Curated Information
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Curated Information Page
PubMed Id: 20961851 
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.
Bousquet SM, Monet M, Boulay G (2010) Protein kinase C-dependent phosphorylation of transient receptor potential canonical 6 (TRPC6) on serine 448 causes channel inhibition. J Biol Chem 285, 40534-43 20961851
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S448-p - TRPC6 (mouse)
Orthologous residues
TRPC6 (human): S449‑p, TRPC6 (mouse): S448‑p, TRPC6 (rat): S448‑p, TRPC6 iso2 (rat): S394‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial), A7r5 ('muscle, smooth')
 Cellular systems studied:  cell lines
 Species studied:  human, rat
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKCD (human) pharmacological activator of upstream enzyme, modification site within consensus motif, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
phorbol ester increase
GF109203X phorbol ester inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  activity, inhibited


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