HUMAN:PINK1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	PINK1
Protein Name(s)	Serine/threonine-protein kinase PINK1, mitochondrial BRPK PTEN-induced putative kinase protein 1
External Links
UniProt	Q9BXM7
EMBL	AB053323 AF316873 AK075225 AL391357 BC009534 BC028215
CCDS	CCDS211.1
RefSeq	NP_115785.1
UniGene	Hs.389171
ProteinModelPortal	Q9BXM7
SMR	Q9BXM7
BioGrid	122376
DIP	DIP-29427N
IntAct	Q9BXM7
MINT	MINT-6781189
STRING	9606.ENSP00000364204
PhosphoSite	Q9BXM7
DMDM	48428484
PaxDb	Q9BXM7
PRIDE	Q9BXM7
DNASU	65018
GeneID	65018
KEGG	hsa:65018
UCSC	uc001bdm.3 uc001bdn.3
CTD	65018
GeneCards	GC01P020959
GeneReviews	PINK1
HGNC	HGNC:14581
HPA	CAB026191 HPA001931
MIM	168600 605909 608309
neXtProt	NX_Q9BXM7
Orphanet	2828
PharmGKB	PA33325
eggNOG	COG0515
GeneTree	ENSGT00390000001206
HOGENOM	HOG000231649
HOVERGEN	HBG053601
InParanoid	Q9BXM7
KO	K05688
OMA	GPKQLAP
OrthoDB	EOG7TBC1R
PhylomeDB	Q9BXM7
TreeFam	TF313183
SignaLink	Q9BXM7
ChiTaRS	PINK1
GeneWiki	PINK1
GenomeRNAi	65018
NextBio	67218
PRO	PR:Q9BXM7
Proteomes	UP000005640
Bgee	Q9BXM7
CleanEx	HS_PINK1
Genevestigator	Q9BXM7
GO	GO:0097449 GO:0030424 GO:0044297 GO:0000785 GO:0005737 GO:0005856 GO:0005829 GO:0031307 GO:0097413 GO:0016020 GO:0005743 GO:0005758 GO:0005741 GO:0005739 GO:0005634 GO:0048471 GO:0005524 GO:0055131 GO:0010857 GO:0016301 GO:0000287 GO:0016504 GO:0002020 GO:0043422 GO:0004674 GO:0031625 GO:0032148 GO:0071456 GO:0097237 GO:0035556 GO:0000422 GO:0007005 GO:0010629 GO:1903384 GO:0046329 GO:0043524 GO:1903202 GO:1902176 GO:1903204 GO:2000378 GO:0036289 GO:0018105 GO:0016310 GO:0033603 GO:0043123 GO:1902958 GO:0010952 GO:0033138 GO:0051897 GO:0090200 GO:0032226 GO:0051443 GO:0006468 GO:0016567 GO:0051881 GO:1903146 GO:0043254 GO:0031396 GO:2000377 GO:1902803 GO:0006979 GO:0006950 GO:0038203 GO:0006511
InterPro	IPR011009 IPR000719 IPR008271
Pfam	PF00069
SUPFAM	SSF56112
PROSITE	PS50011 PS00108

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0031307	integral to mitochondrial outer membrane	PMID:18687899^[1]	ECO:0000314			C		Fig. 2 & 4-B First Panel.	complete
involved_in	GO:1900407	regulation of cellular response to oxidative stress	PMID:24446486^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0099074	mitochondrion to lysosome transport	PMID:24446486^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(GO:1900407)	Seeded From UniProt	complete
colocalizes_with	GO:0000151	ubiquitin ligase complex	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:D6WMX4	C		Seeded From UniProt	complete
involved_in	GO:0031398	positive regulation of protein ubiquitination	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:D6WMX4	P		Seeded From UniProt	complete
involved_in	GO:0036289	peptidyl-serine autophosphorylation	PMID:25527497^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0005739	mitochondrion	PMID:24184327^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		C	part_of:(GO:0098780)	Seeded From UniProt	complete
involved_in	GO:0072656	maintenance of protein location in mitochondrion	PMID:25527497^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:D6WMX4	F	has_direct_input:(UniProtKB:P0CG47)	Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:D6WMX4	P	has_direct_input:(UniProtKB:P0CG47)	Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:25527497^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_input:(UniProtKB:Q9BXM7)	Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:25527497^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(UniProtKB:Q9BXM7)\|has_direct_input(UniProtKB:P0CG47)	Seeded From UniProt	complete
involved_in	GO:1904544	positive regulation of free ubiquitin chain polymerization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:D6WMX4	P		Seeded From UniProt	complete
involved_in	GO:0033138	positive regulation of peptidyl-serine phosphorylation	PMID:24660806^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(GO:0005739)	Seeded From UniProt	complete
involved_in	GO:0072655	establishment of protein localization to mitochondrion	PMID:25527497^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0005742	mitochondrial outer membrane translocase complex	PMID:24270810^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
colocalizes_with	GO:0005741	mitochondrial outer membrane	PMID:25527497^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		C	exists_during:(GO:0006468)	Seeded From UniProt	complete
involved_in	GO:1903214	regulation of protein targeting to mitochondrion	PMID:23212910^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:O60260)	Seeded From UniProt	complete
involved_in	GO:0031396	regulation of protein ubiquitination	PMID:23212910^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:O60260)	Seeded From UniProt	complete
involved_in	GO:0010821	regulation of mitochondrion organization	PMID:21508222^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000700)	Seeded From UniProt	complete
involved_in	GO:1903214	regulation of protein targeting to mitochondrion	PMID:21508222^[8]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q9BXM7	P	occurs_in:(CL:0000700) has_regulation_target:(UniProtKB:O60260)	Seeded From UniProt	complete
involved_in	GO:1903955	positive regulation of protein targeting to mitochondrion	PMID:24270810^[6]	ECO:0007001	high throughput mutant phenotypic evidence used in manual assertion		P	has_regulation_target:(UniProtKB:O60260)	Seeded From UniProt	complete
involved_in	GO:0034599	cellular response to oxidative stress	PMID:22764206^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000700)	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:25527291^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:25527291^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0001934	positive regulation of protein phosphorylation	PMID:25244949^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:O60260)	Seeded From UniProt	complete
involved_in	GO:1903214	regulation of protein targeting to mitochondrion	PMID:25244949^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:O60260)	Seeded From UniProt	complete
colocalizes_with	GO:0005739	mitochondrion	PMID:21355049^[12]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q9H300	C		Seeded From UniProt	complete
involved_in	GO:1902902	negative regulation of autophagosome assembly	PMID:19279012^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090258	negative regulation of mitochondrial fission	PMID:19279012^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903147	negative regulation of autophagy of mitochondrion	PMID:19279012^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903852	positive regulation of cristae formation	PMID:19279012^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016242	negative regulation of macroautophagy	PMID:19279012^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:19229105^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:19229105^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:19229105^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0098779	positive regulation of mitophagy in response to mitochondrial depolarization	PMID:20871098^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016239	positive regulation of macroautophagy	PMID:20871098^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031396	regulation of protein ubiquitination	PMID:20871098^[15]	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:0002082	regulation of oxidative phosphorylation	PMID:20871098^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0038203	TORC2 signaling	PMID:21177249^[16]	ECO:0000305	curator inference used in manual assertion	GO:0006468 GO:0031932	P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:21177249^[16]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:Q6R327)	Seeded From UniProt	complete
colocalizes_with	GO:0031932	TORC2 complex	PMID:21177249^[16]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q6R327	C		Seeded From UniProt	complete
enables	GO:0043422	protein kinase B binding	PMID:21177249^[16]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0032148	activation of protein kinase B activity	PMID:21177249^[16]	ECO:0000305	curator inference used in manual assertion	GO:0033138	P	has_regulation_target:(UniProtKB:P31749)	Seeded From UniProt	complete
involved_in	GO:0033138	positive regulation of peptidyl-serine phosphorylation	PMID:21177249^[16]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P31749)	Seeded From UniProt	complete
involved_in	GO:1903384	negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway	PMID:21177249^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	PMID:21563316^[17]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0051897	positive regulation of protein kinase B signaling	PMID:21177249^[16]	ECO:0000305	curator inference used in manual assertion	GO:0033138 GO:0043422	P		Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	PMID:24475098^[18]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q99MQ3	P	has_regulation_target:(UniProtKB:Q9UL15)	Seeded From UniProt	complete
involved_in	GO:2000377	regulation of reactive oxygen species metabolic process	PMID:24475098^[18]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q9UL15	P		Seeded From UniProt	complete
involved_in	GO:0051881	regulation of mitochondrial membrane potential	PMID:24475098^[18]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q9UL15	P		Seeded From UniProt	complete
involved_in	GO:0006979	response to oxidative stress	PMID:24475098^[18]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q9UL15	P		Seeded From UniProt	complete
involved_in	GO:2000378	negative regulation of reactive oxygen species metabolic process	PMID:18560593^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051881	regulation of mitochondrial membrane potential	PMID:18560593^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:21138942^[20]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21138942^[20]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:2000377	regulation of reactive oxygen species metabolic process	PMID:21138942^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051881	regulation of mitochondrial membrane potential	PMID:21138942^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0002020	protease binding	PMID:21138942^[20]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9H300	F		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:16702191^[21]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0000955)	Seeded From UniProt	complete
part_of	GO:0097449	astrocyte projection	PMID:16702191^[21]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0000955) part_of:(CL:0000127)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16702191^[21]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540) part_of:(UBERON:0000955) part_of:(GO:0044297)	Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:16702191^[21]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000125) part_of:(UBERON:0000955)	Seeded From UniProt	complete
part_of	GO:0044297	cell body	PMID:16702191^[21]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540) part_of:(UBERON:0000955)\|part_of:(CL:0000127) part_of:(UBERON:0000955)	Seeded From UniProt	complete
part_of	GO:0030424	axon	PMID:16702191^[21]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540) part_of:(UBERON:0000955)	Seeded From UniProt	complete
involved_in	GO:1903202	negative regulation of oxidative stress-induced cell death	PMID:16632486^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903384	negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway	PMID:23261939^[23]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	PMID:21426348^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005758	mitochondrial intermembrane space	PMID:21426348^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005743	mitochondrial inner membrane	PMID:21426348^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21426348^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:18560593^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000540)	Seeded From UniProt	complete
involved_in	GO:0043524	negative regulation of neuron apoptotic process	PMID:18560593^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(GO:0033554)	Seeded From UniProt	complete
part_of	GO:0031307	integral component of mitochondrial outer membrane	PMID:18687899^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0071456	cellular response to hypoxia	PMID:24553947^[25]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	PMID:24798695^[26]	ECO:0000314	direct assay evidence used in manual assertion		C	exists_during:(GO:0070301)	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:24798695^[26]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:24798695^[26]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:24798695^[26]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0000785	chromatin	PMID:24798695^[26]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:24784582^[27]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000422	autophagy of mitochondrion	PMID:24896179^[28]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903751	negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide	PMID:17579517^[29]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	PMID:17579517^[29]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:Q12931)\|part_of(GO:1902176)	Seeded From UniProt	complete
part_of	GO:0005743	mitochondrial inner membrane	PMID:17579517^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005758	mitochondrial intermembrane space	PMID:17579517^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:17579517^[29]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:Q12931)\|part_of(GO:1902176)	Seeded From UniProt	complete
involved_in	GO:0061136	regulation of proteasomal protein catabolic process	PMID:22078885^[30]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090200	positive regulation of release of cytochrome c from mitochondria	PMID:19880420^[31]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0055131	C3HC4-type RING finger domain binding	PMID:19880420^[31]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60260	F		Seeded From UniProt	complete
involved_in	GO:0043254	regulation of protein complex assembly	PMID:19880420^[31]	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^[31]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031396	regulation of protein ubiquitination	PMID:19880420^[31]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	PMID:19880420^[31]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0010857	calcium-dependent protein kinase activity	PMID:19880420^[31]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:19880420^[31]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:19880420^[31]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0035556	intracellular signal transduction	PMID:14607334^[32]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:20798600^[33]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60260	F		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:23933751^[34]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2001243	negative regulation of intrinsic apoptotic signaling pathway	PMID:15087508^[35]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:14607334^[32]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:20798600^[33]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:23933751^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:20798600^[33]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:15087508^[35]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:14607334^[32]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:14607334^[32]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000422	autophagy of mitochondrion	PMID:23933751^[34]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000422	autophagy of mitochondrion	PMID:20798600^[33]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:14607334^[32]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0090141	positive regulation of mitochondrial fission	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0029891 PANTHER:PTN001121970 RGD:1305769	P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0029891 MGI:MGI:1916193 PANTHER:PTN000540563 UniProtKB:Q9BXM7	P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0029891 PANTHER:PTN001121970 UniProtKB:Q9BXM7 WB:WBGene00017137 ZFIN:ZDB-GENE-041212-53	C		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0029891 MGI:MGI:1916193 PANTHER:PTN001121970 RGD:1305769 UniProtKB:D6WMX4 UniProtKB:Q9BXM7	F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0029891 PANTHER:PTN000540563 UniProtKB:Q9BXM7	F		Seeded From UniProt	complete
involved_in	GO:0000422	autophagy of mitochondrion	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0029891 PANTHER:PTN001121970 UniProtKB:Q9BXM7 WB:WBGene00017137	P		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	PMID:15824318^[37]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:15824318^[37]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1904925	positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B5DFG1 ensembl:ENSRNOP00000069316	P		Seeded From UniProt	complete
involved_in	GO:1904881	cellular response to hydrogen sulfide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B5DFG1 ensembl:ENSRNOP00000069316	P		Seeded From UniProt	complete
involved_in	GO:1904783	positive regulation of NMDA glutamate receptor activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B5DFG1 ensembl:ENSRNOP00000069316	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:B5DFG1 ensembl:ENSRNOP00000069316	P		Seeded From UniProt	complete
involved_in	GO:0090141	positive regulation of mitochondrial fission	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B5DFG1 ensembl:ENSRNOP00000069316	P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B5DFG1 ensembl:ENSRNOP00000069316	P		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B5DFG1 ensembl:ENSRNOP00000069316	F		Seeded From UniProt	complete
part_of	GO:0030426	growth cone	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B5DFG1 ensembl:ENSRNOP00000069316	C		Seeded From UniProt	complete
part_of	GO:0005743	mitochondrial inner membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B5DFG1 ensembl:ENSRNOP00000069316	C		Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B5DFG1 ensembl:ENSRNOP00000069316	C		Seeded From UniProt	complete
involved_in	GO:0002931	response to ischemia	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B5DFG1 ensembl:ENSRNOP00000069316	P		Seeded From UniProt	complete
involved_in	GO:0001934	positive regulation of protein phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B5DFG1 ensembl:ENSRNOP00000069316	P		Seeded From UniProt	complete
involved_in	GO:1903298	negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
involved_in	GO:1902958	positive regulation of mitochondrial electron transport, NADH to ubiquinone	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
involved_in	GO:1901727	positive regulation of histone deacetylase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	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:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
involved_in	GO:0071456	cellular response to hypoxia	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
involved_in	GO:0051091	positive regulation of DNA-binding transcription factor activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
involved_in	GO:0045727	positive regulation of translation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	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:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
involved_in	GO:0043523	regulation of neuron apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
involved_in	GO:0035556	intracellular signal transduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
involved_in	GO:0035307	positive regulation of protein dephosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
involved_in	GO:0034599	cellular response to oxidative stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
involved_in	GO:0033605	positive regulation of catecholamine secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
involved_in	GO:0033603	positive regulation of dopamine secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
involved_in	GO:0032226	positive regulation of synaptic transmission, dopaminergic	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
involved_in	GO:0022904	respiratory electron transport chain	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	F		Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
involved_in	GO:0010310	regulation of hydrogen peroxide metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	P		Seeded From UniProt	complete
part_of	GO:0005743	mitochondrial inner membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	F		Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q99MQ3 ensembl:ENSMUSP00000030536	F		Seeded From UniProt	complete
involved_in	GO:0000422	autophagy of mitochondrion	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR040110	P		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008271	F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR040110	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719	F		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008271	P		Seeded From UniProt	complete
involved_in	GO:2001171	positive regulation of ATP biosynthetic process	PMID:20871098^[15]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0036289	peptidyl-serine autophosphorylation	PMID:23626584^[38]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	PMID:23626584^[38]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_input:(UniProtKB:O60260) part_of:(GO:0051443)	Seeded From UniProt	complete
involved_in	GO:0033138	positive regulation of peptidyl-serine phosphorylation	PMID:18221368^[39]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_regulation_target:(UniProtKB:O43464)	Seeded From UniProt	complete
involved_in	GO:0097237	cellular response to toxic substance	PMID:18221368^[39]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046329	negative regulation of JNK cascade	PMID:18221368^[39]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903146	regulation of autophagy of mitochondrion	PMID:21563316^[17]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051443	positive regulation of ubiquitin-protein transferase activity	PMID:24522549^[40]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_regulation_target:(UniProtKB:O60260)	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:24522549^[40]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	has_input:(UniProtKB:O60260) part_of:(GO:0051443)	Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:24522549^[40]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_input:(UniProtKB:O60260) part_of:(GO:0051443)	Seeded From UniProt	complete
enables	GO:0002020	protease binding	PMID:24522549^[40]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	has_input:(UniProtKB:O43464)	Seeded From UniProt	complete
involved_in	GO:0010952	positive regulation of peptidase activity	PMID:24522549^[40]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_regulation_target:(UniProtKB:O43464)	Seeded From UniProt	complete
enables	GO:0016504	peptidase activator activity	PMID:24522549^[40]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	has_input:(UniProtKB:O43464)	Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:24522549^[40]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903204	negative regulation of oxidative stress-induced neuron death	PMID:24522549^[40]	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^[40]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1902803	regulation of synaptic vesicle transport	PMID:21563316^[17]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902958	positive regulation of mitochondrial electron transport, NADH to ubiquinone	PMID:21138942^[20]	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-5205661	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005758	mitochondrial intermembrane space	Reactome:R-HSA-5205681 Reactome:R-HSA-5205672 Reactome:R-HSA-5205661	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	Reactome:R-HSA-5205682 Reactome:R-HSA-5205672 Reactome:R-HSA-5205652	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		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
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
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	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
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0723	F		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1000 UniProtKB-SubCell:SL-0172	C		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F		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
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
part_of	GO:0005743	mitochondrial inner membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0999 UniProtKB-SubCell:SL-0168	C		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P		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
edit table

Notes

References

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

↑ ^1.0 ^1.1 Zhou, C et al. (2008) The kinase domain of mitochondrial PINK1 faces the cytoplasm. Proc. Natl. Acad. Sci. U.S.A. 105 12022-7 PubMed GONUTS page
↑ ^2.0 ^2.1 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
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Aerts, L et al. (2015) PINK1 kinase catalytic activity is regulated by phosphorylation on serines 228 and 402. J. Biol. Chem. 290 2798-811 PubMed GONUTS page
↑ Gómez-Sánchez, R et al. (2014) Mitochondrial impairment increases FL-PINK1 levels by calcium-dependent gene expression. Neurobiol. Dis. 62 426-40 PubMed GONUTS page
↑ Kazlauskaite, A et al. (2014) Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65. Biochem. J. 460 127-39 PubMed GONUTS page
↑ ^6.0 ^6.1 Hasson, SA et al. (2013) High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy. Nature 504 291-5 PubMed GONUTS page
↑ ^7.0 ^7.1 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
↑ ^8.0 ^8.1 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
↑ Cooper, O et al. (2012) Pharmacological rescue of mitochondrial deficits in iPSC-derived neural cells from patients with familial Parkinson's disease. Sci Transl Med 4 141ra90 PubMed GONUTS page
↑ ^10.0 ^10.1 Wauer, T et al. (2015) Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis. EMBO J. 34 307-25 PubMed GONUTS page
↑ ^11.0 ^11.1 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
↑ Shi, G et al. (2011) Functional alteration of PARL contributes to mitochondrial dysregulation in Parkinson's disease. Hum. Mol. Genet. 20 1966-74 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 ^13.4 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
↑ ^14.0 ^14.1 ^14.2 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
↑ ^15.0 ^15.1 ^15.2 ^15.3 ^15.4 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
↑ ^16.0 ^16.1 ^16.2 ^16.3 ^16.4 ^16.5 ^16.6 ^16.7 Murata, H et al. (2011) A new cytosolic pathway from a Parkinson disease-associated kinase, BRPK/PINK1: activation of AKT via mTORC2. J. Biol. Chem. 286 7182-9 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 Esposito, G et al. (2012) Synaptic vesicle trafficking and Parkinson's disease. Dev Neurobiol 72 134-44 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 ^18.3 Wang, X et al. (2014) BAG5 protects against mitochondrial oxidative damage through regulating PINK1 degradation. PLoS ONE 9 e86276 PubMed GONUTS page
↑ ^19.0 ^19.1 ^19.2 ^19.3 Wood-Kaczmar, A et al. (2008) PINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neurons. PLoS ONE 3 e2455 PubMed GONUTS page
↑ ^20.0 ^20.1 ^20.2 ^20.3 ^20.4 ^20.5 Deas, E et al. (2011) PINK1 cleavage at position A103 by the mitochondrial protease PARL. Hum. Mol. Genet. 20 867-79 PubMed GONUTS page
↑ ^21.0 ^21.1 ^21.2 ^21.3 ^21.4 ^21.5 Gandhi, S et al. (2006) PINK1 protein in normal human brain and Parkinson's disease. Brain 129 1720-31 PubMed GONUTS page
↑ Tang, B et al. (2006) Association of PINK1 and DJ-1 confers digenic inheritance of early-onset Parkinson's disease. Hum. Mol. Genet. 15 1816-25 PubMed GONUTS page
↑ Chien, WL et al. (2013) Increase of oxidative stress by a novel PINK1 mutation, P209A. Free Radic. Biol. Med. 58 160-9 PubMed GONUTS page
↑ ^24.0 ^24.1 ^24.2 ^24.3 Meissner, C et al. (2011) The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking. J. Neurochem. 117 856-67 PubMed GONUTS page
↑ Lin, W et al. (2014) Loss of PINK1 attenuates HIF-1α induction by preventing 4E-BP1-dependent switch in protein translation under hypoxia. J. Neurosci. 34 3079-89 PubMed GONUTS page
↑ ^26.0 ^26.1 ^26.2 ^26.3 ^26.4 Patil, KS et al. (2014) PARK13 regulates PINK1 and subcellular relocation patterns under oxidative stress in neurons. J. Neurosci. Res. 92 1167-77 PubMed GONUTS page
↑ Koyano, F et al. (2014) Ubiquitin is phosphorylated by PINK1 to activate parkin. Nature 510 162-6 PubMed GONUTS page
↑ Bingol, B et al. (2014) The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy. Nature 510 370-5 PubMed GONUTS page
↑ ^29.0 ^29.1 ^29.2 ^29.3 ^29.4 Pridgeon, JW et al. (2007) PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1. PLoS Biol. 5 e172 PubMed GONUTS page
↑ Wang, X et al. (2011) PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility. Cell 147 893-906 PubMed GONUTS page
↑ ^31.0 ^31.1 ^31.2 ^31.3 ^31.4 ^31.5 ^31.6 ^31.7 ^31.8 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
↑ ^32.0 ^32.1 ^32.2 ^32.3 ^32.4 Nakajima, A et al. (2003) BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential. Cancer Lett. 201 195-201 PubMed GONUTS page
↑ ^33.0 ^33.1 ^33.2 ^33.3 Geisler, S et al. (2010) The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations. Autophagy 6 871-8 PubMed GONUTS page
↑ ^34.0 ^34.1 ^34.2 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
↑ ^35.0 ^35.1 Valente, EM et al. (2004) Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 304 1158-60 PubMed GONUTS page
↑ ^36.0 ^36.1 ^36.2 ^36.3 ^36.4 ^36.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^37.0 ^37.1 Beilina, A et al. (2005) Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability. Proc. Natl. Acad. Sci. U.S.A. 102 5703-8 PubMed GONUTS page
↑ ^38.0 ^38.1 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
↑ ^39.0 ^39.1 ^39.2 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
↑ ^40.0 ^40.1 ^40.2 ^40.3 ^40.4 ^40.5 ^40.6 ^40.7 ^40.8 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:18687899-1] 1.0 ^1.1 Zhou, C et al. (2008) The kinase domain of mitochondrial PINK1 faces the cytoplasm. Proc. Natl. Acad. Sci. U.S.A. 105 12022-7 PubMed GONUTS page

[PMID:24446486-2] 2.0 ^2.1 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:25527497-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Aerts, L et al. (2015) PINK1 kinase catalytic activity is regulated by phosphorylation on serines 228 and 402. J. Biol. Chem. 290 2798-811 PubMed GONUTS page

[PMID:24184327-4] Gómez-Sánchez, R et al. (2014) Mitochondrial impairment increases FL-PINK1 levels by calcium-dependent gene expression. Neurobiol. Dis. 62 426-40 PubMed GONUTS page

[PMID:24660806-5] 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:24270810-6] 6.0 ^6.1 Hasson, SA et al. (2013) High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy. Nature 504 291-5 PubMed GONUTS page

[PMID:23212910-7] 7.0 ^7.1 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:21508222-8] 8.0 ^8.1 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:22764206-9] Cooper, O et al. (2012) Pharmacological rescue of mitochondrial deficits in iPSC-derived neural cells from patients with familial Parkinson's disease. Sci Transl Med 4 141ra90 PubMed GONUTS page

[PMID:25527291-10] 10.0 ^10.1 Wauer, T et al. (2015) Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis. EMBO J. 34 307-25 PubMed GONUTS page

[PMID:25244949-11] 11.0 ^11.1 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:21355049-12] Shi, G et al. (2011) Functional alteration of PARL contributes to mitochondrial dysregulation in Parkinson's disease. Hum. Mol. Genet. 20 1966-74 PubMed GONUTS page

[PMID:19279012-13] 13.0 ^13.1 ^13.2 ^13.3 ^13.4 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:19229105-14] 14.0 ^14.1 ^14.2 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:20871098-15] 15.0 ^15.1 ^15.2 ^15.3 ^15.4 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:21177249-16] 16.0 ^16.1 ^16.2 ^16.3 ^16.4 ^16.5 ^16.6 ^16.7 Murata, H et al. (2011) A new cytosolic pathway from a Parkinson disease-associated kinase, BRPK/PINK1: activation of AKT via mTORC2. J. Biol. Chem. 286 7182-9 PubMed GONUTS page

[PMID:21563316-17] 17.0 ^17.1 ^17.2 Esposito, G et al. (2012) Synaptic vesicle trafficking and Parkinson's disease. Dev Neurobiol 72 134-44 PubMed GONUTS page

[PMID:24475098-18] 18.0 ^18.1 ^18.2 ^18.3 Wang, X et al. (2014) BAG5 protects against mitochondrial oxidative damage through regulating PINK1 degradation. PLoS ONE 9 e86276 PubMed GONUTS page

[PMID:18560593-19] 19.0 ^19.1 ^19.2 ^19.3 Wood-Kaczmar, A et al. (2008) PINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neurons. PLoS ONE 3 e2455 PubMed GONUTS page

[PMID:21138942-20] 20.0 ^20.1 ^20.2 ^20.3 ^20.4 ^20.5 Deas, E et al. (2011) PINK1 cleavage at position A103 by the mitochondrial protease PARL. Hum. Mol. Genet. 20 867-79 PubMed GONUTS page

[PMID:16702191-21] 21.0 ^21.1 ^21.2 ^21.3 ^21.4 ^21.5 Gandhi, S et al. (2006) PINK1 protein in normal human brain and Parkinson's disease. Brain 129 1720-31 PubMed GONUTS page

[PMID:16632486-22] Tang, B et al. (2006) Association of PINK1 and DJ-1 confers digenic inheritance of early-onset Parkinson's disease. Hum. Mol. Genet. 15 1816-25 PubMed GONUTS page

[PMID:23261939-23] Chien, WL et al. (2013) Increase of oxidative stress by a novel PINK1 mutation, P209A. Free Radic. Biol. Med. 58 160-9 PubMed GONUTS page

[PMID:21426348-24] 24.0 ^24.1 ^24.2 ^24.3 Meissner, C et al. (2011) The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking. J. Neurochem. 117 856-67 PubMed GONUTS page

[PMID:24553947-25] Lin, W et al. (2014) Loss of PINK1 attenuates HIF-1α induction by preventing 4E-BP1-dependent switch in protein translation under hypoxia. J. Neurosci. 34 3079-89 PubMed GONUTS page

[PMID:24798695-26] 26.0 ^26.1 ^26.2 ^26.3 ^26.4 Patil, KS et al. (2014) PARK13 regulates PINK1 and subcellular relocation patterns under oxidative stress in neurons. J. Neurosci. Res. 92 1167-77 PubMed GONUTS page

[PMID:24784582-27] Koyano, F et al. (2014) Ubiquitin is phosphorylated by PINK1 to activate parkin. Nature 510 162-6 PubMed GONUTS page

[PMID:24896179-28] Bingol, B et al. (2014) The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy. Nature 510 370-5 PubMed GONUTS page

[PMID:17579517-29] 29.0 ^29.1 ^29.2 ^29.3 ^29.4 Pridgeon, JW et al. (2007) PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1. PLoS Biol. 5 e172 PubMed GONUTS page

[PMID:22078885-30] Wang, X et al. (2011) PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility. Cell 147 893-906 PubMed GONUTS page

[PMID:19880420-31] 31.0 ^31.1 ^31.2 ^31.3 ^31.4 ^31.5 ^31.6 ^31.7 ^31.8 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:14607334-32] 32.0 ^32.1 ^32.2 ^32.3 ^32.4 Nakajima, A et al. (2003) BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential. Cancer Lett. 201 195-201 PubMed GONUTS page

[PMID:20798600-33] 33.0 ^33.1 ^33.2 ^33.3 Geisler, S et al. (2010) The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations. Autophagy 6 871-8 PubMed GONUTS page

[PMID:23933751-34] 34.0 ^34.1 ^34.2 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:15087508-35] 35.0 ^35.1 Valente, EM et al. (2004) Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 304 1158-60 PubMed GONUTS page

[PMID:21873635-36] 36.0 ^36.1 ^36.2 ^36.3 ^36.4 ^36.5 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:15824318-37] 37.0 ^37.1 Beilina, A et al. (2005) Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability. Proc. Natl. Acad. Sci. U.S.A. 102 5703-8 PubMed GONUTS page

[PMID:23626584-38] 38.0 ^38.1 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:18221368-39] 39.0 ^39.1 ^39.2 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:24522549-40] 40.0 ^40.1 ^40.2 ^40.3 ^40.4 ^40.5 ^40.6 ^40.7 ^40.8 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

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