Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
HomeAbout PhosphoSiteUsing PhosphoSiteprivacy & cookiesCuration ProcessContact
logos LINCs Logo Mt Sinai Logo NIH Logo NCI Logo
Protein Page:
PINK1 (human)

PINK1 Protects against mitochondrial dysfunction during cellular stress, potentially by phosphorylating mitochondrial proteins. Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy). It is necessary for PARK2 recruitment to dysfunctional mitochondria to initiate their degradation. Interats with PARK2. 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. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC; 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
Cellular Component: axon; chromatin; cytoplasm; cytoskeleton; cytosol; integral to mitochondrial outer membrane; membrane; mitochondrial inner membrane; mitochondrial intermembrane space; mitochondrial outer membrane; mitochondrial outer membrane translocase complex; mitochondrion; nucleus; perinuclear region of cytoplasm; TORC2 complex; ubiquitin ligase complex
Molecular Function: ATP binding; kinase activity; magnesium ion binding; protease 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; macroautophagy; mitochondrion degradation; mitochondrion organization and biogenesis; negative regulation of JNK cascade; negative regulation of macroautophagy; negative regulation of neuron apoptosis; peptidyl-serine phosphorylation; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of macroautophagy; positive regulation of peptidyl-serine phosphorylation; positive regulation of protein amino acid phosphorylation; positive regulation of protein kinase B signaling cascade; positive regulation of protein ubiquitination; positive regulation of ubiquitin-protein ligase activity; protein amino acid phosphorylation; protein stabilization; protein ubiquitination; regulation of mitochondrial membrane potential; regulation of oxidative phosphorylation; regulation of protein complex assembly; regulation of protein ubiquitination; response to oxidative stress; response to stress; 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 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 or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below


Protein Structure Not Found.

STRING  |  cBioPortal  |  Wikipedia  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  KinBase  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene