HUMAN:PRKN2

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	PARK2 (synonyms: PRKN)
Protein Name(s)	E3 ubiquitin-protein ligase parkin Parkinson juvenile disease protein 2 Parkinson disease protein 2
External Links
UniProt	O60260
EMBL	AB009973 EF375726 AF381282 AF381283 AF381286 GU345839 GU345840 GU361467 AK292590 AL445215 AL035697 AL132982 AP000886 AP000887 AP001576 AP001577 AP001578 AP003699 AL035697 AL132982 AL445215 AP000886 AP000887 AP001576 AP001577 AP001578 AP003699 AL132982 AL035697 AL445215 AP000886 AP000887 AP001576 AP001577 AP001578 AP003699 CH471051 CH471051 BC022014 AY564225
CCDS	CCDS5281.1 CCDS5282.1 CCDS5283.1
RefSeq	NP_004553.2 NP_054642.2 NP_054643.2
UniGene	Hs.132954
PDB	1IYF 2JMO 4BM9 4I1F 4I1H
PDBsum	1IYF 2JMO 4BM9 4I1F 4I1H
ProteinModelPortal	O60260
SMR	O60260
BioGrid	111105
DIP	DIP-37655N
IntAct	O60260
MINT	MINT-1351124
STRING	9606.ENSP00000355865
PhosphoSite	O60260
PaxDb	O60260
PRIDE	O60260
DNASU	5071
Ensembl	ENST00000338468 ENST00000366894 ENST00000366896 ENST00000366897 ENST00000366898 ENST00000479615
GeneID	5071
KEGG	hsa:5071
UCSC	uc003qtx.4 uc003qty.4 uc010kke.1
CTD	5071
GeneCards	GC06M161740
GeneReviews	PARK2
HGNC	HGNC:8607
HPA	CAB016257
MIM	168600 600116 602544
neXtProt	NX_O60260
Orphanet	2828
PharmGKB	PA32942
eggNOG	NOG278133
GeneTree	ENSGT00390000011034
HOVERGEN	HBG053682
InParanoid	O60260
KO	K04556
OMA	CESLEIA
OrthoDB	EOG738054
PhylomeDB	O60260
TreeFam	TF314529
Reactome	REACT_75842
SignaLink	O60260
UniPathway	UPA00143
EvolutionaryTrace	O60260
GeneWiki	Parkin_(ligase)
GenomeRNAi	5071
NextBio	19538
PRO	PR:O60260
Proteomes	UP000005640
Bgee	O60260
CleanEx	HS_PARK2
ExpressionAtlas	O60260
Genevestigator	O60260
GO	GO:0016235 GO:0005737 GO:0005829 GO:0005783 GO:0005794 GO:0097413 GO:0005739 GO:0043005 GO:0005634 GO:1990452 GO:0048471 GO:0000151 GO:0003779 GO:0051087 GO:0097602 GO:1990444 GO:0001664 GO:0031072 GO:0042826 GO:0030544 GO:0042802 GO:0019900 GO:0016874 GO:0030165 GO:0019901 GO:0017124 GO:0015631 GO:0043130 GO:0031624 GO:0061630 GO:0031625 GO:0004842 GO:1990381 GO:0008270 GO:0008344 GO:0070842 GO:0044257 GO:1903351 GO:0071287 GO:0097237 GO:0034620 GO:0007417 GO:0042417 GO:0051583 GO:0007612 GO:0000266 GO:0000422 GO:0007005 GO:0032232 GO:0060548 GO:1902236 GO:0033132 GO:0046676 GO:0046329 GO:0010637 GO:0043524 GO:1901215 GO:1903202 GO:1903377 GO:0001933 GO:2000378 GO:0090201 GO:0070050 GO:0042415 GO:0043388 GO:0043123 GO:0090141 GO:0010636 GO:1901800 GO:1902530 GO:0045944 GO:1903265 GO:0043161 GO:0051865 GO:0044314 GO:0035519 GO:0070936 GO:0085020 GO:0070534 GO:0006513 GO:0000209 GO:0016567 GO:0042787 GO:0010506 GO:1900407 GO:0014059 GO:0010906 GO:0032368 GO:1903146 GO:0010821 GO:0046928 GO:2000377 GO:1902803 GO:0034976 GO:0006979 GO:0001964 GO:0035249 GO:0006351 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	Extension	Notes	Status
	GO:0004842	ubiquitin-protein ligase activity	PMID:10888878^[1]	ECO:0000314			F		Figure 5a. Incubation of immunoprecipitated Parkin with ATP, E1, E2, and ubiquitin results in an ubiquitinated signal at 30 kD.	complete
	GO:0000422	mitochondrion degradation	PMID:19029340^[2]	ECO:0000314			P		Figure 4. HeLa cells transfected with the gene for PRKN2 have less mitochondrial mass under depolarizing conditions compared to cells that do not have the parkin gene.	complete
	GO:0005739	mitochondrion	PMID:19029340^[2]	ECO:0000314			C		Figure 1a and 1b. Human cells treated with CCCP (to depolarize the mitochondrial membrane) have increased levels of Parkin associated with them.	complete
	GO:0004842	ubiquitin-protein ligase activity	PMID:11078524^[3]	ECO:0000314			F		Figure 3C shows that Cys421Ala and Cys431Ala mutations significantly decrease the self-ubiquitination of Parkin.	complete CACAO 3927
	GO:0004842	ubiquitin-protein ligase activity	PMID:11078524^[3]	ECO:0000314			F		Figure 1B shows that Parkin selectively interacts with UbcH8.	complete CACAO 3928
	GO:0004842	ubiquitin-protein ligase activity	PMID:11078524^[3]	ECO:0000314			F		Figure 4C shows that ubiquitination of CDCrel-1 is significantly increased in the presence of Parkin.	complete CACAO 3929
	GO:0005829	cytosol	PMID:19029340^[2]	ECO:0000314			C		Figure 1 a and c. Immunostained cells show that parkin is located in the cytosol.	complete
involved_in	GO:0099074	mitochondrion to lysosome transport	PMID:24446486^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	part_of:(GO:1900407)	Seeded From UniProt	complete
colocalizes_with	GO:0099073	mitochondrion-derived vesicle	PMID:24446486^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	exists_during:(GO:0099074)	Seeded From UniProt	complete
involved_in	GO:1900407	regulation of cellular response to oxidative stress	PMID:24446486^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032092	positive regulation of protein binding	PMID:26911690^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q96NA2) has_regulation_target:(UniProtKB:P51149)	Seeded From UniProt	complete
involved_in	GO:1903542	negative regulation of exosomal secretion	PMID:26911690^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903599	positive regulation of autophagy of mitochondrion	PMID:26310625^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	PMID:12925569^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002614)	Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:12925569^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:Q9BT88)	Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:12925569^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:Q9BT88) part_of:(GO:0016567)	Seeded From UniProt	complete
involved_in	GO:0031647	regulation of protein stability	PMID:26911690^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P51149)	Seeded From UniProt	complete
involved_in	GO:1905477	positive regulation of protein localization to membrane	PMID:26911690^[5]	ECO:0000305	curator inference used in manual assertion	GO:0016567	P	has_regulation_target:(UniProtKB:P51149)	Seeded From UniProt	complete
involved_in	GO:1905477	positive regulation of protein localization to membrane	PMID:26911690^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q96QK1)\|has_regulation_target:(UniProtKB:Q13596)	Seeded From UniProt	complete
involved_in	GO:1905366	negative regulation of intralumenal vesicle formation	PMID:26911690^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:26911690^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:P51149) positively_regulates:(GO:0005515) positively_regulates:(GO:0072657)\|occurs_in(CL:0000700) has_direct_input:(UniProtKB:P51149)	Seeded From UniProt	complete
involved_in	GO:1905281	positive regulation of retrograde transport, endosome to Golgi	PMID:26911690^[5]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902236	negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway	PMID:10973942^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031624	ubiquitin conjugating enzyme binding	PMID:10973942^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0036503	ERAD pathway	PMID:10973942^[8]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:10973942^[8]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:10973942^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:10973942^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0043274	phospholipase binding	PMID:19725078^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P30041	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:19725078^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O75306	F		Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:19725078^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P38646	F		Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:19725078^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P10809	F		Seeded From UniProt	complete
involved_in	GO:0010498	proteasomal protein catabolic process	PMID:19725078^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(UniProtKB:P61978) part_of:(GO:0010629)	Seeded From UniProt	complete
involved_in	GO:0010994	free ubiquitin chain polymerization	PMID:24660806^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:P0CG47)	Seeded From UniProt	complete
involved_in	GO:0031648	protein destabilization	PMID:19591802^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P35222) part_of:(GO:0090090)	Seeded From UniProt	complete
involved_in	GO:0090090	negative regulation of canonical Wnt signaling pathway	PMID:19591802^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008013	beta-catenin binding	PMID:19591802^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:19591802^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006513	protein monoubiquitination	PMID:24660806^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q8IXI2)	Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	PMID:19725078^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P12268)	Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	PMID:19725078^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P60174)	Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	PMID:19725078^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P18206)\|has_regulation_target:(UniProtKB:P61978)	Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	PMID:19725078^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P08670)	Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	PMID:19725078^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P00558)	Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	PMID:19725078^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P30041)	Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	PMID:19725078^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P61978)	Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	PMID:19725078^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P10809)	Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	PMID:19725078^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q9BWD1)	Seeded From UniProt	complete
involved_in	GO:0098779	positive regulation of mitophagy in response to mitochondrial depolarization	PMID:23212910^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031396	regulation of protein ubiquitination	PMID:23212910^[12]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q9BXM7	P	has_regulation_target:(UniProtKB:Q8IWA4) has_regulation_target:(UniProtKB:O95140) has_regulation_target:(UniProtKB:O94826)	Seeded From UniProt	complete
colocalizes_with	GO:0005739	mitochondrion	PMID:21508222^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		C	part_of:(CL:0000700)	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21508222^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		C	part_of:(CL:0000700)\|part_of:(GO:0043005)	Seeded From UniProt	complete
involved_in	GO:1900407	regulation of cellular response to oxidative stress	PMID:22314364^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(CHEBI:18243)	Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	PMID:22314364^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P21397)\|has_regulation_target:(UniProtKB:P27338)	Seeded From UniProt	complete
involved_in	GO:0042053	regulation of dopamine metabolic process	PMID:22314364^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P21397)\|has_regulation_target:(UniProtKB:P27338)	Seeded From UniProt	complete
involved_in	GO:1902283	negative regulation of primary amine oxidase activity	PMID:22314364^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(CHEBI:18243)	Seeded From UniProt	complete
involved_in	GO:0061734	parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization	PMID:19029340^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1904049	negative regulation of spontaneous neurotransmitter secretion	PMID:22314364^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(CHEBI:18243) occurs_in:(CL:0000700)	Seeded From UniProt	complete
involved_in	GO:0051582	positive regulation of neurotransmitter uptake	PMID:22314364^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	regulates_transport_of:(CHEBI:18243) occurs_in:(CL:0000700)	Seeded From UniProt	complete
involved_in	GO:0000422	autophagy of mitochondrion	PMID:25621951^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070979	protein K11-linked ubiquitination	PMID:25621951^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070534	protein K63-linked ubiquitination	PMID:25621951^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0085020	protein K6-linked ubiquitination	PMID:25621951^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:25621951^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0070534	protein K63-linked ubiquitination	PMID:20890124^[16]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010821	regulation of mitochondrion organization	PMID:20890124^[16]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903214	regulation of protein targeting to mitochondrion	PMID:20890124^[16]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0044828	negative regulation by host of viral genome replication	PMID:25244949^[17]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q99IB8)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:25244949^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:25244949^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0031396	regulation of protein ubiquitination	PMID:20871098^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q8IWA4) part_of:(GO:0098779)\|has_regulation_target(UniProtKB:O95140) part_of:(GO:0098779)	Seeded From UniProt	complete
involved_in	GO:0098779	positive regulation of mitophagy in response to mitochondrial depolarization	PMID:20871098^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010821	regulation of mitochondrion organization	PMID:19279012^[19]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q9BXM7	P		Seeded From UniProt	complete
enables	GO:0031624	ubiquitin conjugating enzyme binding	PMID:11439185^[20]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P62253	F		Seeded From UniProt	complete
enables	GO:0031624	ubiquitin conjugating enzyme binding	PMID:11439185^[20]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9Y385	F		Seeded From UniProt	complete
involved_in	GO:1902236	negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway	PMID:11439185^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process	PMID:11439185^[20]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:O15354)	Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:11439185^[20]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:O15354)	Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:11439185^[20]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:O15354) part_of:(GO:0043161)	Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:19229105^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:19229105^[21]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:19229105^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:19229105^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0019900	kinase binding	PMID:19229105^[21]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9BXM7	F		Seeded From UniProt	complete
involved_in	GO:0098779	positive regulation of mitophagy in response to mitochondrial depolarization	PMID:20457763^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21753002^[23]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0001891) part_of:(CL:0000540)	Seeded From UniProt	complete
enables	GO:0042826	histone deacetylase binding	PMID:21753002^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9UBN7	F		Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:21753002^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P17987	F		Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:21753002^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P78371	F		Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:21753002^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P10809	F		Seeded From UniProt	complete
enables	GO:0030544	Hsp70 protein binding	PMID:21753002^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P38646	F		Seeded From UniProt	complete
enables	GO:0003779	actin binding	PMID:21753002^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P63261	F		Seeded From UniProt	complete
enables	GO:0015631	tubulin binding	PMID:21753002^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P07437	F		Seeded From UniProt	complete
enables	GO:0015631	tubulin binding	PMID:21753002^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P68363	F		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:18221368^[24]	ECO:0000303	author statement without traceable support used in manual assertion		F	has_direct_input:(UniProtKB:Q12933)\|has_direct_input:(UniProtKB:Q9Y6K9)\|has_direct_input:(UniProtKB:Q9Y6H5)\|has_direct_input:(UniProtKB:P37840)\|has_direct_input:(UniProtKB:O15354)	Seeded From UniProt	complete
involved_in	GO:1900407	regulation of cellular response to oxidative stress	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q95TI4	P		Seeded From UniProt	complete
involved_in	GO:0090141	positive regulation of mitochondrial fission	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q95TI4	P		Seeded From UniProt	complete
involved_in	GO:0070050	neuron cellular homeostasis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q95TI4	P		Seeded From UniProt	complete
involved_in	GO:0055069	zinc ion homeostasis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q95TI4	P		Seeded From UniProt	complete
involved_in	GO:0046329	negative regulation of JNK cascade	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q95TI4	P		Seeded From UniProt	complete
involved_in	GO:0010637	negative regulation of mitochondrial fusion	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q95TI4	P		Seeded From UniProt	complete
involved_in	GO:0008344	adult locomotory behavior	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q95TI4	P		Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q95TI4	P		Seeded From UniProt	complete
involved_in	GO:0006979	response to oxidative stress	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q95TI4	P		Seeded From UniProt	complete
involved_in	GO:0000266	mitochondrial fission	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q95TI4	P		Seeded From UniProt	complete
involved_in	GO:1902803	regulation of synaptic vesicle transport	PMID:21563316^[25]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903202	negative regulation of oxidative stress-induced cell death	PMID:24522549^[26]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000378	negative regulation of reactive oxygen species metabolic process	PMID:18541373^[27]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q9H4P4	P		Seeded From UniProt	complete
part_of	GO:0000151	ubiquitin ligase complex	PMID:17314283^[28]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0070534	protein K63-linked ubiquitination	PMID:17314283^[28]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:Q9Y6K9)	Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:17314283^[28]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:Q12933)	Seeded From UniProt	complete
involved_in	GO:0043388	positive regulation of DNA binding	PMID:17314283^[28]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043123	positive regulation of I-kappaB kinase/NF-kappaB signaling	PMID:17314283^[28]	ECO:0000314	direct assay evidence used in manual assertion		P	part_of:(GO:1901215)	Seeded From UniProt	complete
involved_in	GO:1903377	negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway	PMID:17314283^[28]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:11078524^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
NOT\|part_of	GO:0019005	SCF ubiquitin ligase complex	PMID:12628165^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1990452	Parkin-FBXW7-Cul1 ubiquitin ligase complex	PMID:12628165^[29]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q969H0	C	part_of:(UBERON:0001870)	Seeded From UniProt	complete
enables	GO:0097602	cullin family protein binding	PMID:12628165^[29]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:12628165^[29]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0051865	protein autoubiquitination	PMID:12628165^[29]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:1990444	F-box domain binding	PMID:12628165^[29]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q969H0	F	occurs_in:(UBERON:0001870)	Seeded From UniProt	complete
enables	GO:0031624	ubiquitin conjugating enzyme binding	PMID:12628165^[29]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P68036	F	occurs_in:(UBERON:0001870)	Seeded From UniProt	complete
involved_in	GO:0010821	regulation of mitochondrion organization	PMID:21113145^[30]	ECO:0000314	direct assay evidence used in manual assertion		P	part_of:(GO:0034976)	Seeded From UniProt	complete
involved_in	GO:1902236	negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway	PMID:21113145^[30]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034976	response to endoplasmic reticulum stress	PMID:21113145^[30]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902254	negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator	PMID:23985028^[31]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(GO:0043524)	Seeded From UniProt	complete
involved_in	GO:0043524	negative regulation of neuron apoptotic process	PMID:23985028^[31]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific	PMID:23985028^[31]	ECO:0000314	direct assay evidence used in manual assertion		F	has_input:(ENSEMBL:ENSG00000141510) occurs_at:(SO:0001952)	Seeded From UniProt	complete
enables	GO:0000976	transcription regulatory region sequence-specific DNA binding	PMID:23985028^[31]	ECO:0000314	direct assay evidence used in manual assertion		F	has_input:(UniProtKB:P04637)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:23985028^[31]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:23985028^[31]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:23985028^[31]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P04637) part_of:(GO:0043524)	Seeded From UniProt	complete
involved_in	GO:0051865	protein autoubiquitination	PMID:16352719^[32]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:23858059^[33]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:Q969H0) occurs_in:(CL:0000540) occurs_in:(UBERON:0000955)	Seeded From UniProt	complete
involved_in	GO:0070936	protein K48-linked ubiquitination	PMID:23858059^[33]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:Q969H0) occurs_in:(CL:0000540) occurs_in:(UBERON:0000955)	Seeded From UniProt	complete
involved_in	GO:1901800	positive regulation of proteasomal protein catabolic process	PMID:23858059^[33]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q9WVS6	P	has_regulation_target:(UniProtKB:Q969H0)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:23858059^[33]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540) part_of:(UBERON:0000955)	Seeded From UniProt	complete
part_of	GO:0000151	ubiquitin ligase complex	PMID:12150907^[34]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0000955)	Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:12628165^[29]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:12628165^[29]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903265	positive regulation of tumor necrosis factor-mediated signaling pathway	PMID:23453807^[35]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010636	positive regulation of mitochondrial fusion	PMID:23453807^[35]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043123	positive regulation of I-kappaB kinase/NF-kappaB signaling	PMID:23453807^[35]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:23453807^[35]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q96EP0	F		Seeded From UniProt	complete
colocalizes_with	GO:0071797	LUBAC complex	PMID:23453807^[35]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q96EP0	C		Seeded From UniProt	complete
involved_in	GO:1902530	positive regulation of protein linear polyubiquitination	PMID:23453807^[35]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q96EP0 UniProtKB:Q9BYM8	P	has_regulation_target:(UniProtKB:Q9Y6K9)	Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:23453807^[35]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:O60313) part_of:(GO:0010636)	Seeded From UniProt	complete
involved_in	GO:0090201	negative regulation of release of cytochrome c from mitochondria	PMID:23453807^[35]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:12150907^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1902236	negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway	PMID:23453807^[35]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:21376232^[36]	ECO:0000305	curator inference used in manual assertion	GO:0044257 GO:0070936	P		Seeded From UniProt	complete
involved_in	GO:1902236	negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway	PMID:12150907^[34]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:12150907^[34]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:O15354)	Seeded From UniProt	complete
involved_in	GO:0000209	protein polyubiquitination	PMID:12150907^[34]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:O15354)	Seeded From UniProt	complete
enables	GO:0001664	G protein-coupled receptor binding	PMID:12150907^[34]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O15354	F		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:12150907^[34]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P31689	F		Seeded From UniProt	complete
enables	GO:0030544	Hsp70 protein binding	PMID:12150907^[34]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P11142	F		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:12150907^[34]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9UNE7	F		Seeded From UniProt	complete
involved_in	GO:0097237	cellular response to toxic substance	PMID:12628165^[29]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043524	negative regulation of neuron apoptotic process	PMID:12628165^[29]	ECO:0000314	direct assay evidence used in manual assertion		P	part_of:(GO:0097237)	Seeded From UniProt	complete
enables	GO:0043130	ubiquitin binding	PMID:24784582^[37]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:24784582^[37]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:24896179^[38]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000422	autophagy of mitochondrion	PMID:24896179^[38]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:1990381	ubiquitin-specific protease binding	PMID:24063750^[39]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P54252	F		Seeded From UniProt	complete
involved_in	GO:1901215	negative regulation of neuron death	PMID:21376232^[36]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q6NUN9	P		Seeded From UniProt	complete
involved_in	GO:0070936	protein K48-linked ubiquitination	PMID:21376232^[36]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:Q6NUN9)	Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:21376232^[36]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:Q6NUN9)	Seeded From UniProt	complete
involved_in	GO:0044257	cellular protein catabolic process	PMID:21376232^[36]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(UniProtKB:Q6NUN9) occurs_in:(UBERON:0002038)\|has_input(UniProtKB:Q6NUN9) occurs_in:(UBERON:0002435)	Seeded From UniProt	complete
involved_in	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process	PMID:21376232^[36]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:Q6NUN9)	Seeded From UniProt	complete
involved_in	GO:0090201	negative regulation of release of cytochrome c from mitochondria	PMID:19880420^[40]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070842	aggresome assembly	PMID:14645198^[41]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070534	protein K63-linked ubiquitination	PMID:19880420^[40]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0060548	negative regulation of cell death	PMID:15603737^[42]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051865	protein autoubiquitination	PMID:17512523^[43]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:15603737^[42]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0DMV8 UniProtKB:P0DMV9	F		Seeded From UniProt	complete
involved_in	GO:0043524	negative regulation of neuron apoptotic process	PMID:22511790^[44]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043123	positive regulation of I-kappaB kinase/NF-kappaB signaling	PMID:19880420^[40]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032232	negative regulation of actin filament bundle assembly	PMID:17512523^[43]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0030165	PDZ domain binding	PMID:17512523^[43]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P53667	F		Seeded From UniProt	complete
enables	GO:0019900	kinase binding	PMID:17512523^[43]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P53667	F		Seeded From UniProt	complete
enables	GO:0019900	kinase binding	PMID:19880420^[40]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9BXM7	F		Seeded From UniProt	complete
part_of	GO:0016235	aggresome	PMID:14645198^[41]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:19880420^[40]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:17512523^[43]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:16227987^[45]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:O15354)	Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:19880420^[40]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:Q9Y6K9)	Seeded From UniProt	complete
involved_in	GO:0001933	negative regulation of protein phosphorylation	PMID:17512523^[43]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000209	protein polyubiquitination	PMID:16227987^[45]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000209	protein polyubiquitination	PMID:19880420^[40]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000377	regulation of reactive oxygen species metabolic process	PMID:18541373^[27]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070936	protein K48-linked ubiquitination	PMID:21376232^[36]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070534	protein K63-linked ubiquitination	PMID:15728840^[46]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051865	protein autoubiquitination	PMID:15728840^[46]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:17097639^[47]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:17097639^[47]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:21532592^[48]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P68036	F		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	PMID:20798600^[49]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9BXM7	F		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:23933751^[50]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010506	regulation of autophagy	PMID:20889974^[51]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006513	protein monoubiquitination	PMID:20889974^[51]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:23933751^[50]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:20889974^[51]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:19029340^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	PMID:17097639^[47]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:19029340^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:23933751^[50]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:20889974^[51]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21376232^[36]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:15728840^[46]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:20889974^[51]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:21376232^[36]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:18541373^[27]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	PMID:17097639^[47]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000422	autophagy of mitochondrion	PMID:23933751^[50]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000422	autophagy of mitochondrion	PMID:19029340^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000209	protein polyubiquitination	PMID:18541373^[27]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0000151	ubiquitin ligase complex	PMID:23933751^[50]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1900407	regulation of cellular response to oxidative stress	PMID:21873635^[52]	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^[52]	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^[52]	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^[52]	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^[52]	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^[52]	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^[52]	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^[52]	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^[52]	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^[52]	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^[52]	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^[52]	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^[52]	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^[52]	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^[52]	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^[52]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000188395 UniProtKB:O60260 WB:WBGene00003967	C		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	PMID:20823226^[53]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0046676	negative regulation of insulin secretion	PMID:24187134^[54]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0033132	negative regulation of glucokinase activity	PMID:24187134^[54]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019900	kinase binding	PMID:24187134^[54]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P35557	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21694720^[55]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60260	F		Seeded From UniProt	complete
part_of	GO:0016607	nuclear speck	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0098793	presynapse	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0051583	C		Seeded From UniProt	complete
involved_in	GO:1903861	positive regulation of dendrite extension	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:1903382	negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:1903377	negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:1902530	positive regulation of protein linear polyubiquitination	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:1902236	negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:1901215	negative regulation of neuron death	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:0097237	cellular response to toxic substance	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:0070585	protein localization to mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	F		Seeded From UniProt	complete
involved_in	GO:0051881	regulation of mitochondrial membrane potential	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:0051583	dopamine uptake involved in synaptic transmission	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:0050804	modulation of chemical synaptic transmission	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:0046928	regulation of neurotransmitter secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:0044257	cellular protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:0043524	negative regulation of neuron apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	C		Seeded From UniProt	complete
involved_in	GO:0042417	dopamine metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:0042415	norepinephrine metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:0035249	synaptic transmission, glutamatergic	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:0034976	response to endoplasmic reticulum stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	C		Seeded From UniProt	complete
involved_in	GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:0031648	protein destabilization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:0019538	protein metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:0008344	adult locomotory behavior	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:0007626	locomotory behavior	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:0007612	learning	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	C		Seeded From UniProt	complete
involved_in	GO:0001964	startle response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:0001963	synaptic transmission, dopaminergic	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	P		Seeded From UniProt	complete
involved_in	GO:0000423	mitophagy	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WVS6 ensembl:ENSMUSP00000140587	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
involved_in	GO:0060828	regulation of canonical Wnt signaling pathway	PMID:24115276^[56]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045732	positive regulation of protein catabolic process	PMID:22988876^[57]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_regulation_target:(UniProtKB:P35222) part_of:(GO:0090090)	Seeded From UniProt	complete
involved_in	GO:0090090	negative regulation of canonical Wnt signaling pathway	PMID:22988876^[57]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process	PMID:24115276^[56]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_regulation_target:(UniProtKB:P35222) part_of:(GO:0060828)	Seeded From UniProt	complete
involved_in	GO:0044314	protein K27-linked ubiquitination	PMID:20098416^[58] PMID:23626584^[59]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903202	negative regulation of oxidative stress-induced cell death	PMID:24252804^[60]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034620	cellular response to unfolded protein	PMID:18221368^[24]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070534	protein K63-linked ubiquitination	PMID:18221368^[24]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_input:(UniProtKB:Q12933)\|has_input:(UniProtKB:Q9Y6K9)\|has_input:(UniProtKB:Q9Y6H5)\|has_input:(UniProtKB:P37840)	Seeded From UniProt	complete
enables	GO:0017124	SH3 domain binding	PMID:23626584^[59]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0032368	regulation of lipid transport	PMID:23626584^[59]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903351	cellular response to dopamine	PMID:23626584^[59]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:23626584^[59]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0035519	protein K29-linked ubiquitination	PMID:23626584^[59]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0085020	protein K6-linked ubiquitination	PMID:23626584^[59]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042417	dopamine metabolic process	PMID:23626584^[59]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010906	regulation of glucose metabolic process	PMID:23626584^[59]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0014059	regulation of dopamine secretion	PMID:21563316^[25]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0097413	Lewy body	PMID:24522549^[26]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0071287	cellular response to manganese ion	PMID:23628791^[61]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007417	central nervous system development	PMID:9560156^[62]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:10888878^[1]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0061630	ubiquitin protein ligase activity	Reactome:R-HSA-5689111	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0044267	cellular protein metabolic process	Reactome:R-HSA-392499	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016579	protein deubiquitination	Reactome:R-HSA-5688426	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016236	macroautophagy	Reactome:R-HSA-5205685	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-5689111 Reactome:R-HSA-5689085 Reactome:R-HSA-5688837 Reactome:R-HSA-5667111 Reactome:R-HSA-5658574 Reactome:R-HSA-5205682 Reactome:R-HSA-5205652	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004842	ubiquitin-protein transferase activity	Reactome:R-HSA-5667111 Reactome:R-HSA-5205682	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0256 UniProtKB-SubCell:SL-0095	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
involved_in	GO:0006914	autophagy	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0072	P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496 UniProtKB-SubCell:SL-0173	C		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0091	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 Shimura, H et al. (2000) Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat. Genet. 25 302-5 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 Narendra, D et al. (2008) Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol. 183 795-803 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Zhang, Y et al. (2000) Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc. Natl. Acad. Sci. U.S.A. 97 13354-9 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 McLelland, GL et al. (2014) Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control. EMBO J. 33 282-95 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 Song, P et al. (2016) Parkin Modulates Endosomal Organization and Function of the Endo-Lysosomal Pathway. J. Neurosci. 36 2425-37 PubMed GONUTS page
↑ Zhou, ZD et al. (2015) F-box protein 7 mutations promote protein aggregation in mitochondria and inhibit mitophagy. Hum. Mol. Genet. 24 6314-30 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Huynh, DP et al. (2003) The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI. Hum. Mol. Genet. 12 2587-97 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 Imai, Y et al. (2000) Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J. Biol. Chem. 275 35661-4 PubMed GONUTS page
↑ ^9.00 ^9.01 ^9.02 ^9.03 ^9.04 ^9.05 ^9.06 ^9.07 ^9.08 ^9.09 ^9.10 ^9.11 ^9.12 ^9.13 Davison, EJ et al. (2009) Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function. Proteomics 9 4284-97 PubMed GONUTS page
↑ ^10.0 ^10.1 Kazlauskaite, A et al. (2014) Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65. Biochem. J. 460 127-39 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 Rawal, N et al. (2009) Parkin protects dopaminergic neurons from excessive Wnt/beta-catenin signaling. Biochem. Biophys. Res. Commun. 388 473-8 PubMed GONUTS page
↑ ^12.0 ^12.1 Rakovic, A et al. (2013) 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. J. Biol. Chem. 288 2223-37 PubMed GONUTS page
↑ ^13.0 ^13.1 Seibler, P et al. (2011) Mitochondrial Parkin recruitment is impaired in neurons derived from mutant PINK1 induced pluripotent stem cells. J. Neurosci. 31 5970-6 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 Jiang, H et al. (2012) Parkin controls dopamine utilization in human midbrain dopaminergic neurons derived from induced pluripotent stem cells. Nat Commun 3 668 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 ^15.3 ^15.4 Cunningham, CN et al. (2015) USP30 and parkin homeostatically regulate atypical ubiquitin chains on mitochondria. Nat. Cell Biol. 17 160-9 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Narendra, D et al. (2010) p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both. Autophagy 6 1090-106 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 Hara, Y et al. (2014) Hepatitis C virus core protein suppresses mitophagy by interacting with parkin in the context of mitochondrial depolarization. Am. J. Pathol. 184 3026-39 PubMed GONUTS page
↑ ^18.0 ^18.1 Gegg, ME et al. (2010) Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy. Hum. Mol. Genet. 19 4861-70 PubMed GONUTS page
↑ Dagda, RK et al. (2009) Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. J. Biol. Chem. 284 13843-55 PubMed GONUTS page
↑ ^20.0 ^20.1 ^20.2 ^20.3 ^20.4 ^20.5 Imai, Y et al. (2001) An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 105 891-902 PubMed GONUTS page
↑ ^21.0 ^21.1 ^21.2 ^21.3 ^21.4 Xiong, H et al. (2009) Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation. J. Clin. Invest. 119 650-60 PubMed GONUTS page
↑ Lee, JY et al. (2010) Disease-causing mutations in parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy. J. Cell Biol. 189 671-9 PubMed GONUTS page
↑ ^23.0 ^23.1 ^23.2 ^23.3 ^23.4 ^23.5 ^23.6 ^23.7 ^23.8 Van Humbeeck, C et al. (2011) Parkin interacts with Ambra1 to induce mitophagy. J. Neurosci. 31 10249-61 PubMed GONUTS page
↑ ^24.0 ^24.1 ^24.2 Mills, RD et al. (2008) Biochemical aspects of the neuroprotective mechanism of PTEN-induced kinase-1 (PINK1). J. Neurochem. 105 18-33 PubMed GONUTS page
↑ ^25.0 ^25.1 Esposito, G et al. (2012) Synaptic vesicle trafficking and Parkinson's disease. Dev Neurobiol 72 134-44 PubMed GONUTS page
↑ ^26.0 ^26.1 Gaki, GS & Papavassiliou, AG (2014) Oxidative stress-induced signaling pathways implicated in the pathogenesis of Parkinson's disease. Neuromolecular Med. 16 217-30 PubMed GONUTS page
↑ ^27.0 ^27.1 ^27.2 ^27.3 Yu, F & Zhou, J (2008) Parkin is ubiquitinated by Nrdp1 and abrogates Nrdp1-induced oxidative stress. Neurosci. Lett. 440 4-8 PubMed GONUTS page
↑ ^28.0 ^28.1 ^28.2 ^28.3 ^28.4 ^28.5 Henn, IH et al. (2007) Parkin mediates neuroprotection through activation of IkappaB kinase/nuclear factor-kappaB signaling. J. Neurosci. 27 1868-78 PubMed GONUTS page
↑ ^29.00 ^29.01 ^29.02 ^29.03 ^29.04 ^29.05 ^29.06 ^29.07 ^29.08 ^29.09 ^29.10 Staropoli, JF et al. (2003) Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity. Neuron 37 735-49 PubMed GONUTS page
↑ ^30.0 ^30.1 ^30.2 Bouman, L et al. (2011) Parkin is transcriptionally regulated by ATF4: evidence for an interconnection between mitochondrial stress and ER stress. Cell Death Differ. 18 769-82 PubMed GONUTS page
↑ ^31.0 ^31.1 ^31.2 ^31.3 ^31.4 ^31.5 ^31.6 Sunico, CR et al. (2013) S-Nitrosylation of parkin as a novel regulator of p53-mediated neuronal cell death in sporadic Parkinson's disease. Mol Neurodegener 8 29 PubMed GONUTS page
↑ Smith, WW et al. (2005) Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration. Proc. Natl. Acad. Sci. U.S.A. 102 18676-81 PubMed GONUTS page
↑ ^33.0 ^33.1 ^33.2 ^33.3 Ekholm-Reed, S et al. (2013) Parkin-dependent degradation of the F-box protein Fbw7β promotes neuronal survival in response to oxidative stress by stabilizing Mcl-1. Mol. Cell. Biol. 33 3627-43 PubMed GONUTS page
↑ ^34.0 ^34.1 ^34.2 ^34.3 ^34.4 ^34.5 ^34.6 ^34.7 ^34.8 Imai, Y et al. (2002) CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol. Cell 10 55-67 PubMed GONUTS page
↑ ^35.0 ^35.1 ^35.2 ^35.3 ^35.4 ^35.5 ^35.6 ^35.7 ^35.8 Müller-Rischart, AK et al. (2013) The E3 ligase parkin maintains mitochondrial integrity by increasing linear ubiquitination of NEMO. Mol. Cell 49 908-21 PubMed GONUTS page
↑ ^36.0 ^36.1 ^36.2 ^36.3 ^36.4 ^36.5 ^36.6 ^36.7 ^36.8 Shin, JH et al. (2011) PARIS (ZNF746) repression of PGC-1α contributes to neurodegeneration in Parkinson's disease. Cell 144 689-702 PubMed GONUTS page
↑ ^37.0 ^37.1 Koyano, F et al. (2014) Ubiquitin is phosphorylated by PINK1 to activate parkin. Nature 510 162-6 PubMed GONUTS page
↑ ^38.0 ^38.1 Bingol, B et al. (2014) The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy. Nature 510 370-5 PubMed GONUTS page
↑ Bai, JJ et al. (2013) Ataxin-3 is a multivalent ligand for the parkin Ubl domain. Biochemistry 52 7369-76 PubMed GONUTS page
↑ ^40.0 ^40.1 ^40.2 ^40.3 ^40.4 ^40.5 ^40.6 Sha, D et al. (2010) Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signaling. Hum. Mol. Genet. 19 352-63 PubMed GONUTS page
↑ ^41.0 ^41.1 Muqit, MM et al. (2004) 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. Hum. Mol. Genet. 13 117-35 PubMed GONUTS page
↑ ^42.0 ^42.1 Kalia, SK et al. (2004) BAG5 inhibits parkin and enhances dopaminergic neuron degeneration. Neuron 44 931-45 PubMed GONUTS page
↑ ^43.0 ^43.1 ^43.2 ^43.3 ^43.4 ^43.5 Lim, MK et al. (2007) Parkin interacts with LIM Kinase 1 and reduces its cofilin-phosphorylation activity via ubiquitination. Exp. Cell Res. 313 2858-74 PubMed GONUTS page
↑ Haque, ME et al. (2012) 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. J. Biol. Chem. 287 23162-70 PubMed GONUTS page
↑ ^45.0 ^45.1 LaVoie, MJ et al. (2005) Dopamine covalently modifies and functionally inactivates parkin. Nat. Med. 11 1214-21 PubMed GONUTS page
↑ ^46.0 ^46.1 ^46.2 Lim, KL et al. (2005) Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: implications for Lewy body formation. J. Neurosci. 25 2002-9 PubMed GONUTS page
↑ ^47.0 ^47.1 ^47.2 ^47.3 Huynh, DP et al. (2007) Parkin is an E3 ubiquitin-ligase for normal and mutant ataxin-2 and prevents ataxin-2-induced cell death. Exp. Neurol. 203 531-41 PubMed GONUTS page
↑ Wenzel, DM et al. (2011) UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 474 105-8 PubMed GONUTS page
↑ Geisler, S et al. (2010) The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations. Autophagy 6 871-8 PubMed GONUTS page
↑ ^50.0 ^50.1 ^50.2 ^50.3 ^50.4 Burchell, VS et al. (2013) The Parkinson's disease-linked proteins Fbxo7 and Parkin interact to mediate mitophagy. Nat. Neurosci. 16 1257-65 PubMed GONUTS page
↑ ^51.0 ^51.1 ^51.2 ^51.3 ^51.4 Chen, D et al. (2010) Parkin mono-ubiquitinates Bcl-2 and regulates autophagy. J. Biol. Chem. 285 38214-23 PubMed GONUTS page
↑ ^52.00 ^52.01 ^52.02 ^52.03 ^52.04 ^52.05 ^52.06 ^52.07 ^52.08 ^52.09 ^52.10 ^52.11 ^52.12 ^52.13 ^52.14 ^52.15 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Ko, HS et al. (2010) Phosphorylation by the c-Abl protein tyrosine kinase inhibits parkin's ubiquitination and protective function. Proc. Natl. Acad. Sci. U.S.A. 107 16691-6 PubMed GONUTS page
↑ ^54.0 ^54.1 ^54.2 Hofmeister-Brix, A et al. (2013) Identification of the ubiquitin-like domain of midnolin as a new glucokinase interaction partner. J. Biol. Chem. 288 35824-39 PubMed GONUTS page
↑ Chaugule, VK et al. (2011) Autoregulation of Parkin activity through its ubiquitin-like domain. EMBO J. 30 2853-67 PubMed GONUTS page
↑ ^56.0 ^56.1 Berwick, DC & Harvey, K (2014) The regulation and deregulation of Wnt signaling by PARK genes in health and disease. J Mol Cell Biol 6 3-12 PubMed GONUTS page
↑ ^57.0 ^57.1 Berwick, DC & Harvey, K (2012) The importance of Wnt signalling for neurodegeneration in Parkinson's disease. Biochem. Soc. Trans. 40 1123-8 PubMed GONUTS page
↑ Geisler, S et al. (2010) PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1. Nat. Cell Biol. 12 119-31 PubMed GONUTS page
↑ ^59.0 ^59.1 ^59.2 ^59.3 ^59.4 ^59.5 ^59.6 ^59.7 ^59.8 Trempe, JF & Fon, EA (2013) Structure and Function of Parkin, PINK1, and DJ-1, the Three Musketeers of Neuroprotection. Front Neurol 4 38 PubMed GONUTS page
↑ Dias, V et al. (2013) The role of oxidative stress in Parkinson's disease. J Parkinsons Dis 3 461-91 PubMed GONUTS page
↑ Roth, JA & Eichhorn, M (2013) Down-regulation of LRRK2 in control and DAT transfected HEK cells increases manganese-induced oxidative stress and cell toxicity. Neurotoxicology 37 100-7 PubMed GONUTS page
↑ Kitada, T et al. (1998) Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392 605-8 PubMed GONUTS page

[PMID:10888878-1] 1.0 ^1.1 Shimura, H et al. (2000) Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat. Genet. 25 302-5 PubMed GONUTS page

[PMID:19029340-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 Narendra, D et al. (2008) Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol. 183 795-803 PubMed GONUTS page

[PMID:11078524-3] 3.0 ^3.1 ^3.2 ^3.3 Zhang, Y et al. (2000) Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc. Natl. Acad. Sci. U.S.A. 97 13354-9 PubMed GONUTS page

[PMID:24446486-4] 4.0 ^4.1 ^4.2 McLelland, GL et al. (2014) Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control. EMBO J. 33 282-95 PubMed GONUTS page

[PMID:26911690-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 Song, P et al. (2016) Parkin Modulates Endosomal Organization and Function of the Endo-Lysosomal Pathway. J. Neurosci. 36 2425-37 PubMed GONUTS page

[PMID:26310625-6] Zhou, ZD et al. (2015) F-box protein 7 mutations promote protein aggregation in mitochondria and inhibit mitophagy. Hum. Mol. Genet. 24 6314-30 PubMed GONUTS page

[PMID:12925569-7] 7.0 ^7.1 ^7.2 Huynh, DP et al. (2003) The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI. Hum. Mol. Genet. 12 2587-97 PubMed GONUTS page

[PMID:10973942-8] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 Imai, Y et al. (2000) Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J. Biol. Chem. 275 35661-4 PubMed GONUTS page

[PMID:19725078-9] 9.00 ^9.01 ^9.02 ^9.03 ^9.04 ^9.05 ^9.06 ^9.07 ^9.08 ^9.09 ^9.10 ^9.11 ^9.12 ^9.13 Davison, EJ et al. (2009) Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function. Proteomics 9 4284-97 PubMed GONUTS page

[PMID:24660806-10] 10.0 ^10.1 Kazlauskaite, A et al. (2014) Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65. Biochem. J. 460 127-39 PubMed GONUTS page

[PMID:19591802-11] 11.0 ^11.1 ^11.2 ^11.3 Rawal, N et al. (2009) Parkin protects dopaminergic neurons from excessive Wnt/beta-catenin signaling. Biochem. Biophys. Res. Commun. 388 473-8 PubMed GONUTS page

[PMID:23212910-12] 12.0 ^12.1 Rakovic, A et al. (2013) 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. J. Biol. Chem. 288 2223-37 PubMed GONUTS page

[PMID:21508222-13] 13.0 ^13.1 Seibler, P et al. (2011) Mitochondrial Parkin recruitment is impaired in neurons derived from mutant PINK1 induced pluripotent stem cells. J. Neurosci. 31 5970-6 PubMed GONUTS page

[PMID:22314364-14] 14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 Jiang, H et al. (2012) Parkin controls dopamine utilization in human midbrain dopaminergic neurons derived from induced pluripotent stem cells. Nat Commun 3 668 PubMed GONUTS page

[PMID:25621951-15] 15.0 ^15.1 ^15.2 ^15.3 ^15.4 Cunningham, CN et al. (2015) USP30 and parkin homeostatically regulate atypical ubiquitin chains on mitochondria. Nat. Cell Biol. 17 160-9 PubMed GONUTS page

[PMID:20890124-16] 16.0 ^16.1 ^16.2 Narendra, D et al. (2010) p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both. Autophagy 6 1090-106 PubMed GONUTS page

[PMID:25244949-17] 17.0 ^17.1 ^17.2 Hara, Y et al. (2014) Hepatitis C virus core protein suppresses mitophagy by interacting with parkin in the context of mitochondrial depolarization. Am. J. Pathol. 184 3026-39 PubMed GONUTS page

[PMID:20871098-18] 18.0 ^18.1 Gegg, ME et al. (2010) Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy. Hum. Mol. Genet. 19 4861-70 PubMed GONUTS page

[PMID:19279012-19] Dagda, RK et al. (2009) Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. J. Biol. Chem. 284 13843-55 PubMed GONUTS page

[PMID:11439185-20] 20.0 ^20.1 ^20.2 ^20.3 ^20.4 ^20.5 Imai, Y et al. (2001) An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 105 891-902 PubMed GONUTS page

[PMID:19229105-21] 21.0 ^21.1 ^21.2 ^21.3 ^21.4 Xiong, H et al. (2009) Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation. J. Clin. Invest. 119 650-60 PubMed GONUTS page

[PMID:20457763-22] Lee, JY et al. (2010) Disease-causing mutations in parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy. J. Cell Biol. 189 671-9 PubMed GONUTS page

[PMID:21753002-23] 23.0 ^23.1 ^23.2 ^23.3 ^23.4 ^23.5 ^23.6 ^23.7 ^23.8 Van Humbeeck, C et al. (2011) Parkin interacts with Ambra1 to induce mitophagy. J. Neurosci. 31 10249-61 PubMed GONUTS page

[PMID:18221368-24] 24.0 ^24.1 ^24.2 Mills, RD et al. (2008) Biochemical aspects of the neuroprotective mechanism of PTEN-induced kinase-1 (PINK1). J. Neurochem. 105 18-33 PubMed GONUTS page

[PMID:21563316-25] 25.0 ^25.1 Esposito, G et al. (2012) Synaptic vesicle trafficking and Parkinson's disease. Dev Neurobiol 72 134-44 PubMed GONUTS page

[PMID:24522549-26] 26.0 ^26.1 Gaki, GS & Papavassiliou, AG (2014) Oxidative stress-induced signaling pathways implicated in the pathogenesis of Parkinson's disease. Neuromolecular Med. 16 217-30 PubMed GONUTS page

[PMID:18541373-27] 27.0 ^27.1 ^27.2 ^27.3 Yu, F & Zhou, J (2008) Parkin is ubiquitinated by Nrdp1 and abrogates Nrdp1-induced oxidative stress. Neurosci. Lett. 440 4-8 PubMed GONUTS page

[PMID:17314283-28] 28.0 ^28.1 ^28.2 ^28.3 ^28.4 ^28.5 Henn, IH et al. (2007) Parkin mediates neuroprotection through activation of IkappaB kinase/nuclear factor-kappaB signaling. J. Neurosci. 27 1868-78 PubMed GONUTS page

[PMID:12628165-29] 29.00 ^29.01 ^29.02 ^29.03 ^29.04 ^29.05 ^29.06 ^29.07 ^29.08 ^29.09 ^29.10 Staropoli, JF et al. (2003) Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity. Neuron 37 735-49 PubMed GONUTS page

[PMID:21113145-30] 30.0 ^30.1 ^30.2 Bouman, L et al. (2011) Parkin is transcriptionally regulated by ATF4: evidence for an interconnection between mitochondrial stress and ER stress. Cell Death Differ. 18 769-82 PubMed GONUTS page

[PMID:23985028-31] 31.0 ^31.1 ^31.2 ^31.3 ^31.4 ^31.5 ^31.6 Sunico, CR et al. (2013) S-Nitrosylation of parkin as a novel regulator of p53-mediated neuronal cell death in sporadic Parkinson's disease. Mol Neurodegener 8 29 PubMed GONUTS page

[PMID:16352719-32] Smith, WW et al. (2005) Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration. Proc. Natl. Acad. Sci. U.S.A. 102 18676-81 PubMed GONUTS page

[PMID:23858059-33] 33.0 ^33.1 ^33.2 ^33.3 Ekholm-Reed, S et al. (2013) Parkin-dependent degradation of the F-box protein Fbw7β promotes neuronal survival in response to oxidative stress by stabilizing Mcl-1. Mol. Cell. Biol. 33 3627-43 PubMed GONUTS page

[PMID:12150907-34] 34.0 ^34.1 ^34.2 ^34.3 ^34.4 ^34.5 ^34.6 ^34.7 ^34.8 Imai, Y et al. (2002) CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol. Cell 10 55-67 PubMed GONUTS page

[PMID:23453807-35] 35.0 ^35.1 ^35.2 ^35.3 ^35.4 ^35.5 ^35.6 ^35.7 ^35.8 Müller-Rischart, AK et al. (2013) The E3 ligase parkin maintains mitochondrial integrity by increasing linear ubiquitination of NEMO. Mol. Cell 49 908-21 PubMed GONUTS page

[PMID:21376232-36] 36.0 ^36.1 ^36.2 ^36.3 ^36.4 ^36.5 ^36.6 ^36.7 ^36.8 Shin, JH et al. (2011) PARIS (ZNF746) repression of PGC-1α contributes to neurodegeneration in Parkinson's disease. Cell 144 689-702 PubMed GONUTS page

[PMID:24784582-37] 37.0 ^37.1 Koyano, F et al. (2014) Ubiquitin is phosphorylated by PINK1 to activate parkin. Nature 510 162-6 PubMed GONUTS page

[PMID:24896179-38] 38.0 ^38.1 Bingol, B et al. (2014) The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy. Nature 510 370-5 PubMed GONUTS page

[PMID:24063750-39] Bai, JJ et al. (2013) Ataxin-3 is a multivalent ligand for the parkin Ubl domain. Biochemistry 52 7369-76 PubMed GONUTS page

[PMID:19880420-40] 40.0 ^40.1 ^40.2 ^40.3 ^40.4 ^40.5 ^40.6 Sha, D et al. (2010) Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signaling. Hum. Mol. Genet. 19 352-63 PubMed GONUTS page

[PMID:14645198-41] 41.0 ^41.1 Muqit, MM et al. (2004) 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. Hum. Mol. Genet. 13 117-35 PubMed GONUTS page

[PMID:15603737-42] 42.0 ^42.1 Kalia, SK et al. (2004) BAG5 inhibits parkin and enhances dopaminergic neuron degeneration. Neuron 44 931-45 PubMed GONUTS page

[PMID:17512523-43] 43.0 ^43.1 ^43.2 ^43.3 ^43.4 ^43.5 Lim, MK et al. (2007) Parkin interacts with LIM Kinase 1 and reduces its cofilin-phosphorylation activity via ubiquitination. Exp. Cell Res. 313 2858-74 PubMed GONUTS page

[PMID:22511790-44] Haque, ME et al. (2012) 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. J. Biol. Chem. 287 23162-70 PubMed GONUTS page

[PMID:16227987-45] 45.0 ^45.1 LaVoie, MJ et al. (2005) Dopamine covalently modifies and functionally inactivates parkin. Nat. Med. 11 1214-21 PubMed GONUTS page

[PMID:15728840-46] 46.0 ^46.1 ^46.2 Lim, KL et al. (2005) Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: implications for Lewy body formation. J. Neurosci. 25 2002-9 PubMed GONUTS page

[PMID:17097639-47] 47.0 ^47.1 ^47.2 ^47.3 Huynh, DP et al. (2007) Parkin is an E3 ubiquitin-ligase for normal and mutant ataxin-2 and prevents ataxin-2-induced cell death. Exp. Neurol. 203 531-41 PubMed GONUTS page

[PMID:21532592-48] Wenzel, DM et al. (2011) UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 474 105-8 PubMed GONUTS page

[PMID:20798600-49] Geisler, S et al. (2010) The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations. Autophagy 6 871-8 PubMed GONUTS page

[PMID:23933751-50] 50.0 ^50.1 ^50.2 ^50.3 ^50.4 Burchell, VS et al. (2013) The Parkinson's disease-linked proteins Fbxo7 and Parkin interact to mediate mitophagy. Nat. Neurosci. 16 1257-65 PubMed GONUTS page

[PMID:20889974-51] 51.0 ^51.1 ^51.2 ^51.3 ^51.4 Chen, D et al. (2010) Parkin mono-ubiquitinates Bcl-2 and regulates autophagy. J. Biol. Chem. 285 38214-23 PubMed GONUTS page

[PMID:21873635-52] 52.00 ^52.01 ^52.02 ^52.03 ^52.04 ^52.05 ^52.06 ^52.07 ^52.08 ^52.09 ^52.10 ^52.11 ^52.12 ^52.13 ^52.14 ^52.15 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:20823226-53] Ko, HS et al. (2010) Phosphorylation by the c-Abl protein tyrosine kinase inhibits parkin's ubiquitination and protective function. Proc. Natl. Acad. Sci. U.S.A. 107 16691-6 PubMed GONUTS page

[PMID:24187134-54] 54.0 ^54.1 ^54.2 Hofmeister-Brix, A et al. (2013) Identification of the ubiquitin-like domain of midnolin as a new glucokinase interaction partner. J. Biol. Chem. 288 35824-39 PubMed GONUTS page

[PMID:21694720-55] Chaugule, VK et al. (2011) Autoregulation of Parkin activity through its ubiquitin-like domain. EMBO J. 30 2853-67 PubMed GONUTS page

[PMID:24115276-56] 56.0 ^56.1 Berwick, DC & Harvey, K (2014) The regulation and deregulation of Wnt signaling by PARK genes in health and disease. J Mol Cell Biol 6 3-12 PubMed GONUTS page

[PMID:22988876-57] 57.0 ^57.1 Berwick, DC & Harvey, K (2012) The importance of Wnt signalling for neurodegeneration in Parkinson's disease. Biochem. Soc. Trans. 40 1123-8 PubMed GONUTS page

[PMID:20098416-58] Geisler, S et al. (2010) PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1. Nat. Cell Biol. 12 119-31 PubMed GONUTS page

[PMID:23626584-59] 59.0 ^59.1 ^59.2 ^59.3 ^59.4 ^59.5 ^59.6 ^59.7 ^59.8 Trempe, JF & Fon, EA (2013) Structure and Function of Parkin, PINK1, and DJ-1, the Three Musketeers of Neuroprotection. Front Neurol 4 38 PubMed GONUTS page

[PMID:24252804-60] Dias, V et al. (2013) The role of oxidative stress in Parkinson's disease. J Parkinsons Dis 3 461-91 PubMed GONUTS page

[PMID:23628791-61] Roth, JA & Eichhorn, M (2013) Down-regulation of LRRK2 in control and DAT transfected HEK cells increases manganese-induced oxidative stress and cell toxicity. Neurotoxicology 37 100-7 PubMed GONUTS page

[PMID:9560156-62] Kitada, T et al. (1998) Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392 605-8 PubMed GONUTS page

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