@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 go: . @prefix Protein: . @prefix hgnc: . @prefix geneProductOf: . @prefix hasAgent: . @prefix proteinModification: . @prefix psimod: . @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 hasAgent: sub:_2; a go:0016301 . sub:_2 geneProductOf: hgnc:391; a Protein: . sub:_3 belv:variantOf hgnc:8614; a proteinModification:, psimod:00696 . sub:_4 occursIn: species:9606; rdf:object sub:_3; rdf:predicate belv:increases; rdf:subject sub:_1; a rdf:Statement . sub:assertion rdfs:label "kin(p(HGNC:AKT1)) -> p(HGNC:PAWR,pmod(P,S,249))" . } 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:_6; pav:version "1.4" . sub:_5 prov:value "mutations in the Par-4 gene have not been reported in cancer cells. Accordingly, endogenous Par-4 must be bound and functionally inactivated by an antiapoptotic protein, which prevents Par-4 from executing its proapoptotic functions. Indeed, our recent studies reveal that binding of Akt1 to Par-4 results in both Par-4 phosphorylation and inactivation of its proapoptotic potential (7)."; prov:wasQuotedFrom pubmed:16540633 . sub:_6 rdfs:label "Selventa" . sub:assertion prov:hadPrimarySource pubmed:16540633; prov:wasDerivedFrom beldoc:, sub:_5 . } sub:pubinfo { this: dct:created "2014-07-03T14:30:42.045+02:00"^^xsd:dateTime; pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 . }