Curated Information
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Home > Curated Information Page > PubMed Id: 12730201
Tian JH, Das S, Sheng ZH (2003) Ca2+-dependent phosphorylation of syntaxin-1A by the death-associated protein (DAP) kinase regulates its interaction with Munc18. J Biol Chem 278, 26265-74 12730201
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, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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S188-p - STX1A (rat)
Modsite: IIMDSSIsKQALSEI SwissProt Entrez-Gene
Orthologous residues
STX1A (human): S188‑p, STX1A iso2 (human): S188‑p, STX1A (mouse): S188‑p, STX1A (rat): S188‑p
Characterization
Methods used to characterize site in vivo back-titration
Relevant cell lines - cell types - tissues:  293 (epithelial)
Cellular systems studied:  cell lines
Species studied:  human
Enzymes shown to modify site in vitro
Type Enzyme
KINASE DAPK1 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE DAPK1 (human) co-immunoprecipitation, transfection of inactive enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
ionomycin increase