COP9 constitutive photomorphogenic homolog subunit 5

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COP9 signalosome subunit 5
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols COPS5 ; CSN5; JAB1; MOV-34; SGN5
External IDs OMIM604850 MGI1349415 HomoloGene55992 GeneCards: COPS5 Gene
RNA expression pattern
PBB GE COPS5 201652 at tn.png
PBB GE COPS5 gnf1h08492 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 10987 26754
Ensembl ENSG00000121022 ENSMUSG00000025917
UniProt Q92905 O35864
RefSeq (mRNA) NM_006837 NM_001277101
RefSeq (protein) NP_006828 NP_001264030
Location (UCSC) Chr 8:
67.96 – 68 Mb
Chr 1:
10.02 – 10.04 Mb
PubMed search [1] [2]

COP9 constitutive photomorphogenic homolog subunit 5 (Arabidopsis), also known as COPS5 or Csn5, is a gene conserved from humans to Saccharomyces cerevisiae.[1]

Function[edit]

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 is reported to be involved in the degradation of cyclin-dependent kinase inhibitor CDKN1B/p27Kip1. It is also known to be a coactivator that increases the specificity of JUN/AP1 transcription factors.[1]

Interactions[edit]

COP9 constitutive photomorphogenic homolog subunit 5 has been shown to interact with Macrophage migration inhibitory factor,[2] GFER,[3] BCL3,[4] Ubiquitin carboxy-terminal hydrolase L1,[5] S100A7[6] and C-jun.[7]

See also[edit]

References[edit]

  1. ^ a b "Entrez Gene: COPS5 COP9 constitutive photomorphogenic homolog subunit 5 (Arabidopsis)". 
  2. ^ Kleemann R, Hausser A, Geiger G, Mischke R, Burger-Kentischer A, Flieger O et al. (November 2000). "Intracellular action of the cytokine MIF to modulate AP-1 activity and the cell cycle through Jab1". Nature 408 (6809): 211–6. doi:10.1038/35041591. PMID 11089976. 
  3. ^ Lu C, Li Y, Zhao Y, Xing G, Tang F, Wang Q et al. (January 2002). "Intracrine hepatopoietin potentiates AP-1 activity through JAB1 independent of MAPK pathway". FASEB J. 16 (1): 90–2. doi:10.1096/fj.01-0506fje. PMID 11709497. 
  4. ^ Dechend R, Hirano F, Lehmann K, Heissmeyer V, Ansieau S, Wulczyn FG et al. (June 1999). "The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators". Oncogene 18 (22): 3316–23. doi:10.1038/sj.onc.1202717. PMID 10362352. 
  5. ^ Caballero OL, Resto V, Patturajan M, Meerzaman D, Guo MZ, Engles J et al. (May 2002). "Interaction and colocalization of PGP9.5 with JAB1 and p27(Kip1)". Oncogene 21 (19): 3003–10. doi:10.1038/sj.onc.1205390. PMID 12082530. 
  6. ^ Emberley ED, Niu Y, Leygue E, Tomes L, Gietz RD, Murphy LC et al. (April 2003). "Psoriasin interacts with Jab1 and influences breast cancer progression". Cancer Res. 63 (8): 1954–61. PMID 12702588. 
  7. ^ Claret FX, Hibi M, Dhut S, Toda T, Karin M (October 1996). "A new group of conserved coactivators that increase the specificity of AP-1 transcription factors". Nature 383 (6599): 453–7. doi:10.1038/383453a0. PMID 8837781. 

Further reading[edit]

  • Wolf DA, Zhou C, Wee S (2003). "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. 
  • Claret FX, Hibi M, Dhut S, Toda T, Karin M (1996). "A new group of conserved coactivators that increase the specificity of AP-1 transcription factors". Nature 383 (6599): 453–7. doi:10.1038/383453a0. PMID 8837781. 
  • 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. 
  • Seeger M, Kraft R, Ferrell K, Bech-Otschir D, Dumdey R, Schade R et al. (1998). "A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits". FASEB J. 12 (6): 469–78. PMID 9535219. 
  • Wei N, Tsuge T, Serino G, Dohmae N, Takio K, Matsui M et al. (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. doi:10.1016/S0960-9822(07)00372-7. PMID 9707402. 
  • Tomoda K, Kubota Y, Kato J (1999). "Degradation of the cyclin-dependent-kinase inhibitor p27Kip1 is instigated by Jab1". Nature 398 (6723): 160–5. doi:10.1038/18230. PMID 10086358. 
  • Dechend R, Hirano F, Lehmann K, Heissmeyer V, Ansieau S, Wulczyn FG et al. (1999). "The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators". Oncogene 18 (22): 3316–23. doi:10.1038/sj.onc.1202717. PMID 10362352. 
  • Chauchereau A, Georgiakaki M, Perrin-Wolff M, Milgrom E, Loosfelt H (2000). "JAB1 interacts with both the progesterone receptor and SRC-1". J. Biol. Chem. 275 (12): 8540–8. doi:10.1074/jbc.275.12.8540. PMID 10722692. 
  • Bianchi E, Denti S, Granata A, Bossi G, Geginat J, Villa A et al. (2000). "Integrin LFA-1 interacts with the transcriptional co-activator JAB1 to modulate AP-1 activity". Nature 404 (6778): 617–21. doi:10.1038/35007098. PMID 10766246. 
  • Kleemann R, Hausser A, Geiger G, Mischke R, Burger-Kentischer A, Flieger O et al. (2000). "Intracellular action of the cytokine MIF to modulate AP-1 activity and the cell cycle through Jab1". Nature 408 (6809): 211–6. doi:10.1038/35041591. PMID 11089976. 
  • Bech-Otschir D, Kraft R, Huang X, Henklein P, Kapelari B, Pollmann C et al. (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 et al. (2001). "Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome". Science 292 (5520): 1382–5. doi:10.1126/science.1059780. PMID 11337588. 
  • Tomoda K, Kubota Y, Arata Y, Mori S, Maeda M, Tanaka T et al. (2002). "The cytoplasmic shuttling and subsequent degradation of p27Kip1 mediated by Jab1/CSN5 and the COP9 signalosome complex". J. Biol. Chem. 277 (3): 2302–10. doi:10.1074/jbc.M104431200. PMID 11704659. 
  • Bae MK, Ahn MY, Jeong JW, Bae MH, Lee YM, Bae SK et al. (2002). "Jab1 interacts directly with HIF-1alpha and regulates its stability". J. Biol. Chem. 277 (1): 9–12. doi:10.1074/jbc.C100442200. PMID 11707426. 
  • Lu C, Li Y, Zhao Y, Xing G, Tang F, Wang Q et al. (2002). "Intracrine hepatopoietin potentiates AP-1 activity through JAB1 independent of MAPK pathway". FASEB J. 16 (1): 90–2. doi:10.1096/fj.01-0506fje. PMID 11709497. 
  • Dai YS, Cserjesi P (2002). "The basic helix-loop-helix factor, HAND2, functions as a transcriptional activator by binding to E-boxes as a heterodimer". J. Biol. Chem. 277 (15): 12604–12. doi:10.1074/jbc.M200283200. PMID 11812799. 
  • Wan M, Cao X, Wu Y, Bai S, Wu L, Shi X et al. (2002). "Jab1 antagonizes TGF-beta signaling by inducing Smad4 degradation". EMBO Rep. 3 (2): 171–6. doi:10.1093/embo-reports/kvf024. PMC 1083965. PMID 11818334. 
  • Gemmill RM, Bemis LT, Lee JP, Sozen MA, Baron A, Zeng C et al. (2002). "The TRC8 hereditary kidney cancer gene suppresses growth and functions with VHL in a common pathway". Oncogene 21 (22): 3507–16. doi:10.1038/sj.onc.1205437. PMID 12032852. 
  • Caballero OL, Resto V, Patturajan M, Meerzaman D, Guo MZ, Engles J et al. (2002). "Interaction and colocalization of PGP9.5 with JAB1 and p27(Kip1)". Oncogene 21 (19): 3003–10. doi:10.1038/sj.onc.1205390. PMID 12082530. 
  • Chopra S, Fernandez De Mattos S, Lam EW, Mann DJ (2002). "Jab1 co-activation of c-Jun is abrogated by the serine 10-phosphorylated form of p27Kip1". J. Biol. Chem. 277 (36): 32413–6. doi:10.1074/jbc.C200311200. PMID 12119282.