protein
| ubiquitin conjugating enzyme (E2) dependent and SNCA (synuclein alpha) (ubiquination of ASP22) with GPR37 (PAELR) |
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interacts with programmed cell death-2 isoform 1 (PDCD2-1) and promotes its ubiquitination |
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interacting with PSMA4, through the the C-terminal IBR-RING domain of parkin and the C-terminal part of PSMA4 |
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SYT11 |
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PARK7 promoted by oxidative stress |
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CDCREL1 |
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associating with PFAM |
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interacting with SCNAIP1 (ubiquitination of synphilin-1 by parkin may be involved in the formation of Lewy body inclusions associated with Parkinson disease) |
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interacts with and promotes degradation-independent ubiquitylation of IKKgamma/NEMO (NF-kappaB essential modifier) and TRAF2, two critical components of the NF-kappaB pathway |
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HDAC6 directly binds to PARK2 and mediates its transport in response to proteasome inhibition |
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cell-type dependent functional interaction between PARK2 and LIMK1 (links parkin and LIMK1 in the pathogenesis of familial PD) |
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interacting with PINK1 (phosphorylation by PINK1 on its linker region promotes its mitochondrial translocation, and the RING1 domain of Parkin is critical for this occurrence) |
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directly interacts with PINK1, but did not bind to pathogenic PINK1 mutants (stabilizes PINK1 by interfering with its degradation via the ubiquitin-mediated proteasomal pathway) |
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interacting wiuth RNF41 which catalyze degradation of PARK2 via the ubiquitin-proteasome pathway, suggesting that it may be involved in the development of Parkinson disease via the regulation of PARK2 |
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interacting with PINK1 (PARK7, PINK1, and PARK2 function in common biological processes that are critical for mitochondrial function, such that compromise of their activity leads to human disease) |
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interacting with ABL1 (ABL1 SH3 domain is required for the interaction with parkin) |
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BCL2 anti-apoptotic and autophagy inhibitory protein, is a substrate for parkin (directly interacts with BCL2 specifically through its C terminus and mediates the mono-ubiquitination of BCL2) |
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functional interaction between ATXN3 and PARK2 (both wild-type and polyQ-expanded mutant ataxin-3 can deubiquitinate parkin, regardless of the lysine residue used to assemble poly-Ub chains) ( |
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PARK2 suppresses the transcription of MAOA, MAOB to control oxidative stress induced by dopamine oxidation |
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after mitochondrial fission upon depolarization, prevents or delays refusion of mitochondria, likely by the elimination of mitofusins (MFN1, MFN2) |
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ZNF746 is a parkin (PARK2) interacting substrate (parkin regulates the levels of PARIS via the ubiquitin proteasome system (UPS)) |
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HSPA9 interacting with PARK2 (relatively decreased mortalin expression level and its impaired interaction with PARK2 could affect its roles in mitochondrial function) |
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interacts with and selectively mediates the atypical poly-ubiquitination of MFN1, leading to its enhanced turnover by proteasomal degradation |
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interaction with AMBRA1 (interaction of Parkin with AMBRA1 is a key mechanism for induction of the final clearance step of Parkin-mediated mitophagy) |
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contributes to the functions of TP53 in regulating energy metabolism, and antioxidant defense, and thus the function of TP53 in tumor suppression |
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C1QBP is a novel interactor of parkin in the brain (C1QBP can regulate mitochondrial morphology and dynamics by promoting parkin degradation through autophagy) |
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Ataxin-3 opposes PARK2 ubiquitination by regulating the E2 ubiquitin-conjugating enzyme |
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PRKN and PINK1 are NEDD8 conjugated |
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PARK2 prevented basal and apoptotic stress-induced translocation of BAX to the mitochondria |
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PINK1 autophosphorylation upon membrane potential dissipation is essential for PARK2 recruitment to damaged mitochondria |
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VDAC1, VDAC2, VDAC3 serve as mitochondrial docking sites to recruit PRKN from the cytosol to defective mitochondria |
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mitochondrial hexokinase I (HK1) is a novel PRKN substrate |
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PRKN-mediated HK1 degradation may inhibit glycolysis, and consequently Parkin’s mitochondriallocalization is hindered, suggesting HK1 functions as a negative feedback component |
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PARK2 ubiquitinates TARDBP and facilitates its cytosolic accumulation through a multiprotein complex with HDAC6 |
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UBE2A is a regulator of PRKN-dependent mitophagy suggesting a critical role for UBE2A in maintaining neuronal function |
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PRKN differently regulates PSEN1 and PSEN2 functions by direct control of their promoter transcription |
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NACC1 and PRKN are co-localized within the cell and interact with one another, leading to a decrease in PRKN levels |
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interaction of cytosolic PINK1 with PARK2 represses PARK2 translocation to the mitochondria and subsequent mitophagy |
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PARK2 ubiquitination affects its protein stability and E3 ligase activity, possibly leading to SNCA sequestration and subsequent clearance |
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RHOT1 is a direct PRKN substrate |
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PINK1 acts as an upstream factor for PARK2 and is essential both for the activation of latent E3 PARK2 activity and for recruiting PARK2 onto depolarized mitochondria |
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BECN1 interacts with the Parkinson disease-related protein PARK2 (BECN1 interacts with PARK2 and regulates PARK2 translocation to mitochondria as well as PARK2-induced mitophagy prior to autophagosome formation) |
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UBE2N, UBE2L3 and UBE2D2/3 synergistically contribute to PRKN-mediated mitophagy |
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BCL2 proteins suppressed mitophagy through inhibition of PARK2 translocation to depolarized mitochondria |
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USP8/UBPY, a deubiquitinating enzyme not previously implicated in mitochondrial quality control, is critical for PARK2-mediated mitophagy |
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PINK1 accumulation leads to PARK2 recruitment from the cytosol, which in turn promotes the degradation of the damaged mitochondria by autophagy (mitophagy) |
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BNIP3L is a substrate of PRKN to drive PRKN-mediated mitophagy, and promoting mitophagy in the PINK1/PRKN pathway associated with Parkinson Disease pathogenesis |
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degradation of wildtype and mutant ATXN2 is dependent on FBXW8, and ATXN2 accumulation selectively modulates FBXW8 levels, while PARK2 might act indirectly through FBXW8 |
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transiently interacts with PINK1, and IMMT downregulation leads to a reduction in PINK1 and mislocalization of PRKN |
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PRKN modulates mitochondrial depolarization and apoptosis in a BCL2L1-dependent manner |
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PGAM5 regulates PINK1-PRKN-mediated mitophagy, which can exert a neuroprotective effect against carbonyl cyanide m-chlorophenylhydrazone (CCCP)-induced apoptosis |
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PRKN recruitment to impaired mitochondria for nonselective ubiquitylation is facilitated by MARCH5 |
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similarly to PRKN, PACRG promoted NFKB1 activation in response to TNF |
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