Curated Information
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Curated Information Page
PubMed Id: 20890306 
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.
Jang MS, et al. (2011) Phosphorylation by polo-like kinase 1 induces the tumor-suppressing activity of FADD. Oncogene 30, 471-81 20890306
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S194-p - FADD (human)
Orthologous residues
FADD (human): S194‑p, FADD (mouse): S191‑p, FADD (rat): S194‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  HeLa (cervical), Jurkat (T lymphocyte)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PLK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PLK1 (human) siRNA inhibition of enzyme, co-immunoprecipitation, modification site within consensus motif
 Comments:  causes Plk1 degradation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
taxol increase
siRNA taxol inhibit treatment-induced increase siRNA Plk1
Downstream Regulation
 Effect of modification (process):  apoptosis, altered, carcinogenesis, altered, cell cycle regulation


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