Stateva SR, et al. (2015) Characterization of phospho-(tyrosine)-mimetic calmodulin mutants. PLoS One 10, e0120798 25830911

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 (rat) ▲

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 Characterization Methods used to characterize site in vivo:  mutation of modification site Relevant cell lines - cell types - tissues:  E.coli (bacterial) Cellular systems studied:  cell lines Species studied:  bacteria Enzymes shown to modify site in vitro:  Type Enzyme KINASE Src (human) Downstream Regulation Effect of modification (function):  activity, induced, protein stabilization

Y139-p - Calmodulin (rat) ▲

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 Characterization Methods used to characterize site in vivo:  mutation of modification site Relevant cell lines - cell types - tissues:  E.coli (bacterial) Cellular systems studied:  cell lines Species studied:  bacteria Enzymes shown to modify site in vitro:  Type Enzyme KINASE Src (human) Downstream Regulation Effect of modification (function):  activity, induced, protein stabilization