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 "Once stimulated, FAK undergoes autophosphorylation at tyrosine (Y) 397, followed by phosphorylation of several sites including Y576/Y577 which increases FAK's kinase activity, as well as at Y407, Y861, and Y925.   Also from full text... Activation of FAK is largely accomplished via its phosphorylation. The initial activation step is autophosphorylation at tyrosine 397 which becomes a site for binding the oncogene Src and the p85 subunit of phosphatidylinositol 3-kinase kinase through their SH2 domains [9]. Subsequently, Y576 and Y577 in the kinase loop are phosphorylated which increases FAK’s catalytic activity. Phosphorylation of Y925 produces a binding site for the SH2 domain of the adapter protein Grb2 which then assembles a signaling complex including Ras and Sos, and ultimately activates the ERK pathway [9]." ;
    prov:wasQuotedFrom pubmed:15694384 .
  sub:_6 rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:15694384 ;
    prov:wasDerivedFrom beldoc: , sub:_5 .
}