PSMB4

Proteasome (prosome, macropain) subunit, beta type, 4, also known as PSMB4, is a human gene.

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 proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit.cite web | title = Entrez Gene: PSMB4 proteasome (prosome, macropain) subunit, beta type, 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5692| 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=Rasmussen HH, van Damme J, Puype M, "et al." |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960–9 |year= 1993 |pmid= 1286667 |doi=
*cite journal | author=Lee LW, Moomaw CR, Orth K, "et al." |title=Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome). |journal=Biochim. Biophys. Acta |volume=1037 |issue= 2 |pages= 178–85 |year= 1990 |pmid= 2306472 |doi=
*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=Nothwang HG, Tamura T, Tanaka K, Ichihara A |title=Sequence analyses and inter-species comparisons of three novel human proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine potential proteolytic active-site residues. |journal=Biochim. Biophys. Acta |volume=1219 |issue= 2 |pages= 361–8 |year= 1994 |pmid= 7918633 |doi=
*cite journal | author=Gerards WL, Hop FW, Hendriks IL, Bloemendal H |title=Cloning and expression of a human pro(tea)some beta-subunit cDNA: a homologue of the yeast PRE4-subunit essential for peptidylglutamyl-peptide hydrolase activity. |journal=FEBS Lett. |volume=346 |issue= 2-3 |pages= 151–5 |year= 1994 |pmid= 8013624 |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=McCusker D, Jones T, Sheer D, Trowsdale J |title=Genetic relationships of the genes encoding the human proteasome beta subunits and the proteasome PA28 complex. |journal=Genomics |volume=45 |issue= 2 |pages= 362–7 |year= 1998 |pmid= 9344661 |doi= 10.1006/geno.1997.4948
*cite journal | author=Rossi F, Evstafieva A, Pedrali-Noy G, "et al." |title=HsN3 proteasomal subunit as a target for human immunodeficiency virus type 1 Nef protein. |journal=Virology |volume=237 |issue= 1 |pages= 33–45 |year= 1997 |pmid= 9344905 |doi= 10.1006/viro.1997.8752
*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=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=Lin Y, Martin J, Gruendler C, "et al." |title=A novel link between the proteasome pathway and the signal transduction pathway of the bone morphogenetic proteins (BMPs). |journal=BMC Cell Biol. |volume=3 |issue= |pages= 15 |year= 2002 |pmid= 12097147 |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=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

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