Curated Information
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Home > Curated Information Page > PubMed Id: 17173306
Settimo L, et al. (2007) Conformational changes upon calcium binding and phosphorylation in a synthetic fragment of calmodulin. Biopolymers 88, 373-85 17173306
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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S82-p - Calmodulin (human)
Modsite: RkMkDtDsEEEIrEA SwissProt Entrez-Gene
Orthologous residues
Calmodulin (human): S82‑p, Calmodulin (mouse): S82‑p, Calmodulin (rat): S82‑p, Calmodulin (chicken): S82‑p, Calmodulin (sheep): S82‑p, Calmodulin (cow): S82‑p
Downstream Regulation
Effect of modification (function):  protein conformation