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: 10376603 
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.
Dimmeler S, et al. (1999) Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation. Nature 399, 601-5 10376603
Download Sites

S1177-p - eNOS (human)
Orthologous residues
eNOS (human): S1177‑p, eNOS (mouse): S1176‑p, eNOS (rat): S1176‑p, eNOS (rabbit): S1183‑p, eNOS (pig): S1179‑p, eNOS (cow): S1179‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, immunoprecipitation, mutation of modification site, phosphoamino acid analysis, western blotting
 Relevant cell lines - cell types - tissues:  COS (fibroblast), HUVEC (endothelial)
 Cellular systems studied:  cell lines
 Species studied:  human, monkey
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (human) transfection of inactive enzyme, transfection of constitutively active enzyme
Downstream Regulation
 Effect of modification (function):  enzymatic 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.