| Primary Identifier | IPR040110 | Type | Domain |
| Short Name | PINK1_STKc |
| description | PINK1 is a mitochondrial serine/threonine kinase that acts as a sensor of mitochondrial damage []. It phosphorylates ubiquitin (Ub) and the Ub-like domain (UBL) of the E3 Ub ligase parkin at Ser65. The phosphorylation of Ub and the parkin UBL facilitates the transition from the autoinhibition state to the catalytically active state in parkin []. Upon mitochondrial damage, PINK1 accumulates on the outer mitochondrial membrane (OMM), where it may recruit and activate Parkin []. PINK1 has also been shown to phosphorylate Miro, a component of the primary motor/adaptor complex that anchors kinesin to the mitochondrial surface. The phosphorylation of Miro activates proteasomal degradation of Miro in a Parkin-dependent manner []. PINK1 contains an N-terminal mitochondrial targeting sequence (MTS), a transmembrane domain (TM), a highly conserved serine/threonine kinase domain, and a C-terminal auto-regulatory domain. Mutations of the PINK1 and Parkin genes have been linked to familial Parkinson's disease (PD) []. |
