- PSMF1
Proteasome (prosome, macropain) inhibitor subunit 1 (PI31), also known as PSMF1, is a human
gene .cite web | title = Entrez Gene: PSMF1 proteasome (prosome, macropain) inhibitor subunit 1 (PI31)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9491| accessdate = ]PBB_Summary
section_title =
summary_text = The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core 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. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase 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 protein that inhibits the activation of the proteasome by the 11S and 19S regulators. Alternative transcript variants have been identified for this gene.cite web | title = Entrez Gene: PSMF1 proteasome (prosome, macropain) inhibitor subunit 1 (PI31)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9491| accessdate = ]References
Further reading
PBB_Further_reading
citations =
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*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=
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*cite journal | author=Liou LY, Herrmann CH, Rice AP |title=HIV-1 infection and regulation of Tat function in macrophages. |journal=Int. J. Biochem. Cell Biol. |volume=36 |issue= 9 |pages= 1767–75 |year= 2005 |pmid= 15183343 |doi= 10.1016/j.biocel.2004.02.018
*cite journal | author=Bannwarth S, Gatignol A |title=HIV-1 TAR RNA: the target of molecular interactions between the virus and its host. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 61–71 |year= 2005 |pmid= 15638724 |doi=
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*cite journal | author=McCutchen-Maloney SL, Matsuda K, Shimbara N, "et al." |title=cDNA cloning, expression, and functional characterization of PI31, a proline-rich inhibitor of the proteasome. |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18557–65 |year= 2000 |pmid= 10764772 |doi= 10.1074/jbc.M001697200
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*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=Zaiss DM, Standera S, Kloetzel PM, Sijts AJ |title=PI31 is a modulator of proteasome formation and antigen processing. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 22 |pages= 14344–9 |year= 2002 |pmid= 12374861 |doi= 10.1073/pnas.212257299
*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=PBB_Controls
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