Curated Information
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Curated Information Page
PubMed Id: 15514163 
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.
Haworth RS, et al. (2004) Protein kinase D is a novel mediator of cardiac troponin I phosphorylation and regulates myofilament function. Circ Res 95, 1091-9 15514163
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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S23-p - TNNI3 (rat)
Orthologous residues
TNNI3 (human): S23‑p, TNNI3 (mouse): S23‑p, TNNI3 (rat): S23‑p, TNNI3 (rabbit): S22‑p, TNNI3 (dog): S23‑p, TNNI3 (cow): S24‑p
Characterization
 Methods used to characterize site in vivo phospho-antibody
 Relevant cell lines - cell types - tissues:  myocyte-heart
 Cellular systems studied:  primary cells
 Species studied:  rat
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKD1 (human)

S24-p - TNNI3 (rat)
Orthologous residues
TNNI3 (human): S24‑p, TNNI3 (mouse): S24‑p, TNNI3 (rat): S24‑p, TNNI3 (rabbit): S23‑p, TNNI3 (dog): S24‑p, TNNI3 (cow): S25‑p
Characterization
 Methods used to characterize site in vivo phospho-antibody
 Relevant cell lines - cell types - tissues:  myocyte-heart
 Cellular systems studied:  primary cells
 Species studied:  rat
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKD1 (human)


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