CREB1

CREB1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2LXT
Identifiers
Aliases	CREB1 , CREB, CREB-1, cAMP responsive element binding protein 1
External IDs	OMIM: 123810 MGI: 88494 HomoloGene: 3223 GeneCards: CREB1
Gene location (Human)
Chr.	Chromosome 2 (human)
End	207,605,988 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	64,604,548 bp
RNA expression pattern
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	• GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity ; • GO:0001077, GO:0001212, GO:0001213, GO:0001211, GO:0001205 DNA-binding transcription activator activity, RNA polymerase II-specific ; • cAMP response element binding ; • GO:0001104 transcription coregulator activity ; • GO:0000980 RNA polymerase II cis-regulatory region sequence-specific DNA binding ; • enzyme binding ; • GO:0001948 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 ; • GO:0001200, GO:0001133, GO:0001201 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 ; • GO:0022415 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 ; • aging ; • 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 ; • response to drug ; • 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
	1385
	12912
	ENSG00000118260
	ENSMUSG00000025958
	P16220
	Q01147
NM_004379 ; NM_134442 ; NM_001320793 ; NM_001371426 ; NM_001371427 ;
	NM_001371428
	NM_001037726 ; NM_009952 ; NM_133828
NP_001307722 ; NP_004370 ; NP_604391 ; NP_001358355 ; NP_001358356 ;
	NP_001358357
	NP_001032815 ; NP_034082 ; NP_598589
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated August 23, 2021

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]

Interactions

CREB1 has been shown to interact with:

CEBPB,^[8]
CREB binding protein,^[9]^[10]^[11]^[12]^[13]^[14]^[15]^[16]^[17]^[18]
FHL2,^[19]
FHL3,^[19]
FHL5.^[19]
HTATIP,^[20]
P53,^[15] and
RPS6KA5.^[21]^[22]

Related Research Articles

CREB-TF is a cellular transcription factor. It binds to certain DNA sequences called cAMP response elements (CRE), thereby increasing or decreasing the transcription of the genes. CREB was first described in 1987 as a cAMP-responsive transcription factor regulating the somatostatin gene.

CREB-binding protein, also known as CREBBP or CBP, is a protein that in humans is encoded by the CREBBP gene. The CREB protein carries out its function by activating transcription, where interaction with transcription factors is managed by one or more CREB domains: the nuclear receptor interaction domain (RID), the KIX domain, the cysteine/histidine regions and the interferon response binding domain (IBiD). The CREB protein domains, KIX, TAZ1 and TAZ2, each bind tightly to a sequence spanning both transactivation domains 9aaTADs of transcription factor p53.

The nuclear receptor coactivator 1 (NCOA1) is a transcriptional coregulatory protein that contains several nuclear receptor interacting domains and an intrinsic histone acetyltransferase activity. NCOA1 is recruited to DNA promotion sites by ligand-activated nuclear receptors. NCOA1, in turn, acylates histones, which makes downstream DNA more accessible to transcription. Hence, NCOA1 assists nuclear receptors in the upregulation of DNA expression.

Transcription factor p65 also known as nuclear factor NF-kappa-B p65 subunit is a protein that in humans is encoded by the RELA gene.

Myocyte-specific enhancer factor 2C also known as MADS box transcription enhancer factor 2, polypeptide C is a protein that in humans is encoded by the MEF2C gene. MEF2C is a transcription factor in the Mef2 family.

Cyclic AMP-dependent transcription factor ATF-1 is a protein that in humans is encoded by the ATF1 gene.

Activating transcription factor 4 , also known as ATF4, is a protein that in humans is encoded by the ATF4 gene.

GA-binding protein alpha chain is a protein that in humans is encoded by the GABPA gene.

Ribosomal protein S6 kinase alpha-1 is an enzyme that in humans is encoded by the RPS6KA1 gene.

Activating transcription factor 2, also known as ATF2, is a protein that, in humans, is encoded by the ATF2 gene.

cAMP responsive element modulator is a protein that in humans is encoded by the CREM gene, and it belongs to the cAMP-responsive element binding protein family. It has multiple isoforms, which act either as repressors or activators. CREB family is important for in regulating transcription in response to various stresses, metabolic and developmental signals. CREM transcription factors also play an important role in many physiological systems, such as cardiac function, circadian rhythms, locomotion and spermatogenesis.

General transcription factor II-I is a protein that in humans is encoded by the GTF2I gene.

Cell division protein kinase 8 is an enzyme that in humans is encoded by the CDK8 gene.

CREB-regulated transcription coactivator 1 (CRTC1), previously referred to as TORC1, is a protein that in humans is encoded by the CRTC1 gene. It is expressed in a limited number of tissues that include fetal brain and liver and adult heart, skeletal muscles, liver and salivary glands and various regions of the adult central nervous system.

RISC-loading complex subunit TARBP2 is a protein that in humans is encoded by the TARBP2 gene.

Cyclic AMP-responsive element-binding protein 3 is a protein that in humans is encoded by the CREB3 gene.

CAMP responsive element binding protein-like 1, also known as CREBL1, is a protein which in humans is encoded by the CREBL1 gene.

CREB regulated transcription coactivator 2, also known as CRTC2, is a protein which in humans is encoded by the CRTC2 gene.

Transcription factor MafK is a bZip Maf transcription factor protein that in humans is encoded by the MAFK gene.

The transactivation domain or trans-activating domain (TAD) is a transcription factor scaffold domain which contains binding sites for other proteins such as transcription coregulators. These binding sites are frequently referred to as activation functions (AFs). TADs are named after their amino acid composition. These amino acids are either essential for the activity or simply the most abundant in the TAD. Transactivation by the Gal4 transcription factor is mediated by acidic amino acids, whereas hydrophobic residues in Gcn4 play a similar role. Hence, the TADs in Gal4 and Gcn4 are referred to as acidic or hydrophobic, respectively.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000118260 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025958 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
↑ 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.
↑ "Entrez Gene: CREB1 cAMP responsive element binding protein 1".
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
1 2 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.
↑ 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.
↑ 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.
↑ 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.
1 2 3 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.
↑ 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.
↑ 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.
↑ 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.

External links

CREB1+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
Human CREB1 genome location and CREB1 gene details page in the UCSC Genome Browser .

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

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000118260 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid2974179-5] 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.

[pmid2142119-6] 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".

[pmid12773552-8] 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.

[pmid15073328-9] 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.

[pmid15691881-10] 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.

[pmid8663317-11] 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.

[pmid9413984-12] 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.

[pmid9786917-13] 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.

[pmid12196545-14] 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.

[pmid10848610-15] 1 2 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.

[pmid10866654-16] 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.

[pmid11259575-17] 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.

[pmid12198160-18] 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.

[pmid11046156-19] 1 2 3 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.

[pmid10720489-20] 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.

[pmid9687510-21] 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.

[pmid-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.

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CREB1

Contents

See also

Interactions

Related Research Articles

References

Further reading

External links