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 "1.4" .
  sub:_5 prov:value "Structural studies of Akt revealed that the HM phosphorylation facilitates interaction of this motif with the N lobe of the catalytic domain of Akt, which in turn promotes a disorder to order transition of the aC helix (Yang et al., 2002a, 2002b). The restructured/ ordered aC helix was implied to set the substrate specificity of Akt (Yang et al., 2002a). Despite being widely used as a key indicator of Akt activation, the precise physiological function of Ser473 phosphorylation site remains to be fully understood. The kinase that phosphorylates the HMsite of Akt, often referred to as PDK2, has been controversial. Various kinases have been proposed to act as the PDK2 for Akt, including ILK, DNA-PK, and PKC (Bayascas and Alessi, 2005; Dong and Liu, 2005; Feng et al., 2004; Kawakami et al., 2004; Troussard et al., 2003; Woodgett, 2005). However, despite a lack of genetic evidence, recent biochemical studies have strongly suggested that TORC2 is the elusive PDK2 for Akt Ser473 (Hresko and Mueckler, 2005; Sarbassov et al., 2005b)." ;
    prov:wasQuotedFrom pubmed:16962653 .
  sub:_6 rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:16962653 ;
    prov:wasDerivedFrom beldoc: , sub:_5 .
}