sub:provenance {
  beldoc: dce:description "Approximately 2000 hand curated statements drawn from 57 PubMeds." ;
    dce:rights "Copyright (c) 2011-2012, Selventa. All Rights Reserved." ;
    dce:title "BEL Framework Small Corpus Document" ;
    dcterms:license "Creative Commons Attribution-Non-Commercial-ShareAlike 3.0 Unported License" ;
    pav:authoredBy sub:_7 ;
    pav:version "1.6" .
  sub:_6 prov:value """Raf is also phosphorylated at other serine and threonine residues, the most important
of which are S338 and tyrosine (Y) 341, which are situated adjacent to the
C-Raf kinase domain.140  Phosphorylation of these residues relieves the inhibitory
effects of the regulatory domain on the kinase domain.141  S338, which is the
evolutionarily conserved PAK phosphorylation site that resides on the amino-terminal
side of the kinase domain, is critical for Raf activation.134-136,140,142
This site is also phosphorylated in response to stimulation by growth factors,
integrins, Ras, PAK1, and PAK3.78,136,143""" ;
    prov:wasQuotedFrom pubmed:16170185 .
  sub:_7 rdfs:comment "support@belframework.org" ;
    rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:16170185 ;
    prov:wasDerivedFrom beldoc: , sub:_6 .
}