Curated Information
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Home > Curated Information Page > PubMed Id: 22389500
Lee D, et al. (2012) Inositol 1,4,5-trisphosphate 3-kinase A is a novel microtubule-associated protein: PKA-dependent phosphoregulation of microtubule binding affinity. J Biol Chem 287, 15981-95 22389500
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 (mouse)
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 mutation of modification site, phospho-antibody, western blotting
Relevant cell lines - cell types - tissues:  'neuron, hippocampal'-brain, 293 (epithelial), brain
Cellular systems studied:  cell lines
Species studied:  human, mouse, rat
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKACA (human) transfection of inactive enzyme, transfection of wild-type enzyme, pharmacological inhibitor of upstream enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
H-89 NKH_477 inhibit treatment-induced increase
NKH_477 increase
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Effect of modification (process):  cytoskeletal reorganization, neural plasticity
Comments:  Phosphorylation at S119 inhibits the ITPKA and microtubule binding