PSMC5

Proteasome (prosome, macropain) 26S subunit, ATPase, 5, also known as PSMC5, is a human gene.cite web | title = Entrez Gene: PSMC5 proteasome (prosome, macropain) 26S subunit, ATPase, 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5705| 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 ATPase subunits, a member of the triple-A family of ATPases which have a chaperone-like activity. In addition to participation in proteasome functions, this subunit may participate in transcriptional regulation since it has been shown to interact with the thyroid hormone receptor and retinoid X receptor-alpha.cite web | title = Entrez Gene: PSMC5 proteasome (prosome, macropain) 26S subunit, ATPase, 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5705| 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=Nelbock P, Dillon PJ, Perkins A, Rosen CA |title=A cDNA for a protein that interacts with the human immunodeficiency virus Tat transactivator. |journal=Science |volume=248 |issue= 4963 |pages= 1650–3 |year= 1990 |pmid= 2194290 |doi=
*cite journal | author=Akiyama K, Yokota K, Kagawa S, "et al." |title=cDNA cloning of a new putative ATPase subunit p45 of the human 26S proteasome, a homolog of yeast transcriptional factor Sug1p. |journal=FEBS Lett. |volume=363 |issue= 1-2 |pages= 151–6 |year= 1995 |pmid= 7729537 |doi=
*cite journal | author=Lee JW, Choi HS, Gyuris J, "et al." |title=Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. |journal=Mol. Endocrinol. |volume=9 |issue= 2 |pages= 243–54 |year= 1995 |pmid= 7776974 |doi=
*cite journal | author=Lee JW, Ryan F, Swaffield JC, "et al." |title=Interaction of thyroid-hormone receptor with a conserved transcriptional mediator. |journal=Nature |volume=374 |issue= 6517 |pages= 91–4 |year= 1995 |pmid= 7870181 |doi= 10.1038/374091a0
*cite journal | author=Shaw DR, Ennis HL |title=Molecular cloning and developmental regulation of Dictyostelium discoideum homologues of the human and yeast HIV1 Tat-binding protein. |journal=Biochem. Biophys. Res. Commun. |volume=193 |issue= 3 |pages= 1291–6 |year= 1993 |pmid= 8323548 |doi= 10.1006/bbrc.1993.1765
*cite journal | author=Ohana B, Moore PA, Ruben SM, "et al." |title=The type 1 human immunodeficiency virus Tat binding protein is a transcriptional activator belonging to an additional family of evolutionarily conserved genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 1 |pages= 138–42 |year= 1993 |pmid= 8419915 |doi=
*cite journal | author=Dubiel W, Ferrell K, Rechsteiner M |title=Peptide sequencing identifies MSS1, a modulator of HIV Tat-mediated transactivation, as subunit 7 of the 26 S protease. |journal=FEBS Lett. |volume=323 |issue= 3 |pages= 276–8 |year= 1993 |pmid= 8500623 |doi=
*cite journal | author=vom Baur E, Zechel C, Heery D, "et al." |title=Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and the putative transcriptional intermediary factors mSUG1 and TIF1. |journal=EMBO J. |volume=15 |issue= 1 |pages= 110–24 |year= 1996 |pmid= 8598193 |doi=
*cite journal | author=Andersson B, Wentland MA, Ricafrente JY, "et al." |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138
*cite journal | author=Wang W, Chevray PM, Nathans D |title=Mammalian Sug1 and c-Fos in the nuclear 26S proteasome. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 16 |pages= 8236–40 |year= 1996 |pmid= 8710853 |doi=
*cite journal | author=Hoyle J, Tan KH, Fisher EM |title=Localization of genes encoding two human one-domain members of the AAA family: PSMC5 (the thyroid hormone receptor-interacting protein, TRIP1) and PSMC3 (the Tat-binding protein, TBP1). |journal=Hum. Genet. |volume=99 |issue= 2 |pages= 285–8 |year= 1997 |pmid= 9048938 |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=Yu W, Andersson B, Worley KC, "et al." |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi=
*cite journal | author=Weeda G, Rossignol M, Fraser RA, "et al." |title=The XPB subunit of repair/transcription factor TFIIH directly interacts with SUG1, a subunit of the 26S proteasome and putative transcription factor. |journal=Nucleic Acids Res. |volume=25 |issue= 12 |pages= 2274–83 |year= 1997 |pmid= 9173976 |doi=
*cite journal | author=Chen Y, Sharp ZD, Lee WH |title=HEC binds to the seventh regulatory subunit of the 26 S proteasome and modulates the proteolysis of mitotic cyclins. |journal=J. Biol. Chem. |volume=272 |issue= 38 |pages= 24081–7 |year= 1997 |pmid= 9295362 |doi=
*cite journal | author=Tipler CP, Hutchon SP, Hendil K, "et al." |title=Purification and characterization of 26S proteasomes from human and mouse spermatozoa. |journal=Mol. Hum. Reprod. |volume=3 |issue= 12 |pages= 1053–60 |year= 1998 |pmid= 9464850 |doi=
*cite journal | author=Tanahashi N, Suzuki M, Fujiwara T, "et al." |title=Chromosomal localization and immunological analysis of a family of human 26S proteasomal ATPases. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 1 |pages= 229–32 |year= 1998 |pmid= 9473509 |doi=

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