HUMAN:LRRK2

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	LRRK2 (synonyms: PARK8)
Protein Name(s)	Leucine-rich repeat serine/threonine-protein kinase 2 Dardarin
External Links
UniProt	Q5S007
EMBL	AY792511 AC079630 AC084290 AC107023 AL834529
CCDS	CCDS31774.1
RefSeq	NP_940980.3
UniGene	Hs.187636
PDB	2ZEJ 3D6T
PDBsum	2ZEJ 3D6T
ProteinModelPortal	Q5S007
SMR	Q5S007
BioGrid	125700
DIP	DIP-29684N
IntAct	Q5S007
MINT	MINT-7997594
STRING	9606.ENSP00000298910
BindingDB	Q5S007
ChEMBL	CHEMBL1075104
GuidetoPHARMACOLOGY	2059
PhosphoSite	Q5S007
DMDM	294862450
MaxQB	Q5S007
PaxDb	Q5S007
PRIDE	Q5S007
Ensembl	ENST00000298910
GeneID	120892
KEGG	hsa:120892
UCSC	uc001rmg.4
CTD	120892
GeneCards	GC12P040590
GeneReviews	LRRK2
HGNC	HGNC:18618
HPA	CAB037160 HPA014293
MIM	168600 607060 609007
neXtProt	NX_Q5S007
Orphanet	2828
PharmGKB	PA134968052
eggNOG	COG4886
GeneTree	ENSGT00530000063477
HOGENOM	HOG000293315
HOVERGEN	HBG081937
InParanoid	Q5S007
KO	K08844
OMA	FKIRDQP
PhylomeDB	Q5S007
TreeFam	TF313679
SignaLink	Q5S007
ChiTaRS	LRRK2
EvolutionaryTrace	Q5S007
GeneWiki	LRRK2
GenomeRNAi	120892
NextBio	80641
PRO	PR:Q5S007
Proteomes	UP000005640
Bgee	Q5S007
CleanEx	HS_LRRK2
ExpressionAtlas	Q5S007
Genevestigator	Q5S007
GO	GO:0030424 GO:0005737 GO:0032473 GO:0031410 GO:0005829 GO:0030425 GO:0032839 GO:0005783 GO:0005768 GO:0005615 GO:0070062 GO:0005794 GO:0016234 GO:0005764 GO:0045121 GO:0005743 GO:0005759 GO:0031966 GO:0005741 GO:0005739 GO:0043005 GO:0043025 GO:0043204 GO:0005886 GO:0008021 GO:0043195 GO:0005802 GO:0003779 GO:0005524 GO:0030276 GO:0001948 GO:0005525 GO:0034211 GO:0005096 GO:0003924 GO:0042802 GO:0044325 GO:0016301 GO:0004708 GO:0036479 GO:0042803 GO:0051018 GO:0004672 GO:0004674 GO:0017048 GO:0000149 GO:0017075 GO:0015631 GO:0000187 GO:0000186 GO:0006914 GO:0034613 GO:1903351 GO:0071287 GO:0034599 GO:0008340 GO:0006897 GO:0035640 GO:0006184 GO:0048312 GO:0035556 GO:0035641 GO:0000165 GO:0034260 GO:1903206 GO:1902823 GO:2000469 GO:0032091 GO:0001933 GO:0010955 GO:1903217 GO:1903215 GO:1903125 GO:0007528 GO:0070997 GO:0048812 GO:0021772 GO:0018105 GO:0018107 GO:0010508 GO:0060161 GO:0043547 GO:0043406 GO:0043068 GO:0032436 GO:1902499 GO:0032092 GO:0001934 GO:0031398 GO:0046777 GO:0070585 GO:0006468 GO:0072593 GO:2000172 GO:0061001 GO:0060159 GO:0060079 GO:0035564 GO:0040012 GO:0042391 GO:0051900 GO:0090140 GO:1902692 GO:1901214 GO:0014041 GO:0010738 GO:0051966 GO:2000300 GO:1902803 GO:0006979 GO:0007264 GO:0022028
Gene3D	1.25.10.10 1.25.40.20 2.130.10.10 3.40.50.300
InterPro	IPR020683 IPR011989 IPR016024 IPR011009 IPR001611 IPR025875 IPR003591 IPR013684 IPR027417 IPR000719 IPR017441 IPR020859 IPR008271 IPR005225 IPR001806 IPR015943 IPR001680 IPR017986
Pfam	PF00560 PF12799 PF13855 PF08477 PF00069
PRINTS	PR00449
SMART	SM00369 SM00320
SUPFAM	SSF48371 SSF50978 SSF52540 SSF56112
TIGRFAMs	TIGR00231
PROSITE	PS51450 PS00107 PS50011 PS00108 PS51424

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:0007029	endoplasmic reticulum organization	PMID:25201882^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0060628	regulation of ER to Golgi vesicle-mediated transport	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	P		Seeded From UniProt	complete
involved_in	GO:0070973	protein localization to endoplasmic reticulum exit site	PMID:25201882^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0070971	endoplasmic reticulum exit site	PMID:25201882^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0031647	regulation of protein stability	PMID:26014385^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:26014385^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:28720718^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:28720718^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:28720718^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1905279	regulation of retrograde transport, endosome to Golgi	PMID:23395371^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q7KVL7	P	occurs_in:(CL:0000700)	Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	PMID:23395371^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044753	amphisome	PMID:19640926^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005902	microvillus	PMID:19640926^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044754	autolysosome	PMID:19640926^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0097487	multivesicular body, internal vesicle	PMID:19640926^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:19640926^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0016242	negative regulation of macroautophagy	PMID:19640926^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0099400	caveola neck	PMID:19640926^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:25500533^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:Q14155)	Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:25500533^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:Q14155)	Seeded From UniProt	complete
involved_in	GO:0035751	regulation of lysosomal lumen pH	PMID:22012985^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1905289	regulation of CAMKK-AMPK signaling cascade	PMID:22012985^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	PMID:19625296^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540)	Seeded From UniProt	complete
part_of	GO:0030426	growth cone	PMID:19625296^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540)	Seeded From UniProt	complete
enables	GO:0030159	receptor signaling complex adaptor activity	PMID:22899650^[9]	ECO:0000305	curator inference used in manual assertion	GO:0005515	F	part_of:(GO:0090263) has_input:(GO:1990909)	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:22899650^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:22899650^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0090263	positive regulation of canonical Wnt signaling pathway	PMID:22899650^[9]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:O14640 UniProtKB:O14641 UniProtKB:O75581 UniProtKB:Q92997	P	occurs_at:(GO:0016020)	Seeded From UniProt	complete
part_of	GO:1990909	Wnt signalosome	PMID:22899650^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0001934	positive regulation of protein phosphorylation	PMID:22012985^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q13131)	Seeded From UniProt	complete
involved_in	GO:0009267	cellular response to starvation	PMID:24211199^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010506	regulation of autophagy	PMID:24211199^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(GO:0009267)	Seeded From UniProt	complete
enables	GO:1904713	beta-catenin destruction complex binding	PMID:24115276^[11]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:1990909	Wnt signalosome	PMID:24115276^[11]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0019722	calcium-mediated signaling	PMID:25416817^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(GO:0007040)	Seeded From UniProt	complete
involved_in	GO:0007040	lysosome organization	PMID:25416817^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1904887	Wnt signalosome assembly	PMID:22899650^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O75581	P		Seeded From UniProt	complete
involved_in	GO:1902902	negative regulation of autophagosome assembly	PMID:23916833^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	PMID:23916833^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(GO:1902902)	Seeded From UniProt	complete
enables	GO:0016301	kinase activity	PMID:23916833^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	part_of:(GO:1902902)	Seeded From UniProt	complete
involved_in	GO:0007030	Golgi organization	PMID:24510904^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005798	Golgi-associated vesicle	PMID:24510904^[14]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002609)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:19625296^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:22764206^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000540) occurs_in:(GO:0030424)	Seeded From UniProt	complete
involved_in	GO:0051646	mitochondrion localization	PMID:22764206^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000540) occurs_in:(GO:0030424)	Seeded From UniProt	complete
involved_in	GO:0034599	cellular response to oxidative stress	PMID:22764206^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000700)	Seeded From UniProt	complete
involved_in	GO:1902236	negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway	PMID:21857923^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034599	cellular response to oxidative stress	PMID:21857923^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000187	activation of MAPK activity	PMID:21857923^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(GO:0033554) part_of:(GO:1901215)	Seeded From UniProt	complete
involved_in	GO:1901215	negative regulation of neuron death	PMID:21857923^[16]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q9TZM3	P	part_of:(GO:0033554)	Seeded From UniProt	complete
involved_in	GO:1903351	cellular response to dopamine	PMID:23628791^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071287	cellular response to manganese ion	PMID:23628791^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043406	positive regulation of MAP kinase activity	PMID:23628791^[17]	ECO:0000305	curator inference used in manual assertion	GO:0006468	P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:23628791^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902499	positive regulation of protein autoubiquitination	PMID:16352719^[18]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:O60260)	Seeded From UniProt	complete
enables	GO:0044325	ion channel binding	PMID:21370995^[19]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P21796	F		Seeded From UniProt	complete
involved_in	GO:0032092	positive regulation of protein binding	PMID:21370995^[19]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P21796) has_regulation_target:(UniProtKB:P12236)	Seeded From UniProt	complete
involved_in	GO:1903217	negative regulation of protein processing involved in protein targeting to mitochondrion	PMID:21370995^[19]	ECO:0000305	curator inference used in manual assertion	GO:0010955 GO:1903215	P		Seeded From UniProt	complete
involved_in	GO:1903215	negative regulation of protein targeting to mitochondrion	PMID:21370995^[19]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P12532)	Seeded From UniProt	complete
involved_in	GO:0010955	negative regulation of protein processing	PMID:21370995^[19]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P12532)	Seeded From UniProt	complete
involved_in	GO:0034613	cellular protein localization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	P	has_input:(UniProtKB:P05132) occurs_in:(GO:0030425)\|has_input(UniProtKB:P31324) occurs_in:(GO:0030425)	Seeded From UniProt	complete
involved_in	GO:0061001	regulation of dendritic spine morphogenesis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	P	occurs_in:(CL:0002613)	Seeded From UniProt	complete
involved_in	GO:0060159	regulation of dopamine receptor signaling pathway	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	P	occurs_in:(UBERON:0001890)	Seeded From UniProt	complete
involved_in	GO:0060079	excitatory postsynaptic potential	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	P	occurs_in:(CL:0002613)	Seeded From UniProt	complete
involved_in	GO:0051966	regulation of synaptic transmission, glutamatergic	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	P	occurs_in:(CL:0002613)	Seeded From UniProt	complete
involved_in	GO:0035556	intracellular signal transduction	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	P	occurs_in:(CL:0002609)	Seeded From UniProt	complete
involved_in	GO:0010738	regulation of protein kinase A signaling	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	P	occurs_in:(CL:0002609)	Seeded From UniProt	complete
involved_in	GO:0001933	negative regulation of protein phosphorylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	P	occurs_in:(UBERON:0001890)	Seeded From UniProt	complete
involved_in	GO:0031398	positive regulation of protein ubiquitination	PMID:20173330^[20]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:O60271)	Seeded From UniProt	complete
involved_in	GO:0034599	cellular response to oxidative stress	PMID:21362567^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006897	endocytosis	PMID:24576675^[22]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P34216 UniProtKB:P39013	P	part_of:(GO:0070301)	Seeded From UniProt	complete
involved_in	GO:0072593	reactive oxygen species metabolic process	PMID:24576675^[22]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006897	endocytosis	PMID:24576675^[22]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903206	negative regulation of hydrogen peroxide-induced cell death	PMID:24576675^[22]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:21850687^[23]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P30048)	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21850687^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0031410	cytoplasmic vesicle	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	C		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	C		Seeded From UniProt	complete
part_of	GO:0005768	endosome	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	C		Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	C		Seeded From UniProt	complete
part_of	GO:0005743	mitochondrial inner membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	C		Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	C		Seeded From UniProt	complete
part_of	GO:0030425	dendrite	PMID:17120249^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030424	axon	PMID:17120249^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043204	perikaryon	PMID:17120249^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1903125	negative regulation of thioredoxin peroxidase activity by peptidyl-threonine phosphorylation	PMID:21850687^[23]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:P30048)	Seeded From UniProt	complete
enables	GO:0036479	peroxidase inhibitor activity	PMID:21850687^[23]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P30048)	Seeded From UniProt	complete
involved_in	GO:2000300	regulation of synaptic vesicle exocytosis	PMID:23949442^[25]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0002608)	Seeded From UniProt	complete
involved_in	GO:1902803	regulation of synaptic vesicle transport	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	P	occurs_in:(GO:0043195) occurs_in:(CL:0002609)	Seeded From UniProt	complete
involved_in	GO:1902692	regulation of neuroblast proliferation	PMID:21168496^[26]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1901214	regulation of neuron death	PMID:24403142^[27]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051900	regulation of mitochondrial depolarization	PMID:22736029^[28]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051018	protein kinase A binding	PMID:24464040^[29]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P31324	F		Seeded From UniProt	complete
involved_in	GO:0032091	negative regulation of protein binding	PMID:23949442^[25]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(UniProtKB:P60879) has_input:(UniProtKB:Q9Z266) occurs_in:(UBERON:0000955)	Seeded From UniProt	complete
part_of	GO:0031966	mitochondrial membrane	PMID:22736029^[28]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0030276	clathrin binding	PMID:21307259^[30]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q68FD5	F	occurs_in:(UBERON:0000955)	Seeded From UniProt	complete
involved_in	GO:0018107	peptidyl-threonine phosphorylation	PMID:23949442^[25]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:O95295)	Seeded From UniProt	complete
enables	GO:0017075	syntaxin-1 binding	PMID:21307259^[30]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P61264	F	occurs_in:(UBERON:0000955)	Seeded From UniProt	complete
part_of	GO:0016234	inclusion body	PMID:24403142^[27]	ECO:0000315	mutant phenotype evidence used in manual assertion		C	exists_during:(GO:0007569)	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:24403142^[27]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:22736029^[28]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:23949442^[25]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:O95295)	Seeded From UniProt	complete
enables	GO:0003779	actin binding	PMID:21307259^[30]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P62737	F	occurs_in:(UBERON:0000955)	Seeded From UniProt	complete
enables	GO:0000149	SNARE binding	PMID:21307259^[30]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P46460	F	occurs_in:(UBERON:0000955)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[31]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:22664934^[32]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001827)	Seeded From UniProt	complete
involved_in	GO:2000172	regulation of branching morphogenesis of a nerve	PMID:21168496^[26]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070997	neuron death	PMID:19692353^[33]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0061001	regulation of dendritic spine morphogenesis	PMID:21168496^[26]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0060161	positive regulation of dopamine receptor signaling pathway	PMID:20659558^[34]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048312	intracellular distribution of mitochondria	PMID:21159966^[35]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0043025	neuronal cell body	PMID:21696411^[36]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043025	neuronal cell body	PMID:21048939^[37]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	PMID:21048939^[37]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0042391	regulation of membrane potential	PMID:21159966^[35]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0040012	regulation of locomotion	PMID:19692353^[33]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035640	exploration behavior	PMID:20659558^[34]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035564	regulation of kidney size	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	P		Seeded From UniProt	complete
enables	GO:0034211	GTP-dependent protein kinase activity	PMID:17260967^[38]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0032839	dendrite cytoplasm	PMID:21696411^[36]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	P		Seeded From UniProt	complete
involved_in	GO:0022028	tangential migration from the subventricular zone to the olfactory bulb	PMID:21168496^[26]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0021772	olfactory bulb development	PMID:21168496^[26]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0018107	peptidyl-threonine phosphorylation	PMID:21048939^[37]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	PMID:19576176^[39]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0017048	Rho GTPase binding	PMID:21048939^[37]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P60953	F		Seeded From UniProt	complete
enables	GO:0015631	tubulin binding	PMID:21159966^[35]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0014041	regulation of neuron maturation	PMID:21168496^[26]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010508	positive regulation of autophagy	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	P		Seeded From UniProt	complete
involved_in	GO:0008340	determination of adult lifespan	PMID:19692353^[33]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007528	neuromuscular junction development	PMID:21159966^[35]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006979	response to oxidative stress	PMID:19692353^[33]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046039	GTP metabolic process	PMID:21048939^[37]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:17260967^[38]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004708	MAP kinase kinase activity	PMID:19302196^[40]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:19576176^[39]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:21048939^[37]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	PMID:21048939^[37]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0001934	positive regulation of protein phosphorylation	PMID:20659558^[34]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000186	activation of MAPKK activity	PMID:19302196^[40]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090394	negative regulation of excitatory postsynaptic potential	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q5S006	P	occurs_in:(CL:0000598) occurs_in:(UBERON:0000956)	Seeded From UniProt	complete
involved_in	GO:0048812	neuron projection morphogenesis	PMID:17114044^[41]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:16980962^[42]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:17200152^[43]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:16269541^[44]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:17442267^[45]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:16321986^[46]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0044325	ion channel binding	PMID:22012985^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q8NHX9	F		Seeded From UniProt	complete
part_of	GO:0043204	perikaryon	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:F1LNJ1	C		Seeded From UniProt	complete
involved_in	GO:0043068	positive regulation of programmed cell death	PMID:17200152^[43]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:16321986^[46]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F		Seeded From UniProt	complete
enables	GO:0034211	GTP-dependent protein kinase activity	PMID:17200152^[43]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0032473	cytoplasmic side of mitochondrial outer membrane	PMID:16269541^[44]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0031398	positive regulation of protein ubiquitination	PMID:16352719^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030425	dendrite	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:F1LNJ1	C		Seeded From UniProt	complete
part_of	GO:0030424	axon	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:F1LNJ1	C		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	PMID:17114044^[41]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0010508	positive regulation of autophagy	PMID:22012985^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:21850687^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16352719^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16321986^[46]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:16980962^[42]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:17442267^[45]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005096	GTPase activator activity	PMID:17442267^[45]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:17200152^[43]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:21850687^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:16269541^[44]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:17442267^[45]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:16321986^[46]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000165	MAPK cascade	PMID:17200152^[43]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1905279	regulation of retrograde transport, endosome to Golgi	PMID:21873635^[47]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000585172 UniProtKB:Q5S007	P		Seeded From UniProt	complete
involved_in	GO:1902902	negative regulation of autophagosome assembly	PMID:21873635^[47]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000585172 UniProtKB:Q5S007	P		Seeded From UniProt	complete
involved_in	GO:1902803	regulation of synaptic vesicle transport	PMID:21873635^[47]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1913975 PANTHER:PTN000585172	P		Seeded From UniProt	complete
involved_in	GO:0061001	regulation of dendritic spine morphogenesis	PMID:21873635^[47]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1913975 PANTHER:PTN000585172 UniProtKB:Q5S007	P		Seeded From UniProt	complete
part_of	GO:0045121	membrane raft	PMID:21873635^[47]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1913975 PANTHER:PTN000585172	C		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	PMID:21873635^[47]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000585172 RGD:1561168 UniProtKB:Q5S007	C		Seeded From UniProt	complete
part_of	GO:0031966	mitochondrial membrane	PMID:21873635^[47]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000585172 UniProtKB:Q5S007	C		Seeded From UniProt	complete
involved_in	GO:0019722	calcium-mediated signaling	PMID:21873635^[47]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000585172 UniProtKB:Q5S007	P		Seeded From UniProt	complete
enables	GO:0017048	Rho GTPase binding	PMID:21873635^[47]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1913975 PANTHER:PTN000585172 UniProtKB:Q5S007	F		Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:21873635^[47]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000585172 UniProtKB:Q5S007	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:21873635^[47]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1913975 PANTHER:PTN000585172 UniProtKB:Q5S007	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[47]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000585172 UniProtKB:Q5S007	C		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	PMID:21873635^[47]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1913975 PANTHER:PTN000585172 UniProtKB:Q5S007	C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:21873635^[47]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1913975 PANTHER:PTN000585172 UniProtKB:Q5S007	C		Seeded From UniProt	complete
part_of	GO:0005768	endosome	PMID:21873635^[47]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1913975 PANTHER:PTN000585172	C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:21873635^[47]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1913975 PANTHER:PTN000585172	C		Seeded From UniProt	complete
involved_in	GO:0034260	negative regulation of GTPase activity	PMID:22423108^[48]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:22423108^[48]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:27357661^[49]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F	occurs_in:(GO:0005886)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:27013965^[50]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F	occurs_in:(GO:0005886)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:26824392^[51]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F	occurs_in:(GO:0005886)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24904275^[52]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F	occurs_in:(GO:0005886)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24591621^[53]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F	occurs_in:(GO:0005886)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24275654^[54]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F	occurs_in:(GO:0005886)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23241358^[55]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F	occurs_in:(GO:0005886)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23220480^[56]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F	occurs_in:(GO:0005886)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22952686^[57]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F	occurs_in:(GO:0005886)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22363216^[58]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F	occurs_in:(GO:0005886)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21073465^[59]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F	occurs_in:(GO:0005886)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20515039^[60]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F	occurs_in:(GO:0005886)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19733152^[61]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F	occurs_in:(GO:0005886)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19712061^[62]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F	occurs_in:(GO:0005886)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18397888^[63]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F	occurs_in:(GO:0005886)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18230735^[64]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F	occurs_in:(GO:0005886)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16321986^[46]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5S007	F	occurs_in:(GO:0005886)	Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0043547	positive regulation of GTPase activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0005096	P		Seeded From UniProt	complete
involved_in	GO:0043547	positive regulation of GTPase activity	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0005096	P		Seeded From UniProt	complete
part_of	GO:0098794	postsynapse	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0060079	C		Seeded From UniProt	complete
part_of	GO:0098794	postsynapse	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0060079	C		Seeded From UniProt	complete
involved_in	GO:1904469	positive regulation of tumor necrosis factor secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	P		Seeded From UniProt	complete
involved_in	GO:1903980	positive regulation of microglial cell activation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	P		Seeded From UniProt	complete
involved_in	GO:1900244	positive regulation of synaptic vesicle endocytosis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	P		Seeded From UniProt	complete
involved_in	GO:0140058	neuron projection arborization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	P		Seeded From UniProt	complete
involved_in	GO:0071407	cellular response to organic cyclic compound	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	P		Seeded From UniProt	complete
involved_in	GO:0051770	positive regulation of nitric-oxide synthase biosynthetic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	P		Seeded From UniProt	complete
part_of	GO:0045202	synapse	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	C		Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	C		Seeded From UniProt	complete
part_of	GO:0043204	perikaryon	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	C		Seeded From UniProt	complete
part_of	GO:0043025	neuronal cell body	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	C		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	C		Seeded From UniProt	complete
part_of	GO:0030425	dendrite	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	C		Seeded From UniProt	complete
part_of	GO:0030424	axon	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	C		Seeded From UniProt	complete
involved_in	GO:0021756	striatum development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	C		Seeded From UniProt	complete
involved_in	GO:0010977	negative regulation of neuron projection development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	P		Seeded From UniProt	complete
involved_in	GO:0007283	spermatogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1LNJ1 ensembl:ENSRNOP00000005438	C		Seeded From UniProt	complete
part_of	GO:1990909	Wnt signalosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	C		Seeded From UniProt	complete
part_of	GO:1990904	ribonucleoprotein complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	C		Seeded From UniProt	complete
enables	GO:1904713	beta-catenin destruction complex binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	F		Seeded From UniProt	complete
involved_in	GO:1902803	regulation of synaptic vesicle transport	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	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:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
involved_in	GO:1900242	regulation of synaptic vesicle endocytosis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
part_of	GO:0099523	presynaptic cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	C		Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	C		Seeded From UniProt	complete
involved_in	GO:0090394	negative regulation of excitatory postsynaptic potential	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
involved_in	GO:0070973	protein localization to endoplasmic reticulum exit site	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
part_of	GO:0070971	endoplasmic reticulum exit site	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	C		Seeded From UniProt	complete
involved_in	GO:0061001	regulation of dendritic spine morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
involved_in	GO:0060828	regulation of canonical Wnt signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
involved_in	GO:0060628	regulation of ER to Golgi vesicle-mediated transport	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
involved_in	GO:0060159	regulation of dopamine receptor signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
involved_in	GO:0060079	excitatory postsynaptic potential	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
involved_in	GO:0051966	regulation of synaptic transmission, glutamatergic	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
enables	GO:0051018	protein kinase A binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	F		Seeded From UniProt	complete
part_of	GO:0045202	synapse	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	C		Seeded From UniProt	complete
part_of	GO:0045121	membrane raft	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	F		Seeded From UniProt	complete
involved_in	GO:0035641	locomotory exploration behavior	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
involved_in	GO:0035564	regulation of kidney size	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	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:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
involved_in	GO:0034613	cellular protein localization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		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:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
part_of	GO:0031410	cytoplasmic vesicle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	C		Seeded From UniProt	complete
part_of	GO:0030425	dendrite	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	C		Seeded From UniProt	complete
enables	GO:0017048	Rho GTPase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	F		Seeded From UniProt	complete
involved_in	GO:0010738	regulation of protein kinase A signaling	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
involved_in	GO:0010508	positive regulation of autophagy	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
involved_in	GO:0010468	regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
part_of	GO:0008021	synaptic vesicle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	C		Seeded From UniProt	complete
involved_in	GO:0007030	Golgi organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
involved_in	GO:0007029	endoplasmic reticulum organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
involved_in	GO:0006606	protein import into nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	C		Seeded From UniProt	complete
part_of	GO:0005802	trans-Golgi network	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	C		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	C		Seeded From UniProt	complete
part_of	GO:0005768	endosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	C		Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	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:Q5S006 ensembl:ENSMUSP00000052584	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:Q5S006 ensembl:ENSMUSP00000052584	C		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:Q5S006 ensembl:ENSMUSP00000052584	F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	F		Seeded From UniProt	complete
involved_in	GO:0001933	negative regulation of protein phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q5S006 ensembl:ENSMUSP00000052584	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:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR017441	F		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005225	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
enables	GO:0005525	GTP binding	PMID:22899650^[9]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:22899650^[9]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	part_of:(GO:0090263)	Seeded From UniProt	complete
enables	GO:0008017	microtubule binding	PMID:24115276^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1904887	Wnt signalosome assembly	PMID:24115276^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0039706	co-receptor binding	PMID:24115276^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	has_direct_input:(UniProtKB:O75581) part_of:(GO:0060070) occurs_at:(GO:0016020)	Seeded From UniProt	complete
involved_in	GO:0060070	canonical Wnt signaling pathway	PMID:24115276^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0060828	regulation of canonical Wnt signaling pathway	PMID:22988876^[65]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090140	regulation of mitochondrial fission	PMID:24252804^[66]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070585	protein localization to mitochondrion	PMID:24252804^[66]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_input:(UniProtKB:O00429) causally_upstream_of:(GO:0090140)	Seeded From UniProt	complete
part_of	GO:0043195	terminal bouton	PMID:21563316^[67]	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^[67]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902823	negative regulation of late endosome to lysosome transport	PMID:23949442^[25]	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-8857583 Reactome:R-HSA-8857577 Reactome:R-HSA-8857565	ECO:0000304	author statement supported by traceable reference used in manual assertion		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:0030154	cell differentiation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0221	P		Seeded From UniProt	complete
part_of	GO:0031410	cytoplasmic vesicle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0968	C		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
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
part_of	GO:0005764	lysosome	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0458 UniProtKB-SubCell:SL-0158	C		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
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:0005096	GTPase activator activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0343	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
part_of	GO:0005768	endosome	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0967 UniProtKB-SubCell:SL-0101	C		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
enables	GO:0005525	GTP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0342	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472 UniProtKB-SubCell:SL-0162	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
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
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:0030054	cell junction	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0965	C		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:0045202	synapse	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0770	C		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:0005794	Golgi apparatus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0333 UniProtKB-SubCell:SL-0132	C		Seeded From UniProt	complete
part_of	GO:0042995	cell projection	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0966	C		Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0170	C		Seeded From UniProt	complete
part_of	GO:0030425	dendrite	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0283	C		Seeded From UniProt	complete
part_of	GO:0030672	synaptic vesicle membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0260	C		Seeded From UniProt	complete
part_of	GO:0030424	axon	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0279	C		Seeded From UniProt	complete
part_of	GO:0043204	perikaryon	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0197	C		Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 ^1.2 Cho, HJ et al. (2014) Leucine-rich repeat kinase 2 regulates Sec16A at ER exit sites to allow ER-Golgi export. EMBO J. 33 2314-31 PubMed GONUTS page
↑ ^2.0 ^2.1 Guerreiro, PS et al. (2016) LRRK2 Promotes Tau Accumulation, Aggregation and Release. Mol. Neurobiol. 53 3124-3135 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Chen, ZC et al. (2017) Phosphorylation of amyloid precursor protein by mutant LRRK2 promotes AICD activity and neurotoxicity in Parkinson's disease. Sci Signal 10 PubMed GONUTS page
↑ ^4.0 ^4.1 MacLeod, DA et al. (2013) RAB7L1 interacts with LRRK2 to modify intraneuronal protein sorting and Parkinson's disease risk. Neuron 77 425-39 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 Alegre-Abarrategui, J et al. (2009) LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular model. Hum. Mol. Genet. 18 4022-34 PubMed GONUTS page
↑ ^6.0 ^6.1 Chia, R et al. (2014) Phosphorylation of LRRK2 by casein kinase 1α regulates trans-Golgi clustering via differential interaction with ARHGEF7. Nat Commun 5 5827 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 Gómez-Suaga, P et al. (2012) Leucine-rich repeat kinase 2 regulates autophagy through a calcium-dependent pathway involving NAADP. Hum. Mol. Genet. 21 511-25 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Sancho, RM et al. (2009) Mutations in the LRRK2 Roc-COR tandem domain link Parkinson's disease to Wnt signalling pathways. Hum. Mol. Genet. 18 3955-68 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 ^9.4 ^9.5 ^9.6 ^9.7 Berwick, DC & Harvey, K (2012) LRRK2 functions as a Wnt signaling scaffold, bridging cytosolic proteins and membrane-localized LRP6. Hum. Mol. Genet. 21 4966-79 PubMed GONUTS page
↑ ^10.0 ^10.1 Manzoni, C et al. (2013) Pathogenic Parkinson's disease mutations across the functional domains of LRRK2 alter the autophagic/lysosomal response to starvation. Biochem. Biophys. Res. Commun. 441 862-6 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 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
↑ ^12.0 ^12.1 Hockey, LN et al. (2015) Dysregulation of lysosomal morphology by pathogenic LRRK2 is corrected by TPC2 inhibition. J. Cell. Sci. 128 232-8 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 Manzoni, C et al. (2013) Inhibition of LRRK2 kinase activity stimulates macroautophagy. Biochim. Biophys. Acta 1833 2900-2910 PubMed GONUTS page
↑ ^14.0 ^14.1 Beilina, A et al. (2014) Unbiased screen for interactors of leucine-rich repeat kinase 2 supports a common pathway for sporadic and familial Parkinson disease. Proc. Natl. Acad. Sci. U.S.A. 111 2626-31 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 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
↑ ^16.0 ^16.1 ^16.2 ^16.3 Yuan, Y et al. (2011) Dysregulated LRRK2 signaling in response to endoplasmic reticulum stress leads to dopaminergic neuron degeneration in C. elegans. PLoS ONE 6 e22354 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 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
↑ ^18.0 ^18.1 ^18.2 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
↑ ^19.0 ^19.1 ^19.2 ^19.3 ^19.4 Cui, J et al. (2011) Expression of leucine-rich repeat kinase 2 (LRRK2) inhibits the processing of uMtCK to induce cell death in a cell culture model system. Biosci. Rep. 31 429-37 PubMed GONUTS page
↑ Hsu, CH et al. (2010) LRRK2 and the stress response: interaction with MKKs and JNK-interacting proteins. Neurodegener Dis 7 68-75 PubMed GONUTS page
↑ Nguyen, HN et al. (2011) LRRK2 mutant iPSC-derived DA neurons demonstrate increased susceptibility to oxidative stress. Cell Stem Cell 8 267-80 PubMed GONUTS page
↑ ^22.0 ^22.1 ^22.2 ^22.3 Pereira, C et al. (2014) LRRK2, but not pathogenic mutants, protects against H2O2 stress depending on mitochondrial function and endocytosis in a yeast model. Biochim. Biophys. Acta 1840 2025-31 PubMed GONUTS page
↑ ^23.0 ^23.1 ^23.2 ^23.3 ^23.4 ^23.5 Angeles, DC et al. (2011) Mutations in LRRK2 increase phosphorylation of peroxiredoxin 3 exacerbating oxidative stress-induced neuronal death. Hum. Mutat. 32 1390-7 PubMed GONUTS page
↑ ^24.0 ^24.1 ^24.2 Biskup, S et al. (2006) Localization of LRRK2 to membranous and vesicular structures in mammalian brain. Ann. Neurol. 60 557-69 PubMed GONUTS page
↑ ^25.0 ^25.1 ^25.2 ^25.3 ^25.4 Yun, HJ et al. (2013) LRRK2 phosphorylates Snapin and inhibits interaction of Snapin with SNAP-25. Exp. Mol. Med. 45 e36 PubMed GONUTS page
↑ ^26.0 ^26.1 ^26.2 ^26.3 ^26.4 ^26.5 Winner, B et al. (2011) Adult neurogenesis and neurite outgrowth are impaired in LRRK2 G2019S mice. Neurobiol. Dis. 41 706-16 PubMed GONUTS page
↑ ^27.0 ^27.1 ^27.2 Skibinski, G et al. (2014) Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies. J. Neurosci. 34 418-33 PubMed GONUTS page
↑ ^28.0 ^28.1 ^28.2 Papkovskaia, TD et al. (2012) G2019S leucine-rich repeat kinase 2 causes uncoupling protein-mediated mitochondrial depolarization. Hum. Mol. Genet. 21 4201-13 PubMed GONUTS page
↑ Parisiadou, L et al. (2014) LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activity. Nat. Neurosci. 17 367-76 PubMed GONUTS page
↑ ^30.0 ^30.1 ^30.2 ^30.3 Piccoli, G et al. (2011) LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool. J. Neurosci. 31 2225-37 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ Böhm, D et al. (2012) Comparison of tear protein levels in breast cancer patients and healthy controls using a de novo proteomic approach. Oncol. Rep. 28 429-38 PubMed GONUTS page
↑ ^33.0 ^33.1 ^33.2 ^33.3 Venderova, K et al. (2009) Leucine-Rich Repeat Kinase 2 interacts with Parkin, DJ-1 and PINK-1 in a Drosophila melanogaster model of Parkinson's disease. Hum. Mol. Genet. 18 4390-404 PubMed GONUTS page
↑ ^34.0 ^34.1 ^34.2 Melrose, HL et al. (2010) Impaired dopaminergic neurotransmission and microtubule-associated protein tau alterations in human LRRK2 transgenic mice. Neurobiol. Dis. 40 503-17 PubMed GONUTS page
↑ ^35.0 ^35.1 ^35.2 ^35.3 Lee, S et al. (2010) LRRK2 kinase regulates synaptic morphology through distinct substrates at the presynaptic and postsynaptic compartments of the Drosophila neuromuscular junction. J. Neurosci. 30 16959-69 PubMed GONUTS page
↑ ^36.0 ^36.1 Sharma, S et al. (2011) LRRK2 expression in idiopathic and G2019S positive Parkinson's disease subjects: a morphological and quantitative study. Neuropathol. Appl. Neurobiol. 37 777-90 PubMed GONUTS page
↑ ^37.0 ^37.1 ^37.2 ^37.3 ^37.4 ^37.5 ^37.6 Haebig, K et al. (2010) ARHGEF7 (Beta-PIX) acts as guanine nucleotide exchange factor for leucine-rich repeat kinase 2. PLoS ONE 5 e13762 PubMed GONUTS page
↑ ^38.0 ^38.1 Ito, G et al. (2007) GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease. Biochemistry 46 1380-8 PubMed GONUTS page
↑ ^39.0 ^39.1 Qing, H et al. (2009) Lrrk2 phosphorylates alpha synuclein at serine 129: Parkinson disease implications. Biochem. Biophys. Res. Commun. 387 149-52 PubMed GONUTS page
↑ ^40.0 ^40.1 Gloeckner, CJ et al. (2009) The Parkinson disease-associated protein kinase LRRK2 exhibits MAPKKK activity and phosphorylates MKK3/6 and MKK4/7, in vitro. J. Neurochem. 109 959-68 PubMed GONUTS page
↑ ^41.0 ^41.1 MacLeod, D et al. (2006) The familial Parkinsonism gene LRRK2 regulates neurite process morphology. Neuron 52 587-93 PubMed GONUTS page
↑ ^42.0 ^42.1 Smith, WW et al. (2006) Kinase activity of mutant LRRK2 mediates neuronal toxicity. Nat. Neurosci. 9 1231-3 PubMed GONUTS page
↑ ^43.0 ^43.1 ^43.2 ^43.3 ^43.4 West, AB et al. (2007) Parkinson's disease-associated mutations in LRRK2 link enhanced GTP-binding and kinase activities to neuronal toxicity. Hum. Mol. Genet. 16 223-32 PubMed GONUTS page
↑ ^44.0 ^44.1 ^44.2 West, AB et al. (2005) Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity. Proc. Natl. Acad. Sci. U.S.A. 102 16842-7 PubMed GONUTS page
↑ ^45.0 ^45.1 ^45.2 ^45.3 Lewis, PA et al. (2007) The R1441C mutation of LRRK2 disrupts GTP hydrolysis. Biochem. Biophys. Res. Commun. 357 668-71 PubMed GONUTS page
↑ ^46.0 ^46.1 ^46.2 ^46.3 ^46.4 Gloeckner, CJ et al. (2006) The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity. Hum. Mol. Genet. 15 223-32 PubMed GONUTS page
↑ ^47.00 ^47.01 ^47.02 ^47.03 ^47.04 ^47.05 ^47.06 ^47.07 ^47.08 ^47.09 ^47.10 ^47.11 ^47.12 ^47.13 ^47.14 ^47.15 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^48.0 ^48.1 Xiong, Y et al. (2012) ArfGAP1 is a GTPase activating protein for LRRK2: reciprocal regulation of ArfGAP1 by LRRK2. J. Neurosci. 32 3877-86 PubMed GONUTS page
↑ Guaitoli, G et al. (2016) Structural model of the dimeric Parkinson's protein LRRK2 reveals a compact architecture involving distant interdomain contacts. Proc. Natl. Acad. Sci. U.S.A. 113 E4357-66 PubMed GONUTS page
↑ Nixon-Abell, J et al. (2016) Protective LRRK2 R1398H Variant Enhances GTPase and Wnt Signaling Activity. Front Mol Neurosci 9 18 PubMed GONUTS page
↑ Steger, M et al. (2016) Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases. Elife 5 PubMed GONUTS page
↑ Cirnaru, MD et al. (2014) LRRK2 kinase activity regulates synaptic vesicle trafficking and neurotransmitter release through modulation of LRRK2 macro-molecular complex. Front Mol Neurosci 7 49 PubMed GONUTS page
↑ Liao, J et al. (2014) Parkinson disease-associated mutation R1441H in LRRK2 prolongs the "active state" of its GTPase domain. Proc. Natl. Acad. Sci. U.S.A. 111 4055-60 PubMed GONUTS page
↑ Law, BM et al. (2014) A direct interaction between leucine-rich repeat kinase 2 and specific β-tubulin isoforms regulates tubulin acetylation. J. Biol. Chem. 289 895-908 PubMed GONUTS page
↑ Biosa, A et al. (2013) GTPase activity regulates kinase activity and cellular phenotypes of Parkinson's disease-associated LRRK2. Hum. Mol. Genet. 22 1140-56 PubMed GONUTS page
↑ Ohta, E et al. (2013) Dominant-negative effects of LRRK2 heterodimers: a possible mechanism of neurodegeneration in Parkinson's disease caused by LRRK2 I2020T mutation. Biochem. Biophys. Res. Commun. 430 560-6 PubMed GONUTS page
↑ Civiero, L et al. (2012) Biochemical characterization of highly purified leucine-rich repeat kinases 1 and 2 demonstrates formation of homodimers. PLoS ONE 7 e43472 PubMed GONUTS page
↑ Stafa, K et al. (2012) GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1. PLoS Genet. 8 e1002526 PubMed GONUTS page
↑ Daniëls, V et al. (2011) Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant. J. Neurochem. 116 304-15 PubMed GONUTS page
↑ Berger, Z et al. (2010) Membrane localization of LRRK2 is associated with increased formation of the highly active LRRK2 dimer and changes in its phosphorylation. Biochemistry 49 5511-23 PubMed GONUTS page
↑ Greggio, E et al. (2009) The Parkinson's disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sites. Biochem. Biophys. Res. Commun. 389 449-54 PubMed GONUTS page
↑ Klein, CL et al. (2009) Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment. J. Neurochem. 111 703-15 PubMed GONUTS page
↑ Greggio, E et al. (2008) The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation. J. Biol. Chem. 283 16906-14 PubMed GONUTS page
↑ Deng, J et al. (2008) Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPase. Proc. Natl. Acad. Sci. U.S.A. 105 1499-504 PubMed GONUTS page
↑ 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
↑ ^66.0 ^66.1 Dias, V et al. (2013) The role of oxidative stress in Parkinson's disease. J Parkinsons Dis 3 461-91 PubMed GONUTS page
↑ ^67.0 ^67.1 Esposito, G et al. (2012) Synaptic vesicle trafficking and Parkinson's disease. Dev Neurobiol 72 134-44 PubMed GONUTS page

[PMID:25201882-1] 1.0 ^1.1 ^1.2 Cho, HJ et al. (2014) Leucine-rich repeat kinase 2 regulates Sec16A at ER exit sites to allow ER-Golgi export. EMBO J. 33 2314-31 PubMed GONUTS page

[PMID:26014385-2] 2.0 ^2.1 Guerreiro, PS et al. (2016) LRRK2 Promotes Tau Accumulation, Aggregation and Release. Mol. Neurobiol. 53 3124-3135 PubMed GONUTS page

[PMID:28720718-3] 3.0 ^3.1 ^3.2 Chen, ZC et al. (2017) Phosphorylation of amyloid precursor protein by mutant LRRK2 promotes AICD activity and neurotoxicity in Parkinson's disease. Sci Signal 10 PubMed GONUTS page

[PMID:23395371-4] 4.0 ^4.1 MacLeod, DA et al. (2013) RAB7L1 interacts with LRRK2 to modify intraneuronal protein sorting and Parkinson's disease risk. Neuron 77 425-39 PubMed GONUTS page

[PMID:19640926-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 Alegre-Abarrategui, J et al. (2009) LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular model. Hum. Mol. Genet. 18 4022-34 PubMed GONUTS page

[PMID:25500533-6] 6.0 ^6.1 Chia, R et al. (2014) Phosphorylation of LRRK2 by casein kinase 1α regulates trans-Golgi clustering via differential interaction with ARHGEF7. Nat Commun 5 5827 PubMed GONUTS page

[PMID:22012985-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 Gómez-Suaga, P et al. (2012) Leucine-rich repeat kinase 2 regulates autophagy through a calcium-dependent pathway involving NAADP. Hum. Mol. Genet. 21 511-25 PubMed GONUTS page

[PMID:19625296-8] 8.0 ^8.1 ^8.2 Sancho, RM et al. (2009) Mutations in the LRRK2 Roc-COR tandem domain link Parkinson's disease to Wnt signalling pathways. Hum. Mol. Genet. 18 3955-68 PubMed GONUTS page

[PMID:22899650-9] 9.0 ^9.1 ^9.2 ^9.3 ^9.4 ^9.5 ^9.6 ^9.7 Berwick, DC & Harvey, K (2012) LRRK2 functions as a Wnt signaling scaffold, bridging cytosolic proteins and membrane-localized LRP6. Hum. Mol. Genet. 21 4966-79 PubMed GONUTS page

[PMID:24211199-10] 10.0 ^10.1 Manzoni, C et al. (2013) Pathogenic Parkinson's disease mutations across the functional domains of LRRK2 alter the autophagic/lysosomal response to starvation. Biochem. Biophys. Res. Commun. 441 862-6 PubMed GONUTS page

[PMID:24115276-11] 11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 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:25416817-12] 12.0 ^12.1 Hockey, LN et al. (2015) Dysregulation of lysosomal morphology by pathogenic LRRK2 is corrected by TPC2 inhibition. J. Cell. Sci. 128 232-8 PubMed GONUTS page

[PMID:23916833-13] 13.0 ^13.1 ^13.2 Manzoni, C et al. (2013) Inhibition of LRRK2 kinase activity stimulates macroautophagy. Biochim. Biophys. Acta 1833 2900-2910 PubMed GONUTS page

[PMID:24510904-14] 14.0 ^14.1 Beilina, A et al. (2014) Unbiased screen for interactors of leucine-rich repeat kinase 2 supports a common pathway for sporadic and familial Parkinson disease. Proc. Natl. Acad. Sci. U.S.A. 111 2626-31 PubMed GONUTS page

[PMID:22764206-15] 15.0 ^15.1 ^15.2 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:21857923-16] 16.0 ^16.1 ^16.2 ^16.3 Yuan, Y et al. (2011) Dysregulated LRRK2 signaling in response to endoplasmic reticulum stress leads to dopaminergic neuron degeneration in C. elegans. PLoS ONE 6 e22354 PubMed GONUTS page

[PMID:23628791-17] 17.0 ^17.1 ^17.2 ^17.3 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:16352719-18] 18.0 ^18.1 ^18.2 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:21370995-19] 19.0 ^19.1 ^19.2 ^19.3 ^19.4 Cui, J et al. (2011) Expression of leucine-rich repeat kinase 2 (LRRK2) inhibits the processing of uMtCK to induce cell death in a cell culture model system. Biosci. Rep. 31 429-37 PubMed GONUTS page

[PMID:20173330-20] Hsu, CH et al. (2010) LRRK2 and the stress response: interaction with MKKs and JNK-interacting proteins. Neurodegener Dis 7 68-75 PubMed GONUTS page

[PMID:21362567-21] Nguyen, HN et al. (2011) LRRK2 mutant iPSC-derived DA neurons demonstrate increased susceptibility to oxidative stress. Cell Stem Cell 8 267-80 PubMed GONUTS page

[PMID:24576675-22] 22.0 ^22.1 ^22.2 ^22.3 Pereira, C et al. (2014) LRRK2, but not pathogenic mutants, protects against H2O2 stress depending on mitochondrial function and endocytosis in a yeast model. Biochim. Biophys. Acta 1840 2025-31 PubMed GONUTS page

[PMID:21850687-23] 23.0 ^23.1 ^23.2 ^23.3 ^23.4 ^23.5 Angeles, DC et al. (2011) Mutations in LRRK2 increase phosphorylation of peroxiredoxin 3 exacerbating oxidative stress-induced neuronal death. Hum. Mutat. 32 1390-7 PubMed GONUTS page

[PMID:17120249-24] 24.0 ^24.1 ^24.2 Biskup, S et al. (2006) Localization of LRRK2 to membranous and vesicular structures in mammalian brain. Ann. Neurol. 60 557-69 PubMed GONUTS page

[PMID:23949442-25] 25.0 ^25.1 ^25.2 ^25.3 ^25.4 Yun, HJ et al. (2013) LRRK2 phosphorylates Snapin and inhibits interaction of Snapin with SNAP-25. Exp. Mol. Med. 45 e36 PubMed GONUTS page

[PMID:21168496-26] 26.0 ^26.1 ^26.2 ^26.3 ^26.4 ^26.5 Winner, B et al. (2011) Adult neurogenesis and neurite outgrowth are impaired in LRRK2 G2019S mice. Neurobiol. Dis. 41 706-16 PubMed GONUTS page

[PMID:24403142-27] 27.0 ^27.1 ^27.2 Skibinski, G et al. (2014) Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies. J. Neurosci. 34 418-33 PubMed GONUTS page

[PMID:22736029-28] 28.0 ^28.1 ^28.2 Papkovskaia, TD et al. (2012) G2019S leucine-rich repeat kinase 2 causes uncoupling protein-mediated mitochondrial depolarization. Hum. Mol. Genet. 21 4201-13 PubMed GONUTS page

[PMID:24464040-29] Parisiadou, L et al. (2014) LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activity. Nat. Neurosci. 17 367-76 PubMed GONUTS page

[PMID:21307259-30] 30.0 ^30.1 ^30.2 ^30.3 Piccoli, G et al. (2011) LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool. J. Neurosci. 31 2225-37 PubMed GONUTS page

[PMID:19056867-31] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:22664934-32] Böhm, D et al. (2012) Comparison of tear protein levels in breast cancer patients and healthy controls using a de novo proteomic approach. Oncol. Rep. 28 429-38 PubMed GONUTS page

[PMID:19692353-33] 33.0 ^33.1 ^33.2 ^33.3 Venderova, K et al. (2009) Leucine-Rich Repeat Kinase 2 interacts with Parkin, DJ-1 and PINK-1 in a Drosophila melanogaster model of Parkinson's disease. Hum. Mol. Genet. 18 4390-404 PubMed GONUTS page

[PMID:20659558-34] 34.0 ^34.1 ^34.2 Melrose, HL et al. (2010) Impaired dopaminergic neurotransmission and microtubule-associated protein tau alterations in human LRRK2 transgenic mice. Neurobiol. Dis. 40 503-17 PubMed GONUTS page

[PMID:21159966-35] 35.0 ^35.1 ^35.2 ^35.3 Lee, S et al. (2010) LRRK2 kinase regulates synaptic morphology through distinct substrates at the presynaptic and postsynaptic compartments of the Drosophila neuromuscular junction. J. Neurosci. 30 16959-69 PubMed GONUTS page

[PMID:21696411-36] 36.0 ^36.1 Sharma, S et al. (2011) LRRK2 expression in idiopathic and G2019S positive Parkinson's disease subjects: a morphological and quantitative study. Neuropathol. Appl. Neurobiol. 37 777-90 PubMed GONUTS page

[PMID:21048939-37] 37.0 ^37.1 ^37.2 ^37.3 ^37.4 ^37.5 ^37.6 Haebig, K et al. (2010) ARHGEF7 (Beta-PIX) acts as guanine nucleotide exchange factor for leucine-rich repeat kinase 2. PLoS ONE 5 e13762 PubMed GONUTS page

[PMID:17260967-38] 38.0 ^38.1 Ito, G et al. (2007) GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease. Biochemistry 46 1380-8 PubMed GONUTS page

[PMID:19576176-39] 39.0 ^39.1 Qing, H et al. (2009) Lrrk2 phosphorylates alpha synuclein at serine 129: Parkinson disease implications. Biochem. Biophys. Res. Commun. 387 149-52 PubMed GONUTS page

[PMID:19302196-40] 40.0 ^40.1 Gloeckner, CJ et al. (2009) The Parkinson disease-associated protein kinase LRRK2 exhibits MAPKKK activity and phosphorylates MKK3/6 and MKK4/7, in vitro. J. Neurochem. 109 959-68 PubMed GONUTS page

[PMID:17114044-41] 41.0 ^41.1 MacLeod, D et al. (2006) The familial Parkinsonism gene LRRK2 regulates neurite process morphology. Neuron 52 587-93 PubMed GONUTS page

[PMID:16980962-42] 42.0 ^42.1 Smith, WW et al. (2006) Kinase activity of mutant LRRK2 mediates neuronal toxicity. Nat. Neurosci. 9 1231-3 PubMed GONUTS page

[PMID:17200152-43] 43.0 ^43.1 ^43.2 ^43.3 ^43.4 West, AB et al. (2007) Parkinson's disease-associated mutations in LRRK2 link enhanced GTP-binding and kinase activities to neuronal toxicity. Hum. Mol. Genet. 16 223-32 PubMed GONUTS page

[PMID:16269541-44] 44.0 ^44.1 ^44.2 West, AB et al. (2005) Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity. Proc. Natl. Acad. Sci. U.S.A. 102 16842-7 PubMed GONUTS page

[PMID:17442267-45] 45.0 ^45.1 ^45.2 ^45.3 Lewis, PA et al. (2007) The R1441C mutation of LRRK2 disrupts GTP hydrolysis. Biochem. Biophys. Res. Commun. 357 668-71 PubMed GONUTS page

[PMID:16321986-46] 46.0 ^46.1 ^46.2 ^46.3 ^46.4 Gloeckner, CJ et al. (2006) The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity. Hum. Mol. Genet. 15 223-32 PubMed GONUTS page

[PMID:21873635-47] 47.00 ^47.01 ^47.02 ^47.03 ^47.04 ^47.05 ^47.06 ^47.07 ^47.08 ^47.09 ^47.10 ^47.11 ^47.12 ^47.13 ^47.14 ^47.15 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:22423108-48] 48.0 ^48.1 Xiong, Y et al. (2012) ArfGAP1 is a GTPase activating protein for LRRK2: reciprocal regulation of ArfGAP1 by LRRK2. J. Neurosci. 32 3877-86 PubMed GONUTS page

[PMID:27357661-49] Guaitoli, G et al. (2016) Structural model of the dimeric Parkinson's protein LRRK2 reveals a compact architecture involving distant interdomain contacts. Proc. Natl. Acad. Sci. U.S.A. 113 E4357-66 PubMed GONUTS page

[PMID:27013965-50] Nixon-Abell, J et al. (2016) Protective LRRK2 R1398H Variant Enhances GTPase and Wnt Signaling Activity. Front Mol Neurosci 9 18 PubMed GONUTS page

[PMID:26824392-51] Steger, M et al. (2016) Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases. Elife 5 PubMed GONUTS page

[PMID:24904275-52] Cirnaru, MD et al. (2014) LRRK2 kinase activity regulates synaptic vesicle trafficking and neurotransmitter release through modulation of LRRK2 macro-molecular complex. Front Mol Neurosci 7 49 PubMed GONUTS page

[PMID:24591621-53] Liao, J et al. (2014) Parkinson disease-associated mutation R1441H in LRRK2 prolongs the "active state" of its GTPase domain. Proc. Natl. Acad. Sci. U.S.A. 111 4055-60 PubMed GONUTS page

[PMID:24275654-54] Law, BM et al. (2014) A direct interaction between leucine-rich repeat kinase 2 and specific β-tubulin isoforms regulates tubulin acetylation. J. Biol. Chem. 289 895-908 PubMed GONUTS page

[PMID:23241358-55] Biosa, A et al. (2013) GTPase activity regulates kinase activity and cellular phenotypes of Parkinson's disease-associated LRRK2. Hum. Mol. Genet. 22 1140-56 PubMed GONUTS page

[PMID:23220480-56] Ohta, E et al. (2013) Dominant-negative effects of LRRK2 heterodimers: a possible mechanism of neurodegeneration in Parkinson's disease caused by LRRK2 I2020T mutation. Biochem. Biophys. Res. Commun. 430 560-6 PubMed GONUTS page

[PMID:22952686-57] Civiero, L et al. (2012) Biochemical characterization of highly purified leucine-rich repeat kinases 1 and 2 demonstrates formation of homodimers. PLoS ONE 7 e43472 PubMed GONUTS page

[PMID:22363216-58] Stafa, K et al. (2012) GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1. PLoS Genet. 8 e1002526 PubMed GONUTS page

[PMID:21073465-59] Daniëls, V et al. (2011) Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant. J. Neurochem. 116 304-15 PubMed GONUTS page

[PMID:20515039-60] Berger, Z et al. (2010) Membrane localization of LRRK2 is associated with increased formation of the highly active LRRK2 dimer and changes in its phosphorylation. Biochemistry 49 5511-23 PubMed GONUTS page

[PMID:19733152-61] Greggio, E et al. (2009) The Parkinson's disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sites. Biochem. Biophys. Res. Commun. 389 449-54 PubMed GONUTS page

[PMID:19712061-62] Klein, CL et al. (2009) Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment. J. Neurochem. 111 703-15 PubMed GONUTS page

[PMID:18397888-63] Greggio, E et al. (2008) The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation. J. Biol. Chem. 283 16906-14 PubMed GONUTS page

[PMID:18230735-64] Deng, J et al. (2008) Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPase. Proc. Natl. Acad. Sci. U.S.A. 105 1499-504 PubMed GONUTS page

[PMID:22988876-65] 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:24252804-66] 66.0 ^66.1 Dias, V et al. (2013) The role of oxidative stress in Parkinson's disease. J Parkinsons Dis 3 461-91 PubMed GONUTS page

[PMID:21563316-67] 67.0 ^67.1 Esposito, G et al. (2012) Synaptic vesicle trafficking and Parkinson's disease. Dev Neurobiol 72 134-44 PubMed GONUTS page

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