sub:provenance {
  beldoc: dce:description "Approximately 61,000 statements." ;
    dce:rights "Copyright (c) 2011-2012, Selventa. All rights reserved." ;
    dce:title "BEL Framework Large Corpus Document" ;
    pav:authoredBy sub:_6 ;
    pav:version "20131211" .
  sub:_5 prov:value "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." ;
    prov:wasQuotedFrom pubmed:16962653 .
  sub:_6 rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:16962653 ;
    prov:wasDerivedFrom beldoc: , sub:_5 .
}