PSMA1

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Proteasome (prosome, macropain) subunit, alpha type, 1
File:PBB Protein PSMA1 image.jpg
PDB rendering based on 1iru.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols PSMA1 ; HC2; MGC14542; MGC14575; MGC14751; MGC1667; MGC21459; MGC22853; MGC23915; NU; PROS30
External IDs Template:OMIM5 Template:MGI HomoloGene2080
RNA expression pattern
File:PBB GE PSMA1 210759 s at tn.png
File:PBB GE PSMA1 201676 x at tn.png
File:PBB GE PSMA1 211746 x 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, 1, also known as PSMA1, 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. Two alternative transcripts encoding different isoforms have been identified.[1]

References

  1. 1.0 1.1 "Entrez Gene: PSMA1 proteasome (prosome, macropain) subunit, alpha type, 1".

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.
  • Silva Pereira I, Bey F, Coux O, Scherrer K (1992). "Two mRNAs exist for the Hs PROS-30 gene encoding a component of human prosomes". Gene. 120 (2): 235–42. PMID 1398136.
  • Shimbara N, Orino E, Sone S; et al. (1992). "Regulation of gene expression of proteasomes (multi-protease complexes) during growth and differentiation of human hematopoietic cells". J. Biol. Chem. 267 (25): 18100–9. PMID 1517242.
  • Kanayama H, Tanaka K, Aki M; et al. (1992). "Changes in expressions of proteasome and ubiquitin genes in human renal cancer cells". Cancer Res. 51 (24): 6677–85. PMID 1660345.
  • 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.
  • Bey F, Silva Pereira I, Coux O; et al. (1993). "The prosomal RNA-binding protein p27K is a member of the alpha-type human prosomal gene family". Mol. Gen. Genet. 237 (1–2): 193–205. PMID 7681138.
  • 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.
  • 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.
  • Gerards WL, de Jong WW, Bloemendal H, Boelens W (1998). "The human proteasomal subunit HsC8 induces ring formation of other alpha-type subunits". J. Mol. Biol. 275 (1): 113–21. doi:10.1006/jmbi.1997.1429. PMID 9451443.
  • Tipler CP, Hutchon SP, Hendil K; et al. (1998). "Purification and characterization of 26S proteasomes from human and mouse spermatozoa". Mol. Hum. Reprod. 3 (12): 1053–60. PMID 9464850.
  • Henry L, Baz A, Château MT; et al. (1998). "Proteasome (prosome) subunit variations during the differentiation of myeloid U937 cells". Analytical cellular pathology : the journal of the European Society for Analytical Cellular Pathology. 15 (3): 131–44. PMID 9497851.
  • 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.
  • Dahlmann B, Kopp F, Kristensen P, Hendil KB (1999). "Identical subunit topographies of human and yeast 20S proteasomes". Arch. Biochem. Biophys. 363 (2): 296–300. doi:10.1006/abbi.1999.1104. PMID 10068451.
  • Elenich LA, Nandi D, Kent AE; et al. (1999). "The complete primary structure of mouse 20S proteasomes". Immunogenetics. 49 (10): 835–42. PMID 10436176.
  • Tanahashi N, Murakami Y, Minami Y; et al. (2000). "Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis". J. Biol. Chem. 275 (19): 14336–45. PMID 10799514.
  • 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.

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