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CREB3
Identifiers
Aliases	CREB3, LUMAN, LZIP, sLZIP, cAMP responsive element binding protein 3
External IDs	OMIM: 606443; MGI: 99946; HomoloGene: 31375; GeneCards: CREB3; OMA:CREB3 - orthologs
Gene location (Human) Chr. Chromosome 9 (human) Band 9p13.3 Start 35,732,598 bp End 35,736,999 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4 A5|4 23.05 cM Start 43,562,332 bp End 43,567,060 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in anterior pituitary right testis popliteal artery tibial arteries ascending aorta left testis Descending thoracic aorta right adrenal gland left adrenal gland left adrenal cortex Top expressed in ascending aorta aortic valve Paneth cell Epithelium of choroid plexus supraoptic nucleus calvaria substantia nigra endothelial cell of lymphatic vessel Pituitary Gland facial motor nucleus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA binding RNA polymerase II transcription regulatory region sequence-specific DNA binding protein homodimerization activity protein dimerization activity cAMP response element binding protein binding DNA-binding transcription factor activity CCR1 chemokine receptor binding DNA-binding transcription activator activity, RNA polymerase II-specific chromatin binding RNA polymerase II cis-regulatory region sequence-specific DNA binding transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding protein binding cAMP response element binding DNA-binding transcription factor activity, RNA polymerase II-specific Cellular component cytoplasm integral component of membrane nuclear body endoplasmic reticulum membrane membrane integral component of endoplasmic reticulum membrane soma endoplasmic reticulum nucleus cytosol Golgi membrane nucleoplasm Golgi apparatus Biological process negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway regulation of transcription, DNA-templated release from viral latency positive regulation of cell migration cytoplasmic sequestering of transcription factor negative regulation of cell cycle positive regulation of monocyte chemotaxis transcription, DNA-templated response to endoplasmic reticulum stress induction of positive chemotaxis positive regulation of transcription, DNA-templated chemotaxis response to unfolded protein regulation of cell population proliferation regulation of cell growth establishment of viral latency positive regulation of deacetylase activity positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response viral process positive regulation of transcription by RNA polymerase II positive regulation of defense response to virus by host positive regulation of calcium ion transport transcription by RNA polymerase II endoplasmic reticulum unfolded protein response regulation of apoptotic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10488 12913 Ensembl ENSG00000107175 ENSMUSG00000028466 UniProt O43889 Q61817 RefSeq (mRNA) NM_006368 NM_013497 RefSeq (protein) NP_006359 n/a Location (UCSC) Chr 9: 35.73 – 35.74 Mb Chr 4: 43.56 – 43.57 Mb PubMed search
Wikidata
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Cyclic AMP-responsive element-binding protein 3 is a protein that in humans is encoded by the CREB3 gene.

This gene encodes a transcription factor that is a member of the leucine zipper family of DNA binding proteins. This protein binds to the cAMP-responsive element, an octameric palindrome. The protein interacts with host cell factor C1, which also associates with the herpes simplex virus (HSV) protein VP16 that induces transcription of HSV immediate-early genes. This protein and VP16 both bind to the same site on host cell factor C1. It is thought that the interaction between this protein and host cell factor C1 plays a role in the establishment of latency during HSV infection. An additional transcript variant has been identified, but its biological validity has not been determined.

Interactions

CREB3 has been shown to interact with Host cell factor C1.

See also

• CREB

References

1. ^ GRCh38: Ensembl release 89: ENSG00000107175 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000028466 – 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. Lu R, Yang P, O'Hare P, Misra V (Sep 1997). "Luman, a new member of the CREB/ATF family, binds to herpes simplex virus VP16-associated host cellular factor". Mol Cell Biol. 17 (9): 5117–26. doi:10.1128/MCB.17.9.5117. PMC 232362. PMID 9271389.
6. ^ "Entrez Gene: CREB3 cAMP responsive element binding protein 3".
7. Lu R, Yang P, Padmakumar S, Misra V (Aug 1998). "The herpesvirus transactivator VP16 mimics a human basic domain leucine zipper protein, luman, in its interaction with HCF". J. Virol. 72 (8): 6291–7. doi:10.1128/JVI.72.8.6291-6297.1998. ISSN 0022-538X. PMC 109766. PMID 9658067.
8. Freiman RN, Herr W (Dec 1997). "Viral mimicry: common mode of association with HCF by VP16 and the cellular protein LZIP". Genes Dev. 11 (23): 3122–7. doi:10.1101/gad.11.23.3122. ISSN 0890-9369. PMC 316754. PMID 9389645.

Further reading

• Freiman RN, Herr W (1998). "Viral mimicry: common mode of association with HCF by VP16 and the cellular protein LZIP". Genes Dev. 11 (23): 3122–7. doi:10.1101/gad.11.23.3122. PMC 316754. PMID 9389645.
• Lu R, Yang P, Padmakumar S, Misra V (1998). "The herpesvirus transactivator VP16 mimics a human basic domain leucine zipper protein, luman, in its interaction with HCF". J. Virol. 72 (8): 6291–7. doi:10.1128/JVI.72.8.6291-6297.1998. PMC 109766. PMID 9658067.
• Lu R, Misra V (2000). "Potential role for luman, the cellular homologue of herpes simplex virus VP16 (alpha gene trans-inducing factor), in herpesvirus latency". J. Virol. 74 (2): 934–43. doi:10.1128/JVI.74.2.934-943.2000. PMC 111614. PMID 10623756.
• Mahajan SS, Wilson AC (2000). "Mutations in host cell factor 1 separate its role in cell proliferation from recruitment of VP16 and LZIP". Mol. Cell. Biol. 20 (3): 919–28. doi:10.1128/MCB.20.3.919-928.2000. PMC 85209. PMID 10629049.
• Jin DY, Wang HL, Zhou Y, et al. (2000). "Hepatitis C virus core protein-induced loss of LZIP function correlates with cellular transformation". EMBO J. 19 (4): 729–40. doi:10.1093/emboj/19.4.729. PMC 305611. PMID 10675342.
• Luciano RL, Wilson AC (2000). "N-terminal transcriptional activation domain of LZIP comprises two LxxLL motifs and the host cell factor-1 binding motif". Proc. Natl. Acad. Sci. U.S.A. 97 (20): 10757–62. Bibcode:2000PNAS...9710757L. doi:10.1073/pnas.190062797. PMC 27096. PMID 10984507.
• Raggo C, Rapin N, Stirling J, et al. (2002). "Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis". Mol. Cell. Biol. 22 (16): 5639–49. doi:10.1128/MCB.22.16.5639-5649.2002. PMC 133973. PMID 12138176.
• Mahajan SS, Little MM, Vazquez R, Wilson AC (2003). "Interaction of HCF-1 with a cellular nuclear export factor". J. Biol. Chem. 277 (46): 44292–9. doi:10.1074/jbc.M205440200. PMC 4291127. PMID 12235138.
• Luciano RL, Wilson AC (2002). "An activation domain in the C-terminal subunit of HCF-1 is important for transactivation by VP16 and LZIP". Proc. Natl. Acad. Sci. U.S.A. 99 (21): 13403–8. Bibcode:2002PNAS...9913403L. doi:10.1073/pnas.202200399. PMC 129685. PMID 12271126.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Ko J, Jang SW, Kim YS, et al. (2004). "Human LZIP binds to CCR1 and differentially affects the chemotactic activities of CCR1-dependent chemokines". FASEB J. 18 (7): 890–2. doi:10.1096/fj.03-0867fje. PMID 15001559. S2CID 24742296.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Misra V, Rapin N, Akhova O, et al. (2005). "Zhangfei is a potent and specific inhibitor of the host cell factor-binding transcription factor Luman". J. Biol. Chem. 280 (15): 15257–66. doi:10.1074/jbc.M500728200. PMID 15705566.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Liang G, Audas TE, Li Y, et al. (2007). "Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element". Mol. Cell. Biol. 26 (21): 7999–8010. doi:10.1128/MCB.01046-06. PMC 1636730. PMID 16940180.
• Blot G, Lopez-Vergès S, Treand C, et al. (2007). "Luman, a new partner of HIV-1 TMgp41, interferes with Tat-mediated transcription of the HIV-1 LTR". J. Mol. Biol. 364 (5): 1034–47. doi:10.1016/j.jmb.2006.09.080. PMID 17054986.
• Jang SW, Kim YS, Lee YH, Ko J (2007). "Role of human LZIP in differential activation of the NF-kappaB pathway that is induced by CCR1-dependent chemokines". J. Cell. Physiol. 211 (3): 630–7. doi:10.1002/jcp.20968. PMID 17192849. S2CID 40274182.
• Jang SW, Kim YS, Kim YR, et al. (2007). "Regulation of human LZIP expression by NF-kappaB and its involvement in monocyte cell migration induced by Lkn-1". J. Biol. Chem. 282 (15): 11092–100. doi:10.1074/jbc.M607962200. PMID 17296613.

External links

• CREB3+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
• Human CREB3 genome location and CREB3 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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