Curated Information
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Curated Information Page
PubMed Id: 17192268 
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.
Chen CJ, et al. (2007) Mutation analysis of the short cytoplasmic domain of the cell-cell adhesion molecule CEACAM1 identifies residues that orchestrate actin binding and lumen formation. J Biol Chem 282, 5749-60 17192268
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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T492-p - CEACAM1 (human)
Orthologous residues
CEACAM1 (human): T492‑p, CEACAM1 iso8 (human): , CEACAM1 iso9 (human): , CEACAM1 (mouse): , CEACAM1 (rat): S487‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, immunoprecipitation, mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  MCF-7 (breast cell)
 Cellular systems studied:  cell lines
 Species studied:  human
Downstream Regulation
 Effect of modification (process):  apoptosis, altered, cytoskeletal reorganization
 Comments:  plays a role in cell polarization and lumen formation

S494-p - CEACAM1 (human)
Orthologous residues
CEACAM1 (human): S494‑p, CEACAM1 iso8 (human): , CEACAM1 iso9 (human): , CEACAM1 (mouse): T489‑p, CEACAM1 (rat): S489‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, immunoprecipitation, mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  MCF-7 (breast cell)
 Cellular systems studied:  cell lines
 Species studied:  human
Downstream Regulation
 Effect of modification (process):  apoptosis, altered, cytoskeletal reorganization
 Comments:  plays a role in cell polarization and lumen formation


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