a tyrosine kinase-like kinase of the RAF family. Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May play a role in the postsynaptic responses of hippocampal neuron. Frequently mutated in thyroid cancers, skin melanomas and at lower frequency in a wide range of human cancers. An activating mutation, mimicking phosphorylation of the activation loop, is seen in 60% of malignant melanoma samples. Raf mutations are generally exclusive to Ras activating mutations. Activating mutations are also seen in ~10% of colorectal cancers, in lung cancers and gliomas, and at a lower rate in several other tumors. Inactivating mutations are also seen and may result in activation of c-Raf and Erk. Mutations in B-Raf, MEK1 and MEK2 also associated with cardiofaciocutaneous syndrome, displaying morphological, cardiac and mental defects. Approved Inhibitor: Nexavar/Sorafenib. Note: This description may include information from UniProtKB.
Protein type: Protein kinase, Ser/Thr (non-receptor); Protein kinase, TKL; EC 22.214.171.124; Kinase, protein; TKL group; RAF family
Molecular Function: protein serine/threonine kinase activity; protein binding; metal ion binding; receptor signaling protein activity; ATP binding; protein kinase activity
Biological Process: regulation of proteasomal ubiquitin-dependent protein catabolic process; protein modification process; protein amino acid phosphorylation; positive regulation of peptidyl-serine phosphorylation; regulation of TOR signaling pathway; negative regulation of apoptosis
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.