PSMC2

From Wikipedia, the free encyclopedia

Proteasome (prosome, macropain) 26S subunit, ATPase, 2

Identifiers

PSMC2; S7; MGC3004; MSS1; Nbla10058

External IDs

OMIM: 154365 MGI: 109555 HomoloGene: 2096

Gene ontology
Molecular Function:	• nucleotide binding • ATP binding • hydrolase activity • nucleoside-triphosphatase activity
Cellular Component:	• proteasome complex (sensu Eukaryota) • nucleus • cytoplasm • cytosol
Biological Process:	• proteolysis • protein catabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002803 (mRNA)
NP_002794 (protein)

NM_011188 (mRNA)
NP_035318 (protein)

Location

Chr 7: 102.78 - 102.8 Mb

Chr 5: 21.3 - 21.32 Mb

Pubmed search

[1]

[2]

Proteasome (prosome, macropain) 26S subunit, ATPase, 2, also known as PSMC2, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: PSMC2 proteasome (prosome, macropain) 26S subunit, ATPase, 2.

[edit] Further reading

Coux O, Tanaka K, Goldberg AL (1996). "Structure and functions of the 20S and 26S proteasomes.". Annu. Rev. Biochem. 65: 801–47. doi:10.1146/annurev.bi.65.070196.004101. PMID 8811196.
Goff SP (2003). "Death by deamination: a novel host restriction system for HIV-1.". Cell 114 (3): 281–3. PMID 12914693.
Shibuya H, Irie K, Ninomiya-Tsuji J, et al. (1992). "New human gene encoding a positive modulator of HIV Tat-mediated transactivation.". Nature 357 (6380): 700–2. doi:10.1038/357700a0. PMID 1377363.
Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317–20. PMID 1602151.
Nacken W, Kingsman AJ, Kingsman SM, et al. (1995). "A homologue of the human MSS1 gene, a positive modulator of HIV-1 gene expression, is massively expressed in Xenopus oocytes.". Biochim. Biophys. Acta 1261 (2): 293–5. PMID 7711076.
Ghislain M, Udvardy A, Mann C (1993). "S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase.". Nature 366 (6453): 358–62. doi:10.1038/366358a0. PMID 8247132.
Dubiel W, Ferrell K, Rechsteiner M (1993). "Peptide sequencing identifies MSS1, a modulator of HIV Tat-mediated transactivation, as subunit 7 of the 26 S protease.". FEBS Lett. 323 (3): 276–8. PMID 8500623.
Seeger M, Ferrell K, Frank R, Dubiel W (1997). "HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation.". J. Biol. Chem. 272 (13): 8145–8. PMID 9079628.
Chen Y, Sharp ZD, Lee WH (1997). "HEC binds to the seventh regulatory subunit of the 26 S proteasome and modulates the proteolysis of mitotic cyclins.". J. Biol. Chem. 272 (38): 24081–7. PMID 9295362.
Tanahashi N, Suzuki M, Fujiwara T, et al. (1998). "Chromosomal localization and immunological analysis of a family of human 26S proteasomal ATPases.". Biochem. Biophys. Res. Commun. 243 (1): 229–32. PMID 9473509.
Madani N, Kabat D (1998). "An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein.". J. Virol. 72 (12): 10251–5. PMID 9811770.
Simon JH, Gaddis NC, Fouchier RA, Malim MH (1998). "Evidence for a newly discovered cellular anti-HIV-1 phenotype.". Nat. Med. 4 (12): 1397–400. doi:10.1038/3987. PMID 9846577.
Zheng L, Chen Y, Lee WH (1999). "Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins.". Mol. Cell. Biol. 19 (8): 5417–28. PMID 10409732.
Gorbea C, Taillandier D, Rechsteiner M (2000). "Mapping subunit contacts in the regulatory complex of the 26 S proteasome. S2 and S5b form a tetramer with ATPase subunits S4 and S7.". J. Biol. Chem. 275 (2): 875–82. PMID 10625621.
Mulder LC, Muesing MA (2000). "Degradation of HIV-1 integrase by the N-end rule pathway.". J. Biol. Chem. 275 (38): 29749–53. doi:10.1074/jbc.M004670200. PMID 10893419.
Hwang J, Fauzi H, Fukuda K, et al. (2001). "The RNA aptamer-binding site of hepatitis C virus NS3 protease.". Biochem. Biophys. Res. Commun. 279 (2): 557–62. doi:10.1006/bbrc.2000.4007. PMID 11118325.
Yanagi S, Shimbara N, Tamura T (2001). "Tissue and cell distribution of a mammalian proteasomal ATPase, MSS1, and its complex formation with the basal transcription factors.". Biochem. Biophys. Res. Commun. 279 (2): 568–73. doi:10.1006/bbrc.2000.3969. PMID 11118327.
Hartmann-Petersen R, Tanaka K, Hendil KB (2001). "Quaternary structure of the ATPase complex of human 26S proteasomes determined by chemical cross-linking.". Arch. Biochem. Biophys. 386 (1): 89–94. doi:10.1006/abbi.2000.2178. PMID 11361004.
Sheehy AM, Gaddis NC, Choi JD, Malim MH (2002). "Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein.". Nature 418 (6898): 646–50. doi:10.1038/nature00939. PMID 12167863.