Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential.
Hereditary early-onset Parkinson's disease caused by mutations in PINK1.
Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability.
Association of PINK1 and DJ-1 confers digenic inheritance of early-onset Parkinson's disease.
Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin.
PINK1 protein in normal human brain and Parkinson's disease.
PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1.
Biochemical aspects of the neuroprotective mechanism of PTEN-induced kinase-1 (PINK1).
PINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neurons.
The kinase domain of mitochondrial PINK1 faces the cytoplasm.
PINK1 controls mitochondrial localization of Parkin through direct phosphorylation.
Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation.
Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission.
Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signaling.
PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy.
The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations.
Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy.
PINK1 cleavage at position A103 by the mitochondrial protease PARL.
A new cytosolic pathway from a Parkinson disease-associated kinase, BRPK/PINK1: activation of AKT via mTORC2.
Functional alteration of PARL contributes to mitochondrial dysregulation in Parkinson's disease.
The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking.
Mitochondrial Parkin recruitment is impaired in neurons derived from mutant PINK1 induced pluripotent stem cells.
Synaptic vesicle trafficking and Parkinson's disease.
PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility.
Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment.
Pharmacological rescue of mitochondrial deficits in iPSC-derived neural cells from patients with familial Parkinson's disease.
Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition.
Phosphatase and tensin homolog (PTEN)-induced putative kinase 1 (PINK1)-dependent ubiquitination of endogenous Parkin attenuates mitophagy: study in human primary fibroblasts and induced pluripotent stem cell-derived neurons.
Increase of oxidative stress by a novel PINK1 mutation, P209A.
SARM1 and TRAF6 bind to and stabilize PINK1 on depolarized mitochondria.
The Parkinson's disease-linked proteins Fbxo7 and Parkin interact to mediate mitophagy.
Mitochondrial impairment increases FL-PINK1 levels by calcium-dependent gene expression.
High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy.
Cytosolic cleaved PINK1 represses Parkin translocation to mitochondria and mitophagy.
Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control.
BAG5 protects against mitochondrial oxidative damage through regulating PINK1 degradation.
Oxidative stress-induced signaling pathways implicated in the pathogenesis of Parkinson's disease.
Loss of PINK1 attenuates HIF-1α induction by preventing 4E-BP1-dependent switch in protein translation under hypoxia.
Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65.
PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity.
Ubiquitin is phosphorylated by PINK1 to activate parkin.
PARK13 regulates PINK1 and subcellular relocation patterns under oxidative stress in neurons.
The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy.
Phosphorylation of mitochondrial polyubiquitin by PINK1 promotes Parkin mitochondrial tethering.
Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis.
PINK1 kinase catalytic activity is regulated by phosphorylation on serines 228 and 402.
Phospho-tyrosine dependent protein-protein interaction network.
Rewiring of the Human Mitochondrial Interactome during Neuronal Reprogramming Reveals Regulators of the Respirasome and Neurogenesis.
Decision between mitophagy and apoptosis by Parkin via VDAC1 ubiquitination.
The mitochondrial inner membrane protein LETM1 modulates cristae organization through its LETM domain.
PINK1 phosphorylates Drp1(S616) to regulate mitophagy-independent mitochondrial dynamics.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
OGT Regulates Hematopoietic Stem Cell Maintenance via PINK1-Dependent Mitophagy.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
The role of the individual TOM subunits in the association of PINK1 with depolarized mitochondria.
TIM23 facilitates PINK1 activation by safeguarding against OMA1-mediated degradation in damaged mitochondria.
GRAF1 integrates PINK1-Parkin signaling and actin dynamics to mediate cardiac mitochondrial homeostasis.
Mechanism of human PINK1 activation at the TOM complex in a reconstituted system.
Pink1 is recruited from the cytoplasm to the mitochondria
Uncleaved Pink1 accumulates in damaged mitochondria
Pink1 is cleaved on healthy mitochondria
PINK1-PRKN Mediated Mitophagy
PINK1 is autophosphorylated
PINK1 phosphorylates Ub on MOM proteins
PINK1 phosphorylates PRKN at S65