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:_6 ;
    pav:version "1.6" .
  sub:_5 prov:value """Hydroxylation at two proline residues on the HIF polypeptide mediates interactions
between the b-domain of the von Hippel–Lindau protein (pVHL) and HIF [60]. Each
site can interact independently with pVHL, potentially contributing to the extremely
rapid proteolysis of HIF-a that is observed under normoxic conditions. These
sites contain a conserved LxxLAP motif and are targeted by proline hydroxylases
(PHD) that, in mammalian cells, are provided by three isoforms termed PHD 1–3
[61].""" ;
    prov:wasQuotedFrom pubmed:15350900 .
  sub:_6 rdfs:comment "support@belframework.org" ;
    rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:15350900 ;
    prov:wasDerivedFrom beldoc: , sub:_5 .
}