PSMA3

From Wikipedia, the free encyclopedia

Proteasome (prosome, macropain) subunit, alpha type, 3

PDB rendering based on 1iru.

Available structures: 1iru

Identifiers

Symbol(s)

PSMA3; HC8; MGC12306; MGC32631; PSC3

External IDs

OMIM: 176843 MGI: 104883 HomoloGene: 2082

Gene ontology
Molecular Function:	• threonine endopeptidase activity • protein binding
Cellular Component:	• nucleus • cytoplasm • 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_002788 (mRNA)
NP_002779 (protein)

NM_011184 (mRNA)
NP_035314 (protein)

Location

Chr 14: 57.78 - 57.81 Mb

n/a

Pubmed search

[1]

[2]

Proteasome (prosome, macropain) subunit, alpha type, 3, also known as PSMA3, is a human gene.

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. Two alternative transcripts encoding different isoforms have been identified.^[1]

[edit] References

^ Entrez Gene: PSMA3 proteasome (prosome, macropain) subunit, alpha type, 3.

[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.
Tamura T, Lee DH, Osaka F, et al. (1991). "Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes).". Biochim. Biophys. Acta 1089 (1): 95–102. PMID 2025653.
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.
Akioka H, Forsberg NE, Ishida N, et al. (1995). "Isolation and characterization of the HC8 subunit gene of the human proteasome.". Biochem. Biophys. Res. Commun. 207 (1): 318–23. doi:10.1006/bbrc.1995.1190. PMID 7857283.
Castaño JG, Mahillo E, Arizti P, Arribas J (1996). "Phosphorylation of C8 and C9 subunits of the multicatalytic proteinase by casein kinase II and identification of the C8 phosphorylation sites by direct mutagenesis.". Biochemistry 35 (12): 3782–9. doi:10.1021/bi952540s. PMID 8619999.
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.
Gerards WL, de Jong WW, Bloemendal H, Boelens W (1998). "The human proteasomal subunit HsC8 induces ring formation of other alpha-type subunits.". J. Mol. Biol. 275 (1): 113–21. doi:10.1006/jmbi.1997.1429. PMID 9451443.
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.
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.
Connell P, Ballinger CA, Jiang J, et al. (2001). "The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins.". Nat. Cell Biol. 3 (1): 93–6. doi:10.1038/35050618. PMID 11146632.
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.
Boelens WC, Croes Y, de Jong WW (2001). "Interaction between alphaB-crystallin and the human 20S proteasomal subunit C8/alpha7.". Biochim. Biophys. Acta 1544 (1-2): 311–9. PMID 11341940.
Touitou R, Richardson J, Bose S, et al. (2001). "A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome.". EMBO J. 20 (10): 2367–75. doi:10.1093/emboj/20.10.2367. PMID 11350925.
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.
Claverol S, Burlet-Schiltz O, Girbal-Neuhauser E, et al. (2003). "Mapping and structural dissection of human 20 S proteasome using proteomic approaches.". Mol. Cell Proteomics 1 (8): 567–78. PMID 12376572.
Bae MH, Jeong CH, Kim SH, et al. (2003). "Regulation of Egr-1 by association with the proteasome component C8.". Biochim. Biophys. Acta 1592 (2): 163–7. PMID 12379479.
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.