Curated Information
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Curated Information Page
PubMed Id: 16938849 
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.
Baumgartner M, et al. (2006) The Nck-interacting kinase phosphorylates ERM proteins for formation of lamellipodium by growth factors. Proc Natl Acad Sci U S A 103, 13391-6 16938849
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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T567-p - ezrin (rat) ▲
Orthologous residues
ezrin (human): T567‑p, ezrin (mouse): T567‑p, ezrin (rat): T567‑p
Characterization
 Methods used to characterize site in vivo:  mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  breast cancer
 Relevant cell lines - cell types - tissues:  MTLn3 (breast cell)
 Cellular systems studied:  cell lines
 Species studied:  rat
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE Nik (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Nik (human) phospho-motif antibody, co-immunoprecipitation, genetic transfer of dominant-negative enzyme, pharmacological activator of upstream enzyme, genetic transfer of wild-type enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
EGF increase
EGF Nik (human) inhibit treatment-induced increase dominant negative
PDGF increase
PDGF Nik (human) inhibit treatment-induced increase dominant negative
thrombin increase
thrombin Nik (human) no effect upon treatment-induced increase dominant negative
Downstream Regulation
 Effect of modification (process):  cytoskeletal reorganization

T558-p - moesin (rat) ▲
Orthologous residues
moesin (human): T558‑p, moesin (mouse): T558‑p, moesin (rat): T558‑p
Characterization
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE Nik (human)


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