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: EC 184.108.40.206; Protein kinase, Ser/Thr (non-receptor); Autophagy; Protein kinase, STE; Kinase, protein; STE group; STE20 family; MST subfamily
Molecular Function: protein dimerization activity; protein serine/threonine kinase activator activity; protein serine/threonine kinase activity; identical protein binding; protein binding; protein homodimerization activity; magnesium ion binding; transcription factor binding; ATP binding; receptor signaling protein serine/threonine kinase activity
Biological Process: patterning of blood vessels; keratinocyte differentiation; negative regulation of cell proliferation; peptidyl-serine phosphorylation; central nervous system development; positive regulation of protein binding; apoptosis; positive regulation of apoptosis; protein amino acid autophosphorylation; cell morphogenesis; positive regulation of fat cell differentiation; signal transduction; neural tube formation; negative regulation of organ growth; protein amino acid phosphorylation
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.