Curated Information
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Home > Curated Information Page > PubMed Id: 11500364
Wang X, et al. (2001) Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase. EMBO J 20, 4370-9 11500364
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, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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S366-p - EEF2K (human)
Modsite: sPQVRtLsGSRPPLL SwissProt Entrez-Gene
Orthologous residues
EEF2K (human): S366‑p, EEF2K (mouse): S365‑p, EEF2K (rat): S365‑p
Characterization
Methods used to characterize site in vivo immunoprecipitation, phospho-antibody, western blotting
Relevant cell lines - cell types - tissues:  293 (epithelial), ES (stem)
Cellular systems studied:  cell lines
Species studied:  human
Enzymes shown to modify site in vitro
Type Enzyme
KINASE p70S6K (human)
KINASE p90RSK (human)
KINASE P70S6KB (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE p90RSK (human)
KINASE p70S6K (human) genetic knockout/knockin of upstream enzyme, pharmacological inhibitor of upstream enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
IGF-1 increase
rapamycin IGF-1 inhibit treatment-induced increase
LY294002 IGF-1 inhibit treatment-induced increase
PD184352 IGF-1 no effect upon treatment-induced increase
U0126 IGF-1 no effect upon treatment-induced increase
phorbol_ester increase
PD184352 phorbol_ester inhibit treatment-induced increase
rapamycin phorbol_ester no effect upon treatment-induced increase