Ashpole NM, et al. (2012) Ca2+/Calmodulin-dependent Protein Kinase II (CaMKII) Regulates Cardiac Sodium Channel NaV1.5 Gating by Multiple Phosphorylation Sites. J Biol Chem 287, 19856-69 22514276

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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S516-p - SCN5A (human) ▲

Modsite: LsLTrGLsRTsMKPR SwissProt Entrez-Gene Orthologous residues SCN5A (human): S516‑p, SCN5A (mouse): S516‑p, SCN5A (rat): S517‑p Characterization Methods used to characterize site in vivo:  mutation of modification site Relevant cell lines - cell types - tissues:  293 (epithelial) Cellular systems studied:  cell lines Species studied:  human Enzymes shown to modify site in vitro:  Type Enzyme KINASE CAMK2D (human) KINASE CAMK2D (rat) Downstream Regulation Effect of modification (function):  activity, inhibited

T594-p - SCN5A (human) ▲

Modsite: LHGkKNStVDCNGVV SwissProt Entrez-Gene Orthologous residues SCN5A (human): T594‑p, SCN5A (mouse): T594‑p, SCN5A (rat): T595‑p Characterization Methods used to characterize site in vivo:  mutation of modification site Relevant cell lines - cell types - tissues:  293 (epithelial) Cellular systems studied:  cell lines Species studied:  human Enzymes shown to modify site in vitro:  Type Enzyme KINASE CAMK2D (human) KINASE CAMK2D (rat) Downstream Regulation Effect of modification (function):  activity, inhibited