Curated Information
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Curated Information Page
PubMed Id: 16621795 
Wagner LE, Betzenhauser MJ, Yule DI (2006) ATP binding to a unique site in the type-1 S2- inositol 1,4,5-trisphosphate receptor defines susceptibility to phosphorylation by protein kinase A. J Biol Chem 281, 17410-9 16621795
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, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
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S1756-p - IP3R1 (rat)
Orthologous residues
IP3R1 (human): S1764‑p, IP3R1 iso3 (human): S1716‑p, IP3R1 (mouse): S1755‑p, IP3R1 iso2 (mouse): S1740‑p, IP3R1 (rat): S1756‑p
 Methods used to characterize site in vivo phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  293 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
forskolin increase
ATP forskolin augment treatment-induced increase mutation (glycine to alanine) of an ATP-binding site on IP3R1 inhibits phosphorylation

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