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. This subunit has been shown to interact with an orphan member of the nuclear hormone receptor superfamily highly expressed in liver, and with gankyrin, a liver oncoprotein. Two transcript variants encoding different isoforms have been identified.
26S protease regulatory subunit 6B; 26S proteasome AAA-ATPase subunit RPT3; 26S proteasome regulatory subunit 6B; CAR interacing protein 21; CAR interacting protein 21; CIP21; MB67-interacting protein; MGC13687; MGC23214; MGC8570; MIP224; protease 26S subunit 6; proteasome (prosome, macropain) 26S subunit, ATPase, 4; proteasome 26S ATPase subunit 4; proteasome 26S subunit ATPase 4; proteasome 26S subunit, ATPase 4; PSMC4; RPT3; S6; S6 ATPase; Tat-binding protein 7; TBP7; TBP-7
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