Curated Information
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Home > Curated Information Page > PubMed Id: 28486561
Horváth D, et al. (2017) Myosin phosphatase and RhoA-activated kinase modulate neurotransmitter release by regulating SNAP-25 of SNARE complex. PLoS One 12, e0177046 28486561
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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T138-p - SNAP-25 (mouse)
Modsite: GGFIRRVtNDARENE SwissProt Entrez-Gene
Orthologous residues
SNAP‑25 (human): T138‑p, SNAP‑25 iso2 (human): T138‑p, SNAP‑25 (mouse): T138‑p, SNAP‑25 (rat): T138‑p
Characterization
Methods used to characterize site in vivo immunoprecipitation, mass spectrometry, phospho-antibody, western blotting
Disease tissue studied:  neuroblastoma
Relevant cell lines - cell types - tissues:  B50 (neural crest)
Cellular systems studied:  cell lines
Species studied:  rat
Enzymes shown to modify site in vitro
Type Enzyme
KINASE ROCK2 (human)
PHOSPHATASE PPP1CA (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ROCK2 (rat) co-immunoprecipitation, pharmacological inhibitor of upstream enzyme, phospho-antibody, phosphopeptide analysis
PHOSPHATASE MYPT1 (rat) siRNA inhibition of enzyme, co-immunoprecipitation, phospho-antibody
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Effect of modification (process):  exocytosis, inhibited
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
STX1A (mouse) Disrupts co-immunoprecipitation