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 .
}