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 .
}