PSMB5

From Wikipedia, the free encyclopedia

Proteasome (prosome, macropain) subunit, beta type, 5

PDB rendering based on 1iru.

Available structures: 1iru

Identifiers

Symbol(s)

PSMB5; X; LMPX; MB1; MGC104214

External IDs

OMIM: 600306 MGI: 1194513 HomoloGene: 55690

Gene ontology
Molecular Function:	• chymotrypsin activity • threonine endopeptidase activity • protein binding
Cellular Component:	• cytosol • proteasome core complex (sensu Eukaryota)
Biological Process:	• ubiquitin-dependent protein catabolic process • response to oxidative stress • proteasomal ubiquitin-dependent protein catabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002797 (mRNA)
NP_002788 (protein)

NM_011186 (mRNA)
NP_035316 (protein)

Location

Chr 14: 22.56 - 22.57 Mb

Chr 14: 53.57 - 53.57 Mb

Pubmed search

[1]

[2]

Proteasome (prosome, macropain) subunit, beta type, 5, also known as PSMB5, 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 3i (proteasome beta 8 subunit).^[1]

[edit] References

^ ^a ^b Entrez Gene: PSMB5 proteasome (prosome, macropain) subunit, beta type, 5.

[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.
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.
Belich MP, Glynne RJ, Senger G, et al. (1995). "Proteasome components with reciprocal expression to that of the MHC-encoded LMP proteins.". Curr. Biol. 4 (9): 769–76. PMID 7820546.
Kristensen P, Johnsen AH, Uerkvitz W, et al. (1995). "Human proteasome subunits from 2-dimensional gels identified by partial sequencing.". Biochem. Biophys. Res. Commun. 207 (3): 1059. PMID 7864893.
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.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Abdulla S, Beck S, Belich M, et al. (1996). "Divergent intron arrangement in the MB1/LMP7 proteasome gene pair.". Immunogenetics 44 (4): 254–8. PMID 8753855.
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.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Kohda K, Matsuda Y, Ishibashi T, et al. (1998). "Structural analysis and chromosomal localization of the mouse Psmb5 gene coding for the constitutively expressed beta-type proteasome subunit.". Immunogenetics 47 (1): 77–87. PMID 9382924.
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.
Rodriguez-Vilariño S, Arribas J, Arizti P, Castaño JG (2000). "Proteolytic processing and assembly of the C5 subunit into the proteasome complex.". J. Biol. Chem. 275 (9): 6592–9. PMID 10692467.
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.