Florio VA, et al. (1994) Phosphorylation of the 61-kDa calmodulin-stimulated cyclic nucleotide phosphodiesterase at serine 120 reduces its affinity for calmodulin. Biochemistry 33, 8948-54 8043581

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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S120-p - PDE1A (cow) ▲
Modsite: EEKPRFRsIVHVVQA SwissProt Entrez-Gene Orthologous residues PDE1A (human): S120‑p, PDE1A iso5 (human): S120‑p, PDE1A (mouse): S120‑p, PDE1A (rat): S120‑p, PDE1A (cow): S120‑p Characterization Enzymes shown to modify site in vitro:  Type Enzyme KINASE PKACA (rat)

S138-p - PDE1A (cow) ▲
Modsite: VERMYRKsYHMVGLA SwissProt Entrez-Gene Orthologous residues PDE1A (human): T138‑p, PDE1A iso5 (human): T138‑p, PDE1A (mouse): N138‑p, PDE1A (rat): N138‑p, PDE1A (cow): S138‑p Characterization Enzymes shown to modify site in vitro:  Type Enzyme KINASE PKACA (rat)