PSMB6

From Wikipedia, the free encyclopedia

Proteasome (prosome, macropain) subunit, beta type, 6

PDB rendering based on 1iru.

Available structures: 1iru

Identifiers

Symbol(s)

PSMB6; Y; DELTA; LMPY; MGC5169

External IDs

OMIM: 600307 MGI: 104880 HomoloGene: 2092

Gene ontology
Molecular Function:	• threonine endopeptidase activity
Cellular Component:	• cytosol • proteasome core complex (sensu Eukaryota)
Biological Process:	• ubiquitin-dependent protein catabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_002798 (mRNA)
NP_002789 (protein)

NM_008946 (mRNA)
NP_032972 (protein)

Location

Chr 17: 4.65 - 4.65 Mb

n/a

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: PSMB6 proteasome (prosome, macropain) subunit, beta type, 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.
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.