Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Curated Information Page
PubMed Id: 10473631 
FĂ©raille E, et al. (1999) Insulin-induced stimulation of Na+,K(+)-ATPase activity in kidney proximal tubule cells depends on phosphorylation of the alpha-subunit at Tyr-10. Mol Biol Cell 10, 2847-59 10473631
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.
Information from this record has been curated, but not yet edited in PhosphoSitePlus® and may be incomplete.
Download Sites

Y10-p - ATP1A1 (rat)
Orthologous residues
ATP1A1 (human): Y10‑p, ATP1A1 iso2 (human): Y10‑p, ATP1A1 iso3 (human): , ATP1A1 (mouse): Y10‑p, ATP1A1 (rat): Y10‑p
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, phospho-antibody, phosphoamino acid analysis, western blotting
 Relevant cell lines - cell types - tissues:  OK (renal)
 Cellular systems studied:  cell lines
 Species studied:  opossum
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
vanadate increase
insulin increase
genistein insulin inhibit treatment-induced increase
genistein decrease
Downstream Regulation
 Effect of modification (function):  activity, induced

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.