Curated Information
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Curated Information Page
PubMed Id: 17360471 
Ring AM, et al. (2007) An SGK1 site in WNK4 regulates Na+ channel and K+ channel activity and has implications for aldosterone signaling and K+ homeostasis. Proc Natl Acad Sci U S A 104, 4025-9 17360471
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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S1169-p - WNK4 (mouse)
Orthologous residues
WNK4 (human): S1190‑p, WNK4 (mouse): S1169‑p, WNK4 (rat): S1169‑p
 Methods used to characterize site in vivo immunoprecipitation, mutation of modification site
 Relevant cell lines - cell types - tissues:  293T (epithelial), oocyte [CPEB (mouse)]
 Cellular systems studied:  cell lines
 Species studied:  frog, human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE SGK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE SGK1 (human) co-immunoprecipitation
Downstream Regulation
 Effect of modification (function):  activity, inhibited
 Comments:  WNK4 phosphorylation abrogates its basal inhibition of ENaC and ROMK channels

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