|FUNCTION: 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. MAY CATALYZE BASAL PROCESSING OF INTRACELLULAR ANTIGENS.
* CATALYTIC ACTIVITY: Cleavage at peptide bonds with very broad specificity.
* PATHWAY: Involved in an ATP/ubiquitin-dependent non-lysosomal proteolytic pathway.
* SUBUNIT: The proteasome is composed of at least 15 non identical subunits which form a highly ordered ring-shaped structure. This subunit can be displaced by the equivalent immune-specific subunit PSMB9.
* SUBCELLULAR LOCATION: Cytoplasmic and nuclear.
* SIMILARITY: BELONGS TO PEPTIDASE FAMILY T1B.
Last Update 13-Mar-03