@prefix this: <http://www.tkuhn.ch/bel2nanopub/RArDm-xyBtNg3h7dT20d3hjMeghMjVutR-TwCSGIQOO6Q> .
@prefix sub: <http://www.tkuhn.ch/bel2nanopub/RArDm-xyBtNg3h7dT20d3hjMeghMjVutR-TwCSGIQOO6Q#> .
@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:76;
    a Protein: .
  
  sub:_2 geneProductOf: hgnc:1516;
    a Protein: .
  
  sub:_3 occursIn: species:9606;
    rdf:object sub:_2;
    rdf:predicate belv:increases;
    rdf:subject sub:_1;
    a rdf:Statement .
  
  sub:assertion rdfs:label "p(HGNC:ABL1) -> p(HGNC:CAT)" .
}

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 "The results demonstrate that catalase, a major effector of the cellular defence against hydrogen peroxide, interacts with c-Abl and Arg. The results show that hydrogen peroxide induced binding of c-Abl and Arg to catalase. The SH3 domains of c-Abl and Arg bound directly to catalase at a 293 PFNP296 site. c-Abl and Arg phosphorylated catalase at Tyr-231 and Tyr-386 in vitro and in the response of cells to Hydrogen peroxide. The functional significance of the interaction is supported by the demonstration that cells deficient in both c-Abl and Arg exhibit substantial increases in hydrogen peroxide levels. Cells expressing Myc-catalase and c-Abl also showed phosphorylation of catalase at tyrosine. By contrast, tyrosine phosphorylation of catalase was inhibited in cells expressing c-Abl (K-R-inactive mutant). Catalase was also subject to tyrosine phosphorylation in cells expressing kinase-active Arg, but not kinase-inactive Arg (K-R- inactive mutant). The deletion of catalase 293 PFNP296 site abrogates the interaction between ABL1 and catalase.";
    prov:wasQuotedFrom pubmed:12777400 .
  
  sub:_5 rdfs:label "Selventa" .
  
  sub:assertion prov:hadPrimarySource pubmed:12777400;
    prov:wasDerivedFrom beldoc:, sub:_4 .
}

sub:pubinfo {
  this: dct:created "2014-07-03T14:30:12.942+02:00"^^xsd:dateTime;
    pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 .
}