Curated Information
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Curated Information Page
PubMed Id: 20850356 
This page summarizes selected information from the article 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.
Xu W, et al. (2010) Integrin-induced PIP5K1C kinase polarization regulates neutrophil polarization, directionality, and in vivo infiltration. Immunity 33, 340-50 20850356
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Y649-p - PIP5K1C (human)
Orthologous residues
PIP5K1C (human): Y649‑p, PIP5K1C (mouse): Y644‑p, PIP5K1C iso2 (mouse): Y610‑p, PIP5K1C (rat): Y671‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  neutrophil
 Cellular systems studied:  primary cultured cells
 Species studied:  mouse
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Src (human) pharmacological inhibitor of upstream enzyme, inhibition of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
FAK (human) increase FRNK or Y397F-FAK decreased
PP2 decrease
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
AP-2 beta (human) Induces co-immunoprecipitation
 Comments:  stimulates PIP5KG polarization


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