Curated Information
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Home > Curated Information Page > PubMed Id: 18198173
Shi Y, et al. (2008) cAMP-dependent protein kinase phosphorylation produces interdomain movement in SUR2B leading to activation of the vascular KATP channel. J Biol Chem 283, 7523-30 18198173
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, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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S1387-p - ABCC9 (mouse)
Modsite: HTLRsRLsIILQDPI SwissProt Entrez-Gene
Orthologous residues
ABCC9 (human): S1390‑p, ABCC9 iso2 (human): S1390‑p, ABCC9 (mouse): S1387‑p, ABCC9 (rat): S1386‑p
Characterization
Methods used to characterize site in vivo mutation of modification site
Relevant cell lines - cell types - tissues:  293 (epithelial)
Cellular systems studied:  cell lines
Species studied:  human
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKACA (human) pharmacological inhibitor of upstream enzyme, pharmacological activator of upstream enzyme
Downstream Regulation
Effect of modification (function):  activity, induced, protein conformation
Comments:  Molecular modeling shows phosphorylated S1387 interacts with Y506 and R1462 leading to channel activation.