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Cyclic AMP-responsive element-binding protein 1 (CREB-1) (cAMP-responsive element-binding protein 1)

 CREB1_MOUSE             Reviewed;         341 AA.
Q01147;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
18-JUL-2018, entry version 188.
RecName: Full=Cyclic AMP-responsive element-binding protein 1;
Short=CREB-1;
Short=cAMP-responsive element-binding protein 1;
Name=Creb1; Synonyms=Creb-1;
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 [GENOMIC DNA / MRNA].
PubMed=1532935;
Ruppert S., Cole T.J., Boshart M., Schmid E., Schuetz G.;
"Multiple mRNA isoforms of the transcription activator protein CREB:
generation by alternative splicing and specific expression in primary
spermatocytes.";
EMBO J. 11:1503-1512(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
PubMed=1387109; DOI=10.1016/0888-7543(92)90010-P;
Cole T.J., Copeland N.G., Gilbert D.J., Jenkins N.A., Schuetz G.,
Ruppert R.;
"The mouse CREB (cAMP responsive element binding protein) gene:
structure, promoter analysis, and chromosomal localization.";
Genomics 13:974-982(1992).
[3]
INTERACTION WITH CREBBP, PHOSPHORYLATION AT SER-133, AND MUTAGENESIS
OF 137-ILE-LEU-138.
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).
[4]
PHOSPHORYLATION AT SER-133 AND SER-142, MUTAGENESIS OF SER-142, AND
FUNCTION.
PubMed=11970866; DOI=10.1016/S0896-6273(02)00656-6;
Gau D., Lemberger T., von Gall C., Kretz O., Le Minh N., Gass P.,
Schmid W., Schibler U., Korf H.W., Schuetz G.;
"Phosphorylation of CREB Ser142 regulates light-induced phase shifts
of the circadian clock.";
Neuron 34:245-253(2002).
[5]
PHOSPHORYLATION AT SER-133, AND MUTAGENESIS OF SER-133.
PubMed=18690222; DOI=10.1038/ni.1644;
Ananieva O., Darragh J., Johansen C., Carr J.M., McIlrath J.,
Park J.M., Wingate A., Monk C.E., Toth R., Santos S.G., Iversen L.,
Arthur J.S.;
"The kinases MSK1 and MSK2 act as negative regulators of Toll-like
receptor signaling.";
Nat. Immunol. 9:1028-1036(2008).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
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).
[7]
PHOSPHORYLATION.
PubMed=20852621; DOI=10.1038/nm.2214;
Zhang E.E., Liu Y., Dentin R., Pongsawakul P.Y., Liu A.C., Hirota T.,
Nusinow D.A., Sun X., Landais S., Kodama Y., Brenner D.A.,
Montminy M., Kay S.A.;
"Cryptochrome mediates circadian regulation of cAMP signaling and
hepatic gluconeogenesis.";
Nat. Med. 16:1152-1156(2010).
[8]
FUNCTION IN ADIPOCYTE DIFFERENTIATION, INTERACTION WITH CREBL2, AND
SUBCELLULAR LOCATION.
PubMed=21728997; DOI=10.1042/BJ20101475;
Ma X., Zhang H., Yuan L., Jing H., Thacker P., Li D.;
"CREBL2, interacting with CREB, induces adipogenesis in 3T3-L1
adipocytes.";
Biochem. J. 439:27-38(2011).
[9]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH THE SOMATOSTATIN
CAMP RESPONSE ELEMENT (SSCRE).
PubMed=10952992; DOI=10.1074/jbc.M007293200;
Schumacher M.A., Goodman R.H., Brennan R.G.;
"The structure of a CREB bZIP.somatostatin CRE complex reveals the
basis for selective dimerization and divalent cation-enhanced DNA
binding.";
J. Biol. Chem. 275:35242-35247(2000).
-!- FUNCTION: Phosphorylation-dependent transcription factor that
stimulates transcription upon binding to the DNA cAMP response
element (CRE), a sequence present in many viral and cellular
promoters. Transcription activation is enhanced by the TORC
coactivators which act independently of Ser-133 phosphorylation.
Involved in different cellular processes including the
synchronization of circadian rhythmicity and the differentiation
of adipose cells. {ECO:0000269|PubMed:11970866,
ECO:0000269|PubMed:21728997}.
-!- SUBUNIT: Interacts with PPRC1. Binds DNA as a dimer. This dimer is
stabilized by magnesium ions. Interacts, through the bZIP domain,
with the coactivators TORC1/CRTC1, TORC2/CRTC2 and TORC3/CRTC3.
Interacts (phosphorylated form) with TOX3 (By similarity). When
phosphorylated on Ser-133, binds CREBBP. Interacts with ARRB1.
Binds to HIPK2 (By similarity). Interacts with SGK1 (By
similarity). Interacts with CREBL2; regulates CREB1
phosphorylation, stability and transcriptional activity.
{ECO:0000250, ECO:0000269|PubMed:10952992,
ECO:0000269|PubMed:21728997, ECO:0000269|PubMed:8552098}.
-!- INTERACTION:
P45481:Crebbp; NbExp=2; IntAct=EBI-2291098, EBI-296306;
Q32M00:Crebl2; NbExp=4; IntAct=EBI-2291098, EBI-5314489;
Q09472:EP300 (xeno); NbExp=2; IntAct=EBI-2291098, EBI-447295;
P10085:Myod1; NbExp=2; IntAct=EBI-2291098, EBI-4405734;
Q60974:Ncor1; NbExp=5; IntAct=EBI-2291098, EBI-349004;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00312, ECO:0000255|PROSITE-ProRule:PRU00978,
ECO:0000269|PubMed:21728997}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=At least 6 isoforms are produced.;
Name=1;
IsoId=Q01147-1; Sequence=Displayed;
Name=2; Synonyms=CREB-delta;
IsoId=Q01147-2; Sequence=VSP_000597;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:1387109}.
-!- PTM: Phosphorylation of Ser-133 allows CREBBP binding. Stimulated
by phosphorylation. Phosphorylated Ser-142 can be detected in the
suprachiasmatic nucleus (SCN), the amygdala, the cortex, and the
hippocampus but not in the striatum nor in the cerebellum. In the
SCN, phosphorylation of Ser-142 and Ser-133 are stimulated by
light exposure and submitted to circadian oscillations. In the
retina, only phosphorylation of Ser-133 can be detected upon light
exposure. Phosphorylation of both Ser-133 and Ser-142 in the SCN
regulates the activity of CREB and participates in circadian
rhythm generation. Phosphorylated upon calcium influx by CaMK4 and
CaMK2 on Ser-133. CaMK4 is much more potent than CAMK2 in
activating CREB. Phosphorylated by CaMK2 on Ser-142.
Phosphorylation of Ser-142 blocks CREB-mediated transcription even
when Ser-133 is phosphorylated. Phosphorylated by CaMK1.
Phosphorylation of Ser-271 by HIPK2 in response to genotoxic
stress promotes CREB1 activity, facilitating the recruitment of
the coactivator CBP (By similarity). Phosphorylated at Ser-133 by
RPS6KA3, RPS6KA4 and RPS6KA5 in response to mitogenic or stress
stimuli. CREBL2 positively regulates phosphorylation at Ser-133
thereby stimulating CREB1 transcriptional activity. In liver,
phosphorylation is induced by fasting or glucagon in a circadian
fashion. {ECO:0000250, ECO:0000269|PubMed:11970866,
ECO:0000269|PubMed:18690222, ECO:0000269|PubMed:20852621,
ECO:0000269|PubMed:8552098}.
-!- PTM: Sumoylated with SUMO1. Sumoylation on Lys-304, but not on
Lys-285, is required for nuclear localization of this protein.
Sumoylation is enhanced under hypoxia, promoting nuclear
localization and stabilization (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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EMBL; X67719; CAA47953.1; -; Genomic_DNA.
EMBL; X67721; CAA47953.1; JOINED; Genomic_DNA.
EMBL; X67724; CAA47953.1; JOINED; Genomic_DNA.
EMBL; X67725; CAA47953.1; JOINED; Genomic_DNA.
EMBL; X67726; CAA47953.1; JOINED; Genomic_DNA.
EMBL; X67727; CAA47953.1; JOINED; Genomic_DNA.
EMBL; X67728; CAA47953.1; JOINED; Genomic_DNA.
EMBL; X67719; CAA47954.1; -; Genomic_DNA.
EMBL; X67721; CAA47954.1; JOINED; Genomic_DNA.
EMBL; X67722; CAA47954.1; JOINED; Genomic_DNA.
EMBL; X67724; CAA47954.1; JOINED; Genomic_DNA.
EMBL; X67725; CAA47954.1; JOINED; Genomic_DNA.
EMBL; X67726; CAA47954.1; JOINED; Genomic_DNA.
EMBL; X67727; CAA47954.1; JOINED; Genomic_DNA.
EMBL; X67728; CAA47954.1; JOINED; Genomic_DNA.
EMBL; M95106; AAA37456.1; -; mRNA.
CCDS; CCDS15004.1; -. [Q01147-1]
CCDS; CCDS15005.1; -. [Q01147-2]
PIR; S20955; S20955.
PIR; S42699; S42699.
RefSeq; NP_034082.1; NM_009952.2. [Q01147-1]
RefSeq; NP_598589.2; NM_133828.2. [Q01147-2]
RefSeq; XP_006495713.1; XM_006495650.3. [Q01147-1]
RefSeq; XP_006495714.1; XM_006495651.3. [Q01147-2]
RefSeq; XP_017169569.1; XM_017314080.1. [Q01147-1]
RefSeq; XP_017169588.1; XM_017314099.1. [Q01147-2]
UniGene; Mm.422634; -.
PDB; 1DH3; X-ray; 3.00 A; A/C=285-339.
PDBsum; 1DH3; -.
ProteinModelPortal; Q01147; -.
SMR; Q01147; -.
BioGrid; 198873; 17.
ComplexPortal; CPX-6; ATF4-CREB1 transcription factor complex.
CORUM; Q01147; -.
IntAct; Q01147; 11.
MINT; Q01147; -.
STRING; 10090.ENSMUSP00000059973; -.
iPTMnet; Q01147; -.
PhosphoSitePlus; Q01147; -.
EPD; Q01147; -.
PaxDb; Q01147; -.
PeptideAtlas; Q01147; -.
PRIDE; Q01147; -.
Ensembl; ENSMUST00000049932; ENSMUSP00000059973; ENSMUSG00000025958. [Q01147-1]
Ensembl; ENSMUST00000087366; ENSMUSP00000084624; ENSMUSG00000025958. [Q01147-2]
Ensembl; ENSMUST00000185594; ENSMUSP00000139995; ENSMUSG00000025958. [Q01147-2]
Ensembl; ENSMUST00000190348; ENSMUSP00000140112; ENSMUSG00000025958. [Q01147-1]
GeneID; 12912; -.
KEGG; mmu:12912; -.
UCSC; uc007bgr.1; mouse. [Q01147-1]
CTD; 1385; -.
MGI; MGI:88494; Creb1.
eggNOG; KOG3584; Eukaryota.
eggNOG; ENOG410ZZJZ; LUCA.
GeneTree; ENSGT00390000008655; -.
HOGENOM; HOG000007365; -.
HOVERGEN; HBG011077; -.
InParanoid; Q01147; -.
KO; K05870; -.
OMA; QXISTIA; -.
OrthoDB; EOG091G0FTJ; -.
PhylomeDB; Q01147; -.
TreeFam; TF106464; -.
Reactome; R-MMU-198693; AKT phosphorylates targets in the nucleus.
Reactome; R-MMU-199920; CREB phosphorylation.
Reactome; R-MMU-375165; NCAM signaling for neurite out-growth.
Reactome; R-MMU-442720; CREB phosphorylation through the activation of Adenylate Cyclase.
Reactome; R-MMU-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-MMU-442742; CREB phosphorylation through the activation of Ras.
Reactome; R-MMU-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
ChiTaRS; Creb1; mouse.
EvolutionaryTrace; Q01147; -.
PRO; PR:Q01147; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000025958; -.
CleanEx; MM_CREB1; -.
ExpressionAtlas; Q01147; baseline and differential.
Genevisible; Q01147; MM.
GO; GO:1990589; C:ATF4-CREB1 transcription factor complex; IDA:ParkinsonsUK-UCL.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0000785; C:chromatin; ISO:MGI.
GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005719; C:nuclear euchromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:1990763; F:arrestin family protein binding; ISO:MGI.
GO; GO:0035497; F:cAMP response element binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:MGI.
GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; ISO:MGI.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0001225; F:RNA polymerase II transcription coactivator binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0007409; P:axonogenesis; IMP:MGI.
GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:BHF-UCL.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IDA:MGI.
GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEA:Ensembl.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl.
GO; GO:0071294; P:cellular response to zinc ion; IDA:MGI.
GO; GO:0034670; P:chemotaxis to arachidonic acid; ISO:MGI.
GO; GO:0007623; P:circadian rhythm; IDA:UniProtKB.
GO; GO:0007595; P:lactation; IMP:MGI.
GO; GO:0060428; P:lung epithelium development; IMP:MGI.
GO; GO:0060430; P:lung saccule development; IMP:MGI.
GO; GO:0030879; P:mammary gland development; IMP:MGI.
GO; GO:0007613; P:memory; IMP:MGI.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; ISO:MGI.
GO; GO:0021983; P:pituitary gland development; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0055025; P:positive regulation of cardiac muscle tissue development; IMP:MGI.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IGI:UniProtKB.
GO; GO:0046887; P:positive regulation of hormone secretion; IMP:MGI.
GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IGI:UniProtKB.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:MGI.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:MGI.
GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:UniProtKB.
GO; GO:0032916; P:positive regulation of transforming growth factor beta3 production; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
GO; GO:0008361; P:regulation of cell size; IGI:MGI.
GO; GO:0042752; P:regulation of circadian rhythm; ISO:MGI.
GO; GO:0048145; P:regulation of fibroblast proliferation; ISO:MGI.
GO; GO:0060251; P:regulation of glial cell proliferation; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IDA:MGI.
GO; GO:0033762; P:response to glucagon; IMP:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:1902065; P:response to L-glutamate; IEA:Ensembl.
GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
GO; GO:0010033; P:response to organic substance; ISO:MGI.
GO; GO:0033363; P:secretory granule organization; IMP:MGI.
GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
GO; GO:0060509; P:Type I pneumocyte differentiation; IMP:MGI.
GO; GO:0008542; P:visual learning; ISO:MGI.
InterPro; IPR004827; bZIP.
InterPro; IPR003102; Coactivator_CBP_pKID.
InterPro; IPR029802; CREB1.
InterPro; IPR001630; Leuzip_CREB.
PANTHER; PTHR22952:SF200; PTHR22952:SF200; 1.
Pfam; PF00170; bZIP_1; 1.
Pfam; PF02173; pKID; 1.
PRINTS; PR00041; LEUZIPPRCREB.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
PROSITE; PS50953; KID; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Biological rhythms;
Complete proteome; Differentiation; DNA-binding; Isopeptide bond;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 341 Cyclic AMP-responsive element-binding
protein 1.
/FTId=PRO_0000076598.
DOMAIN 101 160 KID. {ECO:0000255|PROSITE-
ProRule:PRU00312}.
DOMAIN 283 341 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 284 309 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 311 332 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
SITE 314 314 Required for binding TORCs.
{ECO:0000250}.
MOD_RES 133 133 Phosphoserine; by CaMK1, CaMK2, CaMK4,
PKB/AKT1 or PKB/AKT2, RPS6KA3, RPS6KA4,
RPS6KA5 and SGK1. {ECO:0000255|PROSITE-
ProRule:PRU00312,
ECO:0000269|PubMed:11970866,
ECO:0000269|PubMed:18690222,
ECO:0000269|PubMed:8552098}.
MOD_RES 142 142 Phosphoserine; by CaMK2.
{ECO:0000250|UniProtKB:P15337,
ECO:0000255|PROSITE-ProRule:PRU00312}.
MOD_RES 271 271 Phosphoserine; by HIPK2.
{ECO:0000250|UniProtKB:P16220,
ECO:0000255|PROSITE-ProRule:PRU00312}.
CROSSLNK 136 136 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P16220}.
CROSSLNK 285 285 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P16220}.
CROSSLNK 304 304 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P16220}.
VAR_SEQ 88 101 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_000597.
MUTAGEN 133 133 S->A: Loss of phosphorylation by RPS6KA4
and RPS6KA5.
{ECO:0000269|PubMed:18690222}.
MUTAGEN 137 138 IL->AA: Abolishes CREBBP binding.
{ECO:0000269|PubMed:8552098}.
MUTAGEN 142 142 S->A: Attenuates light-induced phase
shifts of locomotion and expression of c-
Fos and mPer1 in the SCN.
{ECO:0000269|PubMed:11970866}.
HELIX 286 333 {ECO:0000244|PDB:1DH3}.
SEQUENCE 341 AA; 36674 MW; CF2958DE9174968A CRC64;
MTMESGADNQ QSGDAAVTEA ENQQMTVQAQ PQIATLAQVS MPAAHATSSA PTVTLVQLPN
GQTVQVHGVI QAAQPSVIQS PQVQTVQSSC KDLKRLFSGT QISTIAESED SQESVDSVTD
SQKRREILSR RPSYRKILND LSSDAPGVPR IEEEKSEEET SAPAITTVTV PTPIYQTSSG
QYIAITQGGA IQLANNGTDG VQGLQTLTMT NAAATQPGTT ILQYAQTTDG QQILVPSNQV
VVQAASGDVQ TYQIRTAPTS TIAPGVVMAS SPALPTQPAE EAARKREVRL MKNREAAREC
RRKKKEYVKC LENRVAVLEN QNKTLIEELK ALKDLYCHKS D


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EIAAB09243 cAMP-responsive element-binding protein 3-like protein 3,CREB3L3,CREBH,Cyclic AMP-responsive element-binding protein 3-like protein 3,Homo sapiens,Human,HYST1481,Transcription factor CREB-H
EIAAB09321 cAMP-responsive element-binding protein 5,CREB5,CREB-5,CREBPA,CRE-BPa,Cyclic AMP-responsive element-binding protein 5,Homo sapiens,Human
U1318h CLIA cAMP-responsive element-binding protein 1,CREB1,CREB-1,Cyclic AMP-responsive element-binding protein 1,Homo sapiens,Human 96T
E1318h ELISA kit cAMP-responsive element-binding protein 1,CREB1,CREB-1,Cyclic AMP-responsive element-binding protein 1,Homo sapiens,Human 96T
E1318h ELISA cAMP-responsive element-binding protein 1,CREB1,CREB-1,Cyclic AMP-responsive element-binding protein 1,Homo sapiens,Human 96T
EIAAB09318 Bos taurus,Bovine,cAMP-responsive element-binding protein 3,CREB3,CREB-3,Cyclic AMP-responsive element-binding protein 3,Luman
EIAAB09244 cAMP-responsive element-binding protein 3-like protein 3,Creb3l3,Crebh,Cyclic AMP-responsive element-binding protein 3-like protein 3,Mouse,Mus musculus,Transcription factor CREB-H
EIAAB09242 cAMP-responsive element-binding protein 3-like protein 3,Creb3l3,Cyclic AMP-responsive element-binding protein 3-like protein 3,Rat,Rattus norvegicus,Transcription factor CREB-H
EIAAB09322 cAMP-responsive element-binding protein 5,Creb5,CREB-5,CRE-BPa,Cyclic AMP-responsive element-binding protein 5,Mouse,Mus musculus
EIAAB09320 cAMP-responsive element-binding protein 3,CREB3,CREB-3,Cyclic AMP-responsive element-binding protein 3,Homo sapiens,Human,Luman,LZIP,Transcription factor LZIP-alpha
EIAAB09319 cAMP-responsive element-binding protein 3,Creb3,CREB-3,Cyclic AMP-responsive element-binding protein 3,Lzip,Mouse,Mus musculus,Transcription factor LZIP
EIAAB09240 Bbf2h7,cAMP-responsive element-binding protein 3-like protein 2,Creb3l2,Cyclic AMP-responsive element-binding protein 3-like protein 2,Mouse,Mus musculus
EIAAB09238 cAMP-responsive element-binding protein 3-like protein 1,CREB3L1,Cyclic AMP-responsive element-binding protein 3-like protein 1,Homo sapiens,Human,OASIS,OASIS,Old astrocyte specifically-induced substa
EIAAB09236 cAMP-responsive element-binding protein 3-like protein 1,Creb3l1,Cyclic AMP-responsive element-binding protein 3-like protein 1,Mouse,Mus musculus,OASIS,Oasis,Old astrocyte specifically-induced substa
EIAAB09237 cAMP-responsive element-binding protein 3-like protein 1,Creb3l1,Cyclic AMP-responsive element-binding protein 3-like protein 1,OASIS,Oasis,Old astrocyte specifically-induced substance,Rat,Rattus norv
EIAAB09239 BBF2 human homolog on chromosome 7,BBF2H7,cAMP-responsive element-binding protein 3-like protein 2,CREB3L2,Cyclic AMP-responsive element-binding protein 3-like protein 2,Homo sapiens,Human


 

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