Curated Information
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Curated Information Page
PubMed Id: 9674711 
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.
Hock B, et al. (1998) Tyrosine-614, the major autophosphorylation site of the receptor tyrosine kinase HEK2, functions as multi-docking site for SH2-domain mediated interactions. Oncogene 17, 255-60 9674711
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Y614-p - EphB3 (human)
Orthologous residues
EphB3 (human): Y614‑p, EphB3 (mouse): Y609‑p, EphB3 (rat): Y609‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  COS (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  monkey
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE EphB3 (human) transfection of wild-type enzyme
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Fyn (human) Induces not reported co-immunoprecipitation
RASA1 (human) Induces not reported co-immunoprecipitation
CRK (human) Induces not reported co-immunoprecipitation


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