Curated Information

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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

S425-p - KCNJ2 (human)

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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
methylxanthine, forskolin				increase

Downstream Regulation

Effect of modification (function): inhibition

Comments: reduces an inward rectifier current of Kir2.1 V227F

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