. . . . . . . . . . . . . . . . "p(SFAM:\"AKT Family\",pmod(P,T,308)) => kin(p(SFAM:\"AKT Family\"))" . "Approximately 61,000 statements." . "Copyright (c) 2011-2012, Selventa. All rights reserved." . "BEL Framework Large Corpus Document" . . "20131211" . "We next examined the Akt T-loop Thr308 phosphorylation in wild-type and SIN1-/- cells. We found that although Ser473 phosphorylation was completely abolished in the SIN1-/- cells, Thr308 phosphorylation of Akt was not blocked (Figure 3A). These results indicate that SIN1 is not essential for Akt Thr308 phosphorylation and that the Ser473 phosphorylation is not a prerequisite for Thr308 phosphorylation. Akt, Singly Phosphorylated at Thr308, Remains Active and Functional in Response to Growth Factor Stimulation in SIN1-/- Cells Since Akt Thr308 phosphorylation was not dependent on Ser473 phosphorylation in SIN1-/- cells, we then asked whether this Thr308 singly phosphorylated Akt is still active and whether lack of Ser473 phosphorylation would have a global effect on the phosphorylation of Akt targets. Using an in vitro kinase assay, we found that Akt retained a substantial amount of enzymatic activity in SIN1-/- cells, although lower than that in wild-type cells (Figure 3B). Thus, singly phosphorylated (Thr308) Akt is an active but weaker enzyme." . . "Selventa" . . . . "2014-07-03T14:33:03.254+02:00"^^ . . .