PINK1 Protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins. Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy) by mediating activation and translocation of PRKN. Targets PRKN to dysfunctional depolarized mitochondria through the phosphorylation of MFN2. Activates PRKN in 2 steps: (1) by mediating phosphorylation at 'Ser-65' of PRKN and (2) mediating phosphorylation of ubiquitin, converting PRKN to its fully-active form. Required for ubiquinone reduction by mitochondrial complex I by mediating phosphorylation of complex I subunit NDUFA10. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Highly expressed in heart, skeletal muscle and testis, and at lower levels in brain, placenta, liver, kidney, pancreas, prostate, ovary and small intestine. Present in the embryonic testis from an early stage of development. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: EC 2.7.11.1; Kinase, protein; Membrane protein, integral; Mitochondrial; NKF2 family; Other group; Protein kinase, Other; Protein kinase, Ser/Thr (non-receptor)
Chromosomal Location of human Ortholog: 1p36.12
Cellular Component:  astrocyte projection; axon; cell body; chromatin; cytoplasm; cytoskeleton; cytosol; growth cone; integral component of mitochondrial outer membrane; Lewy body; membrane; mitochondrial inner membrane; mitochondrial intermembrane space; mitochondrial outer membrane; mitochondrion; nucleus; perinuclear region of cytoplasm
Molecular Function:  ATP binding; C3HC4-type RING finger domain binding; calcium-dependent protein kinase activity; kinase activity; magnesium ion binding; peptidase activator activity; protease binding; protein binding; protein kinase activity; protein kinase B binding; protein serine/threonine kinase activity; ubiquitin protein ligase binding
Biological Process:  activation of protein kinase B activity; autophagy of mitochondrion; cellular response to hydrogen sulfide; cellular response to hypoxia; cellular response to oxidative stress; cellular response to toxic substance; establishment of protein localization to mitochondrion; intracellular signal transduction; macroautophagy; maintenance of protein location in mitochondrion; mitochondrion organization; mitochondrion to lysosome transport; negative regulation of autophagosome assembly; negative regulation of autophagy of mitochondrion; negative regulation of gene expression; negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway; negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; negative regulation of intrinsic apoptotic signaling pathway; negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide; negative regulation of JNK cascade; negative regulation of macroautophagy; negative regulation of mitochondrial fission; negative regulation of neuron apoptotic process; negative regulation of oxidative stress-induced cell death; negative regulation of oxidative stress-induced neuron death; negative regulation of reactive oxygen species metabolic process; peptidyl-serine autophosphorylation; peptidyl-serine phosphorylation; positive regulation of ATP biosynthetic process; positive regulation of cristae formation; positive regulation of DNA-binding transcription factor activity; positive regulation of dopamine secretion; positive regulation of free ubiquitin chain polymerization; positive regulation of histone deacetylase activity; positive regulation of I-kappaB kinase/NF-kappaB signaling; positive regulation of macroautophagy; positive regulation of mitochondrial electron transport, NADH to ubiquinone; positive regulation of mitophagy in response to mitochondrial depolarization; positive regulation of NMDA glutamate receptor activity; positive regulation of peptidase activity; positive regulation of peptidyl-serine phosphorylation; positive regulation of protein dephosphorylation; positive regulation of protein kinase B signaling; positive regulation of protein phosphorylation; positive regulation of protein ubiquitination; positive regulation of release of cytochrome c from mitochondria; positive regulation of synaptic transmission, dopaminergic; positive regulation of translation; positive regulation of ubiquitin-protein transferase activity; protein phosphorylation; protein stabilization; protein ubiquitination; regulation of autophagy of mitochondrion; regulation of cellular response to oxidative stress; regulation of hydrogen peroxide metabolic process; regulation of mitochondrial membrane potential; regulation of mitochondrion organization; regulation of oxidative phosphorylation; regulation of proteasomal protein catabolic process; regulation of protein complex assembly; regulation of protein targeting to mitochondrion; regulation of protein ubiquitination; regulation of reactive oxygen species metabolic process; regulation of synaptic vesicle transport; respiratory electron transport chain; response to ischemia; response to oxidative stress; TORC2 signaling; ubiquitin-dependent protein catabolic process
Disease: Parkinson Disease 6, Autosomal Recessive Early-onset
Reference #:  Q9BXM7 (UniProtKB)
Alt. Names/Synonyms: BRPK; FLJ27236; PARK6; PINK1; protein kinase BRPK; PTEN induced kinase 1; PTEN induced putative kinase 1; PTEN-induced putative kinase protein 1; Serine/threonine-protein kinase PINK1, mitochondrial
Gene Symbols: PINK1
Molecular weight: 62,769 Da
Basal Isoelectric point: 9.43  Predict pI for various phosphorylation states
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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PINK1

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Cross-references to other databases:  AlphaFold  |  STRING  |  cBioPortal  |  Wikipedia  |  neXtProt  |  Protein Atlas  |  BioGPS  |  KinBase  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene