Curated Information
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Home > Curated Information Page > PubMed Id: 15888551
Wang D, Sun H, Lang F, Yun CC (2005) Activation of NHE3 by dexamethasone requires phosphorylation of NHE3 at Ser663 by SGK1. Am J Physiol Cell Physiol 289, C802-10 15888551
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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S663-p - NHE3 (rabbit)
Modsite: TMRKRLEsFKSAKLG SwissProt Entrez-Gene
Orthologous residues
NHE3 (human): S663‑p, NHE3 (mouse): S659‑p, NHE3 (rat): S661‑p, NHE3 (rabbit): S663‑p
Methods used to characterize site in vivo [32P] ATP in vitro, immunoprecipitation, mutation of modification site, western blotting
Relevant cell lines - cell types - tissues:  IEC-6 (epithelial)
Cellular systems studied:  cell lines
Species studied:  opossum
Enzymes shown to modify site in vitro
Type Enzyme
KINASE SGK1 (human)
Comments:  Wild-type NHE-3 was phosphorylated on S663 while mutant S663A showed significantly less level of phosphorylation.
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
dexamethasone increase Dexamethasone induced NHE-3 activity was inhibited in S663A mutant but not at another serine residue S607A. Dexamethasone induces phosphorylation of S663 which precedes the increase in NHE-3 activity.
Downstream Regulation
Effect of modification (function):  activity, induced, intracellular localization
Comments:  Dexamthasone increases NHE-3 on the membrane surface in wild-type but not in S663A mutant.