PSMD3

From Wikipedia, the free encyclopedia


Proteasome (prosome, macropain) 26S subunit, non-ATPase, 3
Identifiers
Symbol(s) PSMD3; P58; RPN3; S3
External IDs MGI: 98858 HomoloGene: 2102
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 5709 22123
Ensembl ENSG00000108344 ENSMUSG00000017221
Uniprot O43242 Q3TP95
Refseq NM_002809 (mRNA)
NP_002800 (protein)		 NM_009439 (mRNA)
NP_033465 (protein)
Location Chr 17: 35.39 - 35.41 Mb Chr 11: 98.5 - 98.51 Mb
Pubmed search [1] [2]

Proteasome (prosome, macropain) 26S subunit, non-ATPase, 3, also known as PSMD3, 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 one of the non-ATPase subunits of the 19S regulator lid.[1]

[edit] References

  1. ^ a b Entrez Gene: PSMD3 proteasome (prosome, macropain) 26S subunit, non-ATPase, 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. 
  • Kominami K, Okura N, Kawamura M, et al. (1997). "Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1.". Mol. Biol. Cell 8 (1): 171–87. PMID 9017604. 
  • 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. 
  • 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. 
  • 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. 
  • Harris RS, Sheehy AM, Craig HM, et al. (2003). "DNA deamination: not just a trigger for antibody diversification but also a mechanism for defense against retroviruses.". Nat. Immunol. 4 (7): 641–3. doi:10.1038/ni0703-641. PMID 12830140. 
  • Gu Y, Sundquist WI (2003). "Good to CU.". Nature 424 (6944): 21–2. doi:10.1038/424021a. PMID 12840737. 
  • Mariani R, Chen D, Schröfelbauer B, et al. (2003). "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.". Cell 114 (1): 21–31. PMID 12859895. 
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