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
Gene Ontology annotation based on curation of immunofluorescence data
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
Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase.
Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity.
Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1.
An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin.
Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease.
CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity.
Parkin accumulation in aggresomes due to proteasome impairment.
Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity.
The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI.
A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death.
Parkin is recruited into aggresomes in a stress-specific manner: over-expression of parkin reduces aggresome formation but can be dissociated from parkin's effect on neuronal survival.
BAG5 inhibits parkin and enhances dopaminergic neuron degeneration.
Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: implications for Lewy body formation.
14-3-3eta is a novel regulator of parkin ubiquitin ligase.
Towards a proteome-scale map of the human protein-protein interaction network.
Dopamine covalently modifies and functionally inactivates parkin.
Parkin ubiquitinates and promotes the degradation of RanBP2.
Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration.
Functional modulation of parkin through physical interaction with SUMO-1.
Parkin is an E3 ubiquitin-ligase for normal and mutant ataxin-2 and prevents ataxin-2-induced cell death.
Parkin mediates neuroprotection through activation of IkappaB kinase/nuclear factor-kappaB signaling.
Parkin interacts with LIM Kinase 1 and reduces its cofilin-phosphorylation activity via ubiquitination.
Biochemical aspects of the neuroprotective mechanism of PTEN-induced kinase-1 (PINK1).
Parkin is ubiquitinated by Nrdp1 and abrogates Nrdp1-induced oxidative stress.
PINK1 controls mitochondrial localization of Parkin through direct phosphorylation.
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy.
Direct binding with histone deacetylase 6 mediates the reversible recruitment of parkin to the centrosome.
An empirical framework for binary interactome mapping.
Programmed cell death-2 isoform1 is ubiquitinated by parkin and increased in the substantia nigra of patients with autosomal recessive Parkinson's disease.
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.
Evidence for the presence of full-length PARK2 mRNA and Parkin protein in human blood.
Parkin protects dopaminergic neurons from excessive Wnt/beta-catenin signaling.
Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function.
Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signaling.
PINK1-dependent recruitment of Parkin to mitochondria in mitophagy.
PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1.
PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy.
Disease-causing mutations in parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy.
The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations.
Phosphorylation by the c-Abl protein tyrosine kinase inhibits parkin's ubiquitination and protective function.
Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy.
Molecular chaperone-mediated rescue of mitophagy by a Parkin RING1 domain mutant.
Parkin mono-ubiquitinates Bcl-2 and regulates autophagy.
p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both.
Parkin is transcriptionally regulated by ATF4: evidence for an interconnection between mitochondrial stress and ER stress.
PARIS (ZNF746) repression of PGC-1α contributes to neurodegeneration in Parkinson's disease.
Mitochondrial Parkin recruitment is impaired in neurons derived from mutant PINK1 induced pluripotent stem cells.
UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids.
Synaptic vesicle trafficking and Parkinson's disease.
Autoregulation of Parkin activity through its ubiquitin-like domain.
Parkin interacts with Ambra1 to induce mitophagy.
PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility.
Parkin interacts with Klokin1 for mitochondrial import and maintenance of membrane potential.
Parkin controls dopamine utilization in human midbrain dopaminergic neurons derived from induced pluripotent stem cells.
Inactivation of Pink1 gene in vivo sensitizes dopamine-producing neurons to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and can be rescued by autosomal recessive Parkinson disease genes, Parkin or DJ-1.
Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition.
The importance of Wnt signalling for neurodegeneration in Parkinson's disease.
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.
The E3 ligase parkin maintains mitochondrial integrity by increasing linear ubiquitination of NEMO.
PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria.
Structure and Function of Parkin, PINK1, and DJ-1, the Three Musketeers of Neuroprotection.
Down-regulation of LRRK2 in control and DAT transfected HEK cells increases manganese-induced oxidative stress and cell toxicity.
Mutations in the intellectual disability gene Ube2a cause neuronal dysfunction and impair parkin-dependent mitophagy.
Parkin-catalyzed ubiquitin-ester transfer is triggered by PINK1-dependent phosphorylation.
Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases.
Parkin-dependent degradation of the F-box protein Fbw7β promotes neuronal survival in response to oxidative stress by stabilizing Mcl-1.
The Parkinson's disease-linked proteins Fbxo7 and Parkin interact to mediate mitophagy.
S-Nitrosylation of parkin as a novel regulator of p53-mediated neuronal cell death in sporadic Parkinson's disease.
Ataxin-3 is a multivalent ligand for the parkin Ubl domain.
The regulation and deregulation of Wnt signaling by PARK genes in health and disease.
Identification of the ubiquitin-like domain of midnolin as a new glucokinase interaction partner.
The role of oxidative stress in Parkinson's disease.
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.
Oxidative stress-induced signaling pathways implicated in the pathogenesis of Parkinson's disease.
Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65.
Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism.
PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity.
Ubiquitin is phosphorylated by PINK1 to activate parkin.
The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy.
MUL1 acts in parallel to the PINK1/parkin pathway in regulating mitofusin and compensates for loss of PINK1/parkin.
Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network.
Hepatitis C virus core protein suppresses mitophagy by interacting with parkin in the context of mitochondrial depolarization.
USP30 and parkin homeostatically regulate atypical ubiquitin chains on mitochondria.
Quantitative interaction proteomics of neurodegenerative disease proteins.
F-box protein 7 mutations promote protein aggregation in mitochondria and inhibit mitophagy.
Parkin Modulates Endosomal Organization and Function of the Endo-Lysosomal Pathway.
Prohibitin 2 Is an Inner Mitochondrial Membrane Mitophagy Receptor.
Synaptotagmin-11 is a critical mediator of parkin-linked neurotoxicity and Parkinson's disease-like pathology.
Physiological and pathophysiological characteristics of ataxin-3 isoforms.
The AMPK-Parkin axis negatively regulates necroptosis and tumorigenesis by inhibiting the necrosome.
Decision between mitophagy and apoptosis by Parkin via VDAC1 ubiquitination.
Quantitative fragmentomics allow affinity mapping of interactomes.
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism.
PINK1-PRKN Mediated Mitophagy
PARK2 K63-Ubiquitinates SNCAIP
Regulation of necroptotic cell death
ATXN3 deubiquitinates polyUb-PARK2
Parkin binds Ub:UBE2N:UBE2V1
Misfolded proteins bind PRKN:UBE2N:UBE2V1:Ub
PolyUb:misfolded proteins dissociate from PRKN:UBE2N:UBE2V1
Parkin transfers Ub to misfolded proteins
Ub:misfolded proteins polymerize to PolyUb:misfolded proteins
PRKN polyubiquitinates RIPK3
PRKN ubiquitinates MOM substrates
PRKN binds p-S-Ub:MOM proteins
PINK1 phosphorylates PRKN at S65