@prefix this: . @prefix sub: . @prefix beldoc: . @prefix rdfs: . @prefix rdf: . @prefix xsd: . @prefix dct: . @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 "20131211" . 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: dct:created "2014-07-03T14:31:41.963+02:00"^^xsd:dateTime; pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 . }