Curated Information
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PubMed Id: 16306994 
Hüttelmaier S, et al. (2005) Spatial regulation of beta-actin translation by Src-dependent phosphorylation of ZBP1. Nature 438, 512-5 16306994
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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Y396-p - IGF2BP1 (chicken)
Orthologous residues
IGF2BP1 (human): Y396‑p, IGF2BP1 (mouse): Y396‑p, IGF2BP1 (rat): Y396‑p, IGF2BP1 (chicken): Y396‑p
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  293 (epithelial) [IGF2BP1 (human)], 293 (epithelial) [Src (human)], NG108-15 (neuron) [IGF2BP1 (human)], NG108-15 (neuron) [Src (human)]
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Src (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Src (human) transfection of constitutively active enzyme, transfection of inactive enzyme
Downstream Regulation
 Effect of modification (function):  activity, inhibited, molecular association, regulation
 Comments:  IMP-1 Y396 phosphorylation interferes with its binding to beta-actin mRNA, thereby promoting beta-actin translation.

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