Proteasome (prosome, macropain) subunit, alpha type, 6, also known as PSMA6, is a human gene.cite web | title = Entrez Gene: PSMA6 proteasome (prosome, macropain) subunit, alpha type, 6| url =| accessdate = ]

section_title =
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. A pseudogene has been identified on the Y chromosome.cite web | title = Entrez Gene: PSMA6 proteasome (prosome, macropain) subunit, alpha type, 6| url =| accessdate = ]


Further reading

citations =
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*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=
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*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=Gerards WL, de Jong WW, Bloemendal H, Boelens W |title=The human proteasomal subunit HsC8 induces ring formation of other alpha-type subunits. |journal=J. Mol. Biol. |volume=275 |issue= 1 |pages= 113–21 |year= 1998 |pmid= 9451443 |doi= 10.1006/jmbi.1997.1429
*cite journal | author=Henry L, Baz A, Château MT, "et al." |title=Proteasome (prosome) subunit variations during the differentiation of myeloid U937 cells. |journal=Analytical cellular pathology : the journal of the European Society for Analytical Cellular Pathology |volume=15 |issue= 3 |pages= 131–44 |year= 1998 |pmid= 9497851 |doi=
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*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=Feng Y, Longo DL, Ferris DK |title=Polo-like kinase interacts with proteasomes and regulates their activity. |journal=Cell Growth Differ. |volume=12 |issue= 1 |pages= 29–37 |year= 2001 |pmid= 11205743 |doi=
*cite journal | author=Engidawork E, Juranville JF, Fountoulakis M, "et al." |title=Selective upregulation of the ubiquitin-proteasome proteolytic pathway proteins, proteasome zeta chain and isopeptidase T in fetal Down syndrome. |journal=J. Neural Transm. Suppl. |volume= |issue= 61 |pages= 117–30 |year= 2002 |pmid= 11771738 |doi=
*cite journal | author=Sjakste T, Sjakste N, Scherrer K |title=Exon/intron organisation of human proteasome PROS-27 K gene. |journal=DNA Seq. |volume=12 |issue= 4 |pages= 261–5 |year= 2002 |pmid= 11924531 |doi=

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