Curated Information

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Curated Information Page

PubMed Id: 9930704

This page summarizes selected information from the article 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.

Harding HP, Zhang Y, Ron D (1999) Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397, 271-4 9930704

S52-p - eIF2-alpha (human)

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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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