PSMA4

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Proteasome (prosome, macropain) subunit, alpha type, 4
PDB rendering based on 1iru.
Available structures: 1iru
Identifiers
Symbol(s) PSMA4; HC9; HsT17706; MGC111191; MGC12467; MGC24813
External IDs MGI: 1347060 HomoloGene: 2083
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 5685 26441
Ensembl ENSG00000041357 ENSMUSG00000032301
Uniprot P25789 Q3TL95
Refseq NM_002789 (mRNA)
NP_002780 (protein)		 NM_011966 (mRNA)
NP_036096 (protein)
Location Chr 15: 76.62 - 76.63 Mb Chr 9: 54.75 - 54.76 Mb
Pubmed search [1] [2]

Proteasome (prosome, macropain) subunit, alpha type, 4, also known as PSMA4, is a human gene.

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]

[edit] References

  1. ^ Entrez Gene: PSMA4 proteasome (prosome, macropain) subunit, alpha type, 4.

[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. 
  • Goff SP (2003). "Death by deamination: a novel host restriction system for HIV-1.". Cell 114 (3): 281-3. PMID 12914693. 
  • 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. 
  • 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. 
  • Kato S, Sekine S, Oh SW, et al. (1995). "Construction of a human full-length cDNA bank.". Gene 150 (2): 243-50. PMID 7821789. 
  • Arribas J, Arizti P, Castaño JG (1994). "Antibodies against the C2 COOH-terminal region discriminate the active and latent forms of the multicatalytic proteinase complex.". J. Biol. Chem. 269 (17): 12858-64. PMID 8175701. 
  • Castaño JG, Mahillo E, Arizti P, Arribas J (1996). "Phosphorylation of C8 and C9 subunits of the multicatalytic proteinase by casein kinase II and identification of the C8 phosphorylation sites by direct mutagenesis.". Biochemistry 35 (12): 3782-9. doi:10.1021/bi952540s. PMID 8619999. 
  • Palmer A, Rivett AJ, Thomson S, et al. (1996). "Subpopulations of proteasomes in rat liver nuclei, microsomes and cytosol.". Biochem. J. 316 ( Pt 2): 401-7. PMID 8687380. 
  • 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. 
  • 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. 
  • 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. 
  • Lecossier D, Bouchonnet F, Clavel F, Hance AJ (2003). "Hypermutation of HIV-1 DNA in the absence of the Vif protein.". Science 300 (5622): 1112. doi:10.1126/science.1083338. PMID 12750511. 
  • Zhang H, Yang B, Pomerantz RJ, et al. (2003). "The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA.". Nature 424 (6944): 94-8. doi:10.1038/nature01707. PMID 12808465. 
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