@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 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:1341830; a Protein: . sub:_3 occursIn: species:10090; rdf:object sub:_1; rdf:predicate belv:increases; rdf:subject go:0034976; a rdf:Statement . sub:assertion rdfs:label "bp(GO:\"response to endoplasmic reticulum stress\") -> kin(p(MGI:Eif2ak3))" . } 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 "1.4" . sub:_4 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:_5 rdfs:label "Selventa" . sub:assertion prov:hadPrimarySource pubmed:17170114; prov:wasDerivedFrom beldoc:, sub:_4 . } sub:pubinfo { this: dct:created "2014-07-03T14:30:48.774+02:00"^^xsd:dateTime; pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 . }