Curated Information
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Home > Curated Information Page > PubMed Id: 30466786
Mo SJ, et al. (2019) PKA-dependent phosphorylation of IP3K-A at Ser119 regulates a binding affinity with EB3. Biochem Biophys Res Commun 508, 52-59 30466786
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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S119-p - ITPKA (rat)
Modsite: LQQPRRLsTSSLSST SwissProt Entrez-Gene
Orthologous residues
ITPKA (human): S121‑p, ITPKA (mouse): S119‑p, ITPKA (rat): S119‑p
Characterization
Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
Relevant cell lines - cell types - tissues:  'neuron, hippocampal', HEK293T (epithelial)
Cellular systems studied:  cell lines
Species studied:  human, rat
Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKACA (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKACA (human) pharmacological activator of upstream enzyme, pharmacological inhibitor of upstream enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
NKH_477 increase
H-89 decrease
long-term_potentiation increase increase followed by decrease
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Effect of modification (process):  cytoskeletal reorganization, neural plasticity
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
EB3 (human) Disrupts co-immunoprecipitation, in vitro, pull-down assay, microscopy-colocalization