a metastasis suppressor that regulates extracellular matrix remodeling and tumor survival. Binds to and inhibits Raf-1. Phosphorylation by classic and atypical but not novel PKC isoforms dissociates this complex, relieving inhibition of the Raf/MAP kinase signaling cascade. Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation. Cleaved into hippocampal cholinergic neurostimulating peptide (HCMP) that appears to be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Expressed in brain. Increased expression in aged senescence-accelerated mice. Note: This description may include information from UniProtKB.
Protein type: Protein kinase, regulatory subunit; Lipid binding protein
Cellular Component: cytoplasm; nucleus
Molecular Function: serine-type endopeptidase inhibitor activity; protein binding; enzyme binding; phosphatidylethanolamine binding; protein kinase binding; ATP binding
SS: 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.