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 "Src, Lyn and Lck tyrosine kinases phosphorylate DAPP1 at Tyr(139) in vitro at similar rates in the presence or absence of PtdIns(3,4,5)P(3), and overexpression of these kinases in HEK-293 cells induces the phosphorylation of Tyr(139). co-expression of DAPP1 with Src, Lyn or Lck induced a very high level of phosphorylation of DAPP1 at Tyr139, even in unstimulated cells, which was not increased further by agonist stimulation of cells. As Src-family kinases activate the PI 3-kinase pathway in many cells [1], it is possible that the overexpression of Src, Lyn or Lck in HEK-293 cells induces the activation of PI 3-kinase, thereby promoting DAPP1 phosphorylation in unstimulated cells. As Src-family tyrosine kinases are located at the plasma membrane by virtue of myristoylation and palmitoylation of their N-termini [26], it is likely that the role of PtdIns(3,4,5)P3 is to recruit DAPP1 to the cell membrane, where it can be phosphorylated with Src-family tyrosine kinases." ;
    prov:wasQuotedFrom pubmed:10880360 .
  sub:_6 rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:10880360 ;
    prov:wasDerivedFrom beldoc: , sub:_5 .
}