Curated Information
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Home > Curated Information Page > PubMed Id: 24189060
Okatsu K, et al. (2013) A Dimeric PINK1-containing Complex on Depolarized Mitochondria Stimulates Parkin Recruitment. J Biol Chem 288, 36372-84 24189060
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

S402-p - PINK1 (human)
Modsite: GLQLPFSsWYVDRGG SwissProt Entrez-Gene
Orthologous residues
PINK1 (human): S402‑p, PINK1 (mouse): S401‑p, PINK1 (rat): S401‑p
Downstream Regulation
Effect of modification (function):  protein conformation
Comments:  PINK1 complex formation, Parkin recruitment onto depolarized mitochondria