PSMD7

From Wikipedia, the free encyclopedia


Proteasome (prosome, macropain) 26S subunit, non-ATPase, 7 (Mov34 homolog)
Identifiers
Symbol(s) PSMD7; S12; P40; MOV34
External IDs OMIM: 157970 MGI1351511 HomoloGene2104
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 5713 17463
Ensembl ENSG00000103035 ENSMUSG00000039067
Uniprot P51665 P26516
Refseq NM_002811 (mRNA)
NP_002802 (protein)
NM_010817 (mRNA)
NP_034947 (protein)
Location Chr 16: 72.89 - 72.9 Mb Chr 8: 110.47 - 110.48 Mb
Pubmed search [1] [2]

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]

[edit] References

[edit] 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.