a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspase APAF1; this step is thought to be one of the earliest in the caspase activation cascade. Alternative splicing results in two isoforms. Note: This description may include information from UniProtKB.
Molecular Function: peptidase activity; protein binding; cysteine-type endopeptidase activity; SH3 domain binding; protein kinase binding; cysteine-type peptidase activity
Biological Process: caspase activation; positive regulation of apoptosis; apoptosis; DNA damage response, signal transduction; response to lipopolysaccharide; proteolysis; response to organic cyclic substance; response to estradiol stimulus; response to antibiotic; regulation of apoptosis; DNA damage response, signal transduction resulting in induction of apoptosis; positive regulation of neuron apoptosis; response to cobalt ion; response to DNA damage stimulus; aging; response to UV
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.