Carøe Nordgaard J, Kruse LS, Gammeltoft S, Kruuse CR (2014) Role of Ser102 and Ser104 as Regulators of cGMP Hydrolysis by PDE5A. PLoS One 9, e107627 25247292

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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S102-p - PDE5A (human) ▲

Modsite: GTPTRKIsAsEFDRP SwissProt Entrez-Gene Orthologous residues PDE5A (human): S102‑p, PDE5A (mouse): S92‑p, PDE5A (rat): S60‑p, PDE5A (cow): S92‑p Characterization Methods used to characterize site in vivo:  mutation of modification site Disease tissue studied:  neuroblastoma Relevant cell lines - cell types - tissues:  SKNAS (neural crest) Cellular systems studied:  cell lines Species studied:  human Downstream Regulation Effect of modification (function):  enzymatic activity, inhibited, protein conformation

S104-p - PDE5A (human) ▲

Modsite: PTRKIsAsEFDRPLR SwissProt Entrez-Gene Orthologous residues PDE5A (human): S104‑p, PDE5A (mouse): S94‑p, PDE5A (rat): S62‑p, PDE5A (cow): S94‑p Characterization Methods used to characterize site in vivo:  mutation of modification site Disease tissue studied:  neuroblastoma Relevant cell lines - cell types - tissues:  SKNAS (neural crest) Cellular systems studied:  cell lines Species studied:  human Downstream Regulation Effect of modification (function):  enzymatic activity, inhibited, protein conformation