@prefix dcterms: .
@prefix this: .
@prefix sub: .
@prefix beldoc: .
@prefix rdfs: .
@prefix rdf: .
@prefix xsd: .
@prefix dce: .
@prefix pav: .
@prefix np: .
@prefix belv: .
@prefix prov: .
@prefix Protein: .
@prefix mgi: .
@prefix geneProductOf: .
@prefix species: .
@prefix occursIn: .
@prefix pubmed: .
@prefix orcid: .
sub:Head {
this: np:hasAssertion sub:assertion;
np:hasProvenance sub:provenance;
np:hasPublicationInfo sub:pubinfo;
a np:Nanopublication .
}
sub:assertion {
sub:_1 geneProductOf: mgi:87859;
a Protein: .
sub:_2 geneProductOf: mgi:1270860;
a Protein: .
sub:_3 occursIn: species:10090;
rdf:object sub:_2;
rdf:predicate belv:increases;
rdf:subject sub:_1;
a rdf:Statement .
sub:assertion rdfs:label "p(MGI:Abl1) -> p(MGI:Plscr2)" .
}
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 "Phospholipid scramblase 1 (PLSCR1) is a plasma membrane protein that has been proposed to play a role in the transbilayer movement of plasma membrane phospholipids. PLSCR1 contains multiple proline-rich motifs resembling Src homology 3 (SH3) domain-binding sites, which highly specific for binding to the Abl SH3 domain. Endogenous PLSCR1 was immunoprecipitated from either Abl-/- or Abl+/+ murine fibroblasts using antibody specific for murine PLSCR1 the data indicated that Tyr phosphorylation of PLSCR1 detected in the Abl+/+ fibroblasts was virtually abolished in the Abl-/- fibroblasts, implying that the c-Abl kinase accounts for most, if not all, of the Tyr phosphorylation of PLSCR1 detected in mammalian cells.";
prov:wasQuotedFrom pubmed:11390389 .
sub:_5 rdfs:label "Selventa" .
sub:assertion prov:hadPrimarySource pubmed:11390389;
prov:wasDerivedFrom beldoc:, sub:_4 .
}
sub:pubinfo {
this: dcterms:created "2014-07-03T14:29:56.456+02:00"^^xsd:dateTime;
pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 .
}