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serine/threonine protein kinase PINK1, mitochondrial; PTEN-induced putative kinase protein 1; BRPK (PINK1)

Function: - protects against mitochondrial dysfunction during cellular stress, potentially by phosphorylating mitochondrial proteins - phosphorylates ubiquitin & the ubiquitin-like domain of Parkin [4] - interacts with the mitochondrial outer membrane - may be modulated by mitochondrial reactive oxygen species [4] - autophosphorylated Cofactor: Mg+2 Structure: - belongs to the protein kinase superfamily, Ser/Thr protein kinase family - may be homologous to CaM kinases - contains 1 protein kinase domain Compartment: - mitochondrial outer membrane; single-pass membrane protein Alternative splicing: named isoforms=2 Expression: - highly expressed in heart, skeletal muscle & testis, & at lower levels in brain, placenta, liver, kidney, pancreas, prostate, ovary & small intestine - present in the embryonic testis from an early stage of development Pathology: - defects in PINK1 are the cause of Parkinson's disease type 6

Related

mutated in multiple advanced cancers 1; protein tyrosine phosphatase PTEN; phosphatase & tensin homolog deleted on chromosome ten; phosphatase & tensin homolog; phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase & dual-specificity protein phosphatase PTEN (PTEN, MMAC1, TEP1) Parkinson's disease 6, autosomal recessive PINK1 gene mutation

General

mitochondrial membrane protein serine/threonine kinase

Properties

SIZE: entity length = 581 aa MW = 63 kD COMPARTMENT: mitochondria STATE: active state MOTIF: Mitochondrial intermembrane {78-93} transmembrane domain {94-110} kinase domain SITE: 156-511 MOTIF: ATP-binding site NAME: ATP-binding site SITE: 162-170 ATP-binding site NAME: ATP-binding site SITE: 186-186 aspartate residue {D362}

Database Correlations

OMIM correlations MORBIDMAP 608309 UniProt Q9BXM7 Pfam PF00069 Entrez Gene 65018 Kegg hsa:65018 ENZYME 2.7.11.1

References

  1. UniProt :accession Q9BXM7
  2. GeneReviews http://www.ncbi.nlm.nih.gov/sites/genetests/lab/gene/PINK1
  3. Valente EM et al. Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 304:1158-60, 2004 PMID: 15087508
  4. Gan ZY, Callegari S, Cobbold SA et al Activation mechanism of PINK1 Nature 2021. December 21 PMID: 34933320 https://www.nature.com/articles/s41586-021-04340-2