@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 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: mgi:1341830;
a Protein: .
sub:_3 belv:variantOf mgi:95299;
a proteinModification:, psimod:00696 .
sub:_4 occursIn: species:10090;
rdf:object sub:_3;
rdf:predicate belv:directlyIncreases;
rdf:subject sub:_1;
a rdf:Statement .
sub:assertion rdfs:label "kin(p(MGI:Eif2ak3)) => p(MGI:Eif2s1,pmod(P,S,52))" .
}
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 "{From full text} For example, phosphorylation of eIF2{alpha} by GCN2 (EIF2AK4) is enhanced by amino acid limitation, UV irradiation, and proteasome inhibition (13?16). Phosphorylation of eIF2{alpha} inhibits general protein synthesis by reducing the levels of eIF2-GTP that are required for binding of initiator tRNA to the translation apparatus. Concomitant with lowered protein synthesis, eIF2{alpha} phosphorylation leads to preferential translation of ATF4, a basic zipper (bZIP) transcription activator important for directing transcription of stress-related genes (17?20). Reduced protein synthesis conserves energy and provides the cell time for ATF4 and other stress-responsive transcription factors to reconfigure gene expression slated to alleviate damage elicited by the underlying stress. Other members of the eIF2 kinase family include PEK/Perk (EIF2AK3), whose activity is enhanced by endoplasmic reticulum (ER) stress (21, 22); HRI (EIF2AK1), which is regulated by heme deficiency and oxidative stress (23); and PKR (EIF2AK2), which functions in an antiviral pathway (24).{P@S52 is the common phosphorylation site between all 4 kinases and confirmed in Uniprot}";
prov:wasQuotedFrom pubmed:17170114 .
sub:_6 rdfs:label "Selventa" .
sub:assertion prov:hadPrimarySource pubmed:17170114;
prov:wasDerivedFrom beldoc:, sub:_5 .
}
sub:pubinfo {
this: dcterms:created "2014-07-03T14:30:48.777+02:00"^^xsd:dateTime;
pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 .
}