COPS6

COP9 signalosome complex subunit 6 is a protein that in humans is encoded by the COPS6 gene.^[5]

COPS6
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4D10, 4D18, 4QFT, 4R14, 4WSN
Identifiers
Aliases	COPS6, CSN6, MOV34-34KD, COP9 signalosome subunit 6
External IDs	OMIM: 614729; MGI: 1349439; HomoloGene: 4977; GeneCards: COPS6; OMA:COPS6 - orthologs
Gene location (Human) Chr. Chromosome 7 (human)[1] Band 7q22.1 Start 100,088,969 bp[1] End 100,092,187 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5|5 G2 Start 138,159,333 bp[2] End 138,162,908 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium apex of heart muscle of thigh right frontal lobe anterior pituitary muscle layer of sigmoid colon body of uterus nucleus accumbens right hemisphere of cerebellum ectocervix Top expressed in medial ganglionic eminence right kidney interventricular septum efferent ductule lens abdominal wall epithelium of lens endothelial cell of lymphatic vessel yolk sac neural tube More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding Cellular component cytoplasm COP9 signalosome nucleus nucleoplasm cytosol Biological process transcription-coupled nucleotide-excision repair viral process nucleotide-excision repair, DNA damage recognition protein deneddylation post-translational protein modification Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10980 26893 Ensembl ENSG00000168090 ENSMUSG00000019494 UniProt Q7L5N1 O88545 RefSeq (mRNA) NM_006833 NM_012002 RefSeq (protein) NP_006824 NP_036132 Location (UCSC) Chr 7: 100.09 – 100.09 Mb Chr 5: 138.16 – 138.16 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Function

The protein encoded by this gene is one of the eight subunits of COP9 signalosome, a highly conserved protein complex that functions as an important regulator in multiple signaling pathways. The structure and function of COP9 signalosome is similar to that of the 19S regulatory particle of 26S proteasome. COP9 signalosome has been shown to interact with SCF-type E3 ubiquitin ligases and act as a positive regulator of E3 ubiquitin ligases. This protein belongs to translation initiation factor 3 (eIF3) superfamily. It is involved in the regulation of cell cycle and likely to be a cellular cofactor for HIV-1 accessory gene product Vpr.^[6]

Interactions

COPS6 has been shown to interact with EIF3S6.^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000168090 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000019494 – 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. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA (Dec 2002). "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.
6. "Entrez Gene: COPS6 COP9 constitutive photomorphogenic homolog subunit 6 (Arabidopsis)".
7. Hoareau Alves K, Bochard V, Réty S, Jalinot P (Sep 2002). "Association of the mammalian proto-oncoprotein Int-6 with the three protein complexes eIF3, COP9 signalosome and 26S proteasome". FEBS Lett. 527 (1–3): 15–21. doi:10.1016/S0014-5793(02)03147-2. PMID 12220626. S2CID 39308598.

Further reading

• Wolf DA, Zhou C, Wee S (2004). "The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases?". Nat. Cell Biol. 5 (12): 1029–33. doi:10.1038/ncb1203-1029. PMID 14647295. S2CID 37458780.
• Muthumani K, Choo AY, Premkumar A, Hwang DS, Thieu KP, Desai BM, Weiner DB (2006). "Human immunodeficiency virus type 1 (HIV-1) Vpr-regulated cell death: insights into mechanism". Cell Death Differ. 12 (Suppl 1): 962–70. doi:10.1038/sj.cdd.4401583. PMID 15832179.
• Mittmeyer HJ (1976). "[Distribution pattern of rigor mortis in various joint regions]". Beitr. Gerichtl. Med. 33: 85–96. PMID 1222062.
• He J, Choe S, Walker R, Di Marzio P, Morgan DO, Landau NR (1995). "Human immunodeficiency virus type 1 viral protein R (Vpr) arrests cells in the G2 phase of the cell cycle by inhibiting p34cdc2 activity". J. Virol. 69 (11): 6705–11. doi:10.1128/JVI.69.11.6705-6711.1995. PMC 189580. PMID 7474080.
• Re F, Braaten D, Franke EK, Luban J (1995). "Human immunodeficiency virus type 1 Vpr arrests the cell cycle in G2 by inhibiting the activation of p34cdc2-cyclin B". J. Virol. 69 (11): 6859–64. doi:10.1128/JVI.69.11.6859-6864.1995. PMC 189600. PMID 7474100.
• Di Marzio P, Choe S, Ebright M, Knoblauch R, Landau NR (1996). "Mutational analysis of cell cycle arrest, nuclear localization and virion packaging of human immunodeficiency virus type 1 Vpr". J. Virol. 69 (12): 7909–16. doi:10.1128/JVI.69.12.7909-7916.1995. PMC 189735. PMID 7494303.
• Jowett JB, Planelles V, Poon B, Shah NP, Chen ML, Chen IS (1995). "The human immunodeficiency virus type 1 vpr gene arrests infected T cells in the G2 + M phase of the cell cycle". J. Virol. 69 (10): 6304–13. doi:10.1128/JVI.69.10.6304-6313.1995. PMC 189529. PMID 7666531.
• Zhao LJ, Mukherjee S, Narayan O (1994). "Biochemical mechanism of HIV-I Vpr function. Specific interaction with a cellular protein". J. Biol. Chem. 269 (22): 15577–82. doi:10.1016/S0021-9258(17)40719-8. PMID 8195203.
• Poon B, Jowett JB, Stewart SA, Armstrong RW, Rishton GM, Chen IS (1997). "Human immunodeficiency virus type 1 vpr gene induces phenotypic effects similar to those of the DNA alkylating agent, nitrogen mustard". J. Virol. 71 (5): 3961–71. doi:10.1128/JVI.71.5.3961-3971.1997. PMC 191548. PMID 9094673.
• Asano K, Vornlocher HP, Richter-Cook NJ, Merrick WC, Hinnebusch AG, Hershey JW (1997). "Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly". J. Biol. Chem. 272 (43): 27042–52. doi:10.1074/jbc.272.43.27042. PMID 9341143.
• Mahalingam S, Ayyavoo V, Patel M, Kieber-Emmons T, Kao GD, Muschel RJ, Weiner DB (1998). "HIV-1 Vpr interacts with a human 34-kDa mov34 homologue, a cellular factor linked to the G2/M phase transition of the mammalian cell cycle". Proc. Natl. Acad. Sci. U.S.A. 95 (7): 3419–24. Bibcode:1998PNAS...95.3419M. doi:10.1073/pnas.95.7.3419. PMC 19851. PMID 9520381.
• Seeger M, Kraft R, Ferrell K, Bech-Otschir D, Dumdey R, Schade R, Gordon C, Naumann M, Dubiel W (1998). "A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits". FASEB J. 12 (6): 469–78. doi:10.1096/fasebj.12.6.469. PMID 9535219. S2CID 25424324.
• Wei N, Tsuge T, Serino G, Dohmae N, Takio K, Matsui M, Deng XW (1998). "The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex". Curr. Biol. 8 (16): 919–22. Bibcode:1998CBio....8..919W. doi:10.1016/S0960-9822(07)00372-7. PMID 9707402. S2CID 13873982.
• Elder RT, Yu M, Chen M, Edelson S, Zhao Y (2000). "Cell cycle G2 arrest induced by HIV-1 Vpr in fission yeast (Schizosaccharomyces pombe) is independent of cell death and early genes in the DNA damage checkpoint". Virus Res. 68 (2): 161–73. doi:10.1016/S0168-1702(00)00167-2. PMID 10958988.
• Ramanathan MP, Ayyavoo V, Weiner DB (2001). "Choice of expression vector alters the localization of a human cellular protein". DNA Cell Biol. 20 (2): 101–5. doi:10.1089/104454901750070300. PMID 11244567.
• Bech-Otschir D, Kraft R, Huang X, Henklein P, Kapelari B, Pollmann C, Dubiel W (2001). "COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system". EMBO J. 20 (7): 1630–9. doi:10.1093/emboj/20.7.1630. PMC 145508. PMID 11285227.
• Lyapina S, Cope G, Shevchenko A, Serino G, Tsuge T, Zhou C, Wolf DA, Wei N, Shevchenko A, Deshaies RJ (2001). "Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome". Science. 292 (5520): 1382–5. Bibcode:2001Sci...292.1382L. doi:10.1126/science.1059780. PMID 11337588. S2CID 14224920.
• Elder RT, Yu M, Chen M, Zhu X, Yanagida M, Zhao Y (2001). "HIV-1 Vpr induces cell cycle G2 arrest in fission yeast (Schizosaccharomyces pombe) through a pathway involving regulatory and catalytic subunits of PP2A and acting on both Wee1 and Cdc25". Virology. 287 (2): 359–70. doi:10.1006/viro.2001.1007. PMID 11531413.
• Hrimech M, Yao XJ, Branton PE, Cohen EA (2002). "Retraction". EMBO J. 21 (14): 3918. doi:10.1093/emboj/cdf420. PMC 126131. PMID 12110603.

External links

• Human COPS6 genome location and COPS6 gene details page in the UCSC Genome Browser.