Pink1
entrez
298575
canonical
uniprot
B5DFG1
canonical
ensembl
ENSRNOG00000015385
resolver
ensembl
ENSRNOG00055022185
resolver
ensembl
ENSRNOG00060031840
resolver
ensembl
ENSRNOG00065025716
resolver
ensp
ENSRNOP00000058880
resolver
ensp
ENSRNOP00000069316
resolver
ensp
ENSRNOP00055031097
resolver
ensp
ENSRNOP00060045630
resolver
ensp
ENSRNOP00065036409
resolver
enst
ENSRNOT00000065497
resolver
enst
ENSRNOT00000083474
resolver
enst
ENSRNOT00055038158
resolver
enst
ENSRNOT00060055185
resolver
enst
ENSRNOT00065044396
resolver
genesymbol
Pink1
resolver
uniprot
D3Z9M9
resolver
uniprot_entry
D3Z9M9_RAT
resolver
uniprot_entry
PINK1_RAT
resolver
amino_acid_sequence
MAVRQALGRGLQLGRALLLRFAPKPGPVSGWGKPGPGAAWGRGERPGRVSSPGAQPRPLGLPLPDRYRFFRQSVAGLAARIQRQFVVRARGGAGPCGRAVFLAFGLGLGLIEEKQAESRRAASACQEIQAIFTQKNKQVSDPLDTRRWQGFRLEDYLIGQAIGKGCNAAVYEATMPTLPQHLEKAKHLGLLGKGPDVVSKGADGEQAPGAPAFPFAIKMMWNISAGSSSEAILSKMSQELVPASRMALDGEYGAVTYRRSRDGPKQLAPHPNIIRVFRAFTSSVPLLPGALADYPDMLPPHYYPEGLGHGRTLFLVMKNYPCTLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGCCLADERVGLQLPFNSSSVERGGNGSLMAPEVSTAHSGPHAVIDYSKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPKSVPPETRQLVRSLLQREANKRPSARIAANVLHLSLWGEHLLALKNLKLDKMIAWLLQQSAATLLADRLREKSCVETKLQMLFLANLECEALCQAALLLSSWRAAP
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Serine/threonine-protein kinase which acts as a sensor of mitochondrial damage and protects against mitochondrial dysfunction during cellular stress (By similarity). It phosphorylates mitochondrial proteins to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components (By similarity). In healthy mitochondria, PINK1 is translocated across the mitochondrial outer membrane (MOM) via the translocase of the outer membrane (TOM) complex, and inserted into the mitochondrial inner membrane (MIM) via the translocase of the inner membrane (TIM23) complex where it is cleaved and released into the cytosol (By similarity). Depending on the severity of mitochondrial damage, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to eliminating severely damaged mitochondria via PINK1-PRKN-dependent mitophagy (By similarity). When cellular stress results in irreversible mitochondrial damage, PINK1 accumulates at the outer mitochondrial membrane (OMM) where it phosphorylates pre-existing polyubiquitin chains at 'Ser-65', recruits PRKN from the cytosol to the OMM and activates PRKN by phosphorylation at 'Ser-65' (By similarity). Activated PRKN then ubiquitinates VDAC1 and other OMM proteins to initiate mitophagy (By similarity). The PINK1-PRKN pathway also promotes fission of damaged mitochondria by phosphorylating and thus promoting the PRKN-dependent degradation of mitochondrial proteins involved in fission such as MFN2 (By similarity). This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes (By similarity). Also promotes mitochondrial fission independently of PRKN and ATG7-mediated mitophagy, via the phosphorylation and activation of DNM1L (By similarity). Regulates motility of damaged mitochondria by promoting the ubiquitination and subsequent degradation of MIRO1 and MIRO2; in motor neurons, this likely inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria undergoing mitophagy in the soma (By similarity). Required for ubiquinone reduction by mitochondrial complex I by mediating phosphorylation of complex I subunit NDUFA10 (By similarity). Phosphorylates LETM1, positively regulating its mitochondrial calcium transport activity (By similarity). {ECO:0000250|UniProtKB:Q99MQ3, ECO:0000250|UniProtKB:Q9BXM7}.
uniprot
proteins
mass_dalton
63219
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved. In healthy cells, the precursor is continuously imported into the inner mitochondrial membrane (IMM), where it is proteolytically cleaved by mitochondrial-processing peptidase (MPP) and then undergoes further proteolytic cleavage by PARL or AFG3L2 to give rise to the 52 kDa short form. The 52 kDa short form is then released into the cytosol where it rapidly undergoes proteasome-dependent degradation. In unhealthy cells, when cellular stress conditions lead to the loss of mitochondrial membrane potential, mitochondrial import is impaired leading to the precursor accumulating on the outer mitochondrial membrane (OMM). If accumulation at the OMM fails and it is imported into the depolarized mitochondria, it undergoes cleavage by the IMM protease OMA1, promoting its subsequent degradation by the proteasome. {ECO:0000250|UniProtKB:Q9BXM7}.; PTM: Autophosphorylated. Loss of mitochondrial membrane potential results in the precursor accumulating on the outer mitochondrial membrane (OMM) where it is activated by autophosphorylation. Autophosphorylation at Ser-227 and Ser-401 is sufficient and essential for selective recruitment of PRKN to depolarized mitochondria, via PINK1-dependent phosphorylation of ubiquitin and maybe PRKN. {ECO:0000250|UniProtKB:Q9BXM7}.
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Ser/Thr protein kinase family
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
29934347
uniprot
proteins
pubmed
31536960
uniprot
proteins
sequence_length
580
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:31536960}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q99MQ3}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BXM7}. Note=Localizes mostly in mitochondrion and the two smaller proteolytic processed fragments localize mainly in cytosol (By similarity). In healthy mitochondria, PINK1 is translocated across the mitochondrial membranes (By similarity). Upon mitochondrial membrane depolarization following damage, PINK1 import is stalled, which induces its accumulation in the outer mitochondrial membrane and the activation of its kinase activity (By similarity). {ECO:0000250|UniProtKB:Q9BXM7}.
uniprot
proteins