@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 go: .
@prefix Protein: .
@prefix mgi: .
@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 hasAgent: sub:_2;
a go:0016301 .
sub:_2 geneProductOf: mgi:99928;
a Protein: .
sub:_3 hasAgent: sub:_4;
a go:0003824 .
sub:_4 geneProductOf: mgi:96550;
a Protein: .
sub:_5 hasAgent: sub:_6;
a go:0042789 .
sub:_6 geneProductOf: mgi:103035;
a Protein: .
sub:_7 rdf:object sub:_5;
rdf:predicate belv:directlyIncreases;
rdf:subject sub:_3;
a rdf:Statement .
sub:_8 occursIn: species:10090;
rdf:object sub:_7;
rdf:predicate belv:directlyIncreases;
rdf:subject sub:_1;
a rdf:Statement .
sub:assertion rdfs:label "cat(p(MGI:Il2rb)) => tscript(p(MGI:Stat5b))", "kin(p(MGI:Jak3)) => (cat(p(MGI:Il2rb)) => tscript(p(MGI:Stat5b)))" .
}
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:_10;
pav:version "20131211" .
sub:_10 rdfs:label "Selventa" .
sub:_9 prov:value "Stat5 proteins activated by IL-2. The phosphorylated tyrosines on IL-2Rbeta can then serve as docking sites for signaling molecules that otherwise cannot associate with IL-2Rbeta, including the adaptor protein Shc, Stat5a, and Stat5b (Figure 2). For example, only phosphorylated (but not non-phosphorylated) peptides spanning either Tyr-392 or Tyr-510 of IL-2Rbeta can efficiently compete with IL-2-induced Stat5 DNA binding to a GAS motif IL-2-mediated hetero-dimerization of its receptor triggers a rapid increase in the recruitment of Jak3 and activation of both Jak1 and Jak3 (Johnston et al., 1994; Witthuhn et al., 1994). These kinases phosphorylate the receptor as well as each other, and activate other signaling molecules associated with the receptor. The phosphorylated tyrosines on IL-2Rbeta can then serve as docking sites for signaling molecules that otherwise cannot associate with IL-2Rbeta, including the adaptor protein Shc, Stat5a, and Stat5b";
prov:wasQuotedFrom pubmed:10851055 .
sub:assertion prov:hadPrimarySource pubmed:10851055;
prov:wasDerivedFrom beldoc:, sub:_9 .
}
sub:pubinfo {
this: dcterms:created "2014-07-03T14:31:35.798+02:00"^^xsd:dateTime;
pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 .
}