PSMA7

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Proteasome (prosome, macropain) subunit, alpha type, 7
PDB rendering based on 1iru.
Available structures: 1iru
Identifiers
Symbol(s) PSMA7; C6; HSPC; MGC3755; RC6-1; XAPC7
External IDs OMIM: 606607 MGI: 1347070 HomoloGene: 2086
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 5688 26444
Ensembl ENSG00000101182 ENSMUSG00000027566
Uniprot O14818 Q3THL2
Refseq NM_002792 (mRNA)
NP_002783 (protein)		 NM_011969 (mRNA)
NP_036099 (protein)
Location Chr 20: 60.15 - 60.15 Mb Chr 2: 179.97 - 179.97 Mb
Pubmed search [1] [2]

Proteasome (prosome, macropain) subunit, alpha type, 7, also known as PSMA7, 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. This particular subunit has been shown to interact specifically with the hepatitis B virus X protein, a protein critical to viral replication. In addition, this subunit is involved in regulating hepatitis virus C internal ribosome entry site (IRES) activity, an activity essential for viral replication. This core alpha subunit is also involved in regulating the hypoxia-inducible factor-1alpha, a transcription factor important for cellular responses to oxygen tension. Multiple isoforms of this subunit arising from alternative splicing may exist but alternative transcripts for only two isoforms have been defined. A pseudogene has been identified on chromosome 9.[1]

[edit] References

  1. ^ a b Entrez Gene: PSMA7 proteasome (prosome, macropain) subunit, alpha type, 7.

[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. 
  • 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. 
  • Akioka H, Forsberg NE, Ishida N, et al. (1995). "Isolation and characterization of the HC8 subunit gene of the human proteasome.". Biochem. Biophys. Res. Commun. 207 (1): 318–23. doi:10.1006/bbrc.1995.1190. PMID 7857283. 
  • Huang J, Kwong J, Sun EC, Liang TJ (1996). "Proteasome complex as a potential cellular target of hepatitis B virus X protein.". J. Virol. 70 (8): 5582–91. PMID 8764072. 
  • 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. 
  • Elenich LA, Nandi D, Kent AE, et al. (1999). "The complete primary structure of mouse 20S proteasomes.". Immunogenetics 49 (10): 835–42. PMID 10436176. 
  • Zhang Z, Torii N, Furusaka A, et al. (2000). "Structural and functional characterization of interaction between hepatitis B virus X protein and the proteasome complex.". J. Biol. Chem. 275 (20): 15157–65. doi:10.1074/jbc.M910378199. PMID 10748218. 
  • 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. 
  • Zhang QH, Ye M, Wu XY, et al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells.". Genome Res. 10 (10): 1546–60. PMID 11042152. 
  • 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. 
  • Golubnitschaja-Labudova O, Liu R, Decker C, et al. (2001). "Altered gene expression in lymphocytes of patients with normal-tension glaucoma.". Curr. Eye Res. 21 (5): 867–76. PMID 11262608. 
  • Hartmann-Petersen R, Tanaka K, Hendil KB (2001). "Quaternary structure of the ATPase complex of human 26S proteasomes determined by chemical cross-linking.". Arch. Biochem. Biophys. 386 (1): 89–94. doi:10.1006/abbi.2000.2178. PMID 11361004. 
  • Cho S, Choi YJ, Kim JM, et al. (2001). "Binding and regulation of HIF-1alpha by a subunit of the proteasome complex, PSMA7.". FEBS Lett. 498 (1): 62–6. PMID 11389899. 
  • Krüger M, Beger C, Welch PJ, et al. (2001). "Involvement of proteasome alpha-subunit PSMA7 in hepatitis C virus internal ribosome entry site-mediated translation.". Mol. Cell. Biol. 21 (24): 8357–64. doi:10.1128/MCB.21.24.8357-8364.2001. PMID 11713272. 
  • Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052. 
  • 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. 
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