Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 CREB1_HUMAN             Reviewed;         341 AA.
P16220; P21934; Q6V963; Q9UMA7;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 2.
23-MAY-2018, entry version 219.
RecName: Full=Cyclic AMP-responsive element-binding protein 1;
Short=CREB-1;
Short=cAMP-responsive element-binding protein 1;
Name=CREB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CREB-A).
PubMed=2142528; DOI=10.1073/pnas.87.14.5258;
Berkowitz L.A., Gilman M.Z.;
"Two distinct forms of active transcription factor CREB (cAMP response
element binding protein).";
Proc. Natl. Acad. Sci. U.S.A. 87:5258-5262(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CREB-A).
PubMed=2196176;
Yoshimura T., Fujisawa J., Yoshida M.;
"Multiple cDNA clones encoding nuclear proteins that bind to the tax-
dependent enhancer of HTLV-1: all contain a leucine zipper structure
and basic amino acid domain.";
EMBO J. 9:2537-2542(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CREB-A).
PubMed=1966745;
Waeber G., Meyer T.E., Hoeffler J.P., Habener J.F.;
"Diversification of cyclic AMP-responsive enhancer binding proteins-
generated by alternative exon splicing.";
Trans. Assoc. Am. Physicians 103:28-37(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CREB-B).
PubMed=2974179; DOI=10.1126/science.2974179;
Hoeffler J.P., Meyer T.E., Yun Y., Jameson J.L., Habener J.F.;
"Cyclic AMP-responsive DNA-binding protein: structure based on a
cloned placental cDNA.";
Science 242:1430-1433(1988).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CREB-B).
PubMed=1831258; DOI=10.1093/nar/19.15.4290;
Short M.L., Manohar C.F., Furtado M.R., Ghadge G.D., Wolinsky S.M.,
Thimmapaya B., Jungmann R.A.;
"Nucleotide and derived amino-acid sequences of the CRE-binding
proteins from rat C6 glioma and HeLa cells.";
Nucleic Acids Res. 19:4290-4290(1991).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Testis;
PubMed=15579595; DOI=10.1530/rep.1.00036;
Huang X., Zhang J., Lu L., Yin L., Xu M., Wang Y., Zhou Z., Sha J.;
"Cloning and expression of a novel CREB mRNA splice variant in human
testis.";
Reproduction 128:775-782(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CREB-A).
TISSUE=Eye;
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
PubMed=8381074; DOI=10.1210/endo.132.2.8381074;
Meyer T.E., Waeber G., Lin J., Beckmann W., Habener J.F.;
"The promoter of the gene encoding 3',5'-cyclic adenosine
monophosphate (cAMP) response element binding protein contains cAMP
response elements: evidence for positive autoregulation of gene
transcription.";
Endocrinology 132:770-780(1993).
[9]
INTERACTION WITH HBV PROTEIN X.
PubMed=1827531; DOI=10.1126/science.1827531;
Maguire H.F., Hoeffler J.P., Siddiqui A.;
"HBV X protein alters the DNA binding specificity of CREB and ATF-2 by
protein-protein interactions.";
Science 252:842-844(1991).
[10]
INTERACTION WITH HTLV-1 TAX-1.
PubMed=1386673; DOI=10.1073/pnas.89.15.7070;
Zhao L.J., Giam C.-Z.;
"Human T-cell lymphotropic virus type I (HTLV-I) transcriptional
activator, Tax, enhances CREB binding to HTLV-I 21-base-pair repeats
by protein-protein interaction.";
Proc. Natl. Acad. Sci. U.S.A. 89:7070-7074(1992).
[11]
PHOSPHORYLATION AT SER-133, AND MUTAGENESIS OF SER-133.
PubMed=8065343; DOI=10.1128/MCB.14.9.6107;
Matthews R.P., Guthrie C.R., Wailes L.M., Zhao X., Means A.R.,
McKnight G.S.;
"Calcium/calmodulin-dependent protein kinase types II and IV
differentially regulate CREB-dependent gene expression.";
Mol. Cell. Biol. 14:6107-6116(1994).
[12]
PHOSPHORYLATION AT SER-133.
PubMed=7608156; DOI=10.1074/jbc.270.27.16378;
Lee H.-J.J., Mignacca R.C., Sakamoto K.M.;
"Transcriptional activation of egr-1 by granulocyte-macrophage colony-
stimulating factor but not interleukin 3 requires phosphorylation of
cAMP response element-binding protein (CREB) on serine 133.";
J. Biol. Chem. 270:15979-15983(1995).
[13]
PHOSPHORYLATION AT SER-133.
PubMed=9829964; DOI=10.1074/jbc.273.49.32377;
Du K., Montminy M.;
"CREB is a regulatory target for the protein kinase Akt/PKB.";
J. Biol. Chem. 273:32377-32379(1998).
[14]
PHOSPHORYLATION AT SER-133.
PubMed=9770464; DOI=10.1073/pnas.95.21.12202;
De Cesare D., Jacquot S., Hanauer A., Sassone-Corsi P.;
"Rsk-2 activity is necessary for epidermal growth factor-induced
phosphorylation of CREB protein and transcription of c-fos gene.";
Proc. Natl. Acad. Sci. U.S.A. 95:12202-12207(1998).
[15]
INTERACTION WITH CRTC1.
PubMed=14536081; DOI=10.1016/j.molcel.2003.08.013;
Conkright M.D., Canettieri G., Screaton R., Guzman E., Miraglia L.,
Hogenesch J.B., Montminy M.;
"TORCs: transducers of regulated CREB activity.";
Mol. Cell 12:413-423(2003).
[16]
SUMOYLATION AT LYS-285 AND LYS-304, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF LYS-155; LYS-285 AND LYS-304.
PubMed=12552083; DOI=10.1073/pnas.0337412100;
Comerford K.M., Leonard M.O., Karhausen J., Carey R., Colgan S.P.,
Taylor C.T.;
"Small ubiquitin-related modifier-1 modification mediates resolution
of CREB-dependent responses to hypoxia.";
Proc. Natl. Acad. Sci. U.S.A. 100:986-991(2003).
[17]
INTERACTION WITH CRTC3.
PubMed=14506290; DOI=10.1073/pnas.1932773100;
Iourgenko V., Zhang W., Mickanin C., Daly I., Jiang C., Hexham J.M.,
Orth A.P., Miraglia L., Meltzer J., Garza D., Chirn G.-W.,
McWhinnie E., Cohen D., Skelton J., Terry R., Yu Y., Bodian D.,
Buxton F.P., Zhu J., Song C., Labow M.A.;
"Identification of a family of cAMP response element-binding protein
coactivators by genome-scale functional analysis in mammalian cells.";
Proc. Natl. Acad. Sci. U.S.A. 100:12147-12152(2003).
[18]
INTERACTION WITH CRTC2.
PubMed=15454081; DOI=10.1016/j.cell.2004.09.015;
Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G.,
Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H.,
Okamoto M., Montminy M.;
"The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive
coincidence detector.";
Cell 119:61-74(2004).
[19]
INTERACTION WITH ARRB1.
PubMed=16325578; DOI=10.1016/j.cell.2005.09.011;
Kang J., Shi Y., Xiang B., Qu B., Su W., Zhu M., Zhang M., Bao G.,
Wang F., Zhang X., Yang R., Fan F., Chen X., Pei G., Ma L.;
"A nuclear function of beta-arrestin1 in GPCR signaling: regulation of
histone acetylation and gene transcription.";
Cell 123:833-847(2005).
[20]
PHOSPHORYLATION AT SER-133 BY SGK1, AND INTERACTION WITH SGK1.
PubMed=15733869; DOI=10.1016/j.febslet.2005.01.040;
David S., Kalb R.G.;
"Serum/glucocorticoid-inducible kinase can phosphorylate the cyclic
AMP response element binding protein, CREB.";
FEBS Lett. 579:1534-1538(2005).
[21]
INTERACTION WITH PPRC1.
PubMed=16908542; DOI=10.1128/MCB.00585-06;
Vercauteren K., Pasko R.A., Gleyzer N., Marino V.M., Scarpulla R.C.;
"PGC-1-related coactivator: immediate early expression and
characterization of a CREB/NRF-1 binding domain associated with
cytochrome c promoter occupancy and respiratory growth.";
Mol. Cell. Biol. 26:7409-7419(2006).
[22]
CHROMOSOMAL TRANSLOCATION WITH EWSR1, AND ASSOCIATION WITH ANGIOMATOID
FIBROUS HISTIOCYTOMA.
PubMed=17724745; DOI=10.1002/gcc.20491;
Antonescu C.R., Dal Cin P., Nafa K., Teot L.A., Surti U.,
Fletcher C.D., Ladanyi M.;
"EWSR1-CREB1 is the predominant gene fusion in angiomatoid fibrous
histiocytoma.";
Genes Chromosomes Cancer 46:1051-1060(2007).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[26]
PHOSPHORYLATION AT SER-271 BY HIPK2, MUTAGENESIS OF SER-271, AND
INTERACTION WITH HIPK2.
PubMed=20573984; DOI=10.1091/mbc.E10-01-0015;
Sakamoto K., Huang B.-W., Iwasaki K., Hailemariam K.,
Ninomiya-Tsuji J., Tsuji Y.;
"Regulation of genotoxic stress response by homeodomain-interacting
protein kinase 2 through phosphorylation of cyclic AMP response
element-binding protein at serine 271.";
Mol. Biol. Cell 21:2966-2974(2010).
[27]
INTERACTION WITH TOX3, AND MUTAGENESIS OF SER-133.
PubMed=21172805; DOI=10.1242/jcs.068759;
Dittmer S., Kovacs Z., Yuan S.H., Siszler G., Kogl M., Summer H.,
Geerts A., Golz S., Shioda T., Methner A.;
"TOX3 is a neuronal survival factor that induces transcription
depending on the presence of CITED1 or phosphorylated CREB in the
transcriptionally active complex.";
J. Cell Sci. 124:252-260(2011).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[29]
POSSIBLE INVOLVEMENT IN MULTIPLE CONGENITAL ANOMALIES, VARIANT
GLY-116, AND CHARACTERIZATION OF VARIANT GLY-116.
PubMed=22267179; DOI=10.1002/humu.22027;
Kitazawa S., Kondo T., Mori K., Yokoyama N., Matsuo M., Kitazawa R.;
"A p.D116G mutation in CREB1 leads to novel multiple malformation
syndrome resembling CrebA knockout mouse.";
Hum. Mutat. 33:651-654(2012).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[32]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-136, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- 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.
-!- 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.
When phosphorylated on Ser-133, binds CREBBP (By similarity).
Interacts with CREBL2; regulates CREB1 phosphorylation, stability
and transcriptional activity (By similarity). Interacts
(phosphorylated form) with TOX3. Interacts with ARRB1. Binds to
HIPK2. Interacts with SGK1. {ECO:0000250,
ECO:0000269|PubMed:1386673, ECO:0000269|PubMed:14506290,
ECO:0000269|PubMed:14536081, ECO:0000269|PubMed:15454081,
ECO:0000269|PubMed:15733869, ECO:0000269|PubMed:16325578,
ECO:0000269|PubMed:16908542, ECO:0000269|PubMed:1827531,
ECO:0000269|PubMed:20573984, ECO:0000269|PubMed:21172805}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-711855, EBI-711855;
P03259-2:- (xeno); NbExp=2; IntAct=EBI-711855, EBI-7225021;
P18846:ATF1; NbExp=6; IntAct=EBI-711855, EBI-852794;
Q92793:CREBBP; NbExp=3; IntAct=EBI-711855, EBI-81215;
Q6UUV9:CRTC1; NbExp=3; IntAct=EBI-711855, EBI-1644259;
Q09472:EP300; NbExp=2; IntAct=EBI-711855, EBI-447295;
P0C746:HBZ (xeno); NbExp=2; IntAct=EBI-711855, EBI-10890294;
Q9DGW5:MDV005 (xeno); NbExp=2; IntAct=EBI-711855, EBI-10889526;
O00470:MEIS1; NbExp=9; IntAct=EBI-711855, EBI-1210694;
O95644:NFATC1; NbExp=3; IntAct=EBI-711855, EBI-6907210;
Q13469:NFATC2; NbExp=2; IntAct=EBI-711855, EBI-716258;
Q16649:NFIL3; NbExp=3; IntAct=EBI-711855, EBI-3951858;
Q96RG2:PASK; NbExp=2; IntAct=EBI-711855, EBI-1042651;
Q6SA08:TSSK4; NbExp=5; IntAct=EBI-711855, EBI-1202583;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00312, ECO:0000255|PROSITE-ProRule:PRU00978,
ECO:0000269|PubMed:12552083}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=CREB-A;
IsoId=P16220-1; Sequence=Displayed;
Name=CREB-B;
IsoId=P16220-2; Sequence=VSP_000596;
Name=3; Synonyms=htCREB;
IsoId=P16220-3; Sequence=VSP_043914;
Note=Highly expressed in adult testis and sperm.;
-!- PTM: Stimulated by phosphorylation. Phosphorylation of both Ser-
133 and Ser-142 in the SCN regulates the activity of CREB and
participates in circadian rhythm generation. Phosphorylation of
Ser-133 allows CREBBP binding. In liver, phosphorylation is
induced by fasting or glucagon in a circadian fashion (By
similarity). CREBL2 positively regulates phosphorylation at Ser-
133 thereby stimulating CREB1 transcriptional activity (By
similarity). 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 (By similarity).
Phosphorylation of Ser-271 by HIPK2 in response to genotoxic
stress promotes CREB1 activity, facilitating the recruitment of
the coactivator CBP. Phosphorylated at Ser-133 by RPS6KA3, RPS6KA4
and RPS6KA5 in response to mitogenic or stress stimuli.
{ECO:0000250, ECO:0000269|PubMed:15733869,
ECO:0000269|PubMed:20573984, ECO:0000269|PubMed:7608156,
ECO:0000269|PubMed:8065343, ECO:0000269|PubMed:9770464,
ECO:0000269|PubMed:9829964}.
-!- 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. {ECO:0000269|PubMed:12552083}.
-!- DISEASE: Angiomatoid fibrous histiocytoma (AFH) [MIM:612160]: A
distinct variant of malignant fibrous histiocytoma that typically
occurs in children and adolescents and is manifest by nodular
subcutaneous growth. Characteristic microscopic features include
lobulated sheets of histiocyte-like cells intimately associated
with areas of hemorrhage and cystic pseudovascular spaces, as well
as a striking cuffing of inflammatory cells, mimicking a lymph
node metastasis. Note=The gene represented in this entry may be
involved in disease pathogenesis. A chromosomal aberration
involving CREB1 is found in a patient with angiomatoid fibrous
histiocytoma. Translocation t(2;22)(q33;q12) with CREB1 generates
a EWSR1/CREB1 fusion gene that is most common genetic abnormality
in this tumor type.
-!- DISEASE: Note=A CREB1 mutation has been found in a patient with
multiple congenital anomalies consisting of agenesis of the corpus
callosum, cerebellar hypoplasia, severe neonatal respiratory
distress refractory to surfactant, thymus hypoplasia, and thyroid
follicular hypoplasia. {ECO:0000269|PubMed:22267179}.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; S72459; AAB20597.1; -; Genomic_DNA.
EMBL; X55545; CAA39151.1; -; mRNA.
EMBL; M34356; AAA35717.1; -; mRNA.
EMBL; M34356; AAA35716.1; -; mRNA.
EMBL; M27691; AAA35715.1; -; mRNA.
EMBL; X60003; CAA42620.1; -; mRNA.
EMBL; AY347527; AAQ24858.1; -; mRNA.
EMBL; BC010636; AAH10636.1; -; mRNA.
EMBL; S53724; AAD13869.1; -; Genomic_DNA.
CCDS; CCDS2374.1; -. [P16220-2]
CCDS; CCDS2375.1; -. [P16220-1]
PIR; A37340; A35769.
PIR; B37340; B35769.
PIR; S22298; S22298.
RefSeq; NP_004370.1; NM_004379.4. [P16220-2]
RefSeq; NP_604391.1; NM_134442.4. [P16220-1]
RefSeq; XP_011508947.1; XM_011510645.1. [P16220-1]
RefSeq; XP_011508949.1; XM_011510647.2. [P16220-2]
UniGene; Hs.516646; -.
UniGene; Hs.717136; -.
PDB; 2LXT; NMR; -; C=116-149.
PDBsum; 2LXT; -.
ProteinModelPortal; P16220; -.
SMR; P16220; -.
BioGrid; 107775; 145.
CORUM; P16220; -.
DIP; DIP-765N; -.
IntAct; P16220; 78.
MINT; P16220; -.
STRING; 9606.ENSP00000387699; -.
ChEMBL; CHEMBL5587; -.
DrugBank; DB00131; Adenosine monophosphate.
DrugBank; DB01183; Naloxone.
iPTMnet; P16220; -.
PhosphoSitePlus; P16220; -.
BioMuta; CREB1; -.
DMDM; 117434; -.
EPD; P16220; -.
PaxDb; P16220; -.
PeptideAtlas; P16220; -.
PRIDE; P16220; -.
DNASU; 1385; -.
Ensembl; ENST00000353267; ENSP00000236995; ENSG00000118260. [P16220-2]
Ensembl; ENST00000430624; ENSP00000405539; ENSG00000118260. [P16220-2]
Ensembl; ENST00000432329; ENSP00000387699; ENSG00000118260. [P16220-1]
GeneID; 1385; -.
KEGG; hsa:1385; -.
CTD; 1385; -.
DisGeNET; 1385; -.
EuPathDB; HostDB:ENSG00000118260.14; -.
GeneCards; CREB1; -.
HGNC; HGNC:2345; CREB1.
HPA; CAB003803; -.
HPA; HPA019150; -.
MalaCards; CREB1; -.
MIM; 123810; gene.
MIM; 612160; phenotype.
neXtProt; NX_P16220; -.
OpenTargets; ENSG00000118260; -.
Orphanet; 97338; Melanoma of soft parts.
PharmGKB; PA26864; -.
eggNOG; KOG3584; Eukaryota.
eggNOG; ENOG410ZZJZ; LUCA.
GeneTree; ENSGT00390000008655; -.
HOGENOM; HOG000007365; -.
HOVERGEN; HBG011077; -.
InParanoid; P16220; -.
KO; K05870; -.
OMA; QXISTIA; -.
OrthoDB; EOG091G0FTJ; -.
PhylomeDB; P16220; -.
TreeFam; TF106464; -.
Reactome; R-HSA-111931; PKA-mediated phosphorylation of CREB.
Reactome; R-HSA-111932; CaMK IV-mediated phosphorylation of CREB.
Reactome; R-HSA-198693; AKT phosphorylates targets in the nucleus.
Reactome; R-HSA-199920; CREB phosphorylation.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-2197563; NOTCH2 intracellular domain regulates transcription.
Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-442717; CREB phosphorylation through the activation of CaMKK.
Reactome; R-HSA-442720; CREB phosphorylation through the activation of Adenylate Cyclase.
Reactome; R-HSA-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-HSA-442742; CREB phosphorylation through the activation of Ras.
Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
Reactome; R-HSA-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
SignaLink; P16220; -.
SIGNOR; P16220; -.
ChiTaRS; CREB1; human.
GeneWiki; CREB1; -.
GenomeRNAi; 1385; -.
PMAP-CutDB; P16220; -.
PRO; PR:P16220; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000118260; -.
CleanEx; HS_CREB1; -.
ExpressionAtlas; P16220; baseline and differential.
Genevisible; P16220; HS.
GO; GO:1990589; C:ATF4-CREB1 transcription factor complex; IDA:ParkinsonsUK-UCL.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
GO; GO:0005719; C:nuclear euchromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0035497; F:cAMP response element binding; IDA:BHF-UCL.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:MGI.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:BHF-UCL.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001225; F:RNA polymerase II transcription coactivator binding; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0003712; F:transcription cofactor activity; TAS:ProtInc.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:BHF-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IC:NTNU_SB.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; IDA:BHF-UCL.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEA:Ensembl.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0034670; P:chemotaxis to arachidonic acid; IEA:Ensembl.
GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0060430; P:lung saccule development; IEA:Ensembl.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IDA:BHF-UCL.
GO; GO:0021983; P:pituitary gland development; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0055025; P:positive regulation of cardiac muscle tissue development; IEA:Ensembl.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0046887; P:positive regulation of hormone secretion; IEA:Ensembl.
GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISS:UniProtKB.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IEA:Ensembl.
GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0032916; P:positive regulation of transforming growth factor beta3 production; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
GO; GO:0042752; P:regulation of circadian rhythm; IEA:Ensembl.
GO; GO:0048145; P:regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0060251; P:regulation of glial cell proliferation; IEA:Ensembl.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0033762; P:response to glucagon; ISS: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; IDA:MGI.
GO; GO:0033363; P:secretory granule organization; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
GO; GO:0060509; P:Type I pneumocyte differentiation; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0008542; P:visual learning; IEA:Ensembl.
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;
Chromosomal rearrangement; Complete proteome; Differentiation;
DNA-binding; Host-virus interaction; Isopeptide bond; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 341 Cyclic AMP-responsive element-binding
protein 1.
/FTId=PRO_0000076597.
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.
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:15733869,
ECO:0000269|PubMed:7608156,
ECO:0000269|PubMed:8065343,
ECO:0000269|PubMed:9770464,
ECO:0000269|PubMed:9829964}.
MOD_RES 142 142 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 271 271 Phosphoserine; by HIPK2.
{ECO:0000255|PROSITE-ProRule:PRU00312,
ECO:0000269|PubMed:20573984}.
CROSSLNK 136 136 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 285 285 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000269|PubMed:12552083}.
CROSSLNK 304 304 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000269|PubMed:12552083}.
VAR_SEQ 88 101 Missing (in isoform CREB-B).
{ECO:0000303|PubMed:1831258,
ECO:0000303|PubMed:2974179}.
/FTId=VSP_000596.
VAR_SEQ 162 272 Missing (in isoform 3).
{ECO:0000303|PubMed:15579595}.
/FTId=VSP_043914.
VARIANT 116 116 D -> G (found in a patient with multiple
congenital anomalies; does not affect
CREB1 phosphorylation at S-133; fails to
interact with CREBBP; dbSNP:rs387906617).
{ECO:0000269|PubMed:22267179}.
/FTId=VAR_068077.
MUTAGEN 133 133 S->A: Does not interact with TOX3 and
inhibits induction of transcription by
TOX3. Loss of phosphorylation by CaMK4.
{ECO:0000269|PubMed:21172805,
ECO:0000269|PubMed:8065343}.
MUTAGEN 155 155 K->R: No effect on sumoylation.
{ECO:0000269|PubMed:12552083}.
MUTAGEN 271 271 S->A: Impaired phosphorylation by HIPK2
and subsequent transactivation.
{ECO:0000269|PubMed:20573984}.
MUTAGEN 271 271 S->E: Potentiated transactivation.
{ECO:0000269|PubMed:20573984}.
MUTAGEN 285 285 K->R: Decreased sumoylation, in vivo and
in vitro. {ECO:0000269|PubMed:12552083}.
MUTAGEN 304 304 K->R: Decreased sumoylation, in vivo and
in vitro. Loss of nuclear localization.
{ECO:0000269|PubMed:12552083}.
CONFLICT 4 4 E -> D (in Ref. 5; CAA42620).
{ECO:0000305}.
CONFLICT 8 8 E -> D (in Ref. 5; CAA42620).
{ECO:0000305}.
CONFLICT 160 160 T -> A (in Ref. 5; CAA42620).
{ECO:0000305}.
CONFLICT 167 167 T -> A (in Ref. 5; CAA42620).
{ECO:0000305}.
CONFLICT 169 169 T -> A (in Ref. 5; CAA42620).
{ECO:0000305}.
CONFLICT 176 176 Q -> R (in Ref. 5; CAA42620).
{ECO:0000305}.
CONFLICT 184 184 A -> T (in Ref. 5; CAA42620).
{ECO:0000305}.
CONFLICT 188 188 G -> R (in Ref. 5; CAA42620).
{ECO:0000305}.
CONFLICT 195 195 N -> S (in Ref. 5; CAA42620).
{ECO:0000305}.
CONFLICT 210 210 T -> A (in Ref. 5; CAA42620).
{ECO:0000305}.
CONFLICT 292 292 K -> E (in Ref. 6; AAQ24858).
{ECO:0000305}.
HELIX 120 128 {ECO:0000244|PDB:2LXT}.
HELIX 132 142 {ECO:0000244|PDB:2LXT}.
SEQUENCE 341 AA; 36688 MW; D5E989AE40BF69AF CRC64;
MTMESGAENQ 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


Related products :

Catalog number Product name Quantity
U1318b CLIA Bos taurus,Bovine,cAMP-responsive element-binding protein 1,CREB,CREB1,CREB-1,CREB2,Cyclic AMP-responsive DNA-binding protein,Cyclic AMP-responsive element-binding protein 1 96T
E1318b ELISA Bos taurus,Bovine,cAMP-responsive element-binding protein 1,CREB,CREB1,CREB-1,CREB2,Cyclic AMP-responsive DNA-binding protein,Cyclic AMP-responsive element-binding protein 1 96T
E1318b ELISA kit Bos taurus,Bovine,cAMP-responsive element-binding protein 1,CREB,CREB1,CREB-1,CREB2,Cyclic AMP-responsive DNA-binding protein,Cyclic AMP-responsive element-binding protein 1 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
E1318m ELISA cAMP-responsive element-binding protein 1,Creb1,CREB-1,Creb-1,Cyclic AMP-responsive element-binding protein 1,Mouse,Mus musculus 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
U1318m CLIA 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
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
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


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur