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Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

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PSMA1

Introduction

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

References

  1. ↑ 1.0 1.1 “Entrez Gene: PSMA1 proteasome (prosome, macropain) subunit, alpha type, 1”.
Further reading

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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