Curated Information

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Curated Information Page

PubMed Id: 10025949

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.

Chen ZP, et al. (1999) AMP-activated protein kinase phosphorylation of endothelial NO synthase. FEBS Lett 443, 285-9 10025949

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.

T494-p - eNOS (rat)

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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

Relevant cell lines - cell types - tissues: heart

Cellular systems studied: tissue

Species studied: rat

Enzymes shown to modify site in vitro:

Type	Enzyme
KINASE	AMPKA1 (rat)

Upstream Regulation

Potential in vivo enzymes for site:

Type	Enzyme	Evidence	Notes
KINASE	AMPKA1 (rat)	co-immunoprecipitation

Downstream Regulation

Effect of modification (function): enzymatic activity, inhibited

Comments: Phosphorylated In the absence of Ca2+ inhibiting eNOS, but not during ischaemia.

S1176-p - eNOS (rat)

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