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UniProtKB/Swiss-Prot entry P16220


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CREB1_HUMAN
Primary accession number P16220
Secondary accession numbers P21934 Q9UMA7
Integrated into Swiss-Prot on April 1, 1990
Sequence was last modified on May 1, 1992 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 120)
Name and origin of the protein
Protein name Cyclic AMP-responsive element-binding protein 1
Synonyms cAMP-responsive element-binding protein 1
CREB-1
Gene name
Name: CREB1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CREB-A).
DOI=10.1073/pnas.87.14.5258; PubMed=2142528 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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).
DOI=10.1126/science.2974179; PubMed=2974179 [NCBI, ExPASy, EBI, Israel, Japan]
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).
DOI=10.1093/nar/19.15.4290; PubMed=1831258 [NCBI, ExPASy, EBI, Israel, Japan]
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 [LARGE SCALE MRNA] (ISOFORM CREB-A).
TISSUE=Eye;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
DOI=10.1210/en.132.2.770; PubMed=8381074 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
INTERACTION WITH HBV PROTEIN X.
DOI=10.1126/science.1827531; PubMed=1827531 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
INTERACTION WITH HTLV-1 TAX-1.
DOI=10.1073/pnas.89.15.7070; PubMed=1386673 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
PHOSPHORYLATION AT SER-133.
DOI=10.1074/jbc.270.27.16378; PubMed=7608156 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
INTERACTION WITH CRTC1.
DOI=10.1016/j.molcel.2003.08.013; PubMed=14536081 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
INTERACTION WITH CRTC3.
DOI=10.1073/pnas.1932773100; PubMed=14506290 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
INTERACTION WITH CRTC2.
DOI=10.1016/j.cell.2004.09.015; PubMed=15454081 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
INTERACTION WITH PPRC1.
DOI=10.1128/MCB.00585-06; PubMed=16908542 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111 AND THR-119, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[16]
CHROMOSOMAL TRANSLOCATION WITH EWSR1, AND ASSOCIATION WITH ANGIOMATOID FIBROUS HISTIOCYTOMA.
DOI=10.1002/gcc.20491; PubMed=17724745 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
S72459; AAB20597.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X55545; CAA39151.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34356; AAA35717.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34356; AAA35716.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27691; AAA35715.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X60003; CAA42620.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010636; AAH10636.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S53724; AAD13869.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00027713; -.
IPI00218334; -.
PIR A37340; A35769.
B37340; B35769.
S22298; S22298.
RefSeq NP_604391.1; -.
UniGene Hs.516646
3D structure databases
HSSP P15337; 1KDX. [HSSP ENTRY / PDB]
SMR P16220; 285-339.
ModBase P16220.
Protein-protein interaction databases
IntAct P16220; 11.
PTM databases
PhosphoSite P16220; -.
Enzyme and pathway databases
Pathway_Interaction_DB hnf3bpathway; FOXA2 and FOXA3 transcription factor networks.
hif1_tfpathway; HIF-1-alpha transcription factor network.
lpa4_pathway; LPA4-mediated signaling events.
p38_mk2pathway; p38 signaling mediated by MAPKAP kinases.
smad2_3nuclearpathway; Regulation of nuclear SMAD2/3 signaling.
ret_pathway; Signaling events regulated by Ret tyrosine kinase.
p38alphabetadownstreampathway; Signaling mediated by p38-alpha and p38-beta.
pi3kplctrkpathway; Trk receptor signaling mediated by PI3K and PLC-gamma.
mapktrkpathway; Trk receptor signaling mediated by the MAPK pathway.
lymphangiogenesis_pathway; VEGFR3 signaling in lymphatic endothelium.
Reactome REACT_11061; Signalling by NGF.
Organism-specific databases
GeneCards GC02P208102; -.
H-InvDB HIX0023181; -.
HGNC HGNC:2345; CREB1.
GenAtlas CREB1.
HPA CAB003803; -.
MIM 123810; gene. [NCBI / EBI]
612160; phenotype. [NCBI / EBI]
PharmGKB PA26864; -.
Gene expression databases
ArrayExpress P16220; -.
Bgee P16220; -.
CleanEx HS_CREB1; -.
GermOnline ENSG00000118260; Homo sapiens.
Ontologies
GO
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0046983; Molecular function: protein dimerization activity (inferred from electronic annotation from InterPro).
GO:0043565; Molecular function: sequence-specific DNA binding (inferred from electronic annotation from InterPro).
GO:0003712; Molecular function: transcription cofactor activity (traceable author statement from ProtInc).
GO:0003700; Molecular function: transcription factor activity (inferred from direct assay from MGI).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0045944; Biological process: positive regulation of transcription from RNA polymerase II promoter (inferred from direct assay from MGI).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from direct assay from MGI).
GO:0010033; Biological process: response to organic substance (inferred from direct assay from MGI).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
GO:0006351; Biological process: transcription, DNA-dependent (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR011616; bZIP_1.
IPR003102; Coactivator_CBP_pKID.
IPR001630; Leuzip_CREB.
IPR004827; TF_bZIP.
Graphical view of domain structure.
Pfam PF00170; bZIP_1; 1.
PF02173; pKID; 1.
Pfam graphical view of domain structure.
PRINTS PR00041; LEUZIPPRCREB.
SMART SM00338; BRLZ; 1.
SMART graphical view of domain structure.
PROSITE PS50217; BZIP; 1.
PS00036; BZIP_BASIC; 1.
PS50953; KID; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P16220; -.
Genome annotation databases
Ensembl ENSG00000118260; Homo sapiens. [Contig view]
GeneID 1385; -.
KEGG hsa:1385; -.
Phylogenomic databases
HOGENOM P16220; -.
HOVERGEN P16220; -.
OMA P16220; XKILNDL.
Other
DrugBank DB00131; Adenosine monophosphate.
DB01200; Bromocriptine.
DB01183; Naloxone.
NextBio 5625; -.
PMAP-CutDB P16220; -.
SOURCE CREB1; Homo sapiens.
ProtoNet P16220.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Activator; Alternative splicing; Chromosomal rearrangement; DNA-binding; Host-virus interaction; Nucleus; Phosphoprotein; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   341  341     Cyclic AMP-responsive element-binding protein 1. PRO_0000076597
DOMAIN   101   160  60     KID. 
DOMAIN   311   332  22     Leucine-zipper. 
DNA_BIND   284   305  22     Basic motif. 
SITE   314   314  1     Required for binding TORCs. 
MOD_RES   111   111        Phosphoserine. 
MOD_RES   119   119        Phosphothreonine. 
MOD_RES   133   133        Phosphoserine; by CaMK1, CaMK2 and CaMK4. 
MOD_RES   142   142        Phosphoserine; by CaMK2 (By similarity). 
VAR_SEQ   88   101        Missing (in isoform CREB-B). VSP_000596
CONFLICT   4     4        E -> D (in Ref. 5; CAA42620). 
CONFLICT   8     8        E -> D (in Ref. 5; CAA42620). 
CONFLICT   160   160        T -> A (in Ref. 5; CAA42620). 
CONFLICT   167   167        T -> A (in Ref. 5; CAA42620). 
CONFLICT   169   169        T -> A (in Ref. 5; CAA42620). 
CONFLICT   176   176        Q -> R (in Ref. 5; CAA42620). 
CONFLICT   184   184        A -> T (in Ref. 5; CAA42620). 
CONFLICT   188   188        G -> R (in Ref. 5; CAA42620). 
CONFLICT   195   195        N -> S (in Ref. 5; CAA42620). 
CONFLICT   210   210        T -> A (in Ref. 5; CAA42620). 
Sequence information
Length: 341 AA [This is the length of the unprocessed precursor] Molecular weight: 36688 Da [This is the MW of the unprocessed precursor] CRC64: D5E989AE40BF69AF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTMESGAENQ QSGDAAVTEA ENQQMTVQAQ PQIATLAQVS MPAAHATSSA PTVTLVQLPN 

        70         80         90        100        110        120 
GQTVQVHGVI QAAQPSVIQS PQVQTVQSSC KDLKRLFSGT QISTIAESED SQESVDSVTD 

       130        140        150        160        170        180 
SQKRREILSR RPSYRKILND LSSDAPGVPR IEEEKSEEET SAPAITTVTV PTPIYQTSSG 

       190        200        210        220        230        240 
QYIAITQGGA IQLANNGTDG VQGLQTLTMT NAAATQPGTT ILQYAQTTDG QQILVPSNQV 

       250        260        270        280        290        300 
VVQAASGDVQ TYQIRTAPTS TIAPGVVMAS SPALPTQPAE EAARKREVRL MKNREAAREC 

       310        320        330        340 
RRKKKEYVKC LENRVAVLEN QNKTLIEELK ALKDLYCHKS D 

P16220 in FASTA format

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