Curated Information
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Curated Information Page
PubMed Id: 12107173 
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.
Zou MH, et al. (2002) Modulation by peroxynitrite of Akt- and AMP-activated kinase-dependent Ser1179 phosphorylation of endothelial nitric oxide synthase. J Biol Chem 277, 32552-7 12107173
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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:  phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  BAE
 Cellular systems studied:  cell lines
 Species studied:  cow
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE AMPKA1 (human) transfection of dominant-negative enzyme, transfection of constitutively active enzyme, co-immunoprecipitation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
ONOO(-) increase
5-HT ONOO(-) augment treatment-induced increase
A23187 ONOO(-) augment treatment-induced increase
angiotensin ONOO(-) augment treatment-induced increase


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