQPQP SPHHVSPQTG SPHPGLAVTM ASSMDQGHLG
NPEQSAMLPQ LNTPNRSALS SELSLVGDTT GDTLEKFVEG L
