PSMB5

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Proteasome (prosome, macropain) subunit, beta type, 5
File:PBB Protein PSMB5 image.jpg
PDB rendering based on 1iru.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols PSMB5 ; X; LMPX; MB1; MGC104214
External IDs Template:OMIM5 Template:MGI HomoloGene55690
RNA expression pattern
File:PBB GE PSMB5 208799 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) subunit, beta type, 5, also known as PSMB5, is a human gene.[1]

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure 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. 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 member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit in the proteasome. This catalytic subunit is not present in the immunoproteasome and is replaced by catalytic subunit 3i (proteasome beta 8 subunit).[1]

References

  1. 1.0 1.1 "Entrez Gene: PSMB5 proteasome (prosome, macropain) subunit, beta type, 5".

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.
  • Lee LW, Moomaw CR, Orth K; et al. (1990). "Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome)". Biochim. Biophys. Acta. 1037 (2): 178–85. PMID 2306472.
  • Kristensen P, Johnsen AH, Uerkvitz W; et al. (1995). "Human proteasome subunits from 2-dimensional gels identified by partial sequencing". Biochem. Biophys. Res. Commun. 205 (3): 1785–9. PMID 7811265.
  • Belich MP, Glynne RJ, Senger G; et al. (1995). "Proteasome components with reciprocal expression to that of the MHC-encoded LMP proteins". Curr. Biol. 4 (9): 769–76. PMID 7820546.
  • Kristensen P, Johnsen AH, Uerkvitz W; et al. (1995). "Human proteasome subunits from 2-dimensional gels identified by partial sequencing". Biochem. Biophys. Res. Commun. 207 (3): 1059. PMID 7864893.
  • Akiyama K, Yokota K, Kagawa S; et al. (1994). "cDNA cloning and interferon gamma down-regulation of proteasomal subunits X and Y.". Science. 265 (5176): 1231–4. PMID 8066462.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
  • Abdulla S, Beck S, Belich M; et al. (1996). "Divergent intron arrangement in the MB1/LMP7 proteasome gene pair". Immunogenetics. 44 (4): 254–8. PMID 8753855.
  • 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.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149.
  • Kohda K, Matsuda Y, Ishibashi T; et al. (1998). "Structural analysis and chromosomal localization of the mouse Psmb5 gene coding for the constitutively expressed beta-type proteasome subunit". Immunogenetics. 47 (1): 77–87. PMID 9382924.
  • 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.
  • Elenich LA, Nandi D, Kent AE; et al. (1999). "The complete primary structure of mouse 20S proteasomes". Immunogenetics. 49 (10): 835–42. PMID 10436176.
  • Rodriguez-Vilariño S, Arribas J, Arizti P, Castaño JG (2000). "Proteolytic processing and assembly of the C5 subunit into the proteasome complex". J. Biol. Chem. 275 (9): 6592–9. PMID 10692467.
  • 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.
  • Feng Y, Longo DL, Ferris DK (2001). "Polo-like kinase interacts with proteasomes and regulates their activity". Cell Growth Differ. 12 (1): 29–37. PMID 11205743.
  • 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.

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