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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 ATPase subunits, a member of the triple-A family of ATPases which have a chaperone-like activity. In addition to participation in proteasome functions, this subunit may participate in transcriptional regulation since it has been shown to interact with the thyroid hormone receptor and retinoid X receptor-alpha. Two transcript variants encoding different isoforms have been found for this gene.
Gene Name: | proteasome (prosome, macropain) 26S subunit, ATPase, 5 |
Family/Subfamily: | ATPase , not assigned-ATPase |
Synonyms: | PSMC5, p45, S8, Tat-binding protein homolog 10, SUG-1, MSUG1 protein, Thyroid receptor interactor 1, SUG1, TBP10, p45/SUG, Proteasome subunit p45, TRIP1 |
Target Sequences: | NM_002805 NP_002796.4 P62195 |
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