CREB1

Mammalian protein found in Homo sapiens
CREB1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2LXT

Identifiers
AliasesCREB1, CREB, CREB-1, cAMP responsive element binding protein 1
External IDsOMIM: 123810 MGI: 88494 HomoloGene: 3223 GeneCards: CREB1
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for CREB1
Genomic location for CREB1
Band2q33.3Start207,529,737 bp[1]
End207,605,988 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for CREB1
Genomic location for CREB1
Band1 C2|1 32.74 cMStart64,571,804 bp[2]
End64,643,707 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • secondary oocyte

  • Achilles tendon

  • bone marrow cells

  • superficial temporal artery

  • trabecular bone

  • ganglionic eminence

  • thymus

  • parietal pleura

  • visceral pleura

  • islet of Langerhans
Top expressed in
  • medial ganglionic eminence

  • ciliary body

  • retinal pigment epithelium

  • pineal gland

  • conjunctival fornix

  • maxillary prominence

  • primitive streak

  • vas deferens

  • iris

  • left lung lobe
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
  • DNA-binding transcription factor activity
  • DNA-binding transcription activator activity, RNA polymerase II-specific
  • cAMP response element binding
  • transcription coregulator activity
  • RNA polymerase II cis-regulatory region sequence-specific DNA binding
  • enzyme binding
  • protein binding
  • double-stranded DNA binding
  • DNA binding
  • sequence-specific DNA binding
  • identical protein binding
  • transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding
  • DNA-binding transcription factor activity, RNA polymerase II-specific
  • transcription factor binding
  • Hsp70 protein binding
  • histone acetyltransferase binding
  • arrestin family protein binding
Cellular component
  • mitochondrion
  • nucleus
  • ATF4-CREB1 transcription factor complex
  • chromatin
  • transcription regulator complex
  • nucleoplasm
  • axon
  • mitochondrial matrix
Biological process
  • cellular response to nerve growth factor stimulus
  • positive regulation of lipid biosynthetic process
  • positive regulation of long-term synaptic potentiation
  • rhythmic process
  • cellular response to insulin-like growth factor stimulus
  • transcription by RNA polymerase II
  • response to organic substance
  • mammary gland development
  • protein phosphorylation
  • type I pneumocyte differentiation
  • circadian rhythm
  • positive regulation of multicellular organism growth
  • response to L-glutamate
  • lung saccule development
  • lung epithelium development
  • transforming growth factor beta receptor signaling pathway
  • regulation of apoptotic process
  • cellular response to transforming growth factor beta stimulus
  • response to glucagon
  • regulation of transcription, DNA-templated
  • negative regulation of transcription by competitive promoter binding
  • response to nicotine
  • positive regulation of osteoclast differentiation
  • memory
  • negative regulation of gene expression
  • transcription, DNA-templated
  • positive regulation of transcription, DNA-templated
  • lactation
  • positive regulation of transforming growth factor beta3 production
  • viral process
  • positive regulation of fat cell differentiation
  • negative regulation of neuron death
  • cell differentiation
  • cellular response to hepatocyte growth factor stimulus
  • protein stabilization
  • cellular response to platelet-derived growth factor stimulus
  • regulation of circadian rhythm
  • secretory granule organization
  • regulation of glial cell proliferation
  • visual learning
  • regulation of cell size
  • pituitary gland development
  • positive regulation of RNA polymerase II transcription preinitiation complex assembly
  • response to hypoxia
  • axonogenesis
  • regulation of fibroblast proliferation
  • cellular response to growth factor stimulus
  • human ageing
  • chemotaxis to arachidonic acid
  • response to activity
  • cellular response to zinc ion
  • cellular response to fatty acid
  • positive regulation of apoptotic process
  • positive regulation of hormone secretion
  • signal transduction
  • positive regulation of transcription by RNA polymerase II
  • positive regulation of cardiac muscle tissue development
  • cellular response to leukemia inhibitory factor
  • cellular response to retinoic acid
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

1385

12912

Ensembl

ENSG00000118260

ENSMUSG00000025958

UniProt

P16220

Q01147

RefSeq (mRNA)
NM_004379
NM_134442
NM_001320793
NM_001371426
NM_001371427

NM_001371428

NM_001037726
NM_009952
NM_133828

RefSeq (protein)
NP_001307722
NP_004370
NP_604391
NP_001358355
NP_001358356

NP_001358357

NP_001032815
NP_034082
NP_598589

Location (UCSC)Chr 2: 207.53 – 207.61 MbChr 1: 64.57 – 64.64 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

CAMP responsive element binding protein 1, also known as CREB-1, is a protein that in humans is encoded by the CREB1 gene.[5][6] 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 protein is 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.[7]

See also

Interactions

CREB1 has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000118260 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025958 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Hoeffler JP, Meyer TE, Yun Y, Jameson JL, Habener JF (Dec 1988). "Cyclic AMP-responsive DNA-binding protein: structure based on a cloned placental cDNA". Science. 242 (4884): 1430–3. Bibcode:1988Sci...242.1430H. doi:10.1126/science.2974179. PMID 2974179.
  6. ^ Taylor AK, Klisak I, Mohandas T, Sparkes RS, Li C, Gaynor R, Lusis AJ (Jul 1990). "Assignment of the human gene for CREB1 to chromosome 2q32.3-q34". Genomics. 7 (3): 416–21. doi:10.1016/0888-7543(90)90176-U. PMID 2142119.
  7. ^ "Entrez Gene: CREB1 cAMP responsive element binding protein 1".
  8. ^ Chen Y, Zhuang S, Cassenaer S, Casteel DE, Gudi T, Boss GR, Pilz RB (Jun 2003). "Synergism between calcium and cyclic GMP in cyclic AMP response element-dependent transcriptional regulation requires cooperation between CREB and C/EBP-beta". Molecular and Cellular Biology. 23 (12): 4066–82. doi:10.1128/MCB.23.12.4066-4082.2003. PMC 156132. PMID 12773552.
  9. ^ Shi Y, Venkataraman SL, Dodson GE, Mabb AM, LeBlanc S, Tibbetts RS (Apr 2004). "Direct regulation of CREB transcriptional activity by ATM in response to genotoxic stress". Proceedings of the National Academy of Sciences of the United States of America. 101 (16): 5898–903. Bibcode:2004PNAS..101.5898S. doi:10.1073/pnas.0307718101. PMC 395895. PMID 15073328.
  10. ^ Kim J, Jia L, Stallcup MR, Coetzee GA (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". Journal of Molecular Endocrinology. 34 (1): 107–18. doi:10.1677/jme.1.01701. PMID 15691881.
  11. ^ 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". The Journal of Biological Chemistry. 271 (30): 17957–60. doi:10.1074/jbc.271.30.17957. PMID 8663317.
  12. ^ Radhakrishnan I, Pérez-Alvarado GC, Parker D, Dyson HJ, Montminy MR, Wright PE (Dec 1997). "Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions". Cell. 91 (6): 741–52. doi:10.1016/S0092-8674(00)80463-8. PMID 9413984. S2CID 17268267.
  13. ^ Sano Y, Tokitou F, Dai P, Maekawa T, Yamamoto T, Ishii S (Oct 1998). "CBP alleviates the intramolecular inhibition of ATF-2 function". The Journal of Biological Chemistry. 273 (44): 29098–105. doi:10.1074/jbc.273.44.29098. PMID 9786917.
  14. ^ Zor T, Mayr BM, Dyson HJ, Montminy MR, Wright PE (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". The Journal of Biological Chemistry. 277 (44): 42241–8. doi:10.1074/jbc.M207361200. PMID 12196545.
  15. ^ a b Giebler HA, Lemasson I, Nyborg JK (Jul 2000). "p53 recruitment of CREB binding protein mediated through phosphorylated CREB: a novel pathway of tumor suppressor regulation". Molecular and Cellular Biology. 20 (13): 4849–58. doi:10.1128/MCB.20.13.4849-4858.2000. PMC 85936. PMID 10848610.
  16. ^ Zhang Q, Vo N, Goodman RH (Jul 2000). "Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB". Molecular and Cellular Biology. 20 (14): 4970–8. doi:10.1128/MCB.20.14.4970-4978.2000. PMC 85947. PMID 10866654.
  17. ^ Ernst P, Wang J, Huang M, Goodman RH, Korsmeyer SJ (Apr 2001). "MLL and CREB bind cooperatively to the nuclear coactivator CREB-binding protein". Molecular and Cellular Biology. 21 (7): 2249–58. doi:10.1128/MCB.21.7.2249-2258.2001. PMC 86859. PMID 11259575.
  18. ^ Ledo F, Kremer L, Mellström B, Naranjo JR (Sep 2002). "Ca2+-dependent block of CREB-CBP transcription by repressor DREAM". The EMBO Journal. 21 (17): 4583–92. doi:10.1093/emboj/cdf440. PMC 126180. PMID 12198160.
  19. ^ a b c Fimia GM, 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". Molecular and Cellular Biology. 20 (22): 8613–22. doi:10.1128/MCB.20.22.8613-8622.2000. PMC 102166. PMID 11046156.
  20. ^ Gavaravarapu S, Kamine J (Mar 2000). "Tip60 inhibits activation of CREB protein by protein kinase A". Biochemical and Biophysical Research Communications. 269 (3): 758–66. doi:10.1006/bbrc.2000.2358. PMID 10720489.
  21. ^ Deak M, Clifton AD, Lucocq LM, Alessi DR (Aug 1998). "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB". The EMBO Journal. 17 (15): 4426–41. doi:10.1093/emboj/17.15.4426. PMC 1170775. PMID 9687510.
  22. ^ Wang X, Li W, Williams M, Terada N, Alessi DR, Proud CG (Aug 2001). "Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase". The EMBO Journal. 20 (16): 4370–9. doi:10.1093/emboj/20.16.4370. PMC 125559. PMID 11500364.

Further reading

  • Don J, Stelzer G (Feb 2002). "The expanding family of CREB/CREM transcription factors that are involved with spermatogenesis". Molecular and Cellular Endocrinology. 187 (1–2): 115–24. doi:10.1016/S0303-7207(01)00696-7. PMID 11988318. S2CID 23023082.
  • Pandey SC (Oct 2004). "The gene transcription factor cyclic AMP-responsive element binding protein: role in positive and negative affective states of alcohol addiction". Pharmacology & Therapeutics. 104 (1): 47–58. doi:10.1016/j.pharmthera.2004.08.002. PMID 15500908.
  • Wu H, Zhou Y, Xiong ZQ (Jul 2007). "Transducer of regulated CREB and late phase long-term synaptic potentiation". The FEBS Journal. 274 (13): 3218–23. doi:10.1111/j.1742-4658.2007.05891.x. PMID 17565597. S2CID 15804067.
  • Kitagawa K (Jul 2007). "CREB and cAMP response element-mediated gene expression in the ischemic brain". The FEBS Journal. 274 (13): 3210–7. doi:10.1111/j.1742-4658.2007.05890.x. PMID 17565598. S2CID 29917569.
  • Takemori H, Kajimura J, Okamoto M (Jul 2007). "TORC-SIK cascade regulates CREB activity through the basic leucine zipper domain". The FEBS Journal. 274 (13): 3202–9. doi:10.1111/j.1742-4658.2007.05889.x. PMID 17565599. S2CID 30323449.
  • Siu YT, Jin DY (Jul 2007). "CREB--a real culprit in oncogenesis". The FEBS Journal. 274 (13): 3224–32. doi:10.1111/j.1742-4658.2007.05884.x. PMID 17565603. S2CID 39040147.

External links

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

  • v
  • t
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  • 1dh3: CRYSTAL STRUCTURE OF A CREB BZIP-CRE COMPLEX REVEALS THE BASIS FOR CREB FAIMLY SELECTIVE DIMERIZATION AND DNA BINDING
    1dh3: CRYSTAL STRUCTURE OF A CREB BZIP-CRE COMPLEX REVEALS THE BASIS FOR CREB FAIMLY SELECTIVE DIMERIZATION AND DNA BINDING
  • v
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  • e
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies
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