Curated Information
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Curated Information Page
PubMed Id: 19843922 
This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
Vega AL, Tester DJ, Ackerman MJ, Makielski JC (2009) Protein kinase A-dependent biophysical phenotype for V227F-KCNJ2 mutation in catecholaminergic polymorphic ventricular tachycardia. Circ Arrhythm Electrophysiol 2, 540-7 19843922
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S425-p - KCNJ2 (human)
Orthologous residues
KCNJ2 (human): S425‑p, KCNJ2 (mouse): S426‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  COS (fibroblast) [KCNJ2 (human), transfection]
 Cellular systems studied:  cell lines
 Species studied:  monkey
 Comments:  KCNJ2 wt and V227F mutant
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKACA (human) pharmacological activator of upstream enzyme, modification site within consensus motif
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
forskolin, methylxanthine increase
Downstream Regulation
 Effect of modification (function):  activity, inhibited
 Comments:  reduces an inward rectifier current of Kir2.1 V227F


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