Curated Information
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Curated Information Page
PubMed Id: 20823226 
Ko HS, et al. (2010) Phosphorylation by the c-Abl protein tyrosine kinase inhibits parkin's ubiquitination and protective function. Proc Natl Acad Sci U S A 107, 16691-6 20823226
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.
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Y143-p - PARK2 (human)
Orthologous residues
PARK2 (human): Y143‑p, PARK2 (mouse): Y142‑p
Characterization
 Methods used to characterize site in vivo mass spectrometry (in vitro), phospho-antibody, western blotting
 Disease tissue studied:  neuroblastoma, Parkinson's disease
 Relevant cell lines - cell types - tissues:  'neuron, striatal'-brain, 'neuron, substantia nigra'-brain, SH-SY5Y (neural crest)
 Cellular systems studied:  cell lines, tissue
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Abl (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Abl (human) co-immunoprecipitation, siRNA inhibition of enzyme, transfection of inactive enzyme, pharmacological activator of upstream enzyme, pharmacological inhibitor of upstream enzyme, transfection of wild-type enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
MPP+ increase
STI571 MPP+ inhibit treatment-induced increase
DA increase
STI571 DA inhibit treatment-induced increase
siRNA MPP+ inhibit treatment-induced increase siRNA Abl
Downstream Regulation
 Effect of modification (function):  enzymatic activity, inhibited, ubiquitination
 Comments:  inhibits PARK2 autoubiquitination
Associated Diseases
Diseases: Alterations: Comments:
Parkinson's disease increased


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