DROME:Q7KTX7

Species (Taxon ID)	Drosophila melanogaster (Fruit fly). (7227)
Gene Name(s)	No Information Provided.
Protein Name(s)	CG10523-PB, isoform B (ECO:0000313 with EMBL:AAN12154.1) FI05213p (ECO:0000313 with EMBL:ACH95278.1) PARKIN (ECO:0000313 with EMBL:AAM18800.2) Parkin, isoform C (ECO:0000313 with EMBL:AAN12155.1)
External Links
UniProt	Q7KTX7
EMBL	AY093423 AF510072 AE003593 AE014296 BT044504
RefSeq	NP_730600.1 NP_730601.1
UniGene	Dm.20129
PDB	2LWR 2M48
PDBsum	2LWR 2M48
SMR	Q7KTX7
DIP	DIP-58616N
IntAct	Q7KTX7
EnsemblMetazoa	FBtr0078318 FBtr0078319
GeneID	40336
KEGG	dme:Dmel_CG10523
UCSC	CG10523-RB
CTD	40336
FlyBase	FBgn0041100
eggNOG	COG5272
GeneTree	ENSGT00390000011034
KO	K04556
OMA	CESLEIA
OrthoDB	EOG738054
PhylomeDB	Q7KTX7
GenomeRNAi	40336
NextBio	818239
PRO	PR:Q7KTX7
Proteomes	UP000000803
GO	GO:0005737 GO:0005829 GO:0005739 GO:0016874 GO:0004842 GO:0008270 GO:0008344 GO:0000266 GO:0000422 GO:0007005 GO:0046329 GO:0010637 GO:0070050 GO:0048477 GO:0048078 GO:0090141 GO:0051865 GO:0000209 GO:0016567 GO:0042787 GO:1900407 GO:0010821 GO:0006979 GO:0030382 GO:0007283 GO:0055069
InterPro	IPR003977 IPR000626 IPR029071 IPR002867
Pfam	PF01485 PF00240
PIRSF	PIRSF037880
PRINTS	PR01475
SMART	SM00647 SM00213
SUPFAM	SSF54236
PROSITE	PS50053

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0004842	ubiquitin-protein ligase activity	PMID:17456438^[1]	ECO:0000314			F	Figure 2	complete CACAO 3712
	GO:0044743	intracellular protein transmembrane import	PMID:20194754^[2]	ECO:0000316		UniProtKB:Q0KHV6	P	Figure 2 shows PINK1 is required for Parkin translocation	complete CACAO 10621
	GO:0031398	positive regulation of protein ubiquitination	PMID:20194754^[2]	ECO:0000314			P	Figure 4 shows parkin overexpression can cause mfn ubiquitination in the absense of PINK1	complete CACAO 10622
	GO:0090141	positive regulation of mitochondrial fission	PMID:20194754^[2]	ECO:0000316		UniProtKB:Q0KHV6	P	Figure 1 shows Parkin and PINK1 activity promotes mitochondrial fission	complete CACAO 10623
	GO:0010637	negative regulation of mitochondrial fusion	PMID:20194754^[2]	ECO:0000316		UniProtKB:Q0KHV6	P	Figure 1 shows Parkin and PINK1 activity inhibits mitochondrial fusion	complete CACAO 10624
involved_in	GO:1904457	positive regulation of neuronal action potential	PMID:28435104^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:1904061	positive regulation of locomotor rhythm	PMID:28435104^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:17456438^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0048078	positive regulation of compound eye pigmentation	PMID:19692353^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:1900407	regulation of cellular response to oxidative stress	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0041100 PANTHER:PTN000188399 UniProtKB:O60260	P	Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0017418 FB:FBgn0041100 MGI:MGI:1355296 PANTHER:PTN000188395 TAIR:locus:2057401 UniProtKB:O60260 UniProtKB:P50876	F	Seeded From UniProt	complete
involved_in	GO:0042981	regulation of apoptotic process	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000188399 ZFIN:ZDB-GENE-050417-109	P	Seeded From UniProt	complete
involved_in	GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1355296 PANTHER:PTN000188395	P	Seeded From UniProt	complete
enables	GO:0031624	ubiquitin conjugating enzyme binding	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0017418 FB:FBgn0041100 PANTHER:PTN000188395 UniProtKB:O60260 UniProtKB:O95376 UniProtKB:Q9Y4X5 WB:WBGene00003967	F	Seeded From UniProt	complete
involved_in	GO:0010821	regulation of mitochondrion organization	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0041100 PANTHER:PTN000188399 UniProtKB:O60260	P	Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0017418 FB:FBgn0041100 MGI:MGI:1344361 MGI:MGI:1344363 PANTHER:PTN000188395 UniProtKB:O60260 UniProtKB:O95376 UniProtKB:Q7Z419	P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000188399 RGD:61797 UniProtKB:O60260	C	Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000188399 UniProtKB:O60260	C	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000188399 RGD:61797 UniProtKB:O60260	C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0041100 MGI:MGI:1355296 PANTHER:PTN000188399 RGD:61797 UniProtKB:O60260	C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0017418 FB:FBgn0041100 MGI:MGI:1355296 PANTHER:PTN000188395 RGD:61797 UniProtKB:O60260 UniProtKB:O95376 UniProtKB:Q7Z419 UniProtKB:Q9UBS8 UniProtKB:Q9Y4X5 WB:WBGene00003967 WB:WBGene00016158	C	Seeded From UniProt	complete
involved_in	GO:0001933	negative regulation of protein phosphorylation	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000188399 UniProtKB:O60260	P	Seeded From UniProt	complete
involved_in	GO:0000422	autophagy of mitochondrion	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0041100 PANTHER:PTN000188399 RGD:61797 UniProtKB:O60260	P	Seeded From UniProt	complete
involved_in	GO:0000209	protein polyubiquitination	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0041100 PANTHER:PTN000188395 UniProtKB:O60260 UniProtKB:O95376	P	Seeded From UniProt	complete
part_of	GO:0000151	ubiquitin ligase complex	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000188395 UniProtKB:O60260 WB:WBGene00003967	C	Seeded From UniProt	complete
involved_in	GO:0000266	mitochondrial fission	PMID:18230723^[6]	ECO:0000316	genetic interaction evidence used in manual assertion	FB:FBgn0261276	P	Seeded From UniProt	complete
involved_in	GO:0070050	neuron cellular homeostasis	PMID:17687034^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:17687034^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0008344	adult locomotory behavior	PMID:17687034^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000209	protein polyubiquitination	PMID:17456438^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:17456438^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:17456438^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0031624	ubiquitin conjugating enzyme binding	PMID:17456438^[1]	ECO:0000353	physical interaction evidence used in manual assertion	HGNC:12490	F	Seeded From UniProt	complete
involved_in	GO:0051865	protein autoubiquitination	PMID:17456438^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:17123504^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007283	spermatogenesis	PMID:17123504^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006979	response to oxidative stress	PMID:15911761^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0046329	negative regulation of JNK cascade	PMID:16002472^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:12642658^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:24852371^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0008344	adult locomotory behavior	PMID:24852371^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:24898855^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000422	autophagy of mitochondrion	PMID:24192653^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0055069	zinc ion homeostasis	PMID:20302514^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007283	spermatogenesis	PMID:21383066^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006979	response to oxidative stress	PMID:21383066^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0048477	oogenesis	PMID:21383066^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:20869429^[17]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0048477	oogenesis	PMID:20869429^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:1900407	regulation of cellular response to oxidative stress	PMID:20483372^[18]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0046329	negative regulation of JNK cascade	PMID:20496123^[19]	ECO:0000316	genetic interaction evidence used in manual assertion	FB:FBgn0010303	P	Seeded From UniProt	complete
involved_in	GO:0046329	negative regulation of JNK cascade	PMID:20496123^[19]	ECO:0000316	genetic interaction evidence used in manual assertion	FB:FBgn0000229	P	Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:20194754^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
colocalizes_with	GO:0005739	mitochondrion	PMID:20194754^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0010637	negative regulation of mitochondrial fusion	PMID:20194754^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0090141	positive regulation of mitochondrial fission	PMID:20194754^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000422	autophagy of mitochondrion	PMID:20194754^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:20194754^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0010821	regulation of mitochondrion organization	PMID:19546216^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:18957282^[21]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0030382	sperm mitochondrion organization	PMID:18799731^[22]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:18799731^[22]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:18443288^[23]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000266	mitochondrial fission	PMID:18230723^[6]	ECO:0000316	genetic interaction evidence used in manual assertion	FB:FBgn0026479	P	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:18230723^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000266	mitochondrial fission	PMID:18230723^[6]	ECO:0000316	genetic interaction evidence used in manual assertion	FB:FBgn0029870	P	Seeded From UniProt	complete
involved_in	GO:0008345	larval locomotory behavior	PMID:27430166^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006513	protein monoubiquitination	PMID:29689197^[25]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:29689197^[25]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:29456190^[26]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003977 InterPro:IPR031127	F	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003977	C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003977	C	Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR031127	P	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0539	C	Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000141802	F	Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000141802	P	Seeded From UniProt	complete
part_of	GO:0000151	ubiquitin ligase complex	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000141802	C	Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00143	P	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 Bae, YJ et al. (2007) Drosophila melanogaster Parkin ubiquitinates peanut and septin1 as an E3 ubiquitin-protein ligase. Insect Biochem. Mol. Biol. 37 430-9 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 ^2.7 ^2.8 ^2.9 Ziviani, E et al. (2010) Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc. Natl. Acad. Sci. U.S.A. 107 5018-23 PubMed GONUTS page
↑ ^3.0 ^3.1 Julienne, H et al. (2017) Drosophila PINK1 and parkin loss-of-function mutants display a range of non-motor Parkinson's disease phenotypes. Neurobiol. Dis. 104 15-23 PubMed GONUTS page
↑ Venderova, K et al. (2009) Leucine-Rich Repeat Kinase 2 interacts with Parkin, DJ-1 and PINK-1 in a Drosophila melanogaster model of Parkinson's disease. Hum. Mol. Genet. 18 4390-404 PubMed GONUTS page
↑ ^5.00 ^5.01 ^5.02 ^5.03 ^5.04 ^5.05 ^5.06 ^5.07 ^5.08 ^5.09 ^5.10 ^5.11 ^5.12 ^5.13 ^5.14 ^5.15 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 Poole, AC et al. (2008) The PINK1/Parkin pathway regulates mitochondrial morphology. Proc. Natl. Acad. Sci. U.S.A. 105 1638-43 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Wang, C et al. (2007) Drosophila overexpressing parkin R275W mutant exhibits dopaminergic neuron degeneration and mitochondrial abnormalities. J. Neurosci. 27 8563-70 PubMed GONUTS page
↑ ^8.0 ^8.1 Riparbelli, MG & Callaini, G (2007) The Drosophila parkin homologue is required for normal mitochondrial dynamics during spermiogenesis. Dev. Biol. 303 108-20 PubMed GONUTS page
↑ Whitworth, AJ et al. (2005) Increased glutathione S-transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease. Proc. Natl. Acad. Sci. U.S.A. 102 8024-9 PubMed GONUTS page
↑ Cha, GH et al. (2005) Parkin negatively regulates JNK pathway in the dopaminergic neurons of Drosophila. Proc. Natl. Acad. Sci. U.S.A. 102 10345-50 PubMed GONUTS page
↑ Greene, JC et al. (2003) Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants. Proc. Natl. Acad. Sci. U.S.A. 100 4078-83 PubMed GONUTS page
↑ ^12.0 ^12.1 Cornelissen, T et al. (2014) The deubiquitinase USP15 antagonizes Parkin-mediated mitochondrial ubiquitination and mitophagy. Hum. Mol. Genet. 23 5227-42 PubMed GONUTS page
↑ Yun, J et al. (2014) MUL1 acts in parallel to the PINK1/parkin pathway in regulating mitofusin and compensates for loss of PINK1/parkin. Elife 3 e01958 PubMed GONUTS page
↑ Bhandari, P et al. (2014) Mitochondrial contagion induced by Parkin deficiency in Drosophila hearts and its containment by suppressing mitofusin. Circ. Res. 114 257-65 PubMed GONUTS page
↑ Saini, N & Schaffner, W (2010) Zinc supplement greatly improves the condition of parkin mutant Drosophila. Biol. Chem. 391 513-8 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Saini, N et al. (2011) The parkin mutant phenotype in the fly is largely rescued by metal-responsive transcription factor (MTF-1). Mol. Cell. Biol. 31 2151-61 PubMed GONUTS page
↑ ^17.0 ^17.1 Ottone, C et al. (2011) Diminution of eIF4E activity suppresses parkin mutant phenotypes. Gene 470 12-9 PubMed GONUTS page
↑ Saini, N et al. (2010) Extended lifespan of Drosophila parkin mutants through sequestration of redox-active metals and enhancement of anti-oxidative pathways. Neurobiol. Dis. 40 82-92 PubMed GONUTS page
↑ ^19.0 ^19.1 Hwang, S et al. (2010) Parkin suppresses c-Jun N-terminal kinase-induced cell death via transcriptional regulation in Drosophila. Mol. Cells 29 575-80 PubMed GONUTS page
↑ Lutz, AK et al. (2009) Loss of parkin or PINK1 function increases Drp1-dependent mitochondrial fragmentation. J. Biol. Chem. 284 22938-51 PubMed GONUTS page
↑ Kim, Y et al. (2008) PINK1 controls mitochondrial localization of Parkin through direct phosphorylation. Biochem. Biophys. Res. Commun. 377 975-80 PubMed GONUTS page
↑ ^22.0 ^22.1 Deng, H et al. (2008) The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila. Proc. Natl. Acad. Sci. U.S.A. 105 14503-8 PubMed GONUTS page
↑ Yang, Y et al. (2008) Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery. Proc. Natl. Acad. Sci. U.S.A. 105 7070-5 PubMed GONUTS page
↑ Brooks, DS et al. () Optimization of wrMTrck to monitor Drosophila larval locomotor activity. J. Insect Physiol. 93-94 11-17 PubMed GONUTS page
↑ ^25.0 ^25.1 Tan, KL et al. (2018) Ari-1 Regulates Myonuclear Organization Together with Parkin and Is Associated with Aortic Aneurysms. Dev. Cell 45 226-244.e8 PubMed GONUTS page
↑ Tsai, PI et al. (2018) PINK1 Phosphorylates MIC60/Mitofilin to Control Structural Plasticity of Mitochondrial Crista Junctions. Mol. Cell 69 744-756.e6 PubMed GONUTS page

[PMID:17456438-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 Bae, YJ et al. (2007) Drosophila melanogaster Parkin ubiquitinates peanut and septin1 as an E3 ubiquitin-protein ligase. Insect Biochem. Mol. Biol. 37 430-9 PubMed GONUTS page

[PMID:20194754-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 ^2.7 ^2.8 ^2.9 Ziviani, E et al. (2010) Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc. Natl. Acad. Sci. U.S.A. 107 5018-23 PubMed GONUTS page

[PMID:28435104-3] 3.0 ^3.1 Julienne, H et al. (2017) Drosophila PINK1 and parkin loss-of-function mutants display a range of non-motor Parkinson's disease phenotypes. Neurobiol. Dis. 104 15-23 PubMed GONUTS page

[PMID:19692353-4] Venderova, K et al. (2009) Leucine-Rich Repeat Kinase 2 interacts with Parkin, DJ-1 and PINK-1 in a Drosophila melanogaster model of Parkinson's disease. Hum. Mol. Genet. 18 4390-404 PubMed GONUTS page

[PMID:21873635-5] 5.00 ^5.01 ^5.02 ^5.03 ^5.04 ^5.05 ^5.06 ^5.07 ^5.08 ^5.09 ^5.10 ^5.11 ^5.12 ^5.13 ^5.14 ^5.15 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:18230723-6] 6.0 ^6.1 ^6.2 ^6.3 Poole, AC et al. (2008) The PINK1/Parkin pathway regulates mitochondrial morphology. Proc. Natl. Acad. Sci. U.S.A. 105 1638-43 PubMed GONUTS page

[PMID:17687034-7] 7.0 ^7.1 ^7.2 Wang, C et al. (2007) Drosophila overexpressing parkin R275W mutant exhibits dopaminergic neuron degeneration and mitochondrial abnormalities. J. Neurosci. 27 8563-70 PubMed GONUTS page

[PMID:17123504-8] 8.0 ^8.1 Riparbelli, MG & Callaini, G (2007) The Drosophila parkin homologue is required for normal mitochondrial dynamics during spermiogenesis. Dev. Biol. 303 108-20 PubMed GONUTS page

[PMID:15911761-9] Whitworth, AJ et al. (2005) Increased glutathione S-transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease. Proc. Natl. Acad. Sci. U.S.A. 102 8024-9 PubMed GONUTS page

[PMID:16002472-10] Cha, GH et al. (2005) Parkin negatively regulates JNK pathway in the dopaminergic neurons of Drosophila. Proc. Natl. Acad. Sci. U.S.A. 102 10345-50 PubMed GONUTS page

[PMID:12642658-11] Greene, JC et al. (2003) Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants. Proc. Natl. Acad. Sci. U.S.A. 100 4078-83 PubMed GONUTS page

[PMID:24852371-12] 12.0 ^12.1 Cornelissen, T et al. (2014) The deubiquitinase USP15 antagonizes Parkin-mediated mitochondrial ubiquitination and mitophagy. Hum. Mol. Genet. 23 5227-42 PubMed GONUTS page

[PMID:24898855-13] Yun, J et al. (2014) MUL1 acts in parallel to the PINK1/parkin pathway in regulating mitofusin and compensates for loss of PINK1/parkin. Elife 3 e01958 PubMed GONUTS page

[PMID:24192653-14] Bhandari, P et al. (2014) Mitochondrial contagion induced by Parkin deficiency in Drosophila hearts and its containment by suppressing mitofusin. Circ. Res. 114 257-65 PubMed GONUTS page

[PMID:20302514-15] Saini, N & Schaffner, W (2010) Zinc supplement greatly improves the condition of parkin mutant Drosophila. Biol. Chem. 391 513-8 PubMed GONUTS page

[PMID:21383066-16] 16.0 ^16.1 ^16.2 Saini, N et al. (2011) The parkin mutant phenotype in the fly is largely rescued by metal-responsive transcription factor (MTF-1). Mol. Cell. Biol. 31 2151-61 PubMed GONUTS page

[PMID:20869429-17] 17.0 ^17.1 Ottone, C et al. (2011) Diminution of eIF4E activity suppresses parkin mutant phenotypes. Gene 470 12-9 PubMed GONUTS page

[PMID:20483372-18] Saini, N et al. (2010) Extended lifespan of Drosophila parkin mutants through sequestration of redox-active metals and enhancement of anti-oxidative pathways. Neurobiol. Dis. 40 82-92 PubMed GONUTS page

[PMID:20496123-19] 19.0 ^19.1 Hwang, S et al. (2010) Parkin suppresses c-Jun N-terminal kinase-induced cell death via transcriptional regulation in Drosophila. Mol. Cells 29 575-80 PubMed GONUTS page

[PMID:19546216-20] Lutz, AK et al. (2009) Loss of parkin or PINK1 function increases Drp1-dependent mitochondrial fragmentation. J. Biol. Chem. 284 22938-51 PubMed GONUTS page

[PMID:18957282-21] Kim, Y et al. (2008) PINK1 controls mitochondrial localization of Parkin through direct phosphorylation. Biochem. Biophys. Res. Commun. 377 975-80 PubMed GONUTS page

[PMID:18799731-22] 22.0 ^22.1 Deng, H et al. (2008) The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila. Proc. Natl. Acad. Sci. U.S.A. 105 14503-8 PubMed GONUTS page

[PMID:18443288-23] Yang, Y et al. (2008) Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery. Proc. Natl. Acad. Sci. U.S.A. 105 7070-5 PubMed GONUTS page

[PMID:27430166-24] Brooks, DS et al. () Optimization of wrMTrck to monitor Drosophila larval locomotor activity. J. Insect Physiol. 93-94 11-17 PubMed GONUTS page

[PMID:29689197-25] 25.0 ^25.1 Tan, KL et al. (2018) Ari-1 Regulates Myonuclear Organization Together with Parkin and Is Associated with Aortic Aneurysms. Dev. Cell 45 226-244.e8 PubMed GONUTS page

[PMID:29456190-26] Tsai, PI et al. (2018) PINK1 Phosphorylates MIC60/Mitofilin to Control Structural Plasticity of Mitochondrial Crista Junctions. Mol. Cell 69 744-756.e6 PubMed GONUTS page

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