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CREB-binding protein (EC 2.3.1.48)

 CBP_MOUSE               Reviewed;        2441 AA.
P45481; E9QPH4;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
10-OCT-2018, entry version 203.
RecName: Full=CREB-binding protein;
EC=2.3.1.48 {ECO:0000250|UniProtKB:Q92793};
Name=Crebbp; Synonyms=Cbp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8413673; DOI=10.1038/365855a0;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
INTERACTION WITH NCOA1.
PubMed=8616895; DOI=10.1016/S0092-8674(00)81118-6;
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).
[4]
INTERACTION WITH CREB1, AND MUTAGENESIS OF ARG-600.
PubMed=8552098; DOI=10.1128/MCB.16.2.694;
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).
[5]
INTERACTION WITH NCOA3.
PubMed=9192892; DOI=10.1038/42652;
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).
[6]
FUNCTION, INTERACTION WITH GATA1, AND MUTAGENESIS OF
1690-LYS-CYS-1691.
PubMed=10207073; DOI=10.1128/MCB.19.5.3496;
Hung H.L., Lau J., Kim A.Y., Weiss M.J., Blobel G.A.;
"CREB-Binding protein acetylates hematopoietic transcription factor
GATA-1 at functionally important sites.";
Mol. Cell. Biol. 19:3496-3505(1999).
[7]
INTERACTION WITH CITED1.
PubMed=10722728; DOI=10.1074/jbc.275.12.8825;
Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S.,
Roberts A.B., Isselbacher K.J., Shioda T.;
"The MSG1 non-DNA-binding transactivator binds to the p300/CBP
coactivators, enhancing their functional link to the Smad
transcription factors.";
J. Biol. Chem. 275:8825-8834(2000).
[8]
INTERACTION WITH CARM1, METHYLATION AT ARG-600 AND ARG-624, AND
FUNCTION.
PubMed=11701890; DOI=10.1126/science.1065961;
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).
[9]
INTERACTION WITH CITED4.
PubMed=12504852; DOI=10.1006/geno.2002.7005;
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).
[10]
INTERACTION WITH MAF.
PubMed=11943779; DOI=10.1074/jbc.M201821200;
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).
[11]
INTERACTION WITH DDX5.
PubMed=12527917; DOI=10.1038/sj.onc.1206067;
Rossow K.L., Janknecht R.;
"Synergism between p68 RNA helicase and the transcriptional
coactivators CBP and p300.";
Oncogene 22:151-156(2003).
[12]
FUNCTION IN ACETYLATION OF FOXO1.
PubMed=15220471; DOI=10.1073/pnas.0400593101;
Daitoku H., Hatta M., Matsuzaki H., Aratani S., Ohshima T.,
Miyagishi M., Nakajima T., Fukamizu A.;
"Silent information regulator 2 potentiates Foxo1-mediated
transcription through its deacetylase activity.";
Proc. Natl. Acad. Sci. U.S.A. 101:10042-10047(2004).
[13]
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.
PubMed=16287980; DOI=10.1073/pnas.0504460102;
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).
[14]
INTERACTION WITH DDX17.
PubMed=17226766; DOI=10.1002/jcb.21250;
Shin S., Janknecht R.;
"Concerted activation of the Mdm2 promoter by p72 RNA helicase and the
coactivators p300 and P/CAF.";
J. Cell. Biochem. 101:1252-1265(2007).
[15]
INTERACTION WITH ZCCHC12.
PubMed=18160706; DOI=10.1128/MCB.01038-07;
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-2064 AND
SER-2350, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-656; LYS-1217; LYS-1596;
LYS-1598 AND LYS-1745, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[18]
INTERACTION WITH ARNTL/BMAL1.
PubMed=24737000; DOI=10.1371/journal.pbio.1001840;
Anafi R.C., Lee Y., Sato T.K., Venkataraman A., Ramanathan C.,
Kavakli I.H., Hughes M.E., Baggs J.E., Growe J., Liu A.C., Kim J.,
Hogenesch J.B.;
"Machine learning helps identify CHRONO as a circadian clock
component.";
PLoS Biol. 12:E1001840-E1001840(2014).
[19]
STRUCTURE BY NMR OF 340-439 IN COMPLEX WITH 220-269 OF CITED2 AND ZINC
IONS.
PubMed=14594809; DOI=10.1074/jbc.M310348200;
De Guzman R.N., Martinez-Yamout M.A., Dyson H.J., Wright P.E.;
"Interaction of the TAZ1 domain of the CREB-binding protein with the
activation domain of CITED2: regulation by competition between
intrinsically unstructured ligands for non-identical binding sites.";
J. Biol. Chem. 279:3042-3049(2004).
-!- FUNCTION: Acetylates histones, giving a specific tag for
transcriptional activation. Also acetylates non-histone proteins,
like NCOA3 and FOXO1. Binds specifically to phosphorylated CREB
and enhances its transcriptional activity toward cAMP-responsive
genes. Acts as a coactivator of ALX1. Acts as a circadian
transcriptional coactivator which enhances the activity of the
circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-
ARNTL/BMAL1 heterodimers. Acetylates PCNA; acetylation promotes
removal of chromatin-bound PCNA and its degradation during
nucleotide excision repair (NER). Functions as a transcriptional
coactivator for SMAD4 in the TGF-beta signaling pathway (By
similarity). {ECO:0000250|UniProtKB:Q92793,
ECO:0000269|PubMed:10207073, ECO:0000269|PubMed:11701890,
ECO:0000269|PubMed:15220471, ECO:0000269|PubMed:16287980}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine. {ECO:0000250|UniProtKB:Q92793}.
-!- SUBUNIT: Interacts with DHX9 (via N-terminus); this interaction
mediates association with RNA polymerase II holoenzyme and
stimulates CREB-dependent transcriptional activation (By
similarity). Interacts (via transactivation domain and C-terminus)
with PCNA; the interaction occurs on chromatin in UV-irradiated
damaged cells (By similarity). Found in a complex containing
NCOA2; NCOA3; IKKA; IKKB and IKBKG. Probably part of a complex
with HIF1A and EP300. The TAZ-type 1 domain interacts with HIF1A.
Interacts with SRCAP, ELF3, MLLT7/FOXO4, N4BP2, NCOA6, PCAF,
PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB and TRERF1. Interacts with
KLF1; the interaction results in acetylation and enhancement of
transcriptional activity of KLF1. Interacts with MAFG; the
interaction acetylates MAFG in the basic region and stimulates
NFE2 transcriptional activity through increasing its DNA-binding
activity. Interacts with IRF2; the interaction acetylates IRF2 and
regulates its activity on the H4 promoter. Interacts (via N-
terminus) with SS18L1/CREST (via C-terminus). Interacts with
FOXO1; the interaction acetylates FOXO1 and inhibits its
transcriptional activity. Interacts with MECOM and MTDH. Interacts
with ASF1A and ASF1B; this promotes histone acetylation. Interacts
with acetylated TP53/p53 and with the acetylated histones H3 and
H4 (By similarity). Interacts with CITED1 (via C-terminus).
Interacts with GATA1; the interaction results in acetylation and
enhancement of transcriptional activity of GATA1. Interacts with
MAF, CARM1. NCOA3, ZCCHC12, DDX17, DDX5 AND CITED4 (C-terminal
region). Interacts with phosphorylated CREB1. Interacts with DAXX;
the interaction is dependent on CBP sumoylation and results in
suppression of the transcriptional activity via recruitment of
HDAC2 to DAXX. Interacts with NPAS2, CLOCK and ARNTL/BMAL1.
Interacts with SMAD4; negatively regulated by ZBTB7A (By
similarity). {ECO:0000250|UniProtKB:Q92793,
ECO:0000269|PubMed:10207073, ECO:0000269|PubMed:10722728,
ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:11943779,
ECO:0000269|PubMed:12504852, ECO:0000269|PubMed:12527917,
ECO:0000269|PubMed:14594809, ECO:0000269|PubMed:16287980,
ECO:0000269|PubMed:17226766, ECO:0000269|PubMed:18160706,
ECO:0000269|PubMed:24737000, ECO:0000269|PubMed:8552098,
ECO:0000269|PubMed:8616895, ECO:0000269|PubMed:9192892}.
-!- INTERACTION:
P03254:- (xeno); NbExp=3; IntAct=EBI-296306, EBI-8599077;
P03255:- (xeno); NbExp=2; IntAct=EBI-296306, EBI-2603114;
P88946:- (xeno); NbExp=6; IntAct=EBI-296306, EBI-936023;
Q9WTL8-4:Arntl; NbExp=2; IntAct=EBI-296306, EBI-644568;
P41182:BCL6 (xeno); NbExp=2; IntAct=EBI-296306, EBI-765407;
O60566:BUB1B (xeno); NbExp=3; IntAct=EBI-296306, EBI-1001438;
P61201:COPS2 (xeno); NbExp=2; IntAct=EBI-296306, EBI-1050386;
Q01147:Creb1; NbExp=2; IntAct=EBI-296306, EBI-2291098;
Q02248:Ctnnb1; NbExp=3; IntAct=EBI-296306, EBI-397872;
P17844:DDX5 (xeno); NbExp=3; IntAct=EBI-296306, EBI-351962;
P27577:Ets1; NbExp=3; IntAct=EBI-296306, EBI-4289053;
P35637:FUS (xeno); NbExp=4; IntAct=EBI-296306, EBI-400434;
P62805:HIST2H4B (xeno); NbExp=2; IntAct=EBI-296306, EBI-302023;
Q60749:Khdrbs1; NbExp=7; IntAct=EBI-296306, EBI-519077;
Q03164:KMT2A (xeno); NbExp=7; IntAct=EBI-296306, EBI-591370;
Q04207:Rela; NbExp=9; IntAct=EBI-296306, EBI-644400;
O95863:SNAI1 (xeno); NbExp=7; IntAct=EBI-296306, EBI-1045459;
P04637:TP53 (xeno); NbExp=9; IntAct=EBI-296306, EBI-366083;
Q62318-1:Trim28; NbExp=2; IntAct=EBI-296306, EBI-6876996;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92793}.
Nucleus. Note=Recruited to nuclear bodies by SS18L1/CREST. In the
presence of ALX1 relocalizes from the cytoplasm to the nucleus.
{ECO:0000250|UniProtKB:Q92793}.
-!- 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. {ECO:0000269|PubMed:11701890}.
-!- PTM: Phosphorylated by CHUK/IKKA at Ser-1383 and Ser-1387; these
phosphorylations promote cell growth by switching the binding
preference of CREBBP from TP53 to NF-kappa-B. {ECO:0000250}.
-!- PTM: Sumoylation negatively regulates transcriptional activity via
the recruitment of DAAX. {ECO:0000269|PubMed:16287980}.
-!- PTM: Autoacetylation is required for binding to protein
substrates, such as acetylated histones and acetylated TP53/p53.
{ECO:0000250|UniProtKB:Q92793}.
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EMBL; S66385; AAB28651.1; -; mRNA.
EMBL; AC132380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS27915.1; -.
PIR; S39161; S39161.
UniGene; Mm.132238; -.
UniGene; Mm.392384; -.
PDB; 1F81; NMR; -; A=1764-1850.
PDB; 1JJS; NMR; -; A=2067-2112.
PDB; 1KBH; NMR; -; B=2059-2117.
PDB; 1KDX; NMR; -; A=586-666.
PDB; 1L8C; NMR; -; A=345-439.
PDB; 1R8U; NMR; -; B=340-439.
PDB; 1SB0; NMR; -; A=586-672.
PDB; 1TOT; NMR; -; A=1700-1751.
PDB; 1U2N; NMR; -; A=340-439.
PDB; 2AGH; NMR; -; B=586-672.
PDB; 2C52; NMR; -; A=2059-2117.
PDB; 2KA4; NMR; -; A=340-439.
PDB; 2KA6; NMR; -; A=1764-1855.
PDB; 2KKJ; NMR; -; A=2059-2117.
PDB; 2L14; NMR; -; A=2059-2117.
PDB; 2LQH; NMR; -; A=586-672.
PDB; 2LQI; NMR; -; A=586-672.
PDB; 2LWW; NMR; -; A=340-439.
PDB; 4I9O; X-ray; 2.00 A; A=586-672.
PDB; 5HOU; NMR; -; A=340-439.
PDB; 5HP0; NMR; -; A=1764-1857.
PDB; 5HPD; NMR; -; A=1764-1855.
PDB; 5U4K; NMR; -; A=586-672.
PDB; 5U7G; X-ray; 2.40 A; A/B=1079-1556.
PDB; 5W0I; X-ray; 1.43 A; A=1083-1198.
PDBsum; 1F81; -.
PDBsum; 1JJS; -.
PDBsum; 1KBH; -.
PDBsum; 1KDX; -.
PDBsum; 1L8C; -.
PDBsum; 1R8U; -.
PDBsum; 1SB0; -.
PDBsum; 1TOT; -.
PDBsum; 1U2N; -.
PDBsum; 2AGH; -.
PDBsum; 2C52; -.
PDBsum; 2KA4; -.
PDBsum; 2KA6; -.
PDBsum; 2KKJ; -.
PDBsum; 2L14; -.
PDBsum; 2LQH; -.
PDBsum; 2LQI; -.
PDBsum; 2LWW; -.
PDBsum; 4I9O; -.
PDBsum; 5HOU; -.
PDBsum; 5HP0; -.
PDBsum; 5HPD; -.
PDBsum; 5U4K; -.
PDBsum; 5U7G; -.
PDBsum; 5W0I; -.
DisProt; DP00348; -.
ProteinModelPortal; P45481; -.
SMR; P45481; -.
CORUM; P45481; -.
DIP; DIP-5974N; -.
IntAct; P45481; 39.
MINT; P45481; -.
STRING; 10090.ENSMUSP00000023165; -.
iPTMnet; P45481; -.
PhosphoSitePlus; P45481; -.
EPD; P45481; -.
MaxQB; P45481; -.
PaxDb; P45481; -.
PRIDE; P45481; -.
MGI; MGI:1098280; Crebbp.
eggNOG; KOG1778; Eukaryota.
eggNOG; COG5076; LUCA.
HOGENOM; HOG000111353; -.
HOVERGEN; HBG000185; -.
InParanoid; P45481; -.
ChiTaRS; Crebbp; mouse.
EvolutionaryTrace; P45481; -.
PRO; PR:P45481; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_CREBBP; -.
GO; GO:0000940; C:condensed chromosome outer kinetochore; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0000123; C:histone acetyltransferase complex; IDA:MGI.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0016605; C:PML body; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:MGI.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0016407; F:acetyltransferase activity; IDA:MGI.
GO; GO:0033613; F:activating transcription factor binding; ISO:MGI.
GO; GO:0008140; F:cAMP response element binding protein binding; IPI:CAFA.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0004402; F:histone acetyltransferase activity; IDA:MGI.
GO; GO:0043426; F:MRF binding; ISS:UniProtKB.
GO; GO:0002039; F:p53 binding; ISO:MGI.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0046982; F:protein heterodimerization activity; IMP:CAFA.
GO; GO:0000987; F:proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:MGI.
GO; GO:0046332; F:SMAD binding; ISO:MGI.
GO; GO:0001093; F:TFIIB-class transcription factor binding; IPI:MGI.
GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0001191; F:transcriptional repressor activity, RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IMP:CAFA.
GO; GO:0008283; P:cell proliferation; ISO:MGI.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IDA:MGI.
GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
GO; GO:0098586; P:cellular response to virus; IMP:CAFA.
GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:MGI.
GO; GO:0016573; P:histone acetylation; ISS:UniProtKB.
GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; ISS:UniProtKB.
GO; GO:0045358; P:negative regulation of interferon-beta biosynthetic process; IMP:CAFA.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0048525; P:negative regulation of viral process; IMP:CAFA.
GO; GO:0060355; P:positive regulation of cell adhesion molecule production; ISO:MGI.
GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IDA:MGI.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; TAS:UniProtKB.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IGI:MGI.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006473; P:protein acetylation; ISO:MGI.
GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
CDD; cd15802; RING_CBP-p300; 1.
Gene3D; 1.10.1630.10; -; 1.
Gene3D; 1.20.1020.10; -; 2.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 2.10.110.40; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR031162; CBP_P300_HAT.
InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
InterPro; IPR003101; KIX_dom.
InterPro; IPR036529; KIX_dom_sf.
InterPro; IPR009110; Nuc_rcpt_coact.
InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
InterPro; IPR037073; Nuc_rcpt_coact_CREBbp_sf.
InterPro; IPR010303; RING_CBP-p300.
InterPro; IPR038547; RING_CBP-p300_sf.
InterPro; IPR035898; TAZ_dom_sf.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR000197; Znf_TAZ.
InterPro; IPR000433; Znf_ZZ.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF09030; Creb_binding; 1.
Pfam; PF06001; DUF902; 1.
Pfam; PF08214; HAT_KAT11; 1.
Pfam; PF02172; KIX; 1.
Pfam; PF02135; zf-TAZ; 2.
Pfam; PF00569; ZZ; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 1.
SMART; SM01250; KAT11; 1.
SMART; SM00551; ZnF_TAZ; 2.
SMART; SM00291; ZnF_ZZ; 1.
SUPFAM; SSF47040; SSF47040; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF57933; SSF57933; 2.
SUPFAM; SSF69125; SSF69125; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS51727; CBP_P300_HAT; 1.
PROSITE; PS50952; KIX; 1.
PROSITE; PS50134; ZF_TAZ; 2.
PROSITE; PS01357; ZF_ZZ_1; 1.
PROSITE; PS50135; ZF_ZZ_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Acyltransferase;
Biological rhythms; Bromodomain; Complete proteome; Cytoplasm;
Isopeptide bond; Metal-binding; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation;
Transferase; Ubl conjugation; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q92793}.
CHAIN 2 2441 CREB-binding protein.
/FTId=PRO_0000211191.
DOMAIN 586 665 KIX. {ECO:0000255|PROSITE-
ProRule:PRU00311}.
DOMAIN 1104 1176 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 1324 1701 CBP/p300-type HAT. {ECO:0000255|PROSITE-
ProRule:PRU01065}.
ZN_FING 346 432 TAZ-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00203}.
ZN_FING 1702 1745 ZZ-type. {ECO:0000255|PROSITE-
ProRule:PRU00228}.
ZN_FING 1766 1847 TAZ-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00203}.
REGION 226 409 Interaction with SRCAP. {ECO:0000250}.
REGION 1125 1171 Interaction with histone.
{ECO:0000250|UniProtKB:Q92793}.
REGION 1163 1181 Interaction with ASF1A.
{ECO:0000250|UniProtKB:Q92793}.
REGION 1434 1436 Interaction with histone.
{ECO:0000250|UniProtKB:Q09472}.
REGION 1435 1437 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q09472}.
REGION 1447 1448 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q09472}.
COMPBIAS 1062 1065 Poly-Glu.
COMPBIAS 1556 1563 Poly-Glu.
COMPBIAS 1944 1949 Poly-Pro.
COMPBIAS 1968 1971 Poly-Gln.
COMPBIAS 2082 2086 Poly-Gln.
COMPBIAS 2200 2216 Poly-Gln.
COMPBIAS 2296 2299 Poly-Gln.
METAL 362 362 Zinc 1.
METAL 366 366 Zinc 1.
METAL 379 379 Zinc 1.
METAL 384 384 Zinc 1.
METAL 393 393 Zinc 2.
METAL 397 397 Zinc 2.
METAL 403 403 Zinc 2.
METAL 408 408 Zinc 2.
METAL 417 417 Zinc 3.
METAL 421 421 Zinc 3.
METAL 426 426 Zinc 3.
METAL 429 429 Zinc 3.
BINDING 1494 1494 Acetyl-CoA; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q09472}.
BINDING 1499 1499 Acetyl-CoA.
{ECO:0000250|UniProtKB:Q09472}.
BINDING 1503 1503 Acetyl-CoA.
{ECO:0000250|UniProtKB:Q09472}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q92793}.
MOD_RES 120 120 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 219 219 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q92793}.
MOD_RES 600 600 Omega-N-methylated arginine.
{ECO:0000305|PubMed:11701890}.
MOD_RES 624 624 Omega-N-methylated arginine.
{ECO:0000305|PubMed:11701890}.
MOD_RES 656 656 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1015 1015 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q92793}.
MOD_RES 1031 1031 Phosphoserine.
{ECO:0000250|UniProtKB:Q92793}.
MOD_RES 1077 1077 Phosphoserine.
{ECO:0000250|UniProtKB:Q92793}.
MOD_RES 1217 1217 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1383 1383 Phosphoserine; by IKKA.
{ECO:0000250|UniProtKB:Q92793}.
MOD_RES 1387 1387 Phosphoserine; by IKKA.
{ECO:0000250|UniProtKB:Q92793}.
MOD_RES 1584 1584 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q92793}.
MOD_RES 1592 1592 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q92793}.
MOD_RES 1593 1593 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q92793}.
MOD_RES 1596 1596 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1598 1598 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1742 1742 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q92793}.
MOD_RES 1745 1745 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1764 1764 Phosphoserine.
{ECO:0000250|UniProtKB:Q92793}.
MOD_RES 2064 2064 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2077 2077 Phosphoserine.
{ECO:0000250|UniProtKB:Q92793}.
MOD_RES 2080 2080 Phosphoserine.
{ECO:0000250|UniProtKB:Q92793}.
MOD_RES 2350 2350 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 999 999 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000269|PubMed:16287980}.
CROSSLNK 1034 1034 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000269|PubMed:16287980}.
CROSSLNK 1057 1057 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000269|PubMed:16287980}.
MUTAGEN 600 600 R->N: Abolishes binding to CREB.
{ECO:0000269|PubMed:8552098}.
MUTAGEN 999 999 K->R: Enhanced transcriptional activity.
No sumoylation, loss of recruitment of
HDAC2 to DAAX and greatly enhanced
transcriptional activity; when associated
with R-1034 and R-1057.
{ECO:0000269|PubMed:16287980}.
MUTAGEN 1015 1015 K->R: No change in sumoylation.
{ECO:0000269|PubMed:16287980}.
MUTAGEN 1034 1034 K->R: Enhanced transcriptional activity.
No sumoylation, loss of recruitment of
HDAC2 to DAAX and greatly enhanced
transcriptional activity; when associated
with R-999 and R-1057.
{ECO:0000269|PubMed:16287980}.
MUTAGEN 1043 1043 K->R: No change in sumoylation.
{ECO:0000269|PubMed:16287980}.
MUTAGEN 1053 1053 K->R: No change in sumoylation.
{ECO:0000269|PubMed:16287980}.
MUTAGEN 1057 1057 K->R: Enhanced transcriptional activity.
No sumoylation, loss of recruitment of
HDAC2 to DAAX and greatly enhanced
transcriptional activity; when associated
with R-999 and R-1034.
{ECO:0000269|PubMed:16287980}.
MUTAGEN 1061 1061 K->R: No change in sumoylation.
{ECO:0000269|PubMed:16287980}.
MUTAGEN 1087 1087 K->R: No change in sumoylation.
MUTAGEN 1690 1691 LC->KL: Abolishes histone
acetyltransferase activity.
{ECO:0000269|PubMed:10207073}.
CONFLICT 400 400 G -> P (in Ref. 1; AAB28651).
{ECO:0000305}.
CONFLICT 530 530 I -> V (in Ref. 1; AAB28651).
{ECO:0000305}.
CONFLICT 670 670 S -> T (in Ref. 1; AAB28651).
{ECO:0000305}.
CONFLICT 826 826 V -> E (in Ref. 1; AAB28651).
{ECO:0000305}.
CONFLICT 978 978 S -> T (in Ref. 1; AAB28651).
{ECO:0000305}.
CONFLICT 1159 1159 W -> R (in Ref. 1; AAB28651).
{ECO:0000305}.
CONFLICT 1239 1239 E -> G (in Ref. 1; AAB28651).
{ECO:0000305}.
CONFLICT 1417 1417 N -> D (in Ref. 1; AAB28651).
{ECO:0000305}.
CONFLICT 1429 1429 R -> C (in Ref. 1; AAB28651).
{ECO:0000305}.
CONFLICT 1466 1466 G -> V (in Ref. 1; AAB28651).
{ECO:0000305}.
CONFLICT 1470 1470 G -> A (in Ref. 1; AAB28651).
{ECO:0000305}.
CONFLICT 1850 1851 KL -> NV (in Ref. 1; AAB28651).
{ECO:0000305}.
CONFLICT 1859 1859 R -> C (in Ref. 1; AAB28651).
{ECO:0000305}.
CONFLICT 1987 1987 A -> D (in Ref. 1; AAB28651).
{ECO:0000305}.
CONFLICT 2060 2060 P -> N (in Ref. 1; AAB28651).
{ECO:0000305}.
CONFLICT 2381 2381 S -> T (in Ref. 1; AAB28651).
{ECO:0000305}.
TURN 343 345 {ECO:0000244|PDB:2KA4}.
HELIX 347 372 {ECO:0000244|PDB:1L8C}.
STRAND 374 376 {ECO:0000244|PDB:1U2N}.
HELIX 384 396 {ECO:0000244|PDB:1L8C}.
HELIX 400 402 {ECO:0000244|PDB:1L8C}.
HELIX 406 420 {ECO:0000244|PDB:1L8C}.
TURN 423 425 {ECO:0000244|PDB:2LWW}.
HELIX 429 433 {ECO:0000244|PDB:1L8C}.
HELIX 436 438 {ECO:0000244|PDB:1R8U}.
HELIX 590 594 {ECO:0000244|PDB:4I9O}.
HELIX 597 611 {ECO:0000244|PDB:4I9O}.
TURN 617 619 {ECO:0000244|PDB:4I9O}.
HELIX 622 642 {ECO:0000244|PDB:4I9O}.
HELIX 646 664 {ECO:0000244|PDB:4I9O}.
TURN 667 671 {ECO:0000244|PDB:1SB0}.
HELIX 1088 1103 {ECO:0000244|PDB:5W0I}.
TURN 1106 1109 {ECO:0000244|PDB:5W0I}.
HELIX 1110 1112 {ECO:0000244|PDB:5W0I}.
HELIX 1118 1121 {ECO:0000244|PDB:5W0I}.
HELIX 1126 1129 {ECO:0000244|PDB:5W0I}.
HELIX 1136 1144 {ECO:0000244|PDB:5W0I}.
HELIX 1151 1168 {ECO:0000244|PDB:5W0I}.
HELIX 1174 1197 {ECO:0000244|PDB:5W0I}.
STRAND 1281 1283 {ECO:0000244|PDB:5U7G}.
TURN 1285 1287 {ECO:0000244|PDB:5U7G}.
STRAND 1290 1292 {ECO:0000244|PDB:5U7G}.
HELIX 1293 1296 {ECO:0000244|PDB:5U7G}.
TURN 1300 1302 {ECO:0000244|PDB:5U7G}.
HELIX 1310 1314 {ECO:0000244|PDB:5U7G}.
HELIX 1334 1350 {ECO:0000244|PDB:5U7G}.
STRAND 1358 1371 {ECO:0000244|PDB:5U7G}.
HELIX 1374 1380 {ECO:0000244|PDB:5U7G}.
TURN 1381 1384 {ECO:0000244|PDB:5U7G}.
STRAND 1388 1403 {ECO:0000244|PDB:5U7G}.
STRAND 1406 1418 {ECO:0000244|PDB:5U7G}.
STRAND 1429 1437 {ECO:0000244|PDB:5U7G}.
HELIX 1444 1446 {ECO:0000244|PDB:5U7G}.
HELIX 1447 1465 {ECO:0000244|PDB:5U7G}.
STRAND 1469 1473 {ECO:0000244|PDB:5U7G}.
STRAND 1483 1487 {ECO:0000244|PDB:5U7G}.
HELIX 1497 1513 {ECO:0000244|PDB:5U7G}.
STRAND 1518 1522 {ECO:0000244|PDB:5U7G}.
HELIX 1523 1530 {ECO:0000244|PDB:5U7G}.
HELIX 1535 1537 {ECO:0000244|PDB:5U7G}.
HELIX 1545 1555 {ECO:0000244|PDB:5U7G}.
TURN 1709 1711 {ECO:0000244|PDB:1TOT}.
STRAND 1713 1726 {ECO:0000244|PDB:1TOT}.
HELIX 1731 1737 {ECO:0000244|PDB:1TOT}.
STRAND 1741 1746 {ECO:0000244|PDB:1TOT}.
HELIX 1765 1785 {ECO:0000244|PDB:1F81}.
HELIX 1794 1808 {ECO:0000244|PDB:1F81}.
HELIX 1812 1815 {ECO:0000244|PDB:1F81}.
HELIX 1818 1833 {ECO:0000244|PDB:1F81}.
STRAND 1840 1843 {ECO:0000244|PDB:5HPD}.
HELIX 1844 1849 {ECO:0000244|PDB:1F81}.
STRAND 2061 2064 {ECO:0000244|PDB:1KBH}.
HELIX 2068 2075 {ECO:0000244|PDB:1JJS}.
STRAND 2076 2079 {ECO:0000244|PDB:1JJS}.
HELIX 2088 2091 {ECO:0000244|PDB:1JJS}.
HELIX 2097 2100 {ECO:0000244|PDB:1JJS}.
HELIX 2102 2104 {ECO:0000244|PDB:1JJS}.
STRAND 2106 2108 {ECO:0000244|PDB:1JJS}.
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


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