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. This gene encodes a non-ATPase subunit of the 19S regulator base that functions as a chaperone protein during 26S proteasome assembly. [provided by RefSeq, Jul 2012],
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Function:
Domain:Rich in dileucine repeats, which have been implicated in trafficking of a variety of transmembrane proteins.,Function:Belongs to the 26S multisubunit protease, which is required for ubiquitin-dependent proteolysis. Does not bind ubiquitin polymers.,similarity:Belongs to the proteasome subunit S5B family.,subunit:26S protease is composed of a multicatalytic protease (proteasome) and a regulatory ATPase complex. Both are multisubunit structures that associate in the presence of ATP to form the protease. Subunit S5B is part of the regulatory complex.,
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Cellular Localization:
proteasome complex,nucleoplasm,cytosol,proteasome regulatory particle, base subcomplex,proteasome accessory complex,