PARK2
Gene Ontology Biological Process
- adult locomotory behavior [ISS]
- aggresome assembly [IMP]
- cellular protein catabolic process [IMP]
- cellular response to dopamine [TAS]
- cellular response to manganese ion [TAS]
- cellular response to toxic substance [IMP]
- cellular response to unfolded protein [TAS]
- central nervous system development [TAS]
- dopamine metabolic process [TAS]
- mitochondrial fission [ISS]
- mitochondrion degradation [IMP, ISS]
- mitochondrion organization [ISS]
- negative regulation of JNK cascade [ISS]
- negative regulation of actin filament bundle assembly [IDA]
- negative regulation of cell death [IDA]
- negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [IDA, IMP]
- negative regulation of glucokinase activity [IDA]
- negative regulation of insulin secretion [IDA]
- negative regulation of mitochondrial fusion [ISS]
- negative regulation of neuron apoptotic process [IDA]
- negative regulation of neuron death [IGI]
- negative regulation of oxidative stress-induced cell death [NAS, TAS]
- negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway [IDA]
- negative regulation of protein phosphorylation [IDA]
- negative regulation of reactive oxygen species metabolic process [IGI]
- negative regulation of release of cytochrome c from mitochondria [IDA]
- neuron cellular homeostasis [ISS]
- positive regulation of DNA binding [IDA]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IDA, IMP]
- positive regulation of mitochondrial fission [ISS]
- positive regulation of mitochondrial fusion [IMP]
- positive regulation of proteasomal protein catabolic process [IGI]
- positive regulation of protein linear polyubiquitination [IGI]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of tumor necrosis factor-mediated signaling pathway [IDA]
- proteasome-mediated ubiquitin-dependent protein catabolic process [IDA]
- protein K27-linked ubiquitination [TAS]
- protein K29-linked ubiquitination [TAS]
- protein K48-linked ubiquitination [IDA]
- protein K6-linked ubiquitination [TAS]
- protein K63-linked ubiquitination [IDA, TAS]
- protein autoubiquitination [IDA]
- protein monoubiquitination [IDA]
- protein polyubiquitination [IDA]
- protein ubiquitination [IDA, IMP]
- protein ubiquitination involved in ubiquitin-dependent protein catabolic process [IC, IDA, NAS, TAS]
- regulation of autophagy [IDA]
- regulation of cellular response to oxidative stress [ISS]
- regulation of dopamine secretion [TAS]
- regulation of glucose metabolic process [TAS]
- regulation of lipid transport [TAS]
- regulation of mitochondrion degradation [TAS]
- regulation of mitochondrion organization [IDA]
- regulation of reactive oxygen species metabolic process [IMP]
- regulation of synaptic vesicle transport [NAS]
- response to endoplasmic reticulum stress [IMP]
- response to oxidative stress [ISS]
- zinc ion homeostasis [ISS]
Gene Ontology Molecular Function- F-box domain binding [IPI]
- G-protein coupled receptor binding [IPI]
- Hsp70 protein binding [IPI]
- PDZ domain binding [IPI]
- SH3 domain binding [TAS]
- actin binding [IPI]
- chaperone binding [IPI]
- cullin family protein binding [IDA]
- heat shock protein binding [IPI]
- histone deacetylase binding [IPI]
- identical protein binding [IPI]
- kinase binding [IPI]
- protein binding [IPI]
- protein kinase binding [IPI]
- tubulin binding [IPI]
- ubiquitin binding [IDA]
- ubiquitin conjugating enzyme binding [IPI]
- ubiquitin protein ligase activity [IDA, NAS]
- ubiquitin protein ligase binding [IPI]
- ubiquitin-protein transferase activity [IDA]
- ubiquitin-specific protease binding [IPI]
- zinc ion binding [TAS]
- F-box domain binding [IPI]
- G-protein coupled receptor binding [IPI]
- Hsp70 protein binding [IPI]
- PDZ domain binding [IPI]
- SH3 domain binding [TAS]
- actin binding [IPI]
- chaperone binding [IPI]
- cullin family protein binding [IDA]
- heat shock protein binding [IPI]
- histone deacetylase binding [IPI]
- identical protein binding [IPI]
- kinase binding [IPI]
- protein binding [IPI]
- protein kinase binding [IPI]
- tubulin binding [IPI]
- ubiquitin binding [IDA]
- ubiquitin conjugating enzyme binding [IPI]
- ubiquitin protein ligase activity [IDA, NAS]
- ubiquitin protein ligase binding [IPI]
- ubiquitin-protein transferase activity [IDA]
- ubiquitin-specific protease binding [IPI]
- zinc ion binding [TAS]
Gene Ontology Cellular Component
UBE2D2
Gene Ontology Biological Process
- MyD88-independent toll-like receptor signaling pathway [TAS]
- TRIF-dependent toll-like receptor signaling pathway [TAS]
- cellular protein modification process [TAS]
- cellular response to hypoxia [TAS]
- innate immune response [TAS]
- protein K48-linked ubiquitination [IDA]
- protein polyubiquitination [IDA]
- protein ubiquitination [IDA]
- regulation of transcription from RNA polymerase II promoter in response to hypoxia [TAS]
- toll-like receptor 3 signaling pathway [TAS]
- toll-like receptor 4 signaling pathway [TAS]
- toll-like receptor signaling pathway [TAS]
- ubiquitin-dependent protein catabolic process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
Publication
Phosphorylation of Parkin at Serine65 is essential for activation: elaboration of a Miro1 substrate-based assay of Parkin E3 ligase activity.
Mutations in PINK1 and Parkin are associated with early-onset Parkinson's disease. We recently discovered that PINK1 phosphorylates Parkin at serine65 (Ser(65)) within its Ubl domain, leading to its activation in a substrate-free activity assay. We now demonstrate the critical requirement of Ser(65) phosphorylation for substrate ubiquitylation through elaboration of a novel in vitro E3 ligase activity assay using full-length untagged ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| PARK2 UBE2D2 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | 1055267 | |
| PARK2 UBE2D2 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - | |
| PARK2 UBE2D2 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | 947904 | |
| PARK2 UBE2D2 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - | |
| PARK2 UBE2D2 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - | |
| UBE2D2 PARK2 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | High | - | BioGRID | 2512675 | |
| PARK2 UBE2D2 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - |
Curated By
- BioGRID