. . . . . . . . . . . . . . . . . . . . . "TextLocation" . "Review" . "p(HGNC:RAF1,pmod(P,S,621)) => complex(p(HGNC:RAF1),p(SFAM:\"14-3-3 Family\"))" . "Approximately 2000 hand curated statements drawn from 57 PubMeds." . "Copyright (c) 2011-2012, Selventa. All Rights Reserved." . "BEL Framework Small Corpus Document" . "Creative Commons Attribution-Non-Commercial-ShareAlike 3.0 Unported License" . . "20131211" . "Phosphorylation. Raf is principally activated by phosphorylation of specific amino\nacid residues as shown for each isoform in Figure 4. From an evolutionary standpoint,\nthe Raf activation sites are highly conserved from yeast to humans. Several\namino acids in Raf, particularly serine (S) 259 and S621, which bind 14-3-3\nand maintain C-Raf in a closed auto-inhibited conformation, are phosphorylated\nin the basal state.137 On stimulation, Ras-GTP displaces 14-3-3 from S259, and\nC-Raf is translocated to the cell membrane, where it can be dephosphorylated at\nS259 by protein phosphatase 2A or other phosphatases.126 S259 also represents the\nsite of inhibitory phosphorylation by PKB/Akt, PKA, and serum glucocorticoid-inducible\nkinase.121,138,139 Phosphorylation at S621 seems to have greater significance\nbecause mutations at this site inactivate Raf's kinase activity. Hence,\na balance of phosphorylation and dephosphorylation is required to prime Raf in\nthe basal state before stimulation by Ras or mitogens.137" . . "support@belframework.org" . "Selventa" . . . . "2014-07-03T14:31:15.680+02:00"^^ . . .