Previous studies have found that ubiquitin phosphorylation occurred on most eligible serine, threonine, and tyrosine residues (Swaney et al., 2013); the phosphorylation of Ser65 of ubiquitin, the phospho-ubiquitin event driving Parkinson's disease key enzymes of PINK1 or Parkin-Ubl is crucial to activate their activities and respond to mitochondrial damage (Ordureau et al., 2014; Pickrell and Youle, 2015). The gene discussed is PRKN; the disease is Parkinson disease.