Ser27
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage PhosphoSitePlus® v6.7.1.1
Powered by Cell Signaling Technology
Home > Phosphorylation Site Page: > Ser27  -  Kv7.1 (human)

Site Information
LPGARRGsAGLAKKC   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 2999203

In vivo Characterization
Methods used to characterize site in vivo:
immunoprecipitation ( 4 ) , mutation of modification site ( 1 , 2 , 4 , 5 ) , phospho-antibody ( 1 , 4 ) , western blotting ( 1 , 4 )
Relevant cell line - cell type - tissue:

Upstream Regulation
Regulatory protein:
Kv7.1 (human) ( 4 )
Putative in vivo kinases:
PKACA (human) ( 2 , 4 )
Treatments:
cAMP_analog ( 1 , 4 ) , IBMX ( 2 ) , isoproterenol ( 2 ) , mutation ( 2 ) , NKH_477 ( 2 ) , okadaic_acid ( 1 , 4 )

Downstream Regulation
Effects of modification on Kv7.1:
activity, induced ( 4 , 5 ) , molecular association, regulation ( 1 ) , protein conformation ( 4 )
Induce interaction with:
KCNE1 (human) ( 1 )

References 

1

Dvir M, et al. (2014) Long QT mutations at the interface between KCNQ1 helix C and KCNE1 disrupt I(KS) regulation by PKA and PIPâ‚‚. J Cell Sci 127, 3943-55
25037568   Curated Info

2

Wu J, et al. (2014) A molecular mechanism for adrenergic-induced long QT syndrome. J Am Coll Cardiol 63, 819-27
24184248   Curated Info

3

Shiromizu T, et al. (2013) Identification of missing proteins in the neXtProt database and unregistered phosphopeptides in the PhosphoSitePlus database as part of the Chromosome-centric Human Proteome Project. J Proteome Res 12, 2414-21
23312004   Curated Info

4

Heijman J, et al. (2012) Dominant-negative control of cAMP-dependent IKs upregulation in human long-QT syndrome type 1. Circ Res 110, 211-9
22095730   Curated Info

5

Yang T, Kanki H, Roden DM (2003) Phosphorylation of the IKs channel complex inhibits drug block: novel mechanism underlying variable antiarrhythmic drug actions. Circulation 108, 132-4
12835205   Curated Info