Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Curated Information Page
PubMed Id: 17360471 
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.
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
Download Sites

S1169-p - WNK4 (mouse)
Orthologous residues
WNK4 (human): S1190‑p, WNK4 (mouse): S1169‑p, WNK4 (rat): S1169‑p
Characterization
 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


Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.