Curated Information
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Curated Information Page
PubMed Id: 12738781 
Nakajima H, Toyoshima-Morimoto F, Taniguchi E, Nishida E (2003) Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate. J Biol Chem 278, 25277-80 12738781
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.
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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S426-p - Myt1 (human)
Orthologous residues
Myt1 (human): S426‑p, Myt1 (mouse): T417‑p, Myt1 (starfish):
Characterization
 Methods used to characterize site in vivo electrophoretic mobility shift, mutation of modification site
 Relevant cell lines - cell types - tissues:  HeLa (cervical) [Myt1 (human)]
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PLK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PLK1 (human) genetic transfer of dominant-negative enzyme, genetic transfer of wild-type enzyme

T495-p - Myt1 (human)
Orthologous residues
Myt1 (human): T495‑p, Myt1 (mouse): S486‑p, Myt1 (starfish): T545‑p
Characterization
 Methods used to characterize site in vivo electrophoretic mobility shift, mutation of modification site
 Relevant cell lines - cell types - tissues:  HeLa (cervical) [Myt1 (human)]
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PLK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PLK1 (human) genetic transfer of dominant-negative enzyme, genetic transfer of wild-type enzyme


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