Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Curated Information Page
PubMed Id: 19553680 
Chen MZ, et al. (2009) Oxidative stress decreases phosphatidylinositol 4,5-bisphosphate levels by deactivating phosphatidylinositol- 4-phosphate 5-kinase beta in a Syk-dependent manner. J Biol Chem 284, 23743-53 19553680
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.
Download Sites

Y105-p - PIP5K1B (human)
Orthologous residues
PIP5K1B (human): Y105‑p, PIP5K1B (mouse): Y105‑p, PIP5K1B (rat): Y105‑p
Characterization
 Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  COS (fibroblast), HeLa (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human, monkey
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Syk (human) pharmacological inhibitor of upstream enzyme, transfection of wild-type enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
H2O2 increase
piceatannol H2O2 inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  enzymatic activity, inhibited, intracellular localization
 Effect of modification (process):  cytoskeletal reorganization


Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.