Curated Information
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Curated Information Page
PubMed Id: 9930704 
Harding HP, Zhang Y, Ron D (1999) Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397, 271-4 9930704
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
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S52-p - eIF2-alpha (human)
Orthologous residues
eIF2‑alpha (human): S52‑p, eIF2‑alpha (mouse): S52‑p, eIF2‑alpha (rat): S52‑p, eIF2‑alpha (rabbit): S51‑p, eIF2‑alpha (fruit fly): S51‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, immunoprecipitation, mutation of modification site
 Relevant cell lines - cell types - tissues:  3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout], COS (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  monkey, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PERK (human)


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