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CAMP responsive element binding protein 1

PDB rendering based on 1dh3.
Available structures
1dh3
Identifiers
Symbols CREB1; CREB; MGC9284
External IDs OMIM123810 MGI88494 HomoloGene3223 GeneCards: CREB1 Gene
RNA expression pattern
PBB GE CREB1 204313 s at tn.png
PBB GE CREB1 204312 x at tn.png
PBB GE CREB1 204314 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1385 12912
Ensembl ENSG00000118260 ENSMUSG00000025958
UniProt P16220 Q547S9
RefSeq (mRNA) NM_004379 NM_009952
RefSeq (protein) NP_004370 NP_034082
Location (UCSC) Chr 2:
208.1 - 208.17 Mb
Chr 1:
64.47 - 64.54 Mb
PubMed search [1] [2]

CAMP responsive element binding protein 1, also known as CREB1, is a human protein and gene. This protein binds the cAMP response element, a DNA nucleotide sequence present in many viral and cellular promoters. The binding of CREB1 stimulates transcription.

This gene encodes a CREB transcription factor that is a member of the leucine zipper family of DNA binding proteins. This protein binds as a homodimer to the cAMP-responsive element, an octameric palindrome. The protein is phosphorylated by several protein kinases, and induces transcription of genes in response to hormonal stimulation of the cAMP pathway. Alternate splicing of this gene results in two transcript variants encoding different isoforms.[1]

Contents

See also

Interactions

CREB1 has been shown to interact with HTATIP,[2] RPS6KA5,[3][4] CREB binding protein,[5][6][7][8][9][10][11][12][13][14] FHL2,[15] FHL3,[15] P53,[11] CEBPB[16] and FHL5.[15]

References

  1. ^ "Entrez Gene: CREB1 cAMP responsive element binding protein 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1385.  
  2. ^ Gavaravarapu, S; Kamine J (Mar. 2000). "Tip60 inhibits activation of CREB protein by protein kinase A". Biochem. Biophys. Res. Commun. (UNITED STATES) 269 (3): 758–66. doi:10.1006/bbrc.2000.2358. ISSN 0006-291X. PMID 10720489.  
  3. ^ Deak, M; Clifton A D, Lucocq L M, Alessi D R (Aug. 1998). "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB". EMBO J. (ENGLAND) 17 (15): 4426–41. doi:10.1093/emboj/17.15.4426. ISSN 0261-4189. PMID 9687510.  
  4. ^ Wang, X; Li W, Williams M, Terada N, Alessi D R, Proud C G (Aug. 2001). "Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase". EMBO J. (England) 20 (16): 4370–9. doi:10.1093/emboj/20.16.4370. ISSN 0261-4189. PMID 11500364.  
  5. ^ Shi, Yuling; Venkataraman Sujatha L, Dodson Gerald E, Mabb Angela M, LeBlanc Scott, Tibbetts Randal S (Apr. 2004). "Direct regulation of CREB transcriptional activity by ATM in response to genotoxic stress". Proc. Natl. Acad. Sci. U.S.A. (United States) 101 (16): 5898–903. doi:10.1073/pnas.0307718101. ISSN 0027-8424. PMID 15073328.  
  6. ^ Kim, J; Jia L, Stallcup M R, Coetzee G A (Feb. 2005). "The role of protein kinase A pathway and cAMP responsive element-binding protein in androgen receptor-mediated transcription at the prostate-specific antigen locus". J. Mol. Endocrinol. (England) 34 (1): 107–18. doi:10.1677/jme.1.01701. ISSN 0952-5041. PMID 15691881.  
  7. ^ Shimomura, A; Ogawa Y, Kitani T, Fujisawa H, Hagiwara M (Jul. 1996). "Calmodulin-dependent protein kinase II potentiates transcriptional activation through activating transcription factor 1 but not cAMP response element-binding protein". J. Biol. Chem. (UNITED STATES) 271 (30): 17957–60. ISSN 0021-9258. PMID 8663317.  
  8. ^ Radhakrishnan, I; Pérez-Alvarado G C, Parker D, Dyson H J, Montminy M R, Wright P E (Dec. 1997). "Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions". Cell (UNITED STATES) 91 (6): 741–52. ISSN 0092-8674. PMID 9413984.  
  9. ^ Sano, Y; Tokitou F, Dai P, Maekawa T, Yamamoto T, Ishii S (Oct. 1998). "CBP alleviates the intramolecular inhibition of ATF-2 function". J. Biol. Chem. (UNITED STATES) 273 (44): 29098–105. ISSN 0021-9258. PMID 9786917.  
  10. ^ Zor, Tsaffrir; Mayr Bernhard M, Dyson H Jane, Montminy Marc R, Wright Peter E (Nov. 2002). "Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators". J. Biol. Chem. (United States) 277 (44): 42241–8. doi:10.1074/jbc.M207361200. ISSN 0021-9258. PMID 12196545.  
  11. ^ a b Giebler, H A; Lemasson I, Nyborg J K (Jul. 2000). "p53 recruitment of CREB binding protein mediated through phosphorylated CREB: a novel pathway of tumor suppressor regulation". Mol. Cell. Biol. (UNITED STATES) 20 (13): 4849–58. ISSN 0270-7306. PMID 10848610.  
  12. ^ Zhang, Q; Vo N, Goodman R H (Jul. 2000). "Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB". Mol. Cell. Biol. (UNITED STATES) 20 (14): 4970–8. ISSN 0270-7306. PMID 10866654.  
  13. ^ Ernst, P; Wang J, Huang M, Goodman R H, Korsmeyer S J (Apr. 2001). "MLL and CREB bind cooperatively to the nuclear coactivator CREB-binding protein". Mol. Cell. Biol. (United States) 21 (7): 2249–58. doi:10.1128/MCB.21.7.2249-2258.2001. ISSN 0270-7306. PMID 11259575.  
  14. ^ Ledo, Fran; Kremer Leonor, Mellström Britt, Naranjo Jose R (Sep. 2002). "Ca2+-dependent block of CREB-CBP transcription by repressor DREAM". EMBO J. (England) 21 (17): 4583–92. ISSN 0261-4189. PMID 12198160.  
  15. ^ a b c Fimia, G M; De Cesare D, Sassone-Corsi P (Nov. 2000). "A family of LIM-only transcriptional coactivators: tissue-specific expression and selective activation of CREB and CREM". Mol. Cell. Biol. (UNITED STATES) 20 (22): 8613–22. ISSN 0270-7306. PMID 11046156.  
  16. ^ Chen, Yongchang; Zhuang Shunhui, Cassenaer Stijn, Casteel Darren E, Gudi Tanima, Boss Gerry R, Pilz Renate B (Jun. 2003). "Synergism between calcium and cyclic GMP in cyclic AMP response element-dependent transcriptional regulation requires cooperation between CREB and C/EBP-beta". Mol. Cell. Biol. (United States) 23 (12): 4066–82. ISSN 0270-7306. PMID 12773552.  

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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