PSMA2

Proteasome (prosome, macropain) subunit, alpha type, 2, also known as PSMA2, is a human gene.cite web | title = Entrez Gene: PSMA2 proteasome (prosome, macropain) subunit, alpha type, 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5683| accessdate = ]

PBB_Summary
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summary_text = 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.cite web | title = Entrez Gene: PSMA2 proteasome (prosome, macropain) subunit, alpha type, 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5683| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Coux O, Tanaka K, Goldberg AL |title=Structure and functions of the 20S and 26S proteasomes. |journal=Annu. Rev. Biochem. |volume=65 |issue= |pages= 801–47 |year= 1996 |pmid= 8811196 |doi= 10.1146/annurev.bi.65.070196.004101
*cite journal | author=Goff SP |title=Death by deamination: a novel host restriction system for HIV-1. |journal=Cell |volume=114 |issue= 3 |pages= 281–3 |year= 2003 |pmid= 12914693 |doi=
*cite journal | author=DeMartino GN, Orth K, McCullough ML, "et al." |title=The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous. |journal=Biochim. Biophys. Acta |volume=1079 |issue= 1 |pages= 29–38 |year= 1991 |pmid= 1888762 |doi=
*cite journal | author=Tamura T, Lee DH, Osaka F, "et al." |title=Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes). |journal=Biochim. Biophys. Acta |volume=1089 |issue= 1 |pages= 95–102 |year= 1991 |pmid= 2025653 |doi=
*cite journal | author=Okumura K, Nogami M, Taguchi H, "et al." |title=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. |journal=Genomics |volume=27 |issue= 2 |pages= 377–9 |year= 1995 |pmid= 7558012 |doi= 10.1006/geno.1995.1062
*cite journal | author=Kristensen P, Johnsen AH, Uerkvitz W, "et al." |title=Human proteasome subunits from 2-dimensional gels identified by partial sequencing. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 3 |pages= 1785–9 |year= 1995 |pmid= 7811265 |doi=
*cite journal | author=Tamura T, Osaka F, Kawamura Y, "et al." |title=Isolation and characterization of alpha-type HC3 and beta-type HC5 subunit genes of human proteasomes. |journal=J. Mol. Biol. |volume=244 |issue= 1 |pages= 117–24 |year= 1994 |pmid= 7966316 |doi= 10.1006/jmbi.1994.1710
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Knuehl C, Seelig A, Brecht B, "et al." |title=Functional analysis of eukaryotic 20S proteasome nuclear localization signal. |journal=Exp. Cell Res. |volume=225 |issue= 1 |pages= 67–74 |year= 1996 |pmid= 8635518 |doi= 10.1006/excr.1996.0157
*cite journal | author=Seeger M, Ferrell K, Frank R, Dubiel W |title=HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8145–8 |year= 1997 |pmid= 9079628 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Madani N, Kabat D |title=An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. |journal=J. Virol. |volume=72 |issue= 12 |pages= 10251–5 |year= 1998 |pmid= 9811770 |doi=
*cite journal | author=Simon JH, Gaddis NC, Fouchier RA, Malim MH |title=Evidence for a newly discovered cellular anti-HIV-1 phenotype. |journal=Nat. Med. |volume=4 |issue= 12 |pages= 1397–400 |year= 1998 |pmid= 9846577 |doi= 10.1038/3987
*cite journal | author=Elenich LA, Nandi D, Kent AE, "et al." |title=The complete primary structure of mouse 20S proteasomes. |journal=Immunogenetics |volume=49 |issue= 10 |pages= 835–42 |year= 1999 |pmid= 10436176 |doi=
*cite journal | author=Mulder LC, Muesing MA |title=Degradation of HIV-1 integrase by the N-end rule pathway. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29749–53 |year= 2000 |pmid= 10893419 |doi= 10.1074/jbc.M004670200
*cite journal | author=Kleijnen MF, Shih AH, Zhou P, "et al." |title=The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome. |journal=Mol. Cell |volume=6 |issue= 2 |pages= 409–19 |year= 2000 |pmid= 10983987 |doi=
*cite journal | author=Sheehy AM, Gaddis NC, Choi JD, Malim MH |title=Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. |journal=Nature |volume=418 |issue= 6898 |pages= 646–50 |year= 2002 |pmid= 12167863 |doi= 10.1038/nature00939
*cite journal | author=Huang X, Seifert U, Salzmann U, "et al." |title=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. |journal=J. Mol. Biol. |volume=323 |issue= 4 |pages= 771–82 |year= 2002 |pmid= 12419264 |doi=
*cite journal | author=Bommel H, Xie G, Rossoll W, "et al." |title=Missense mutation in the tubulin-specific chaperone E (Tbce) gene in the mouse mutant progressive motor neuronopathy, a model of human motoneuron disease. |journal=J. Cell Biol. |volume=159 |issue= 4 |pages= 563–9 |year= 2003 |pmid= 12446740 |doi= 10.1083/jcb.200208001

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