PSMD3

Proteasome (prosome, macropain) 26S subunit, non-ATPase, 3, also known as PSMD3, is a human gene.cite web | title = Entrez Gene: PSMD3 proteasome (prosome, macropain) 26S subunit, non-ATPase, 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5709| 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 one of the non-ATPase subunits of the 19S regulator lid.cite web | title = Entrez Gene: PSMD3 proteasome (prosome, macropain) 26S subunit, non-ATPase, 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5709| 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=Kominami K, Okura N, Kawamura M, "et al." |title=Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1. |journal=Mol. Biol. Cell |volume=8 |issue= 1 |pages= 171–87 |year= 1997 |pmid= 9017604 |doi=
*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=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=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=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=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Gaddis NC, Chertova E, Sheehy AM, "et al." |title=Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions. |journal=J. Virol. |volume=77 |issue= 10 |pages= 5810–20 |year= 2003 |pmid= 12719574 |doi=
*cite journal | author=Lecossier D, Bouchonnet F, Clavel F, Hance AJ |title=Hypermutation of HIV-1 DNA in the absence of the Vif protein. |journal=Science |volume=300 |issue= 5622 |pages= 1112 |year= 2003 |pmid= 12750511 |doi= 10.1126/science.1083338
*cite journal | author=Zhang H, Yang B, Pomerantz RJ, "et al." |title=The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. |journal=Nature |volume=424 |issue= 6944 |pages= 94–8 |year= 2003 |pmid= 12808465 |doi= 10.1038/nature01707
*cite journal | author=Mangeat B, Turelli P, Caron G, "et al." |title=Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. |journal=Nature |volume=424 |issue= 6944 |pages= 99–103 |year= 2003 |pmid= 12808466 |doi= 10.1038/nature01709
*cite journal | author=Harris RS, Bishop KN, Sheehy AM, "et al." |title=DNA deamination mediates innate immunity to retroviral infection. |journal=Cell |volume=113 |issue= 6 |pages= 803–9 |year= 2003 |pmid= 12809610 |doi=
*cite journal | author=Harris RS, Sheehy AM, Craig HM, "et al." |title=DNA deamination: not just a trigger for antibody diversification but also a mechanism for defense against retroviruses. |journal=Nat. Immunol. |volume=4 |issue= 7 |pages= 641–3 |year= 2003 |pmid= 12830140 |doi= 10.1038/ni0703-641
*cite journal | author=Gu Y, Sundquist WI |title=Good to CU. |journal=Nature |volume=424 |issue= 6944 |pages= 21–2 |year= 2003 |pmid= 12840737 |doi= 10.1038/424021a
*cite journal | author=Mariani R, Chen D, Schröfelbauer B, "et al." |title=Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. |journal=Cell |volume=114 |issue= 1 |pages= 21–31 |year= 2003 |pmid= 12859895 |doi=

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