@prefix this: <http://www.tkuhn.ch/bel2nanopub/RAZ4-s-WZDkWOf7oND0EPyYtCCfIN_vkFCrOIbBuIZbXw> .
@prefix sub: <http://www.tkuhn.ch/bel2nanopub/RAZ4-s-WZDkWOf7oND0EPyYtCCfIN_vkFCrOIbBuIZbXw#> .
@prefix beldoc: <http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel> .
@prefix rdfs: <http://www.w3.org/2000/01/rdf-schema#> .
@prefix rdf: <http://www.w3.org/1999/02/22-rdf-syntax-ns#> .
@prefix xsd: <http://www.w3.org/2001/XMLSchema#> .
@prefix dct: <http://purl.org/dc/terms/> .
@prefix dce: <http://purl.org/dc/elements/1.1/> .
@prefix pav: <http://purl.org/pav/> .
@prefix np: <http://www.nanopub.org/nschema#> .
@prefix belv: <http://www.selventa.com/vocabulary/> .
@prefix prov: <http://www.w3.org/ns/prov#> .
@prefix Protein: <http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI_36080> .
@prefix hgnc: <http://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=> .
@prefix geneProductOf: <http://purl.obolibrary.org/obo/RO_0002204> .
@prefix species: <http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?id=> .
@prefix occursIn: <http://purl.obolibrary.org/obo/BFO_0000066> .
@prefix pubmed: <http://www.ncbi.nlm.nih.gov/pubmed/> .
@prefix orcid: <http://orcid.org/> .
sub:Head {
   this: np:hasAssertion sub:assertion ;
    np:hasProvenance sub:provenance ;
    np:hasPublicationInfo sub:pubinfo ;
    a np:Nanopublication .
}
sub:assertion {
   sub:_1 geneProductOf: hgnc:12687 ;
    a Protein: .
  sub:_2 geneProductOf: hgnc:4910 ;
    a Protein: .
  sub:_3 occursIn: species:9606 ;
    rdf:object sub:_2 ;
    rdf:predicate belv:decreases ;
    rdf:subject sub:_1 ;
    a rdf:Statement .
  sub:assertion rdfs:label "p(HGNC:VHL) -| p(HGNC:HIF1A)" .
}
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:_5 ;
    pav:version "1.4" .
  sub:_4 prov:value "Hypoxia-inducible factor (HIF) is a master transcriptional regulator of hypoxia-inducible genes and consists of a labile alpha subunit (such as HIF1alpha) and a stable beta subunit (such as HIF1beta or ARNT). In the presence of oxygen, HIFalpha family members are hydroxylated on one of two conserved prolyl residues by members of the egg-laying-defective nine (EGLN) family. Prolyl hydroxylation generates a binding site for a ubiquitin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor protein, which results in HIFalpha destruction. In addition, the HIFalpha transcriptional activation function is modulated further by asparagine hydroxylation by FIH (factor-inhibiting HIF), which affects recruitment of the coactivators p300 and CBP. These findings provide new mechanistic insights into oxygen sensing by metazoans and are the first examples of protein hydroxylation being used in intracellular signaling. The existence of three human EGLN family members, as well as other putative hydroxylases, raises the possibility that this signal is used in other contexts by other proteins. In the presence of oxygen, HIFalpha family members are hydroxylated on one of two conserved prolyl residues by members of the egg-laying-defective nine (EGLN) family. Prolyl hydroxylation generates a binding site for a ubiquitin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor protein, which results in HIFalpha destruction." ;
    prov:wasQuotedFrom pubmed:15952883 .
  sub:_5 rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:15952883 ;
    prov:wasDerivedFrom beldoc: , sub:_4 .
}
sub:pubinfo {
   this: dct:created "2014-07-03T14:30:36.021+02:00"^^xsd:dateTime ;
    pav:createdBy orcid:0000-0001-6818-334X , orcid:0000-0002-1267-0234 .
}