Curated Information
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Home > Curated Information Page > PubMed Id: 25753203
Kim SS, et al. (2015) PKA regulates calcineurin function through the phosphorylation of RCAN1: Identification of a novel phosphorylation site. Biochem Biophys Res Commun 459, 604-9 25753203
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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S93-p - RCAN1 iso2 (human)
Modsite: AQTLHIGsSHLAPPN SwissProt Entrez-Gene
Orthologous residues
RCAN1 (human): S148‑p, RCAN1 iso2 (human): S93‑p, RCAN1 iso3 (human): S67‑p, RCAN1 (mouse): S146‑p, RCAN1 (rat): S93‑p
Characterization
Methods used to characterize site in vivo mass spectrometry (in vitro), mutation of modification site, western blotting
Relevant cell lines - cell types - tissues:  293 (epithelial)
Cellular systems studied:  cell lines
Species studied:  human
Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKACA (human)
Downstream Regulation
Effect of modification (function):  protein stabilization
Effect of modification (process):  transcription, inhibited
Comments:  enhances the inhibition of calcineurin activity