Curated Information
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Home > Curated Information Page > PubMed Id: 12869534
Matsubara M, Hayashi N, Jing T, Titani K (2003) Regulation of endothelial nitric oxide synthase by protein kinase C. J Biochem (Tokyo) 133, 773-81 12869534
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, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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T497-p - eNOS (cow)
Modsite: AGITRKktFKEVANA SwissProt Entrez-Gene
Orthologous residues
eNOS (human): T495‑p, eNOS (mouse): T494‑p, eNOS (rat): T494‑p, eNOS (rabbit): T501‑p, eNOS (pig): T497‑p, eNOS (cow): T497‑p
Characterization
Methods used to characterize site in vivo phospho-antibody, western blotting
Relevant cell lines - cell types - tissues:  BAEC (endothelial)
Cellular systems studied:  cell lines
Species studied:  cow
Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKCA (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKCA (cow) pharmacological inhibitor of upstream enzyme, pharmacological activator of upstream enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
phorbol_ester increase
staurosporine phorbol_ester inhibit treatment-induced increase
Downstream Regulation
Effect of modification (function):  enzymatic activity, inhibited