Curated Information
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Curated Information Page
PubMed Id: 8552081 
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.
Yang BS, et al. (1996) Ras-mediated phosphorylation of a conserved threonine residue enhances the transactivation activities of c-Ets1 and c-Ets2. Mol Cell Biol 16, 538-47 8552081
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.
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T38-p - Ets-1 (human) ▲
Orthologous residues
Ets‑1 (human): T38‑p, Ets‑1 (mouse): T38‑p, Ets‑1 (rat): T38‑p, Ets‑1 (chicken): T38‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site, phosphoamino acid analysis
 Relevant cell lines - cell types - tissues:  3T3 (fibroblast) [Ets-2 (human)]
 Cellular systems studied:  cell lines
 Species studied:  mouse
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
HRas (human) increase Mutation of the potential phosphorylation site threonine 38 in Ets1 or threonine 72 in Ets2 abrogates Ras superactivation.
Downstream Regulation
 Effect of modification (function):  activation

T72-p - Ets-2 (human) ▲
Orthologous residues
Ets‑2 (human): T72‑p, Ets‑2 (mouse): T72‑p, Ets‑2 (rat): T282‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site, phosphoamino acid analysis
 Relevant cell lines - cell types - tissues:  3T3 (fibroblast) [Ets-2 (human)]
 Cellular systems studied:  cell lines
 Species studied:  mouse
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
HRas (human) increase The Ras-dependent increase in threonine phosphorylation was not observed in Ets2 proteins that had T72A mutations.
Downstream Regulation
 Effect of modification (function):  activation


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