Curated Information
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Curated Information Page
PubMed Id: 22128160 
Li XZ, et al. (2012) Identification of a key motif that determines the differential surface levels of RET and TrkB tyrosine kinase receptors and controls depolarization enhanced RET surface insertion. J Biol Chem 287, 1932-45 22128160
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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T675-p - Ret (human)
Orthologous residues
Ret (human): T675‑p, Ret iso2 (human): T675‑p, Ret iso3 (human): , Ret (mouse): T676‑p, Ret iso2 (mouse): T676‑p, Ret iso4 (mouse): T625‑p, Ret (rat): T676‑p
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  adrenal cancer, pheochromocytoma
 Relevant cell lines - cell types - tissues:  PC-12 (chromaffin)
 Cellular systems studied:  cell lines
 Species studied:  rat
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKCA (human) pharmacological inhibitor of upstream enzyme, pharmacological activator of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
phorbol ester increase
chelerythrine decrease
H-89 no change compared to control
forskolin no change compared to control
depolarization increase
chelerythrine depolarization inhibit treatment-induced increase
H-89 depolarization no effect upon treatment-induced increase
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Effect of modification (process):  signaling pathway regulation
 Comments:  modulates GDNF-induced downstream signaling and cell differentiation

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