Curated Information
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Curated Information Page
PubMed Id: 20420860 
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.
Papoff G, et al. (2010) FADD-calmodulin interaction: a novel player in cell cycle regulation. Biochim Biophys Acta 1803, 898-911 20420860
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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 microscopy-colocalization with upstream kinase, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  HeLa (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CK1A (rat)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CK1A (human) microscopy-colocalization, phospho-antibody, co-immunoprecipitation colocization on spindle during metaphase and anaphase


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