Curated Information
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Curated Information Page
PubMed Id: 10498895 
Choi S, Park S (1999) Phosphorylation at Tyr-838 in the kinase domain of EphA8 modulates Fyn binding to the Tyr-615 site by enhancing tyrosine kinase activity. Oncogene 18, 5413-22 10498895
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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Y615-p - EphA8 (mouse)
Orthologous residues
EphA8 (human): Y616‑p, EphA8 iso2 (human): , EphA8 (mouse): Y615‑p, EphA8 (rat): Y589‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  293T (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE EphA8 (mouse)
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Effect of modification (process):  cell adhesion, altered
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Fyn (human) Induces co-immunoprecipitation

Y838-p - EphA8 (mouse)
Orthologous residues
EphA8 (human): Y839‑p, EphA8 iso2 (human): , EphA8 (mouse): Y838‑p, EphA8 (rat): Y812‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  293T (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE EphA8 (mouse)
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced
 Effect of modification (process):  cell adhesion, altered
 Comments:  Y383 phosphorylation is required for efficient phosphorylation of Y615 and other major sites.


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