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CREB-regulated transcription coactivator 2 (Transducer of regulated cAMP response element-binding protein 2) (TORC-2) (Transducer of CREB protein 2)

 CRTC2_MOUSE             Reviewed;         692 AA.
Q3U182; Q3TA52; Q8BH09;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
05-FEB-2008, sequence version 2.
05-DEC-2018, entry version 109.
RecName: Full=CREB-regulated transcription coactivator 2;
AltName: Full=Transducer of regulated cAMP response element-binding protein 2;
Short=TORC-2;
Short=Transducer of CREB protein 2;
Name=Crtc2; Synonyms=Torc2;
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 [LARGE SCALE MRNA].
STRAIN=NOD; TISSUE=Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Liver, Mammary tumor, and Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-171, AND TISSUE
SPECIFICITY.
PubMed=16148943; DOI=10.1038/nature03967;
Koo S.-H., Flechner L., Qi L., Zhang X., Screaton R.A., Jeffries S.,
Hedrick S., Xu W., Boussouar F., Brindle P., Takemori H., Montminy M.;
"The CREB coactivator TORC2 is a key regulator of fasting glucose
metabolism.";
Nature 437:1109-1111(2005).
[4]
FUNCTION, PHOSPHORYLATION AT SER-171, AND SUBCELLULAR LOCATION.
PubMed=16308421; DOI=10.1126/science.1120781;
Shaw R.J., Lamia K.A., Vasquez D., Koo S.-H., Bardeesy N.,
Depinho R.A., Montminy M., Cantley L.C.;
"The kinase LKB1 mediates glucose homeostasis in liver and therapeutic
effects of metformin.";
Science 310:1642-1646(2005).
[5]
INTERACTION WITH COP1, PHOSPHORYLATION AT SER-171, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF SER-171; VAL-214; PRO-215 AND LYS-628.
PubMed=17805301; DOI=10.1038/nature06128;
Dentin R., Liu Y., Koo S.-H., Hedrick S., Vargas T., Heredia J.,
Yates J. III, Montminy M.;
"Insulin modulates gluconeogenesis by inhibition of the coactivator
TORC2.";
Nature 449:366-369(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-171; SER-434;
SER-612; SER-622 AND SER-623, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, 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).
[9]
TISSUE SPECIFICITY.
PubMed=23699513; DOI=10.1523/JNEUROSCI.4202-12.2013;
Sakamoto K., Norona F.E., Alzate-Correa D., Scarberry D., Hoyt K.R.,
Obrietan K.;
"Clock and light regulation of the CREB coactivator CRTC1 in the
suprachiasmatic circadian clock.";
J. Neurosci. 33:9021-9027(2013).
[10]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-161, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[11]
METHYLATION AT ARG-51; ARG-99; ARG-120; ARG-123; ARG-161 AND ARG-168.
PubMed=24570487; DOI=10.1126/scisignal.2004479;
Han H.S., Jung C.Y., Yoon Y.S., Choi S., Choi D., Kang G., Park K.G.,
Kim S.T., Koo S.H.;
"Arginine methylation of CRTC2 is critical in the transcriptional
control of hepatic glucose metabolism.";
Sci. Signal. 7:RA19-RA19(2014).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-171.
PubMed=29211348; DOI=10.1111/febs.14351;
Sonntag T., Vaughan J.M., Montminy M.;
"14-3-3 proteins mediate inhibitory effects of cAMP on salt-inducible
kinases (SIKs).";
FEBS J. 0:0-0(2017).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-70;
THR-169 AND SER-171, MUTAGENESIS OF SER-171 AND SER-275, AND
INTERACTION WITH 14-3-3 PROTEINS.
PubMed=28235073; DOI=10.1371/journal.pone.0173013;
Sonntag T., Moresco J.J., Vaughan J.M., Matsumura S., Yates J.R. III,
Montminy M.;
"Analysis of a cAMP regulated coactivator family reveals an
alternative phosphorylation motif for AMPK family members.";
PLoS ONE 12:E0173013-E0173013(2017).
-!- FUNCTION: Transcriptional coactivator for CREB1 which activates
transcription through both consensus and variant cAMP response
element (CRE) sites (PubMed:29211348). Acts as a coactivator, in
the SIK/TORC signaling pathway, being active when dephosphorylated
(PubMed:29211348). Acts independently of CREB1 'Ser-133'
phosphorylation. Enhances the interaction of CREB1 with TAF4.
Regulates gluconeogenesis as a component of the LKB1/AMPK/TORC2
signaling pathway. Regulates the expression of specific genes such
as the steroidogenic gene, StAR. Potent coactivator of PPARGC1A
and inducer of mitochondrial biogenesis in muscle cells (By
similarity). {ECO:0000250|UniProtKB:Q53ET0,
ECO:0000269|PubMed:16148943, ECO:0000269|PubMed:16308421,
ECO:0000269|PubMed:29211348}.
-!- SUBUNIT: Binds, as a tetramer, through its N-terminal region, with
the bZIP domain of CREB1. 'Arg-314' in the bZIP domain of CREB1 is
essential for this interaction. Interaction, via its C-terminal,
with TAF4, enhances recruitment of TAF4 to CREB1 (By similarity).
Interacts with PPP3CA/calcineurin alpha, and SIK2 (By similarity).
Interacts with 14-3-3 proteins, YWHAB and YWHAG (PubMed:28235073).
Interaction with COP1 mediates nuclear export and degradation of
CRTC2 (PubMed:17805301). {ECO:0000250|UniProtKB:Q53ET0,
ECO:0000269|PubMed:17805301, ECO:0000269|PubMed:28235073}.
-!- INTERACTION:
P18850:ATF6 (xeno); NbExp=2; IntAct=EBI-8018890, EBI-852157;
F6VAN0:Atf6; NbExp=2; IntAct=EBI-8018890, EBI-6171558;
Q9R1A8:Cop1; NbExp=3; IntAct=EBI-8018890, EBI-15656898;
P29994-1:Itpr1 (xeno); NbExp=2; IntAct=EBI-8018890, EBI-15683709;
P63328:Ppp3ca; NbExp=2; IntAct=EBI-8018890, EBI-397208;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16148943,
ECO:0000269|PubMed:16308421, ECO:0000269|PubMed:17805301,
ECO:0000269|PubMed:29211348}. Nucleus
{ECO:0000269|PubMed:16148943, ECO:0000269|PubMed:16308421,
ECO:0000269|PubMed:17805301, ECO:0000269|PubMed:29211348}.
Note=Translocated from the nucleus to the cytoplasm on interaction
of the phosphorylated form with 14-3-3 protein (By similarity). In
response to cAMP levels and glucagon, relocated to the nucleus
(PubMed:16148943). {ECO:0000250|UniProtKB:Q53ET0,
ECO:0000269|PubMed:16148943}.
-!- TISSUE SPECIFICITY: Expressed in the suprachiasmatic nucleus (SCN)
of the brain. {ECO:0000269|PubMed:23699513}.
-!- PTM: Phosphorylation/dephosphorylation states of Ser-171 are
required for regulating transduction of CREB activity
(PubMed:29211348). TORCs are inactive when phosphorylated, and
active when dephosphorylated at this site (PubMed:29211348). This
primary site of phosphorylation, is regulated by cAMP and calcium
levels and is dependent on the phosphorylation of SIKs (SIK1 and
SIK2) by LKB1 (By similarity). Phosphorylation at Ser-275 by MARK2
is induced under low glucose conditions and dephosphorylated in
response to glucose influx (By similarity). Both insulin and AMPK
increase this phosphorylation of CRTC2 while glucagon suppresses
it (By similarity). Phosphorylation at Ser-275 promotes
interaction with 14-3-3 proteins and translocation to the
cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q53ET0,
ECO:0000269|PubMed:29211348}.
-!- PTM: Asymmetric dimethylation of arginine resisues by PRMT6
enhances the association of CRTC2 with CREB on the promoters of
gluconeogenic genes. {ECO:0000269|PubMed:24570487}.
-!- SIMILARITY: Belongs to the TORC family. {ECO:0000305}.
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EMBL; AK156192; BAE33618.1; -; mRNA.
EMBL; AK172084; BAE42818.1; -; mRNA.
EMBL; BC023831; AAH23831.1; -; mRNA.
EMBL; BC032183; AAH32183.1; -; mRNA.
EMBL; BC033300; AAH33300.1; -; mRNA.
CCDS; CCDS38501.1; -.
RefSeq; NP_083157.1; NM_028881.2.
UniGene; Mm.35627; -.
PDB; 5ZK1; X-ray; 3.05 A; C=17-58.
PDB; 5ZKO; X-ray; 3.05 A; G/H=1-80.
PDBsum; 5ZK1; -.
PDBsum; 5ZKO; -.
ProteinModelPortal; Q3U182; -.
SMR; Q3U182; -.
BioGrid; 216678; 4.
DIP; DIP-46162N; -.
ELM; Q3U182; -.
IntAct; Q3U182; 11.
STRING; 10090.ENSMUSP00000029545; -.
iPTMnet; Q3U182; -.
PhosphoSitePlus; Q3U182; -.
EPD; Q3U182; -.
MaxQB; Q3U182; -.
PaxDb; Q3U182; -.
PeptideAtlas; Q3U182; -.
PRIDE; Q3U182; -.
Ensembl; ENSMUST00000029545; ENSMUSP00000029545; ENSMUSG00000027936.
GeneID; 74343; -.
KEGG; mmu:74343; -.
UCSC; uc008qbt.2; mouse.
CTD; 200186; -.
MGI; MGI:1921593; Crtc2.
eggNOG; ENOG410IGNT; Eukaryota.
eggNOG; ENOG410XPDQ; LUCA.
GeneTree; ENSGT00390000010652; -.
HOGENOM; HOG000111980; -.
HOVERGEN; HBG058314; -.
InParanoid; Q3U182; -.
KO; K16333; -.
OrthoDB; EOG091G03YN; -.
PhylomeDB; Q3U182; -.
TreeFam; TF321571; -.
PRO; PR:Q3U182; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000027936; Expressed in 235 organ(s), highest expression level in cerebellum.
CleanEx; MM_CRTC2; -.
ExpressionAtlas; Q3U182; baseline and differential.
Genevisible; Q3U182; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008140; F:cAMP response element binding protein binding; IBA:GO_Central.
GO; GO:0003682; F:chromatin binding; ISO:MGI.
GO; GO:0006094; P:gluconeogenesis; IDA:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
GO; GO:0043970; P:histone H3-K9 acetylation; IGI:MGI.
GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
GO; GO:1901998; P:toxin transport; IMP:MGI.
InterPro; IPR024786; TORC.
InterPro; IPR024785; TORC_C.
InterPro; IPR024784; TORC_M.
InterPro; IPR024783; TORC_N.
PANTHER; PTHR13589; PTHR13589; 1.
Pfam; PF12886; TORC_C; 1.
Pfam; PF12885; TORC_M; 1.
Pfam; PF12884; TORC_N; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Complete proteome; Cytoplasm;
Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q53ET0}.
CHAIN 2 692 CREB-regulated transcription coactivator
2.
/FTId=PRO_0000318529.
REGION 209 215 Required for interaction with COP1.
{ECO:0000269|PubMed:17805301}.
MOTIF 272 288 Nuclear export signal. {ECO:0000250}.
COMPBIAS 237 241 Poly-Ser.
COMPBIAS 337 413 Ser-rich.
SITE 628 628 Required for ubiquitination and
degradation.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q53ET0}.
MOD_RES 51 51 Asymmetric dimethylarginine; by PRMT6.
{ECO:0000269|PubMed:24570487}.
MOD_RES 70 70 Phosphoserine.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:28235073}.
MOD_RES 86 86 Phosphoserine.
{ECO:0000250|UniProtKB:Q53ET0}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000250|UniProtKB:Q53ET0}.
MOD_RES 99 99 Asymmetric dimethylarginine; by PRMT6.
{ECO:0000269|PubMed:24570487}.
MOD_RES 120 120 Asymmetric dimethylarginine; by PRMT6.
{ECO:0000269|PubMed:24570487}.
MOD_RES 123 123 Asymmetric dimethylarginine; by PRMT6.
{ECO:0000269|PubMed:24570487}.
MOD_RES 136 136 Phosphoserine.
{ECO:0000250|UniProtKB:Q53ET0}.
MOD_RES 161 161 Asymmetric dimethylarginine; by PRMT6.
{ECO:0000244|PubMed:24129315,
ECO:0000269|PubMed:24570487}.
MOD_RES 168 168 Asymmetric dimethylarginine; by PRMT6.
{ECO:0000269|PubMed:24570487}.
MOD_RES 169 169 Phosphothreonine.
{ECO:0000269|PubMed:28235073}.
MOD_RES 171 171 Phosphoserine; by AMPK, MARK2, SIK1 and
SIK2. {ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:16148943,
ECO:0000269|PubMed:16308421,
ECO:0000269|PubMed:17805301,
ECO:0000269|PubMed:28235073,
ECO:0000269|PubMed:29211348}.
MOD_RES 192 192 Phosphothreonine.
{ECO:0000250|UniProtKB:Q53ET0}.
MOD_RES 275 275 Phosphoserine; by MARK2.
{ECO:0000250|UniProtKB:Q53ET0}.
MOD_RES 307 307 Phosphoserine.
{ECO:0000250|UniProtKB:Q53ET0}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000250|UniProtKB:Q53ET0}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000250|UniProtKB:Q53ET0}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 457 457 Phosphoserine.
{ECO:0000250|UniProtKB:Q53ET0}.
MOD_RES 489 489 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q53ET0}.
MOD_RES 490 490 Phosphoserine.
{ECO:0000250|UniProtKB:Q53ET0}.
MOD_RES 493 493 Phosphoserine.
{ECO:0000250|UniProtKB:Q53ET0}.
MOD_RES 502 502 Phosphothreonine.
{ECO:0000250|UniProtKB:Q53ET0}.
MOD_RES 612 612 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 622 622 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 623 623 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 235 235 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q53ET0}.
MUTAGEN 171 171 S->A: Upregulates CREB transcription
factor activity. Reduces interaction with
14-3-3 proteins.
{ECO:0000269|PubMed:28235073}.
MUTAGEN 171 171 S->A: Upregulates CREB-mediated
gluconeogenic gene expression. No
degradation of CRTC2. Loss of SIK2-
mediated phosphorylation.
{ECO:0000269|PubMed:17805301}.
MUTAGEN 213 213 K->R: No effect on COP1-mediated
degradation of TORC1 under forksolin
stimulation.
MUTAGEN 214 214 V->A: No interaction with COP1.
Inhibition of degradation under exposure
to FSK/INS.
{ECO:0000269|PubMed:17805301}.
MUTAGEN 215 215 P->A: No interaction with COP1.
Inhibition of degradation under exposure
to FSK/INS.
{ECO:0000269|PubMed:17805301}.
MUTAGEN 275 275 S->A: Does not affect interaction with
14-3-3 proteins.
{ECO:0000269|PubMed:28235073}.
MUTAGEN 628 628 K->R: Translocates to the nucleus and no
COP1-mediated degradation.
{ECO:0000269|PubMed:17805301}.
CONFLICT 195 195 S -> G (in Ref. 1; BAE33618).
{ECO:0000305}.
CONFLICT 203 203 G -> R (in Ref. 1; BAE42818).
{ECO:0000305}.
HELIX 22 44 {ECO:0000244|PDB:5ZK1}.
HELIX 48 55 {ECO:0000244|PDB:5ZK1}.
SEQUENCE 692 AA; 73216 MW; 5BCBC416D45CFAD8 CRC64;
MATSGANGPG SATASASNPR KFSEKIALQK QRQAEETAAF EEVMMDIGST RLQAQKLRLA
YTRSSHYGGS LPNVNQIGCG LAEFQSPLHS PLDSSRSTRH HGLVERVQRD ARRMVSPLRR
YPRHIDSSPY SPAYLSPPPE SGWRRMMPWG NLPAEKGQLF RLPSALNRTS SDSALHTSVM
NPNPQDTYPG PTPPSVLPSR RGGGFLDGEM DAKVPAIEEN VVDDKHLLKP WDAKKLSSSS
SRPRSCEVPG INIFPSPDQP ANVPVLPPAM NTGGSLPDLT NLHFPPPLPT PLDPEETVYP
SLSGGNSTTN LTHTMTHLGI SGGLGLGPSY DVPGLHSPLS HPSLQSSLSN PNLQASLSSP
QPQLQGSHSH PSLPASSLAH HALPTTSLGH PSLSAPALSS SSSSSSTSSP VLSAPPYPAS
TPGASPRHRR VPLSPLSLPA GPADARRSQQ QLPKQFSPTM SPTLSSITQG VPLDTSKLPT
DQRLPPYPYS PPSLVIPTHP PTPKSLQQLP SQACLVQPSG GQPPGRQPHY GALYPPGSSG
HGQQPYHRPI NDFSLGNLEQ FNMESPSTSL VLDPPAFSEG PGFLGSEGSM SGPQDPHVLN
HQNLTHCSRH GSGPNIILTG DSSPGFSKEI AAALAGVPGF EVSASGLELG LGLEDELRME
PLGLEGLTML SDPCALLPDP AVEDSFRSDR LQ


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EIAAB09460 CREB-regulated transcription coactivator 3,Crtc3,Mouse,Mus musculus,Torc3,TORC-3,Transducer of CREB protein 3,Transducer of regulated cAMP response element-binding protein 3
EIAAB09461 CREB-regulated transcription coactivator 3,CRTC3,Homo sapiens,Human,TORC3,TORC-3,Transducer of CREB protein 3,Transducer of regulated cAMP response element-binding protein 3
EIAAB09457 CREB-regulated transcription coactivator 2,CRTC2,Homo sapiens,Human,TORC2,TORC-2,Transducer of CREB protein 2,Transducer of regulated cAMP response element-binding protein 2
EIAAB09454 CREB-regulated transcription coactivator 1,Crtc1,Mect1,Mucoepidermoid carcinoma translocated protein 1 homolog,Rat,Rattus norvegicus,Torc1,TORC-1,Transducer of CREB protein 1,Transducer of regulated c
EIAAB09453 CREB-regulated transcription coactivator 1,CRTC1,Homo sapiens,Human,KIAA0616,MECT1,Mucoepidermoid carcinoma translocated protein 1,TORC1,TORC-1,Transducer of CREB protein 1,Transducer of regulated cAM
EIAAB09455 CREB-regulated transcription coactivator 1,Crtc1,Kiaa0616,Mect1,Mouse,Mucoepidermoid carcinoma translocated protein 1 homolog,Mus musculus,Torc1,TORC-1,Transducer of CREB protein 1,Transducer of regul
25-879 CREBBP is involved in the transcriptional coactivation of many different transcription factors. First isolated as a nuclear protein that binds to cAMP-response element binding protein (CREB), this gen 0.05 mg
18-662-20054 cAMP response element-binding protein - CREB Polyclonal 0.1 ml
18-003-43168 cAMP response element-binding protein - CREB Polyclonal 0.05 mg Aff Pur
18-003-43793 cAMP response element-binding protein - CREB Polyclonal 0.1 mg Protein A
CSB-E15860m Mouse cAMP response element binding protein(CREB)ELISA Kit 96T
CSB-E13527h Human cAMP response element-binding protein (CREB) ELISA Kit 96T
10-663-45550 cAMP Responsive Element Binding Protein (CREB-1) Human - CREB N_A 1 mg
10-663-45550 cAMP Responsive Element Binding Protein (CREB-1) Human - CREB N_A 0.01 mg
10-663-45550 cAMP Responsive Element Binding Protein (CREB-1) Human - CREB N_A 0.002 mg
CSB-E13527h Human cAMP response element-binding protein (CREB) ELISA Kit SpeciesHuman 96T
U1318m CLIA cAMP-responsive element-binding protein 1,Creb1,CREB-1,Creb-1,Cyclic AMP-responsive element-binding protein 1,Mouse,Mus musculus 96T
E1318m ELISA kit cAMP-responsive element-binding protein 1,Creb1,CREB-1,Creb-1,Cyclic AMP-responsive element-binding protein 1,Mouse,Mus musculus 96T
E1318r ELISA cAMP-responsive element-binding protein 1,Creb1,CREB-1,Creb-1,Cyclic AMP-responsive element-binding protein 1,Rat,Rattus norvegicus 96T
E1318m ELISA cAMP-responsive element-binding protein 1,Creb1,CREB-1,Creb-1,Cyclic AMP-responsive element-binding protein 1,Mouse,Mus musculus 96T
E1318r ELISA kit cAMP-responsive element-binding protein 1,Creb1,CREB-1,Creb-1,Cyclic AMP-responsive element-binding protein 1,Rat,Rattus norvegicus 96T
U1318r CLIA cAMP-responsive element-binding protein 1,Creb1,CREB-1,Creb-1,Cyclic AMP-responsive element-binding protein 1,Rat,Rattus norvegicus 96T


 

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