PSMB6
| Proteasome (prosome, macropain) subunit, beta type, 6 | |||||||||||||
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File:PBB Protein PSMB6 image.jpg PDB rendering based on 1iru. | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | PSMB6 ; Y; DELTA; LMPY; MGC5169 | ||||||||||||
| External IDs | Template:OMIM5 Template:MGI HomoloGene: 2092 | ||||||||||||
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| RNA expression pattern | |||||||||||||
| File:PBB GE PSMB6 208827 at tn.png | |||||||||||||
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| Template:GNF Ortholog box | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | n/a | n/a | |||||||||||
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| 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) subunit, beta type, 6, also known as PSMB6, is a human gene.[1]
The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure 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. 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 a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit in the proteasome. This catalytic subunit is not present in the immunoproteasome and is replaced by catalytic subunit 1i (proteasome beta 9 subunit).[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.
- Goff SP (2003). "Death by deamination: a novel host restriction system for HIV-1". Cell. 114 (3): 281–3. PMID 12914693.
- DeMartino GN, Orth K, McCullough ML; et al. (1991). "The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous". Biochim. Biophys. Acta. 1079 (1): 29–38. PMID 1888762.
- Lee LW, Moomaw CR, Orth K; et al. (1990). "Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome)". Biochim. Biophys. Acta. 1037 (2): 178–85. PMID 2306472.
- Kristensen P, Johnsen AH, Uerkvitz W; et al. (1995). "Human proteasome subunits from 2-dimensional gels identified by partial sequencing". Biochem. Biophys. Res. Commun. 205 (3): 1785–9. PMID 7811265.
- Akiyama K, Yokota K, Kagawa S; et al. (1994). "cDNA cloning and interferon gamma down-regulation of proteasomal subunits X and Y.". Science. 265 (5176): 1231–4. PMID 8066462.
- 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.
- 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.
- Elenich LA, Nandi D, Kent AE; et al. (1999). "The complete primary structure of mouse 20S proteasomes". Immunogenetics. 49 (10): 835–42. PMID 10436176.
- 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.
- Feng Y, Longo DL, Ferris DK (2001). "Polo-like kinase interacts with proteasomes and regulates their activity". Cell Growth Differ. 12 (1): 29–37. PMID 11205743.
- 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.
- Chen M, Rockel T, Steinweger G; et al. (2003). "Subcellular recruitment of fibrillarin to nucleoplasmic proteasomes: implications for processing of a nucleolar autoantigen". Mol. Biol. Cell. 13 (10): 3576–87. doi:10.1091/mbc.02-05-0083. PMID 12388758.
- 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.
- 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.
- Lecossier D, Bouchonnet F, Clavel F, Hance AJ (2003). "Hypermutation of HIV-1 DNA in the absence of the Vif protein". Science. 300 (5622): 1112. doi:10.1126/science.1083338. PMID 12750511.
- Zhang H, Yang B, Pomerantz RJ; et al. (2003). "The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA". Nature. 424 (6944): 94–8. doi:10.1038/nature01707. PMID 12808465.
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