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" ; dc:license "Creative Commons Attribution-Non-Commercial-ShareAlike 3.0 Unported License" ; pav:authoredBysub:_7 ; pav:version "1.6" . sub:_6prov:value """Hydroxylation at two prolyl residues (Pro402 and Pro564 in human HIF-1α) mediates interactions with the von Hippel-Lindau (VHL) E3 ubiquitin ligase complex that targets HIF-α for proteasomal destruction28, 29, 30, 34. Each site can interact independently with VHL E3, potentially contributing to the extremely rapid proteolysis of HIF-α that is observed in oxygenated cells34. These sites contain a conserved LxxLAP motif and are targeted by a newly defined prolyl hydroxylase activity, that in mammalian cells is provided by three isoforms termed PHD (prolyl hydroxylase domain) 1-3 (refs. 31,32).""" ; prov:wasQuotedFrompubmed:12778166 . sub:_7rdfs:comment "support@belframework.org" ; rdfs:label "Selventa" . sub:assertionprov:hadPrimarySourcepubmed:12778166 ; prov:wasDerivedFrombeldoc: , sub:_6 . }