Curated Information
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Curated Information Page
PubMed Id: 21220922 
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.
Diakov A, et al. (2010) Protein kinase B alpha (PKBα) stimulates the epithelial sodium channel (ENaC) heterologously expressed in Xenopus laevis oocytes by two distinct mechanisms. Cell Physiol Biochem 26, 913-24 21220922
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S621-p - ENaC-alpha (rat)
Orthologous residues
ENaC‑alpha (human): S594‑p, ENaC‑alpha (mouse): S621‑p, ENaC‑alpha (rat): S621‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  oocyte
 Cellular systems studied:  primary cells
 Species studied:  frog
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE SGK1 (human) pharmacological activator of upstream enzyme
KINASE Akt1 (human) inhibition of upstream enzyme, transfection of dominant-negative enzyme, transfection of constitutively active enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
okadaic acid increase
Downstream Regulation
 Effect of modification (function):  intracellular localization


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