PSMC2


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&Cmd=ShowDetailView&TermToSearch=5701| 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. This subunit has been shown to interact with several of the basal transcription factors so, in addition to participation in proteasome functions, this subunit may participate in the regulation of transcription. This subunit may also compete with PSMC3 for binding to the HIV tat protein to regulate the interaction between the viral protein and the transcription complex.cite web | title = Entrez Gene: PSMC2 proteasome (prosome, macropain) 26S subunit, ATPase, 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5701| 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=Shibuya H, Irie K, Ninomiya-Tsuji J, "et al." |title=New human gene encoding a positive modulator of HIV Tat-mediated transactivation. |journal=Nature |volume=357 |issue= 6380 |pages= 700–2 |year= 1992 |pmid= 1377363 |doi= 10.1038/357700a0
*cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317–20 |year= 1992 |pmid= 1602151 |doi=
*cite journal | author=Nacken W, Kingsman AJ, Kingsman SM, "et al." |title=A homologue of the human MSS1 gene, a positive modulator of HIV-1 gene expression, is massively expressed in Xenopus oocytes. |journal=Biochim. Biophys. Acta |volume=1261 |issue= 2 |pages= 293–5 |year= 1995 |pmid= 7711076 |doi=
*cite journal | author=Ghislain M, Udvardy A, Mann C |title=S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase. |journal=Nature |volume=366 |issue= 6453 |pages= 358–62 |year= 1993 |pmid= 8247132 |doi= 10.1038/366358a0
*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=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=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=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=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=Zheng L, Chen Y, Lee WH |title=Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins. |journal=Mol. Cell. Biol. |volume=19 |issue= 8 |pages= 5417–28 |year= 1999 |pmid= 10409732 |doi=
*cite journal | author=Gorbea C, Taillandier D, Rechsteiner M |title=Mapping subunit contacts in the regulatory complex of the 26 S proteasome. S2 and S5b form a tetramer with ATPase subunits S4 and S7. |journal=J. Biol. Chem. |volume=275 |issue= 2 |pages= 875–82 |year= 2000 |pmid= 10625621 |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=Hwang J, Fauzi H, Fukuda K, "et al." |title=The RNA aptamer-binding site of hepatitis C virus NS3 protease. |journal=Biochem. Biophys. Res. Commun. |volume=279 |issue= 2 |pages= 557–62 |year= 2001 |pmid= 11118325 |doi= 10.1006/bbrc.2000.4007
*cite journal | author=Yanagi S, Shimbara N, Tamura T |title=Tissue and cell distribution of a mammalian proteasomal ATPase, MSS1, and its complex formation with the basal transcription factors. |journal=Biochem. Biophys. Res. Commun. |volume=279 |issue= 2 |pages= 568–73 |year= 2001 |pmid= 11118327 |doi= 10.1006/bbrc.2000.3969
*cite journal | author=Hartmann-Petersen R, Tanaka K, Hendil KB |title=Quaternary structure of the ATPase complex of human 26S proteasomes determined by chemical cross-linking. |journal=Arch. Biochem. Biophys. |volume=386 |issue= 1 |pages= 89–94 |year= 2001 |pmid= 11361004 |doi= 10.1006/abbi.2000.2178
*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

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Look at other dictionaries:

  • Yugoloth — Characteristics Alignment Neutral Evil Type Outsider (Evil) Publication history Source books Faces of Evil, PSMC, PSMC2, Planes of Conflict, MM2, MM3, Fiend Folio First appearance MM2(1e) In the Dungeons & …   Wikipedia

  • 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

  • PSMC3 — Proteasome (prosome, macropain) 26S subunit, ATPase, 3, also known as PSMC3, is a human gene. PBB Summary section title = summary text = The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2… …   Wikipedia

  • NDC80 — homolog, kinetochore complex component (S. cerevisiae) PDB rendering based on 2igp …   Wikipedia


Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”

We are using cookies for the best presentation of our site. Continuing to use this site, you agree with this.