a protein kinase of the STE20 family. Activated by apoptotic signals as well as other stress conditions. Full activation requires both phosphorylation and caspase-mediated cleavage. Following cleavage by caspase-3, undergoes irreversible autophosphorylation. Full-length is mainly unphosphorylated in the rat thymus and cultured cells, whereas caspase-3-cleaved MST2 in apoptotic cells is highly phosphorylated. Note: This description may include information from UniProtKB.
Protein type: Protein kinase, Ser/Thr (non-receptor); Protein kinase, STE; Kinase, protein; Autophagy; EC 126.96.36.199; STE group; STE20 family; MST subfamily
Cellular Component: protein complex; cytoplasm; cytosol; nucleus
Molecular Function: protein dimerization activity; protein serine/threonine kinase activator activity; protein serine/threonine kinase activity; protein binding; MAP kinase kinase kinase activity; magnesium ion binding; ATP binding; protein kinase activity
Biological Process: central nervous system development; positive regulation of protein binding; protein stabilization; activation of MAPKK activity; apoptosis; positive regulation of apoptosis; regulation of mitotic cell cycle; MAPKKK cascade; positive regulation of JNK cascade; negative regulation of organ growth; signal transduction; protein amino acid phosphorylation; regulation of apoptosis; negative regulation of cell proliferation; positive regulation of protein kinase B signaling cascade; stress-activated protein kinase signaling pathway; positive regulation of fat cell differentiation; positive regulation of transcription factor activity; neural tube formation
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.