PSMD7

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Proteasome (prosome, macropain) 26S subunit, non-ATPase, 7 (Mov34 homolog)
Identifiers
Symbols PSMD7 ; S12; P40; MOV34
External IDs Template:OMIM5 Template:MGI HomoloGene: 2104
RNA expression pattern
File:PBB GE PSMD7 201705 at tn.png
File:PBB GE PSMD7 gnf1h06716 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Proteasome (prosome, macropain) 26S subunit, non-ATPase, 7 (Mov34 homolog), also known as PSMD7, is a human gene.[1]

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a non-ATPase subunit of the 19S regulator. A pseudogene has been identified on chromosome 17.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: PSMD7 proteasome (prosome, macropain) 26S subunit, non-ATPase, 7 (Mov34 homolog)".

Further reading

  • Coux O, Tanaka K, Goldberg AL (1996). "Structure and functions of the 20S and 26S proteasomes". Annu. Rev. Biochem. 65: 801–47. doi:10.1146/annurev.bi.65.070196.004101. PMID 8811196.
  • Goff SP (2003). "Death by deamination: a novel host restriction system for HIV-1". Cell. 114 (3): 281–3. PMID 12914693.
  • Gridley T, Gray DA, Orr-Weaver T; et al. (1990). "Molecular analysis of the Mov 34 mutation: transcript disrupted by proviral integration in mice is conserved in Drosophila". Development. 109 (1): 235–42. PMID 2209467.
  • Winkelmann DA, Kahan L (1983). "Immunochemical accessibility of ribosomal protein S4 in the 30 S ribosome. The interaction of S4 with S5 and S12". J. Mol. Biol. 165 (2): 357–74. PMID 6188845.
  • Tsurumi C, DeMartino GN, Slaughter CA; et al. (1995). "cDNA cloning of p40, a regulatory subunit of the human 26S proteasome, and a homolog of the Mov-34 gene product". Biochem. Biophys. Res. Commun. 210 (2): 600–8. doi:10.1006/bbrc.1995.1701. PMID 7755639.
  • Seeger M, Ferrell K, Frank R, Dubiel W (1997). "HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation". J. Biol. Chem. 272 (13): 8145–8. PMID 9079628.
  • Mahalingam S, Ayyavoo V, Patel M; et al. (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. PMID 9520381.
  • Madani N, Kabat D (1998). "An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein". J. Virol. 72 (12): 10251–5. PMID 9811770.
  • Simon JH, Gaddis NC, Fouchier RA, Malim MH (1998). "Evidence for a newly discovered cellular anti-HIV-1 phenotype". Nat. Med. 4 (12): 1397–400. doi:10.1038/3987. PMID 9846577.
  • Mulder LC, Muesing MA (2000). "Degradation of HIV-1 integrase by the N-end rule pathway". J. Biol. Chem. 275 (38): 29749–53. doi:10.1074/jbc.M004670200. PMID 10893419.
  • Sheehy AM, Gaddis NC, Choi JD, Malim MH (2002). "Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein". Nature. 418 (6898): 646–50. doi:10.1038/nature00939. PMID 12167863.
  • Ramanathan MP, Curley E, Su M; et al. (2003). "Carboxyl terminus of hVIP/mov34 is critical for HIV-1-Vpr interaction and glucocorticoid-mediated signaling". J. Biol. Chem. 277 (49): 47854–60. doi:10.1074/jbc.M203905200. PMID 12237292.
  • Thompson HG, Harris JW, Wold BJ; et al. (2003). "Identification and confirmation of a module of coexpressed genes". Genome Res. 12 (10): 1517–22. doi:10.1101/gr.418402. PMID 12368243.
  • Huang X, Seifert U, Salzmann U; et al. (2002). "The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing". J. Mol. Biol. 323 (4): 771–82. PMID 12419264.
  • 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. doi:10.1073/pnas.242603899. PMID 12477932.
  • Gaddis NC, Chertova E, Sheehy AM; et al. (2003). "Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions". J. Virol. 77 (10): 5810–20. PMID 12719574.
  • Lecossier D, Bouchonnet F, Clavel F, Hance AJ (2003). "Hypermutation of HIV-1 DNA in the absence of the Vif protein". Science. 300 (5622): 1112. doi:10.1126/science.1083338. PMID 12750511.
  • Zhang H, Yang B, Pomerantz RJ; et al. (2003). "The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA". Nature. 424 (6944): 94–8. doi:10.1038/nature01707. PMID 12808465.
  • Mangeat B, Turelli P, Caron G; et al. (2003). "Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts". Nature. 424 (6944): 99–103. doi:10.1038/nature01709. PMID 12808466.

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