Curated Information

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Curated Information Page

PubMed Id: 9346966

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.

Souchelnytskyi S, et al. (1997) Phosphorylation of Ser465 and Ser467 in the C terminus of Smad2 mediates interaction with Smad4 and is required for transforming growth factor-beta signaling. J Biol Chem 272, 28107-15 9346966

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.

S465-p - Smad2 (human)

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Orthologous residues

Smad2 (human): S465‑p, Smad2 (mouse): S465‑p, Smad2 (rat): S465‑p

Characterization

Methods used to characterize site in vivo: [32P] bio-synthetic labeling, mutation of modification site, phosphopeptide mapping

Relevant cell lines - cell types - tissues: COS (fibroblast) [Smad2 (human)], Mv1Lu (epithelial) [Smad2 (human)]

Cellular systems studied: cell lines

Species studied: mink, monkey

Upstream Regulation

Treatments, proteins and their effect on site modification:

Treatments	Referenced Treatments	Manipulated Protein	Referenced Protein	Effect	Notes
TGF-beta				increase

Downstream Regulation

Effect of modification (function): intracellular localization

Modification regulates interactions with:

Interacting molecule	Interacting domains	Effect	Consequences (function)	Consequences (process)	Detection assays
Smad4 (human)		Induces	intracellular localization		microscopy-colocalization

S467-p - Smad2 (human)

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