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- _6 value "Raf is also phosphorylated at other serine and threonine residues, the most important of which are S338 and tyrosine (Y) 341, which are situated adjacent to the C-Raf kinase domain.140 Phosphorylation of these residues relieves the inhibitory effects of the regulatory domain on the kinase domain.141 S338, which is the evolutionarily conserved PAK phosphorylation site that resides on the amino-terminal side of the kinase domain, is critical for Raf activation.134-136,140,142 This site is also phosphorylated in response to stimulation by growth factors, integrins, Ras, PAK1, and PAK3.78,136,143" provenance.
- _6 wasQuotedFrom 16170185 provenance.