@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 hgnc: . @prefix proteinModification: . @prefix psimod: . @prefix go: . @prefix Protein: . @prefix geneProductOf: . @prefix hasAgent: . @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 belv:variantOf hgnc:9393; a proteinModification:, psimod:00696 . sub:_2 hasAgent: sub:_3; a go:0016301 . sub:_3 geneProductOf: hgnc:9393; a Protein: . sub:_4 occursIn: species:9606; rdf:object sub:_2; rdf:predicate belv:directlyIncreases; rdf:subject sub:_1; a rdf:Statement . sub:assertion rdfs:label "p(HGNC:PRKCA,pmod(P,T,638)) => kin(p(HGNC:PRKCA))" . } 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 "20131211" . sub:_5 prov:value "The T638 phosphorylation site is not required for the catalytic function of PKCalpha per se, but serves to control the duration of activation by regulating the rate of dephosphorylation and inactivation of the protein. This is achieved through the cooperative interaction between the T638 and T497 sites; if either of these residues is not phosphorylated, the protein is supersensitive to phosphatase action."; prov:wasQuotedFrom pubmed:8805373 . sub:_6 rdfs:label "Selventa" . sub:assertion prov:hadPrimarySource pubmed:8805373; prov:wasDerivedFrom beldoc:, sub:_5 . } sub:pubinfo { this: dct:created "2014-07-03T14:33:53.913+02:00"^^xsd:dateTime; pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 . }