Curated Information
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Curated Information Page
PubMed Id: 15906275 
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.
Shimada K, et al. (2005) Phosphorylation status of Fas-associated death domain-containing protein (FADD) is associated with prostate cancer progression. J Pathol 206, 423-32 15906275
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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 electrophoretic mobility shift, mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  DU 145 (prostate cell), epithelial-prostate, LNCaP (prostate cell), prostate
 Cellular systems studied:  cell lines, primary cultured cells, tissue
 Species studied:  human
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
taxol increase
neoadjuvant hormonal therapy increase
androgen withdrawal increase
Downstream Regulation
 Effect of modification (process):  apoptosis, inhibited, cell cycle regulation


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