Curated Information
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Curated Information Page
PubMed Id: 10230405 
Hammer GD, et al. (1999) Phosphorylation of the nuclear receptor SF-1 modulates cofactor recruitment: integration of hormone signaling in reproduction and stress. Mol Cell 3, 521-6 10230405
This page summarizes selected information from the record 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.
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S203-p - STF-1 (mouse)
Orthologous residues
STF‑1 (human): S203‑p, STF‑1 (mouse): S203‑p, STF‑1 (rat): S203‑p
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, peptide sequencing, phosphoamino acid analysis, phosphopeptide mapping
 Disease tissue studied:  breast cancer, gestational cancer, gestational trophoblastic choriocarcinoma
 Relevant cell lines - cell types - tissues:  COS (fibroblast), JEG-3 (uterine), MCF-7 (breast cell)
 Cellular systems studied:  cell lines
 Species studied:  human, monkey
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK2 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK2 (human) pharmacological activator of upstream enzyme, modification site within consensus motif, activation of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
EGF increase
RAF1 (human) increase constitutively active
Downstream Regulation
 Effect of modification (function):  activity, induced, molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
SMRT (human) Induces mammalian two-hybrid, pull-down assay
GRIP1 (human) Induces mammalian two-hybrid, pull-down assay

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