The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Belongs to the peptidase T1A family. Note: This description may include information from UniProtKB.
Protein type: EC 220.127.116.11; Protease; Proteasome complex
Biological Process: positive regulation of NF-kappaB transcription factor activity; proteolysis; proteolysis involved in cellular protein catabolic process; skeletal muscle tissue development; ubiquitin-dependent protein catabolic process