Curated Information
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PubMed Id: 9335504 
Kretzschmar M, Doody J, Massagué J (1997) Opposing BMP and EGF signalling pathways converge on the TGF-beta family mediator Smad1. Nature 389, 618-22 9335504
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.
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
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S187-p - Smad1 (human)
Orthologous residues
Smad1 (human): S187‑p, Smad1 (mouse): S187‑p, Smad1 (rat): S187‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  COS (fibroblast), R-1B/L17 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  mink, monkey
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK2 (human)
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Comments:  Erk-mediated phosphorylation inhibits the nuclear accumulation of Smad1.

S195-p - Smad1 (human)
Orthologous residues
Smad1 (human): S195‑p, Smad1 (mouse): S195‑p, Smad1 (rat): S195‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  COS (fibroblast), R-1B/L17 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  mink, monkey
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK2 (human)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
serum starvation decrease
HGF increase
EGF increase
wortmannin EGF no effect upon treatment-induced increase
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Comments:  Erk-mediated phosphorylation inhibits the nuclear accumulation of Smad1.

S206-p - Smad1 (human)
Orthologous residues
Smad1 (human): S206‑p, Smad1 (mouse): S206‑p, Smad1 (rat): S206‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  COS (fibroblast), R-1B/L17 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  mink, monkey
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK2 (human)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
serum starvation decrease
HGF increase
EGF increase
wortmannin EGF no effect upon treatment-induced increase
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Comments:  Erk-mediated phosphorylation inhibits the nuclear accumulation of Smad1.

S214-p - Smad1 (human)
Orthologous residues
Smad1 (human): S214‑p, Smad1 (mouse): S214‑p, Smad1 (rat): S214‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  COS (fibroblast), R-1B/L17 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  mink, monkey
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK2 (human)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
serum starvation decrease
HGF increase
EGF increase
wortmannin EGF no effect upon treatment-induced increase
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Comments:  Erk-mediated phosphorylation inhibits the nuclear accumulation of Smad1.

S462-p - Smad1 (human)
Orthologous residues
Smad1 (human): S462‑p, Smad1 (mouse): S462‑p, Smad1 (rat): S465‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  R-1B/L17 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  mink
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE BMPR1B (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE BMPR1B (human) transfection of wild-type enzyme, activation of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
serum starvation decrease
HGF increase
EGF increase
wortmannin EGF no effect upon treatment-induced increase
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Comments:  BMP-stimulated phosphorylation of Smad1 carboxy-terminal serines induces nuclear accumulation of Smad1.

S463-p - Smad1 (human)
Orthologous residues
Smad1 (human): S463‑p, Smad1 (mouse): S463‑p, Smad1 (rat): S466‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  R-1B/L17 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  mink
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE BMPR1B (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE BMPR1B (human) transfection of wild-type enzyme, activation of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
serum starvation decrease
HGF increase
EGF increase
wortmannin EGF no effect upon treatment-induced increase
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Comments:  BMP-stimulated phosphorylation of Smad1 carboxy-terminal serines induces nuclear accumulation of Smad1.

S465-p - Smad1 (human)
Orthologous residues
Smad1 (human): S465‑p, Smad1 (mouse): S465‑p, Smad1 (rat): S468‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  R-1B/L17 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  mink
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE BMPR1B (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE BMPR1B (human) transfection of wild-type enzyme, activation of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
serum starvation decrease
HGF increase
EGF increase
wortmannin EGF no effect upon treatment-induced increase
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Comments:  BMP-stimulated phosphorylation of Smad1 carboxy-terminal serines induces nuclear accumulation of Smad1.


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