PSMC6

From Wikipedia, the free encyclopedia

Proteasome (prosome, macropain) 26S subunit, ATPase, 6

Identifiers

PSMC6; CADP44; MGC12520; P44; SUG2; p42

External IDs

OMIM: 602708 MGI: 1914339 HomoloGene: 2099

Gene ontology
Molecular Function:	• nucleotide binding • ATP binding • hydrolase activity • ATPase activity • protein binding, bridging
Cellular Component:	• proteasome complex (sensu Eukaryota) • nucleus • cytoplasm • cytosol
Biological Process:	• ubiquitin-dependent protein catabolic process • protein catabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002806 (mRNA)
NP_002797 (protein)

NM_025959 (mRNA)
NP_080235 (protein)

Location

Chr 14: 52.24 - 52.26 Mb

Chr 14: 44.25 - 44.27 Mb

Pubmed search

[1]

[2]

Proteasome (prosome, macropain) 26S subunit, ATPase, 6, also known as PSMC6, 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. Pseudogenes have been identified on chromosomes 8 and 12.^[1]

[edit] References

^ ^a ^b Entrez Gene: PSMC6 proteasome (prosome, macropain) 26S subunit, ATPase, 6.

[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.
Hastings R, Walker G, Eyheralde I, et al. (1999). "Activator complexes containing the proteasomal regulatory ATPases S10b (SUG2) and S6 (TBP1) in different tissues and organisms.". Mol. Biol. Rep. 26 (1-2): 35-8. PMID 10363644.
Goff SP (2003). "Death by deamination: a novel host restriction system for HIV-1.". Cell 114 (3): 281-3. PMID 12914693.
DeMartino GN, Proske RJ, Moomaw CR, et al. (1996). "Identification, purification, and characterization of a PA700-dependent activator of the proteasome.". J. Biol. Chem. 271 (6): 3112-8. PMID 8621709.
Fujiwara T, Watanabe TK, Tanaka K, et al. (1996). "cDNA cloning of p42, a shared subunit of two proteasome regulatory proteins, reveals a novel member of the AAA protein family.". FEBS Lett. 387 (2-3): 184-8. PMID 8674546.
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.
Tipler CP, Hutchon SP, Hendil K, et al. (1998). "Purification and characterization of 26S proteasomes from human and mouse spermatozoa.". Mol. Hum. Reprod. 3 (12): 1053-60. PMID 9464850.
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.
Russell SJ, Steger KA, Johnston SA (1999). "Subcellular localization, stoichiometry, and protein levels of 26 S proteasome subunits in yeast.". J. Biol. Chem. 274 (31): 21943-52. PMID 10419517.
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.
Russell SJ, Gonzalez F, Joshua-Tor L, Johnston SA (2002). "Selective chemical inactivation of AAA proteins reveals distinct functions of proteasomal ATPases.". Chem. Biol. 8 (10): 941-50. PMID 11590019.
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.
Huang X, Seifert U, Salzmann U, et al. (2002). "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.". J. Mol. Biol. 323 (4): 771-82. PMID 12419264.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Reiser G, Bernstein HG (2003). "Neurons and plaques of Alzheimer's disease patients highly express the neuronal membrane docking protein p42IP4/centaurin alpha.". Neuroreport 13 (18): 2417-9. doi:10.1097/01.wnr.0000048005.96487.10. PMID 12499840.
Gaddis NC, Chertova E, Sheehy AM, et al. (2003). "Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions.". J. Virol. 77 (10): 5810-20. PMID 12719574.