Curated Information
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PubMed Id: 22044535 
Wei JD, Kim JY, Kim JH (2011) BLT2 phosphorylation at Thr(355) by Akt is necessary for BLT2-mediated chemotaxis. FEBS Lett 585, 3501-6 22044535
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.
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T355-p - LTB4R2 (human)
Orthologous residues
LTB4R2 (human): T355‑p, LTB4R2 (mouse): T324‑p, LTB4R2 (rat): T324‑p
 Methods used to characterize site in vivo flow cytometry, immunoprecipitation, mutation of modification site, western blotting
 Relevant cell lines - cell types - tissues:  CHO (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  hamster
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (human) transfection of dominant-negative enzyme, transfection of wild-type enzyme, activation of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
LTB4 increase
LY294002 LTB4 inhibit treatment-induced increase
PTX LTB4 inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (process):  cell motility, induced
 Comments:  leads to Rac1 activation and ROS generation, which are critical for LTB4-evoked chemotaxis;

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