Curated Information
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Home > Curated Information Page > PubMed Id: 23949442
Yun HJ, et al. (2013) LRRK2 phosphorylates Snapin and inhibits interaction of Snapin with SNAP-25. Exp Mol Med 45, e36 23949442
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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T117-p - SNAPIN (human)
Modsite: NHsVAKEtARRRAML SwissProt Entrez-Gene
Orthologous residues
SNAPIN (human): T117‑p, SNAPIN (mouse): T117‑p, SNAPIN (rat): T117‑p
Characterization
Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, western blotting
Relevant cell lines - cell types - tissues:  HEK293T (epithelial)
Cellular systems studied:  cell lines
Species studied:  human
Enzymes shown to modify site in vitro
Type Enzyme
KINASE LRRK2 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE LRRK2 (human) co-immunoprecipitation
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
SNAP-25 (human) Disrupts molecular association, regulation pull-down assay, co-immunoprecipitation