[1]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
DOI=10.1038/365855a0; PubMed=8413673 [NCBI, ExPASy, EBI, Israel, Japan]
Chrivia J.C.,
Kwok R.P.S.,
Lamb N.,
Hagiwara M.,
Montminy M.R.,
Goodman R.H.;
"Phosphorylated CREB binds specifically to the nuclear protein CBP.";
Nature 365:855-859(1993).
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[2]
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INTERACTION WITH NCOA1.
DOI=10.1016/S0092-8674(00)81118-6; PubMed=8616895 [NCBI, ExPASy, EBI, Israel, Japan]
Kamei Y.,
Xu L.,
Heinzel T.,
Torchia J.,
Kurokawa R.,
Gloss B.,
Lin S.-C.,
Heyman R.A.,
Rose D.W.,
Glass C.K.,
Rosenfeld M.G.;
"A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors.";
Cell 85:403-414(1996).
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[3]
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INTERACTION WITH CREB1, AND MUTAGENESIS OF ARG-600.
PubMed=8552098 [NCBI, ExPASy, EBI, Israel, Japan]
Parker D.,
Ferreri K.,
Nakajima T.,
LaMorte V.J.,
Evans R.,
Koerber S.C.,
Hoeger C.,
Montminy M.R.;
"Phosphorylation of CREB at Ser-133 induces complex formation with CREB-binding protein via a direct mechanism.";
Mol. Cell. Biol. 16:694-703(1996).
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[4]
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INTERACTION WITH NCOA3.
DOI=10.1038/42652; PubMed=9192892 [NCBI, ExPASy, EBI, Israel, Japan]
Torchia J.,
Rose D.W.,
Inostroza J.,
Kamei Y.,
Westin S.,
Glass C.K.,
Rosenfeld M.G.;
"The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function.";
Nature 387:677-684(1997).
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[5]
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INTERACTION WITH CARM1, METHYLATION AT ARG-600 AND ARG-624, AND FUNCTION.
DOI=10.1126/science.1065961; PubMed=11701890 [NCBI, ExPASy, EBI, Israel, Japan]
Xu W.,
Chen H.,
Du K.,
Asahara H.,
Tini M.,
Emerson B.M.,
Montminy M.,
Evans R.M.;
"A transcriptional switch mediated by cofactor methylation.";
Science 294:2507-2511(2001).
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[6]
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INTERACTION WITH CITED4.
DOI=10.1006/geno.2002.7005; PubMed=12504852 [NCBI, ExPASy, EBI, Israel, Japan]
Yahata T.,
Takedatsu H.,
Dunwoodie S.L.,
Braganca J.,
Swingler T.,
Withington S.L.,
Hur J.,
Coser K.R.,
Isselbacher K.J.,
Bhattacharya S.,
Shioda T.;
"Cloning of mouse Cited4, a member of the CITED family p300/CBP-binding transcriptional coactivators: induced expression in mammary epithelial cells.";
Genomics 80:601-613(2002).
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[7]
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INTERACTION WITH MAF.
DOI=10.1074/jbc.M201821200; PubMed=11943779 [NCBI, ExPASy, EBI, Israel, Japan]
Chen Q.,
Dowhan D.H.,
Liang D.,
Moore D.D.,
Overbeek P.A.;
"CREB-binding protein/p300 co-activation of crystallin gene expression.";
J. Biol. Chem. 277:24081-24089(2002).
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[8]
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SUMOYLATION AT LYS-999; LYS-1015; LYS-1034 AND LYS-1057, INTERACTION WITH DAXX, FUNCTION, AND MUTAGENESIS OF LYS-999; LYS-1015; LYS-1034; LYS-1043; LYS-1053; LYS-1057 AND LYS-1061.
DOI=10.1073/pnas.0504460102; PubMed=16287980 [NCBI, ExPASy, EBI, Israel, Japan]
Kuo H.-Y.,
Chang C.-C.,
Jeng J.-C.,
Hu H.-M.,
Lin D.-Y.,
Maul G.G.,
Kwok R.P.S.,
Shih H.-M.;
"SUMO modification negatively modulates the transcriptional activity of CREB-binding protein via the recruitment of Daxx.";
Proc. Natl. Acad. Sci. U.S.A. 102:16973-16978(2005).
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[9]
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INTERACTION WITH ZCCHC12.
DOI=10.1128/MCB.01038-07; PubMed=18160706 [NCBI, ExPASy, EBI, Israel, Japan]
Cho G.,
Lim Y.,
Zand D.,
Golden J.A.;
"Sizn1 is a novel protein that functions as a transcriptional coactivator of bone morphogenic protein signaling.";
Mol. Cell. Biol. 28:1565-1572(2008).
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- FUNCTION: Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non-histone proteins, like NCOA3 coactivator. Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes (By similarity).
- CATALYTIC ACTIVITY: Acetyl-CoA + histone = CoA + acetylhistone.
- SUBUNIT: Found in a complex containing NCOA2; NCOA3; IKKA; IKKB and IKBKG. Probably part of a complex with HIF1A and EP300. Interacts with phosphorylated CREB1. Interacts with the C-terminal region of CITED4. The TAZ-type 1 domain interacts with HIF1A. Interacts with SRCAP, CARM1, ELF3, MLLT7/FOXO4, N4BP2, NCOA1, NCOA3, NCOA6, PCAF, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB, TRERF1 and ZCCHC12. Interacts with KLF1; the interaction results in acetylation and enhancement of transcriptional activity of KLF1 (By similarity). Interacts with DAXX; the interaction is dependent on CBP sumoylation and results in suppression of the transcriptional activity via recruitment of HDAC2 to DAAX. Interacts with MAF. Interacts with MTDH (By similarity). Interacts with MAFG; the interaction acetylates MAFG in the basic region and stimulates NFE2 transcriptional activity through increasing its DNA-binding activity. Interacts with IRF2; the interaction acetylates IRF2 and regulates its activity on the H4 promoter (By similarity).
- INTERACTION:
P88946:- (xeno); NbExp=4; IntAct=EBI-296306, EBI-936023;
P16220:CREB1 (xeno); NbExp=1; IntAct=EBI-296306, EBI-711855;
Q60749:Khdrbs1; NbExp=3; IntAct=EBI-296306, EBI-519077;
P10242:MYB (xeno); NbExp=1; IntAct=EBI-296306, EBI-298355;
Q04207:Rela; NbExp=1; IntAct=EBI-296306, EBI-644400;
P36956-1:SREBF1 (xeno); NbExp=1; IntAct=EBI-296306, EBI-948328;
P04637:TP53 (xeno); NbExp=2; IntAct=EBI-296306, EBI-366083;
Q64451:Trp53; NbExp=1; IntAct=EBI-296306, EBI-493476;
Q9EPK5:Wwtr1; NbExp=1; IntAct=EBI-296306, EBI-1211920;
- SUBCELLULAR LOCATION: Nucleus.
- PTM: Methylation of the KIX domain by CARM1 blocks association with CREB. This results in the blockade of CREB signaling, and in activation of apoptotic response.
- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By similarity).
- PTM: Sumoylation negatively regulates transcriptional activity via the recruitment of DAAX.
- SIMILARITY: Contains 1 bromo domain.
- SIMILARITY: Contains 1 KIX domain.
- SIMILARITY: Contains 2 TAZ-type zinc fingers.
- SIMILARITY: Contains 1 ZZ-type zinc finger.
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