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: 10514497 
Gallis B, et al. (1999) Identification of flow-dependent endothelial nitric-oxide synthase phosphorylation sites by mass spectrometry and regulation of phosphorylation and nitric oxide production by the phosphatidylinositol 3-kinase inhibitor LY294002. J Biol Chem 274, 30101-8 10514497
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.
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
Download Sites

S116-p - eNOS (cow)
Orthologous residues
eNOS (human): S114‑p, eNOS (mouse): T113‑p, eNOS (rat): T113‑p, eNOS (rabbit): T120‑p, eNOS (pig): S116‑p, eNOS (cow): S116‑p
Characterization
 Methods used to characterize site in vivo 2D analysis, [32P] bio-synthetic labeling, mass spectrometry, peptide sequencing, phosphoamino acid analysis, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  endothelial-aorta
 Cellular systems studied:  primary cells
 Species studied:  cow
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
fluid shear stress increase

S1179-p - eNOS (cow)
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 2D analysis, [32P] bio-synthetic labeling, mass spectrometry, peptide sequencing, phosphoamino acid analysis, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  endothelial-aorta
 Cellular systems studied:  primary cells
 Species studied:  cow
 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) pharmacological inhibitor of upstream 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.