Curated Information
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Curated Information Page
PubMed Id: 16938849 
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
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.
Click on the protein name to open the protein page, and on the RSD number to open the site page.
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T567-p - Ezrin (rat)
Orthologous residues
Ezrin (human): T567‑p, Ezrin (mouse): T567‑p, Ezrin (rat): T567‑p
 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) genetic transfer of wild-type enzyme, co-immunoprecipitation, pharmacological activator of upstream enzyme, genetic transfer of dominant-negative enzyme, phospho-motif antibody
 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
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Nik (human)

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