PSMA5

From Wikipedia, the free encyclopedia

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

PDB rendering based on 1iru.

Available structures: 1iru

Identifiers

Symbol(s)

PSMA5; MGC117302; MGC125802; MGC125803; MGC125804; PSC5; ZETA

External IDs

OMIM: 176844 MGI: 1347009 HomoloGene: 2084

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

Refseq

NM_002790 (mRNA)
NP_002781 (protein)

NM_011967 (mRNA)
NP_036097 (protein)

Location

Chr 1: 109.75 - 109.77 Mb

Chr 3: 108.39 - 108.41 Mb

Pubmed search

[1]

[2]

Proteasome (prosome, macropain) subunit, alpha type, 5, also known as PSMA5, 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 peptidase T1A family, that is a 20S core alpha subunit.^[1]

[edit] References

^ ^a ^b Entrez Gene: PSMA5 proteasome (prosome, macropain) subunit, alpha 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.
Rasmussen HH, van Damme J, Puype M, et al. (1993). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.". Electrophoresis 13 (12): 960-9. PMID 1286667.
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.
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.
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.
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.
Mayau V, Baron B, Buttin G, Debatisse M (1998). "Twelve genes, including the unassigned proteasome zeta subunit gene, ordered within the human 1p13 region.". Mamm. Genome 9 (4): 331-3. PMID 9530635.
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.
Jørgensen L, Hendil KB (1999). "Proteasome subunit zeta, a putative ribonuclease, is also found as a free monomer.". Mol. Biol. Rep. 26 (1-2): 119-23. PMID 10363657.
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.
Engidawork E, Juranville JF, Fountoulakis M, et al. (2002). "Selective upregulation of the ubiquitin-proteasome proteolytic pathway proteins, proteasome zeta chain and isopeptidase T in fetal Down syndrome.". J. Neural Transm. Suppl. (61): 117-30. PMID 11771738.
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.
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.