Official Full Name
caspase 14, apoptosis-related cysteine peptidase
Caspases are a family of cysteine proteases that are key mediators of programmed cell death or apoptosis.1 The precursor form of all caspases is composed of a prodomain and large and small catalytic subunits. The active forms of caspases are generated by several stimuli including ligand-receptor interactions, growth factor deprivation, and inhibitors of cellular functions. All known caspases require cleavage adjacent to aspartates to liberate one large and one small subunit, which associate into an a2b2 tetramer to form the active enzyme. Caspase-14 has a conserved active site pentapeptide, QACRG. However, no proteolytic or biological activities have been identified so far. Its high expression in embryonic tissues and limited expression in adult tissues suggests that it may have some role during ontogenesis.
CASP14; caspase 14, apoptosis-related cysteine peptidase; caspase 14, apoptosis related cysteine protease; caspase-14; apoptosis related cysteine protease; MGC119078; MGC119079; MICE; CASP-14; apoptosis-related cysteine protease; caspase 14, apoptosis-rel; caspase 14, apoptosis-related cysteine protease; CASP17; uncharacterized protein LOC776274; caspase-17/a