Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage PhosphoSitePlus® v6.7.5
Powered by Cell Signaling Technology
Home > Curated Information Page > PubMed Id: 17804409
Zhang Y, et al. (2007) Dynamic receptor-dependent activation of inducible nitric-oxide synthase by ERK-mediated phosphorylation of Ser745. J Biol Chem 282, 32453-61 17804409
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.
Click on the protein name to open the protein page, and on the RSD number to open the site page.
Download

S745-p - iNOS (human)
Modsite: KSRQNLQsPTSSRAT SwissProt Entrez-Gene
Orthologous residues
iNOS (human): S745‑p, iNOS (mouse): S739‑p, iNOS (rat): S742‑p
Characterization
Methods used to characterize site in vivo mass spectrometry, mutation of modification site, phospho-antibody, western blotting
Relevant cell lines - cell types - tissues:  293 (epithelial), HMVEC (endothelial)
Cellular systems studied:  cell lines
Species studied:  human
Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK1 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK1 (human) pharmacological inhibitor of upstream enzyme, pharmacological activator of upstream enzyme, co-immunoprecipitation, microscopy-colocalization, phospho-antibody
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
DAKD increase
PD98059 DAKD inhibit treatment-induced increase
Downstream Regulation
Effect of modification (function):  enzymatic activity, induced