a protein kinase of the STE20 family. Proteolytically activated by caspase during apoptosis. Activated by apoptotic signals as well as other stress conditions. Full activation requires both phosphorylation and caspase-mediated cleavage. Phosphorylation at serine 327 of Mst1, which is close to the caspase-3 recognition site, inhibits caspase-mediated cleavage. Note: This description may include information from UniProtKB.
Protein type: Autophagy; EC 188.8.131.52; Kinase, protein; MST subfamily; Protein kinase, STE; Protein kinase, Ser/Thr (non-receptor); STE group; STE20 family
Cellular Component: cytoplasm; cytosol; nuclear body; nucleoplasm; nucleus; protein complex
Molecular Function: ATP binding; identical protein binding; magnesium ion binding; protein binding; protein dimerization activity; protein homodimerization activity; protein kinase activity; protein serine/threonine kinase activator activity; protein serine/threonine kinase activity; transcription factor binding
Biological Process: apoptosis; branching involved in blood vessel morphogenesis; cell morphogenesis; central nervous system development; endocardium development; keratinocyte differentiation; negative regulation of canonical Wnt signaling pathway; negative regulation of cell proliferation; negative regulation of organ growth; neural tube formation; peptidyl-serine phosphorylation; positive regulation of apoptosis; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; positive regulation of fat cell differentiation; positive regulation of peptidyl-serine phosphorylation; positive regulation of protein binding; positive regulation of protein phosphorylation; positive regulation of protein serine/threonine kinase activity; protein amino acid phosphorylation; protein autophosphorylation; protein stabilization; regulation of mitotic cell cycle; signal transduction; stress-activated protein kinase signaling pathway