Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Curated Information Page
PubMed Id: 20961851 
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
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.
Download Sites

S448-p - TRPC6 (mouse)
Orthologous residues
TRPC6 (human): S449‑p, TRPC6 iso2 (human): S333‑p, TRPC6 (mouse): S448‑p, TRPC6 (rat): S448‑p, TRPC6 iso2 (rat): S394‑p
 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

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.