Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Curated Information Page
PubMed Id: 12447358 
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.
Alonso A, et al. (2003) Tyrosine phosphorylation of VHR phosphatase by ZAP-70. Nat Immunol 4, 44-8 12447358
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
Download Sites

Y38-p - DUSP3 (human)
Orthologous residues
DUSP3 (human): Y38‑p, DUSP3 (mouse): Y38‑p, DUSP3 (rat): Y124‑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
Type Enzyme
KINASE Syk (human)
KINASE ZAP70 (human)
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.

Y138-p - DUSP3 (human)
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
Type Enzyme
KINASE Syk (human)
KINASE ZAP70 (human)
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.


Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.