Curated Information
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Home > Curated Information Page > PubMed Id: 22493455
Panina S, et al. (2012) Significance of calcium binding, tyrosine phosphorylation, and lysine trimethylation for the essential function of calmodulin in vertebrate cells analyzed in a novel gene replacement system. J Biol Chem 287, 18173-81 22493455
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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Y100-p - Calmodulin (chicken)
Modsite: FDKDGNGyISAAELR SwissProt Entrez-Gene
Orthologous residues
Calmodulin (human): Y100‑p, Calmodulin (mouse): Y100‑p, Calmodulin (rat): Y100‑p, Calmodulin (chicken): Y100‑p, Calmodulin (sheep): Y100‑p, Calmodulin (cow): Y100‑p

K116-m3 - Calmodulin (chicken)
Modsite: VMTNLGEkLTDEEVD SwissProt Entrez-Gene
Orthologous residues
Calmodulin (human): K116‑m3, Calmodulin (mouse): K116‑m3, Calmodulin (rat): K116‑m3, Calmodulin (chicken): K116‑m3, Calmodulin (sheep): K116‑m3, Calmodulin (cow): K116‑m3

Y139-p - Calmodulin (chicken)
Modsite: DGDGQVNyEEFVQMM SwissProt Entrez-Gene
Orthologous residues
Calmodulin (human): Y139‑p, Calmodulin (mouse): Y139‑p, Calmodulin (rat): Y139‑p, Calmodulin (chicken): Y139‑p, Calmodulin (sheep): Y139‑p, Calmodulin (cow): Y139‑p