Eto M, et al. (2007) Phosphorylation-induced conformational switching of CPI-17 produces a potent myosin phosphatase inhibitor. Structure 15, 1591-602 18073109

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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T38-p - PPP1R14A (pig) ▲
Modsite: QKRHARVtVKYDRRE SwissProt Entrez-Gene Orthologous residues PPP1R14A (human): T38‑p, PPP1R14A iso2 (human): T38‑p, PPP1R14A (mouse): T38‑p, PPP1R14A (rat): T38‑p, PPP1R14A (pig): T38‑p Characterization Enzymes shown to modify site in vitro:  Type Enzyme KINASE PKCA (human) Downstream Regulation Effect of modification (function):  protein conformation