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P16220 (CREB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 175. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclic AMP-responsive element-binding protein 1

Short name=CREB-1
Short name=cAMP-responsive element-binding protein 1
Gene names
Name:CREB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 structure

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. Ref.9 Ref.10 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.26 Ref.27

Subcellular location

Nucleus Ref.16.

Post-translational modification

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 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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.20 Ref.26

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. Ref.16

Involvement in 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.

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 (Ref.29).

Sequence similarities

Belongs to the bZIP family.

Contains 1 bZIP (basic-leucine zipper) domain.

Contains 1 KID (kinase-inducible) domain.

Ontologies

Keywords
   Biological processDifferentiation
Host-virus interaction
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   LigandDNA-binding
   Molecular functionActivator
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

Notch signaling pathway

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

Type I pneumocyte differentiation

Inferred from electronic annotation. Source: Ensembl

activation of phospholipase C activity

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

lactation

Inferred from electronic annotation. Source: Ensembl

lung saccule development

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription by competitive promoter binding

Inferred from direct assay PubMed 19861239. Source: BHF-UCL

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

pituitary gland development

Inferred from electronic annotation. Source: Ensembl

positive regulation of fat cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of hormone secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of lipid biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19861239. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Inferred from direct assay PubMed 8798441. Source: MGI

protein stabilization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell size

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to organic substance

Inferred from direct assay PubMed 8798441. Source: MGI

secretory granule organization

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement. Source: Reactome

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

synaptic transmission

Traceable author statement. Source: Reactome

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19861239. Source: GOC

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnuclear euchromatin

Inferred from direct assay PubMed 19861239. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRNA polymerase II activating transcription factor binding

Inferred from physical interaction PubMed 19861239. Source: BHF-UCL

RNA polymerase II distal enhancer sequence-specific DNA binding

Inferred from direct assay PubMed 19861239. Source: BHF-UCL

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 19861239. Source: BHF-UCL

RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 19861239. Source: BHF-UCL

cAMP response element binding

Inferred from direct assay PubMed 19861239. Source: BHF-UCL

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 8798441. Source: MGI

transcription cofactor activity

Traceable author statement PubMed 8552098. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform CREB-A (identifier: P16220-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform CREB-B (identifier: P16220-2)

The sequence of this isoform differs from the canonical sequence as follows:
     88-101: Missing.
Isoform 3 (identifier: P16220-3)

Also known as: htCREB;

The sequence of this isoform differs from the canonical sequence as follows:
     162-272: Missing.
Note: Highly expressed in adult testis and sperm.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341Cyclic AMP-responsive element-binding protein 1
PRO_0000076597

Regions

Domain101 – 16060KID
Domain283 – 34159bZIP
Region284 – 30926Basic motif By similarity
Region311 – 33222Leucine-zipper By similarity

Sites

Site3141Required for binding TORCs

Amino acid modifications

Modified residue1331Phosphoserine; by CaMK1, CaMK2, CaMK4, PKB/AKT1 or PKB/AKT2, RPS6KA3, RPS6KA4, RPS6KA5 and SGK1 Ref.11 Ref.12 Ref.13 Ref.14 Ref.20
Modified residue1421Phosphoserine; by CaMK2 By similarity
Modified residue2711Phosphoserine; by HIPK2 Ref.26
Cross-link285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) Ref.16
Cross-link304Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) Ref.16

Natural variations

Alternative sequence88 – 10114Missing in isoform CREB-B.
VSP_000596
Alternative sequence162 – 272111Missing in isoform 3.
VSP_043914
Natural variant1161D → G Found in a patient with multiple congenital anomalies; does not affect CREB1 phosphorylation at S-133; fails to interact with CREBBP. Ref.29
VAR_068077

Experimental info

Mutagenesis1331S → A: Does not interact with TOX3 and inhibits induction of transcription by TOX3. Loss of phosphorylation by CaMK4. Ref.11 Ref.27
Mutagenesis1551K → R: No effect on sumoylation. Ref.16
Mutagenesis2711S → A: Impaired phosphorylation by HIPK2 and subsequent transactivation. Ref.26
Mutagenesis2711S → E: Potentiated transactivation. Ref.26
Mutagenesis2851K → R: Decreased sumoylation, in vivo and in vitro. Ref.16
Mutagenesis3041K → R: Decreased sumoylation, in vivo and in vitro. Loss of nuclear localization. Ref.16
Sequence conflict41E → D in CAA42620. Ref.5
Sequence conflict81E → D in CAA42620. Ref.5
Sequence conflict1601T → A in CAA42620. Ref.5
Sequence conflict1671T → A in CAA42620. Ref.5
Sequence conflict1691T → A in CAA42620. Ref.5
Sequence conflict1761Q → R in CAA42620. Ref.5
Sequence conflict1841A → T in CAA42620. Ref.5
Sequence conflict1881G → R in CAA42620. Ref.5
Sequence conflict1951N → S in CAA42620. Ref.5
Sequence conflict2101T → A in CAA42620. Ref.5
Sequence conflict2921K → E in AAQ24858. Ref.6

Secondary structure

..... 341
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform CREB-A [UniParc].

Last modified May 1, 1992. Version 2.
Checksum: D5E989AE40BF69AF

FASTA34136,688
        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 

« Hide

Isoform CREB-B [UniParc].

Checksum: F5BA8200EE5184B7
Show »

FASTA32735,136
Isoform 3 (htCREB) [UniParc].

Checksum: 9FD8CA28F7632FBD
Show »

FASTA23025,445

References

« Hide 'large scale' references
[1]"Two distinct forms of active transcription factor CREB (cAMP response element binding protein)."
Berkowitz L.A., Gilman M.Z.
Proc. Natl. Acad. Sci. U.S.A. 87:5258-5262(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CREB-A).
[2]"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."
Yoshimura T., Fujisawa J., Yoshida M.
EMBO J. 9:2537-2542(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CREB-A).
[3]"Diversification of cyclic AMP-responsive enhancer binding proteins-generated by alternative exon splicing."
Waeber G., Meyer T.E., Hoeffler J.P., Habener J.F.
Trans. Assoc. Am. Physicians 103:28-37(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CREB-A).
[4]"Cyclic AMP-responsive DNA-binding protein: structure based on a cloned placental cDNA."
Hoeffler J.P., Meyer T.E., Yun Y., Jameson J.L., Habener J.F.
Science 242:1430-1433(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CREB-B).
[5]"Nucleotide and derived amino-acid sequences of the CRE-binding proteins from rat C6 glioma and HeLa cells."
Short M.L., Manohar C.F., Furtado M.R., Ghadge G.D., Wolinsky S.M., Thimmapaya B., Jungmann R.A.
Nucleic Acids Res. 19:4290-4290(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CREB-B).
[6]"Cloning and expression of a novel CREB mRNA splice variant in human testis."
Huang X., Zhang J., Lu L., Yin L., Xu M., Wang Y., Zhou Z., Sha J.
Reproduction 128:775-782(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Testis.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CREB-A).
Tissue: Eye.
[8]"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."
Meyer T.E., Waeber G., Lin J., Beckmann W., Habener J.F.
Endocrinology 132:770-780(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
[9]"HBV X protein alters the DNA binding specificity of CREB and ATF-2 by protein-protein interactions."
Maguire H.F., Hoeffler J.P., Siddiqui A.
Science 252:842-844(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HBV PROTEIN X.
[10]"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."
Zhao L.J., Giam C.-Z.
Proc. Natl. Acad. Sci. U.S.A. 89:7070-7074(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HTLV-1 TAX-1.
[11]"Calcium/calmodulin-dependent protein kinase types II and IV differentially regulate CREB-dependent gene expression."
Matthews R.P., Guthrie C.R., Wailes L.M., Zhao X., Means A.R., McKnight G.S.
Mol. Cell. Biol. 14:6107-6116(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-133, MUTAGENESIS OF SER-133.
[12]"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."
Lee H.-J.J., Mignacca R.C., Sakamoto K.M.
J. Biol. Chem. 270:15979-15983(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-133.
[13]"CREB is a regulatory target for the protein kinase Akt/PKB."
Du K., Montminy M.
J. Biol. Chem. 273:32377-32379(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-133.
[14]"Rsk-2 activity is necessary for epidermal growth factor-induced phosphorylation of CREB protein and transcription of c-fos gene."
De Cesare D., Jacquot S., Hanauer A., Sassone-Corsi P.
Proc. Natl. Acad. Sci. U.S.A. 95:12202-12207(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-133.
[15]"TORCs: transducers of regulated CREB activity."
Conkright M.D., Canettieri G., Screaton R., Guzman E., Miraglia L., Hogenesch J.B., Montminy M.
Mol. Cell 12:413-423(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRTC1.
[16]"Small ubiquitin-related modifier-1 modification mediates resolution of CREB-dependent responses to hypoxia."
Comerford K.M., Leonard M.O., Karhausen J., Carey R., Colgan S.P., Taylor C.T.
Proc. Natl. Acad. Sci. U.S.A. 100:986-991(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-285 AND LYS-304, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-155; LYS-285 AND LYS-304.
[17]"Identification of a family of cAMP response element-binding protein coactivators by genome-scale functional analysis in mammalian cells."
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. expand/collapse author list , Zhu J., Song C., Labow M.A.
Proc. Natl. Acad. Sci. U.S.A. 100:12147-12152(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRTC3.
[18]"The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector."
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.
Cell 119:61-74(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRTC2.
[19]"A nuclear function of beta-arrestin1 in GPCR signaling: regulation of histone acetylation and gene transcription."
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.
Cell 123:833-847(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB1.
[20]"Serum/glucocorticoid-inducible kinase can phosphorylate the cyclic AMP response element binding protein, CREB."
David S., Kalb R.G.
FEBS Lett. 579:1534-1538(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-133 BY SGK1, INTERACTION WITH SGK1.
[21]"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."
Vercauteren K., Pasko R.A., Gleyzer N., Marino V.M., Scarpulla R.C.
Mol. Cell. Biol. 26:7409-7419(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPRC1.
[22]"EWSR1-CREB1 is the predominant gene fusion in angiomatoid fibrous histiocytoma."
Antonescu C.R., Dal Cin P., Nafa K., Teot L.A., Surti U., Fletcher C.D., Ladanyi M.
Genes Chromosomes Cancer 46:1051-1060(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH EWSR1, ASSOCIATION WITH ANGIOMATOID FIBROUS HISTIOCYTOMA.
[23]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
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.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[24]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[26]"Regulation of genotoxic stress response by homeodomain-interacting protein kinase 2 through phosphorylation of cyclic AMP response element-binding protein at serine 271."
Sakamoto K., Huang B.-W., Iwasaki K., Hailemariam K., Ninomiya-Tsuji J., Tsuji Y.
Mol. Biol. Cell 21:2966-2974(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-271 BY HIPK2, MUTAGENESIS OF SER-271, INTERACTION WITH HIPK2.
[27]"TOX3 is a neuronal survival factor that induces transcription depending on the presence of CITED1 or phosphorylated CREB in the transcriptionally active complex."
Dittmer S., Kovacs Z., Yuan S.H., Siszler G., Kogl M., Summer H., Geerts A., Golz S., Shioda T., Methner A.
J. Cell Sci. 124:252-260(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOX3, MUTAGENESIS OF SER-133.
[28]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"A p.D116G mutation in CREB1 leads to novel multiple malformation syndrome resembling CrebA knockout mouse."
Kitazawa S., Kondo T., Mori K., Yokoyama N., Matsuo M., Kitazawa R.
Hum. Mutat. 33:651-654(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN MULTIPLE CONGENITAL ANOMALIES, VARIANT GLY-116, CHARACTERIZATION OF VARIANT GLY-116.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S72459 Genomic DNA. Translation: AAB20597.1.
X55545 mRNA. Translation: CAA39151.1.
M34356 mRNA. Translation: AAA35717.1.
M34356 mRNA. Translation: AAA35716.1.
M27691 mRNA. Translation: AAA35715.1.
X60003 mRNA. Translation: CAA42620.1.
AY347527 mRNA. Translation: AAQ24858.1.
BC010636 mRNA. Translation: AAH10636.1.
S53724 Genomic DNA. Translation: AAD13869.1.
PIRA35769. A37340.
B35769. B37340.
S22298.
RefSeqNP_004370.1. NM_004379.3.
NP_604391.1. NM_134442.3.
UniGeneHs.516646.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LXTNMR-C116-149[»]
ProteinModelPortalP16220.
SMRP16220. Positions 116-149, 285-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107775. 90 interactions.
DIPDIP-765N.
IntActP16220. 36 interactions.
MINTMINT-1338714.
STRING9606.ENSP00000387699.

Chemistry

ChEMBLCHEMBL5587.
DrugBankDB00131. Adenosine monophosphate.
DB01200. Bromocriptine.
DB01183. Naloxone.

PTM databases

PhosphoSiteP16220.

Polymorphism databases

DMDM117434.

Proteomic databases

PaxDbP16220.
PRIDEP16220.

Protocols and materials databases

DNASU1385.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000353267; ENSP00000236995; ENSG00000118260. [P16220-2]
ENST00000374397; ENSP00000363518; ENSG00000118260. [P16220-3]
ENST00000430624; ENSP00000405539; ENSG00000118260. [P16220-2]
ENST00000432329; ENSP00000387699; ENSG00000118260. [P16220-1]
GeneID1385.
KEGGhsa:1385.
UCSCuc002vcc.3. human. [P16220-1]

Organism-specific databases

CTD1385.
GeneCardsGC02P208394.
HGNCHGNC:2345. CREB1.
HPACAB003803.
HPA019150.
MIM123810. gene.
612160. phenotype.
neXtProtNX_P16220.
Orphanet97338. Melanoma of soft part.
PharmGKBPA26864.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300199.
HOGENOMHOG000007365.
HOVERGENHBG011077.
InParanoidP16220.
KOK05870.
OMAQXISTIA.
OrthoDBEOG72G18D.
PhylomeDBP16220.
TreeFamTF106464.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_13685. Neuronal System.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SignaLinkP16220.

Gene expression databases

ArrayExpressP16220.
BgeeP16220.
CleanExHS_CREB1.
GenevestigatorP16220.

Family and domain databases

InterProIPR004827. bZIP.
IPR003102. Coactivator_CBP_pKID.
IPR001630. Leuzip_CREB.
[Graphical view]
PfamPF00170. bZIP_1. 1 hit.
PF02173. pKID. 1 hit.
[Graphical view]
PRINTSPR00041. LEUZIPPRCREB.
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
PS50953. KID. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCREB1.
GenomeRNAi1385.
NextBio5625.
PMAP-CutDBP16220.
PROP16220.
SOURCESearch...

Entry information

Entry nameCREB1_HUMAN
AccessionPrimary (citable) accession number: P16220
Secondary accession number(s): P21934, Q6V963, Q9UMA7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: May 1, 1992
Last modified: April 16, 2014
This is version 175 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM