PSMC6
Proteasome (prosome, macropain) 26S subunit, ATPase, 6 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||||
Symbols | PSMC6 ; CADP44; MGC12520; P44; SUG2; p42 | ||||||||||
External IDs | Template:OMIM5 Template:MGI HomoloGene: 2099 | ||||||||||
| |||||||||||
RNA expression pattern | |||||||||||
File:PBB GE PSMC6 201699 at tn.png | |||||||||||
More reference expression data | |||||||||||
Orthologs | |||||||||||
Template:GNF Ortholog box | |||||||||||
Species | Human | Mouse | |||||||||
Entrez | n/a | n/a | |||||||||
Ensembl | n/a | n/a | |||||||||
UniProt | n/a | n/a | |||||||||
RefSeq (mRNA) | n/a | n/a | |||||||||
RefSeq (protein) | n/a | n/a | |||||||||
Location (UCSC) | n/a | n/a | |||||||||
PubMed search | n/a | n/a |
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]
References
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.
This protein-related article is a stub. You can help Wikipedia by expanding it. |