. . . . . . . . . . . . . . . . . "kin(p(HGNC:PDPK1)) => kin(p(HGNC:AKT2))" . "Approximately 61,000 statements." . "Copyright (c) 2011-2012, Selventa. All rights reserved." . "BEL Framework Large Corpus Document" . . "1.4" . "identified four sites (Ser-124, Thr-308, Thr-450, and Ser-473) on Akt1 that are phosphorylated in vivo. Thr-308 and Ser-473 are inducibly phosphorylated after treatment of cells with extracellular stimuli, whereas Ser-124 and Thr-450 appear to be basally phosphorylated The third mechanism by which 3'-phosphorylated phosphoinositides regulate Akt activity is by controlling the accessibility of Akt as a substrate for PDKs. In in vitro reconstitution assays, the binding of PI3,4,5P to the Akt PH domain is required for PDK-1 to phosphorylate Akt In addition, PDK-1 complexed with either a fragment of PRK2, PRK2, or a PRK2-related peptide may be regulated by increased phospholipid concentrations" . . "Selventa" . . . . "2014-07-03T14:29:49.379+02:00"^^ . . .