PSMD12

From Wikipedia, the free encyclopedia


Proteasome (prosome, macropain) 26S subunit, non-ATPase, 12
Identifiers
Symbol(s) PSMD12; p55; MGC75406
External IDs OMIM: 604450 MGI: 1914247 HomoloGene: 2109
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 5718 66997
Ensembl ENSG00000197170 ENSMUSG00000020720
Uniprot O00232 Q3TRH2
Refseq XM_001134070 (mRNA)
XP_001134070 (protein)		 NM_025894 (mRNA)
NP_080170 (protein)
Location Chr 17: 62.76 - 62.79 Mb Chr 11: 107.3 - 107.31 Mb
Pubmed search [1] [2]

Proteasome (prosome, macropain) 26S subunit, non-ATPase, 12, also known as PSMD12, is a human gene.

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. A pseudogene has been identified on chromosome 3.[1]

[edit] References

  1. ^ Entrez Gene: PSMD12 proteasome (prosome, macropain) 26S subunit, non-ATPase, 12.

[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. 
  • Kanayama HO, Tamura T, Ugai S, et al. (1992). "Demonstration that a human 26S proteolytic complex consists of a proteasome and multiple associated protein components and hydrolyzes ATP and ubiquitin-ligated proteins by closely linked mechanisms.". Eur. J. Biochem. 206 (2): 567-78. PMID 1317798. 
  • 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. 
  • Saito A, Watanabe TK, Shimada Y, et al. (1998). "cDNA cloning and functional analysis of p44.5 and p55, two regulatory subunits of the 26S proteasome.". Gene 203 (2): 241-50. PMID 9426256. 
  • 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. 
  • 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. 
  • Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566-9. doi:10.1038/nbt810. PMID 12665801. 
  • 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. 
  • 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. 
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