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 """In a second hydroxylation-dependent control, b-hydroxylation of an asparaginyl residue
in the C-terminal activation domain of HIF-a (N803 in human HIF-1a) is regulated
by a HIF asparaginyl hydroxylase called FIH (factor inhibiting HIF) [62,63].
Hydroxylation at this site prevents the binding of the transcriptional co-activators
p300/CBP (CREB binding protein). Under normoxic conditions, these hydroxylation
reactions provide a dual mechanism for HIF inactivation that involves proteolytic
destruction and the inhibition of transcriptional activity [64].""" ;
    prov:wasQuotedFrom pubmed:15350900 .
  sub:_7 rdfs:comment "support@belframework.org" ;
    rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:15350900 ;
    prov:wasDerivedFrom beldoc: , sub:_6 .
}