|
Orthologous residues
|
|
DUSP3 (human): Y138‑p, DUSP3 (mouse): Y138‑p, DUSP3 (rat): Y224‑p
|
|
Characterization
|
|
Methods used to characterize site in vivo:
mass spectrometry
|
|
Relevant cell lines - cell types - tissues:
Jurkat (T lymphocyte)
|
|
Cellular systems studied:
cell lines
|
|
Species studied:
human
|
|
Enzymes shown to modify site in vitro:
|
|
|
|
Upstream Regulation
|
|
Potential in vivo enzymes for site:
|
|
Type
|
Enzyme
|
Evidence
|
Notes
|
|
KINASE
|
Syk (human)
|
transfection of wild-type enzyme
|
It is not directly demonstrated that Y138 is phosphorylated in intact cells. It is shown only that tyrosine-phosphorylation of DUSP3 increases in cells transfected with ZAP-70 and Syk but not Csk, Lck, and Fyn.
|
|
KINASE
|
ZAP70 (human)
|
transfection of wild-type enzyme
|
It is not directly demonstrated that Y138 is phosphorylated in intact cells. It is shown only that tyrosine-phosphorylation of DUSP3 increases in cells transfected with ZAP-70 and Syk but not Csk, Lck, and Fyn.
|
|
|
Downstream Regulation
|
|
Effect of modification (function):
enzymatic activity, induced
|
|
Comments:
When ZAP-70 was reintroduced into the ZAP-70(-) JURKAT cells, DUSP3 regained its ability to inhibit MAPK responses.
|
