PSMD9

From Wikipedia, the free encyclopedia

Proteasome (prosome, macropain) 26S subunit, non-ATPase, 9

Identifiers

PSMD9; MGC8644; p27

External IDs

OMIM: 603146 MGI: 1914401 HomoloGene: 2106

Gene ontology
Molecular Function:	• molecular_function • protein binding
Cellular Component:	• cytosol • proteasome regulatory particle (sensu Eukaryota)
Biological Process:	• ubiquitin-dependent protein catabolic process

Orthologs

Human

Mouse

Refseq

NM_002813 (mRNA)
NP_002804 (protein)

NM_026000 (mRNA)
NP_080276 (protein)

Location

Chr 12: 120.81 - 120.84 Mb

Chr 5: 123.49 - 123.51 Mb

Pubmed search

[1]

[2]

Proteasome (prosome, macropain) 26S subunit, non-ATPase, 9, also known as PSMD9, is a human gene.^[1]

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core 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. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase 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 non-ATPase subunit of the 19S regulator.^[1]

[edit] References

^ ^a ^b Entrez Gene: PSMD9 proteasome (prosome, macropain) 26S subunit, non-ATPase, 9.

[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.
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.
Watanabe TK, Saito A, Suzuki M, et al. (1998). "cDNA cloning and characterization of a human proteasomal modulator subunit, p27 (PSMD9).". Genomics 50 (2): 241–50. PMID 9653651.
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.
Thomas MK, Yao KM, Tenser MS, et al. (2000). "Bridge-1, a novel PDZ-domain coactivator of E2A-mediated regulation of insulin gene transcription.". Mol. Cell. Biol. 19 (12): 8492–504. PMID 10567574.
Tanahashi N, Murakami Y, Minami Y, et al. (2000). "Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis.". J. Biol. Chem. 275 (19): 14336–45. PMID 10799514.
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.
Ciarallo S, Subramaniam V, Hung W, et al. (2002). "Altered p27(Kip1) phosphorylation, localization, and function in human epithelial cells resistant to transforming growth factor beta-mediated G(1) arrest.". Mol. Cell. Biol. 22 (9): 2993–3002. PMID 11940657.
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.
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.
Hedberg Y, Ljungberg B, Roos G, Landberg G (2003). "Expression of cyclin D1, D3, E, and p27 in human renal cell carcinoma analysed by tissue microarray.". Br. J. Cancer 88 (9): 1417–23. doi:10.1038/sj.bjc.6600922. PMID 12778072.
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.
Mangeat B, Turelli P, Caron G, et al. (2003). "Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts.". Nature 424 (6944): 99–103. doi:10.1038/nature01709. PMID 12808466.
Harris RS, Bishop KN, Sheehy AM, et al. (2003). "DNA deamination mediates innate immunity to retroviral infection.". Cell 113 (6): 803–9. PMID 12809610.