PSMD11

From Wikipedia, the free encyclopedia
Proteasome (prosome, macropain) 26S subunit, non-ATPase, 11
Identifiers
SymbolsPSMD11; Rpn6; S9; p44.5
External IDsOMIM: 604449 MGI: 1916327 HomoloGene: 2108 GeneCards: PSMD11 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez571769077
EnsemblENSG00000108671ENSMUSG00000017428
UniProtO00231Q8BG32
RefSeq (mRNA)NM_001270482NM_178616
RefSeq (protein)NP_001257411NP_848731
Location (UCSC)Chr 17:
30.77 – 30.81 Mb
Chr 11:
80.43 – 80.47 Mb
PubMed search

26S proteasome non-ATPase regulatory subunit 11 is an enzyme that in humans is encoded by the PSMD11 gene.[1][2][3]

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.[3]

References

  1. Saito A, Watanabe TK, Shimada Y, Fujiwara T, Slaughter CA, DeMartino GN, Tanahashi N, Tanaka K (Jan 1998). "cDNA cloning and functional analysis of p44.5 and p55, two regulatory subunits of the 26S proteasome". Gene 203 (2): 241–50. doi:10.1016/S0378-1119(97)00524-6. PMID 9426256. 
  2. Hoffman L, Rechsteiner M (Apr 1997). "Molecular cloning and expression of subunit 9 of the 26S proteasome". FEBS Lett 404 (2–3): 179–84. doi:10.1016/S0014-5793(97)00126-9. PMID 9119060. 
  3. 3.0 3.1 "Entrez Gene: PSMD11 proteasome (prosome, macropain) 26S subunit, non-ATPase, 11". 

Further reading

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