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 "The signaling cascades from these two receptors join at IKK-like kinase, IKK-i and TBK-1, and these kinases play an important role in phosphorylation and activation of the type-I IFN transcription factor, interferon regulatory factor-3 (IRF-3) ... Qin et al. suggested that IRF-3 is autoinhibited in the resting state by interaction between the N-terminal helix of RD and SRR but that the phosphorylation of Ser385 and/or Ser386 in the 2S site induces destabilization of SRR leading to exposure and phosphorylation of Ser396, Ser398 and other Ser/Thr residues (Ser402, Thr404, Ser405) in the 5ST site that can disrupt the autoinhibitory structure (Qin et al. 2003). " ;
    prov:wasQuotedFrom pubmed:20604809 .
  sub:_6 rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:20604809 ;
    prov:wasDerivedFrom beldoc: , sub:_5 .
}