Curated Information
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Curated Information Page
PubMed Id: 15590641 
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.
Nilius B, et al. (2005) Regulation of the Ca2+ sensitivity of the nonselective cation channel TRPM4. J Biol Chem 280, 6423-33 15590641
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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S1145-p - TRPM4 (human)
Orthologous residues
TRPM4 (human): S1145‑p, TRPM4 (mouse): S1144‑p, TRPM4 (rat): S1139‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKCA (human) mutation in upstream enzyme recognition motif, pharmacological activator of upstream enzyme
Downstream Regulation
 Effect of modification (function):  activity, induced

S1152-p - TRPM4 (human)
Orthologous residues
TRPM4 (human): S1152‑p, TRPM4 (mouse): S1151‑p, TRPM4 (rat): S1146‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKCA (human) mutation in upstream enzyme recognition motif, pharmacological activator of upstream enzyme
Downstream Regulation
 Effect of modification (function):  activity, induced


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