PSMB7

From Wikipedia, the free encyclopedia


Proteasome (prosome, macropain) subunit, beta type, 7
PDB rendering based on 1iru.
Available structures: 1iru
Identifiers
Symbol(s) PSMB7; Z
External IDs OMIM: 604030 MGI107637 HomoloGene2093
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 5695 19177
Ensembl ENSG00000136930 ENSMUSG00000026750
Uniprot Q99436 Q5D098
Refseq NM_002799 (mRNA)
NP_002790 (protein)
NM_011187 (mRNA)
NP_035317 (protein)
Location Chr 9: 126.16 - 126.22 Mb Chr 2: 38.41 - 38.47 Mb
Pubmed search [1] [2]

Proteasome (prosome, macropain) subunit, beta type, 7, also known as PSMB7, 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. Expression of this catalytic subunit is downregulated by gamma interferon and proteolytic processing is required to generate a mature subunit. This subunit is not present in the immunoproteasome and is replaced by catalytic subunit 2i (proteasome beta 10 subunit).[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. 
  • Rivett AJ, Bose S, Brooks P, Broadfoot KI (2001). "Regulation of proteasome complexes by gamma-interferon and phosphorylation.". Biochimie 83 (3-4): 363-6. PMID 11295498. 
  • Goff SP (2003). "Death by deamination: a novel host restriction system for HIV-1.". Cell 114 (3): 281-3. PMID 12914693. 
  • 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. 
  • 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. 
  • Hisamatsu H, Shimbara N, Saito Y, et al. (1996). "Newly identified pair of proteasomal subunits regulated reciprocally by interferon gamma.". J. Exp. Med. 183 (4): 1807-16. PMID 8666937. 
  • 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. 
  • 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. 
  • O'Hare T, Wiens GD, Whitcomb EA, et al. (1999). "Cutting edge: proteasome involvement in the degradation of unassembled Ig light chains.". J. Immunol. 163 (1): 11-4. PMID 10384092. 
  • Elenich LA, Nandi D, Kent AE, et al. (1999). "The complete primary structure of mouse 20S proteasomes.". Immunogenetics 49 (10): 835-42. PMID 10436176. 
  • 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. 
  • 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.