Curated Information

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Curated Information Page

PubMed Id: 10640736

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.

Scaffidi C, et al. (2000) Phosphorylation of FADD/ MORT1 at serine 194 and association with a 70-kDa cell cycle-regulated protein kinase. J Immunol 164, 1236-42 10640736

S194-p - FADD (human)

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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, phospho-antibody, western blotting

Relevant cell lines - cell types - tissues: 293T (epithelial), BJAB (B lymphocyte)

Cellular systems studied: cell lines

Species studied: human

Upstream Regulation

Treatments, proteins and their effect on site modification:

Treatments	Referenced Treatments	Manipulated Protein	Referenced Protein	Effect	Notes
wortmannin				no change compared to control
phorbol ester				no change compared to control

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