Curated Information
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Curated Information Page
PubMed Id: 16332683 
Khan MT, et al. (2006) Akt kinase phosphorylation of inositol 1,4,5-trisphosphate receptors. J Biol Chem 281, 3731-7 16332683
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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S2682-p - IP3R1 (rat)
Orthologous residues
IP3R1 (human): S2690‑p, IP3R1 iso3 (human): S2642‑p, IP3R1 (mouse): S2681‑p, IP3R1 iso2 (mouse): S2666‑p, IP3R1 (rat): S2682‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  COS (fibroblast), DT40 (B lymphocyte)
 Cellular systems studied:  cell lines
 Species studied:  monkey
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (human) transfection of constitutively active enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
insulin increase
LY294002 insulin inhibit treatment-induced increase
LY294002 decrease
Downstream Regulation
 Effect of modification (function):  activity, inhibited
 Comments:  staurosporin-induced caspase-3 activation was enhanced in cells expressing S2682A mutant IP3R1.


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