Curated Information
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Home > Curated Information Page > PubMed Id: 20213743
Lee CH, et al. (2010) CDK5 phosphorylates eNOS at Ser-113 and regulates NO production. J Cell Biochem 110, 112-7 20213743
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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S114-p - eNOS (human)
Modsite: RKLQGRPsPGPPAPE SwissProt Entrez-Gene
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
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CDK5 (human) co-immunoprecipitation, pharmacological inhibitor of upstream enzyme, phospho-antibody, transfection of wild-type enzyme, mutation in upstream enzyme recognition motif
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
seliciclib decrease
Downstream Regulation
Effect of modification (function):  enzymatic activity, induced