PSMC3

PSMC3

Proteasome (prosome, macropain) 26S subunit, ATPase, 3, also known as PSMC3, is a human gene.

PBB_Summary
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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 that have chaperone-like activity. This subunit may compete with PSMC2 for binding to the HIV tat protein to regulate the interaction between the viral protein and the transcription complex. A pseudogene has been identified on chromosome 9.cite web | title = Entrez Gene: PSMC3 proteasome (prosome, macropain) 26S subunit, ATPase, 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5702| 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=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*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=DeMartino GN, Proske RJ, Moomaw CR, "et al." |title=Identification, purification, and characterization of a PA700-dependent activator of the proteasome. |journal=J. Biol. Chem. |volume=271 |issue= 6 |pages= 3112–8 |year= 1996 |pmid= 8621709 |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=Tanaka T, Nakamura T, Takagi H, Sato M |title=Molecular cloning and characterization of a novel TBP-1 interacting protein (TBPIP):enhancement of TBP-1 action on Tat by TBPIP. |journal=Biochem. Biophys. Res. Commun. |volume=239 |issue= 1 |pages= 176–81 |year= 1997 |pmid= 9345291 |doi= 10.1006/bbrc.1997.7447
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |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=
*cite journal | author=Nakamura T, Tanaka T, Takagi H, Sato M |title=Cloning and heterogeneous in vivo expression of Tat binding protein-1 (TBP-1) in the mouse. |journal=Biochim. Biophys. Acta |volume=1399 |issue= 1 |pages= 93–100 |year= 1998 |pmid= 9714759 |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=Park BW, O'Rourke DM, Wang Q, "et al." |title=Induction of the Tat-binding protein 1 gene accompanies the disabling of oncogenic erbB receptor tyrosine kinases. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 11 |pages= 6434–8 |year= 1999 |pmid= 10339605 |doi=
*cite journal | author=Tanahashi N, Murakami Y, Minami Y, "et al." |title=Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis. |journal=J. Biol. Chem. |volume=275 |issue= 19 |pages= 14336–45 |year= 2000 |pmid= 10799514 |doi=
*cite journal | author=Ijichi H, Tanaka T, Nakamura T, "et al." |title=Molecular cloning and characterization of a human homologue of TBPIP, a BRCA1 locus-related gene. |journal=Gene |volume=248 |issue= 1-2 |pages= 99–107 |year= 2000 |pmid= 10806355 |doi=

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  • AAA proteins — Pfam box Symbol = AAA Name = ATPases associated with diverse cellular activities (AAA) width = caption = Pfam= PF00004 InterPro= IPR003959 SMART= PROSITE= PDOC00572 SCOP = 1nsf TCDB = OPM family= OPM protein= PDB=PDB3|1jbkA:201 286 PDB3|1qvrC:193 …   Wikipedia

  • 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… …   Wikipedia

  • PSMC2 — Proteasome (prosome, macropain) 26S subunit, ATPase, 2, also known as PSMC2, is a human gene.cite web | title = Entrez Gene: PSMC2 proteasome (prosome, macropain) 26S subunit, ATPase, 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene… …   Wikipedia

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