PSMD5

From Wikipedia, the free encyclopedia


Proteasome (prosome, macropain) 26S subunit, non-ATPase, 5
Identifiers
Symbol(s) PSMD5; KIAA0072; MGC23145; S5B
External IDs OMIM: 604452 MGI: 1914248 HomoloGene: 37999
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 5711 66998
Ensembl ENSG00000095261 ENSMUSG00000026869
Uniprot Q16401 Q5DU49
Refseq NM_005047 (mRNA)
NP_005038 (protein)		 NM_080554 (mRNA)
NP_542121 (protein)
Location Chr 9: 122.62 - 122.65 Mb Chr 2: 34.67 - 34.69 Mb
Pubmed search [1] [2]

Proteasome (prosome, macropain) 26S subunit, non-ATPase, 5, also known as PSMD5, is a human gene.

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 base.[1]

[edit] References

  1. ^ Entrez Gene: PSMD5 proteasome (prosome, macropain) 26S subunit, non-ATPase, 5.

[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. 
  • Kanayama HO, Tamura T, Ugai S, et al. (1992). "Demonstration that a human 26S proteolytic complex consists of a proteasome and multiple associated protein components and hydrolyzes ATP and ubiquitin-ligated proteins by closely linked mechanisms.". Eur. J. Biochem. 206 (2): 567–78. PMID 1317798. 
  • Deveraux Q, Jensen C, Rechsteiner M (1995). "Molecular cloning and expression of a 26 S protease subunit enriched in dileucine repeats.". J. Biol. Chem. 270 (40): 23726–9. PMID 7559544. 
  • Nomura N, Nagase T, Miyajima N, et al. (1995). "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1.". DNA Res. 1 (5): 223–9. PMID 7584044. 
  • Deveraux Q, Ustrell V, Pickart C, Rechsteiner M (1994). "A 26 S protease subunit that binds ubiquitin conjugates.". J. Biol. Chem. 269 (10): 7059–61. PMID 8125911. 
  • 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. 
  • 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. 
  • Gorbea C, Taillandier D, Rechsteiner M (2000). "Mapping subunit contacts in the regulatory complex of the 26 S proteasome. S2 and S5b form a tetramer with ATPase subunits S4 and S7.". J. Biol. Chem. 275 (2): 875–82. PMID 10625621. 
  • 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. 
  • 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. 
  • Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. 
  • 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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