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: 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.
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

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) pharmacological activator of upstream enzyme, co-immunoprecipitation, phospho-motif antibody, genetic transfer of wild-type enzyme, genetic transfer of dominant-negative 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)


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.