PSMA2

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Proteasome (prosome, macropain) subunit, alpha type, 2
File:PBB Protein PSMA2 image.jpg
PDB rendering based on 1iru.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols PSMA2 ; MU; HC3; PMSA2; PSC2
External IDs Template:OMIM5 Template:MGI HomoloGene: 2081
RNA expression pattern
File:PBB GE PSMA2 201317 s at tn.png
File:PBB GE PSMA2 201316 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, alpha type, 2, also known as PSMA2, 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 peptidase T1A family, that is a 20S core alpha subunit.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: PSMA2 proteasome (prosome, macropain) subunit, alpha type, 2".

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.
  • DeMartino GN, Orth K, McCullough ML; et al. (1991). "The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous". Biochim. Biophys. Acta. 1079 (1): 29–38. PMID 1888762.
  • Tamura T, Lee DH, Osaka F; et al. (1991). "Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes)". Biochim. Biophys. Acta. 1089 (1): 95–102. PMID 2025653.
  • Okumura K, Nogami M, Taguchi H; et al. (1995). "The genes for the alpha-type HC3 (PMSA2) and beta-type HC5 (PMSB1) subunits of human proteasomes map to chromosomes 6q27 and 7p12-p13 by fluorescence in situ hybridization". Genomics. 27 (2): 377–9. doi:10.1006/geno.1995.1062. PMID 7558012.
  • 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.
  • Tamura T, Osaka F, Kawamura Y; et al. (1994). "Isolation and characterization of alpha-type HC3 and beta-type HC5 subunit genes of human proteasomes". J. Mol. Biol. 244 (1): 117–24. doi:10.1006/jmbi.1994.1710. PMID 7966316.
  • 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.
  • Knuehl C, Seelig A, Brecht B; et al. (1996). "Functional analysis of eukaryotic 20S proteasome nuclear localization signal". Exp. Cell Res. 225 (1): 67–74. doi:10.1006/excr.1996.0157. PMID 8635518.
  • 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.
  • 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.
  • Kleijnen MF, Shih AH, Zhou P; et al. (2000). "The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome". Mol. Cell. 6 (2): 409–19. PMID 10983987.
  • 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.
  • Bommel H, Xie G, Rossoll W; et al. (2003). "Missense mutation in the tubulin-specific chaperone E (Tbce) gene in the mouse mutant progressive motor neuronopathy, a model of human motoneuron disease". J. Cell Biol. 159 (4): 563–9. doi:10.1083/jcb.200208001. PMID 12446740.

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