Curated Information
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Home > Curated Information Page > PubMed Id: 22910362
Okatsu K, et al. (2012) PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria. Nat Commun 3, 1016 22910362
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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S228-p - PINK1 (human)
Modsite: MWNISAGsSSEAILN SwissProt Entrez-Gene
Orthologous residues
PINK1 (human): S228‑p, PINK1 (mouse): S227‑p, PINK1 (rat): S227‑p
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PINK1 (human) electrophoretic mobility shift
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
CCCP increase
Downstream Regulation
Effect of modification (function):  intracellular localization
Comments:  promotes mitochondrial localization of parkin

S402-p - PINK1 (human)
Modsite: GLQLPFSsWYVDRGG SwissProt Entrez-Gene
Orthologous residues
PINK1 (human): S402‑p, PINK1 (mouse): S401‑p, PINK1 (rat): S401‑p
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PINK1 (human) electrophoretic mobility shift
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
CCCP increase
Downstream Regulation
Effect of modification (function):  intracellular localization
Comments:  promotes mitochondrial localization of parkin