HUMAN:AT132

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	ATP13A2 (synonyms: PARK9)
Protein Name(s)	Probable cation-transporting ATPase 13A2
External Links
UniProt	Q9NQ11
EMBL	AL354615 AY461712 AK290210 AL049569 CH471134 CH471134 BC030267 AL833966 AJ009947
CCDS	CCDS175.1 CCDS44072.1 CCDS44073.1
RefSeq	NP_001135445.1 NP_001135446.1 NP_071372.1
UniGene	Hs.128866
ProteinModelPortal	Q9NQ11
SMR	Q9NQ11
BioGrid	116973
IntAct	Q9NQ11
MINT	MINT-4781194
STRING	9606.ENSP00000327214
TCDB	3.A.3.10.7
PhosphoSite	Q9NQ11
DMDM	14285364
MaxQB	Q9NQ11
PaxDb	Q9NQ11
PRIDE	Q9NQ11
Ensembl	ENST00000326735 ENST00000341676 ENST00000452699
GeneID	23400
KEGG	hsa:23400
UCSC	uc001baa.2 uc001bab.2 uc001bac.2
CTD	23400
GeneCards	GC01M017312
GeneReviews	ATP13A2
HGNC	HGNC:30213
HPA	CAB037111
MIM	606693 610513
neXtProt	NX_Q9NQ11
Orphanet	306674 314632
PharmGKB	PA134897221
eggNOG	COG0474
GeneTree	ENSGT00530000063001
HOGENOM	HOG000171813
HOVERGEN	HBG065757
InParanoid	Q9NQ11
KO	K13526
OMA	WQLFTVQ
OrthoDB	EOG7B5WV2
PhylomeDB	Q9NQ11
TreeFam	TF300331
ChiTaRS	ATP13A2
GeneWiki	ATP13A2
GenomeRNAi	23400
NextBio	45553
PRO	PR:Q9NQ11
Proteomes	UP000005640
Bgee	Q9NQ11
CleanEx	HS_ATP13A2
ExpressionAtlas	Q9NQ11
Genevestigator	Q9NQ11
GO	GO:0016021 GO:0005765 GO:0005764 GO:0005524 GO:0016887 GO:0019829 GO:0046872 GO:0006200 GO:0071287
Gene3D	2.70.150.10 3.40.1110.10 3.40.50.1000
InterPro	IPR004014 IPR023299 IPR018303 IPR008250 IPR023214 IPR006544 IPR001757
Pfam	PF00122 PF12409
PRINTS	PR00119
SMART	SM00831
SUPFAM	SSF56784 SSF81660
TIGRFAMs	TIGR01494 TIGR01657
PROSITE	PS00154

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:0033157	regulation of intracellular protein transport	PMID:24334770^[1]	ECO:0000303	author statement without traceable support used in manual assertion		P	has_regulation_target:(UniProtKB:P04062)	Seeded From UniProt	complete
involved_in	GO:1905165	regulation of lysosomal protein catabolic process	PMID:24334770^[1]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q9CTG6	P		Seeded From UniProt	complete
involved_in	GO:0034599	cellular response to oxidative stress	PMID:26134396^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1990938	peptidyl-aspartic acid autophosphorylation	PMID:26134396^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0080025	phosphatidylinositol-3,5-bisphosphate binding	PMID:26134396^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0070300	phosphatidic acid binding	PMID:26134396^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:1905103	integral component of lysosomal membrane	PMID:26134396^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1903543	positive regulation of exosomal secretion	PMID:24603074^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	transports_or_maintains_localization_of:(UniProtKB:P37840)	Seeded From UniProt	complete
part_of	GO:0032585	multivesicular body membrane	PMID:24603074^[3]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005771	multivesicular body	PMID:24603074^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540)	Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:24603074^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540)	Seeded From UniProt	complete
part_of	GO:0031982	vesicle	PMID:24603074^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540)	Seeded From UniProt	complete
part_of	GO:0005776	autophagosome	PMID:24603074^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540)	Seeded From UniProt	complete
involved_in	GO:0006882	cellular zinc ion homeostasis	PMID:24603074^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000540)	Seeded From UniProt	complete
involved_in	GO:0055069	zinc ion homeostasis	PMID:24334770^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071287	cellular response to manganese ion	PMID:22285144^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902047	polyamine transmembrane transport	PMID:23205587^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:16964263^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	PMID:16964263^[6]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0010821	regulation of mitochondrion organization	PMID:22186024^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(CL:0002609)	Seeded From UniProt	complete
involved_in	GO:0006874	cellular calcium ion homeostasis	PMID:22186024^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(CL:0002609)	Seeded From UniProt	complete
involved_in	GO:1905037	autophagosome organization	PMID:22186024^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(CL:0002609)	Seeded From UniProt	complete
involved_in	GO:0016243	regulation of autophagosome size	PMID:22186024^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(CL:0002609)	Seeded From UniProt	complete
part_of	GO:0030133	transport vesicle	PMID:22186024^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002609)	Seeded From UniProt	complete
part_of	GO:0043025	neuronal cell body	PMID:22186024^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002609)	Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	PMID:22186024^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002609)	Seeded From UniProt	complete
involved_in	GO:0006879	cellular iron ion homeostasis	PMID:26818499^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000700)	Seeded From UniProt	complete
enables	GO:0030145	manganese ion binding	PMID:22361905^[9]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q12697	F		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:22361905^[9]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q12697	F		Seeded From UniProt	complete
enables	GO:1903135	cupric ion binding	PMID:23202360^[10]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q12697	F		Seeded From UniProt	complete
enables	GO:0030145	manganese ion binding	PMID:23202360^[10]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q12697	F		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:23202360^[10]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q12697	F		Seeded From UniProt	complete
involved_in	GO:0050714	positive regulation of protein secretion	PMID:25392495^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P37840)	Seeded From UniProt	complete
involved_in	GO:1903543	positive regulation of exosomal secretion	PMID:25392495^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005770	late endosome	PMID:25392495^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:25392495^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005771	multivesicular body	PMID:25392495^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1901215	negative regulation of neuron death	PMID:23499937^[12]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:H2L3J0	P	regulates_o_occurs_in:(CL:0000700)\|regulates_o_occurs_in:(CL:0008025)	Seeded From UniProt	complete
involved_in	GO:1905165	regulation of lysosomal protein catabolic process	PMID:23499937^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0052548	regulation of endopeptidase activity	PMID:23499937^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P07339) part_of:(GO:1905165)	Seeded From UniProt	complete
part_of	GO:0005765	lysosomal membrane	PMID:23499937^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0016241	regulation of macroautophagy	PMID:22198378^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010821	regulation of mitochondrion organization	PMID:22198378^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:24252804^[14]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0097734	extracellular exosome biogenesis	PMID:25392495^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005765	lysosomal membrane	PMID:17897319^[15]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:21542062^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0099132	ATP hydrolysis coupled cation transmembrane transport	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0019829	P		Seeded From UniProt	complete
involved_in	GO:0016243	regulation of autophagosome size	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAA4 ensembl:ENSRNOP00000010884	P		Seeded From UniProt	complete
involved_in	GO:0010821	regulation of mitochondrion organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:F1MAA4 ensembl:ENSRNOP00000010884	P		Seeded From UniProt	complete
involved_in	GO:1905165	regulation of lysosomal protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9CTG6 ensembl:ENSMUSP00000039648	P		Seeded From UniProt	complete
involved_in	GO:1905123	regulation of glucosylceramidase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9CTG6 ensembl:ENSMUSP00000039648	P		Seeded From UniProt	complete
involved_in	GO:1903543	positive regulation of exosomal secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9CTG6 ensembl:ENSMUSP00000039648	P		Seeded From UniProt	complete
involved_in	GO:0055069	zinc ion homeostasis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9CTG6 ensembl:ENSMUSP00000039648	P		Seeded From UniProt	complete
part_of	GO:0043025	neuronal cell body	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9CTG6 ensembl:ENSMUSP00000039648	C		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9CTG6 ensembl:ENSMUSP00000039648	C		Seeded From UniProt	complete
involved_in	GO:0034599	cellular response to oxidative stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9CTG6 ensembl:ENSMUSP00000039648	P		Seeded From UniProt	complete
part_of	GO:0012506	vesicle membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9CTG6 ensembl:ENSMUSP00000039648	C		Seeded From UniProt	complete
involved_in	GO:0010821	regulation of mitochondrion organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9CTG6 ensembl:ENSMUSP00000039648	P		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR023299	F		Seeded From UniProt	complete
involved_in	GO:0006812	cation transport	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006544	P		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001757 InterPro:IPR006544	C		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006544	F		Seeded From UniProt	complete
involved_in	GO:0016241	regulation of macroautophagy	PMID:22885599^[17]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071294	cellular response to zinc ion	PMID:26392192^[18]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:26392192^[18]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034599	cellular response to oxidative stress	PMID:26392192^[18]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071287	cellular response to manganese ion	PMID:26392192^[18] PMID:23628791^[19]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005771	multivesicular body	PMID:25548531^[20]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030003	cellular cation homeostasis	PMID:25548531^[20]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005765	lysosomal membrane	PMID:25548531^[20]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1903146	regulation of autophagy of mitochondrion	PMID:25548531^[20]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1904714	regulation of chaperone-mediated autophagy	PMID:22885599^[17]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1901215	negative regulation of neuron death	PMID:22885599^[17]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	regulates_o_occurs_in:(CL:2000097)	Seeded From UniProt	complete
involved_in	GO:1905166	negative regulation of lysosomal protein catabolic process	PMID:22885599^[17]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0043202	lysosomal lumen	Reactome:R-HSA-5692480	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0034220	ion transmembrane transport	Reactome:R-HSA-936837	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019829	cation-transporting ATPase activity	Reactome:R-HSA-5692480	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
part_of	GO: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: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:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
part_of	GO:0005765	lysosomal membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0157	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 Tsunemi, T & Krainc, D (2014) Zn²⁺ dyshomeostasis caused by loss of ATP13A2/PARK9 leads to lysosomal dysfunction and alpha-synuclein accumulation. Hum. Mol. Genet. 23 2791-801 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 Holemans, T et al. (2015) A lipid switch unlocks Parkinson's disease-associated ATP13A2. Proc. Natl. Acad. Sci. U.S.A. 112 9040-5 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 Kong, SM et al. (2014) Parkinson's disease-linked human PARK9/ATP13A2 maintains zinc homeostasis and promotes α-Synuclein externalization via exosomes. Hum. Mol. Genet. 23 2816-33 PubMed GONUTS page
↑ Rentschler, G et al. (2012) ATP13A2 (PARK9) polymorphisms influence the neurotoxic effects of manganese. Neurotoxicology 33 697-702 PubMed GONUTS page
↑ De La Hera, DP et al. (2013) Parkinson's disease-associated human P5B-ATPase ATP13A2 increases spermidine uptake. Biochem. J. 450 47-53 PubMed GONUTS page
↑ ^6.0 ^6.1 Ramirez, A et al. (2006) Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase. Nat. Genet. 38 1184-91 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 ^7.6 Ramonet, D et al. (2012) PARK9-associated ATP13A2 localizes to intracellular acidic vesicles and regulates cation homeostasis and neuronal integrity. Hum. Mol. Genet. 21 1725-43 PubMed GONUTS page
↑ Rajagopalan, S et al. (2016) Regulation of ATP13A2 via PHD2-HIF1α Signaling Is Critical for Cellular Iron Homeostasis: Implications for Parkinson's Disease. J. Neurosci. 36 1086-95 PubMed GONUTS page
↑ ^9.0 ^9.1 Medici, S et al. (2012) Mn(II) and Zn(II) interactions with peptide fragments from Parkinson's disease genes. Dalton Trans 41 4378-88 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 Remelli, M et al. (2013) Interaction of divalent cations with peptide fragments from Parkinson's disease genes. Dalton Trans 42 5964-74 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 Tsunemi, T et al. (2014) ATP13A2/PARK9 regulates secretion of exosomes and α-synuclein. J. Neurosci. 34 15281-7 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 Matsui, H et al. (2013) ATP13A2 deficiency induces a decrease in cathepsin D activity, fingerprint-like inclusion body formation, and selective degeneration of dopaminergic neurons. FEBS Lett. 587 1316-25 PubMed GONUTS page
↑ ^13.0 ^13.1 Gusdon, AM et al. (2012) ATP13A2 regulates mitochondrial bioenergetics through macroautophagy. Neurobiol. Dis. 45 962-72 PubMed GONUTS page
↑ Dias, V et al. (2013) The role of oxidative stress in Parkinson's disease. J Parkinsons Dis 3 461-91 PubMed GONUTS page
↑ Schröder, B et al. (2007) Integral and associated lysosomal membrane proteins. Traffic 8 1676-86 PubMed GONUTS page
↑ Park, JS et al. (2011) Pathogenic effects of novel mutations in the P-type ATPase ATP13A2 (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset parkinsonism. Hum. Mutat. 32 956-64 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 Dehay, B et al. (2012) Lysosomal dysfunction in Parkinson disease: ATP13A2 gets into the groove. Autophagy 8 1389-91 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 ^18.3 Martin, S et al. (2015) Unlocking ATP13A2/PARK9 activity. Cell Cycle 14 3341-2 PubMed GONUTS page
↑ Roth, JA & Eichhorn, M (2013) Down-regulation of LRRK2 in control and DAT transfected HEK cells increases manganese-induced oxidative stress and cell toxicity. Neurotoxicology 37 100-7 PubMed GONUTS page
↑ ^20.0 ^20.1 ^20.2 ^20.3 Lopes da Fonseca, T & Outeiro, TF (2014) ATP13A2 and Alpha-synuclein: a Metal Taste in Autophagy. Exp Neurobiol 23 314-23 PubMed GONUTS page

[PMID:24334770-1] 1.0 ^1.1 ^1.2 Tsunemi, T & Krainc, D (2014) Zn²⁺ dyshomeostasis caused by loss of ATP13A2/PARK9 leads to lysosomal dysfunction and alpha-synuclein accumulation. Hum. Mol. Genet. 23 2791-801 PubMed GONUTS page

[PMID:26134396-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 Holemans, T et al. (2015) A lipid switch unlocks Parkinson's disease-associated ATP13A2. Proc. Natl. Acad. Sci. U.S.A. 112 9040-5 PubMed GONUTS page

[PMID:24603074-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 Kong, SM et al. (2014) Parkinson's disease-linked human PARK9/ATP13A2 maintains zinc homeostasis and promotes α-Synuclein externalization via exosomes. Hum. Mol. Genet. 23 2816-33 PubMed GONUTS page

[PMID:22285144-4] Rentschler, G et al. (2012) ATP13A2 (PARK9) polymorphisms influence the neurotoxic effects of manganese. Neurotoxicology 33 697-702 PubMed GONUTS page

[PMID:23205587-5] De La Hera, DP et al. (2013) Parkinson's disease-associated human P5B-ATPase ATP13A2 increases spermidine uptake. Biochem. J. 450 47-53 PubMed GONUTS page

[PMID:16964263-6] 6.0 ^6.1 Ramirez, A et al. (2006) Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase. Nat. Genet. 38 1184-91 PubMed GONUTS page

[PMID:22186024-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 ^7.6 Ramonet, D et al. (2012) PARK9-associated ATP13A2 localizes to intracellular acidic vesicles and regulates cation homeostasis and neuronal integrity. Hum. Mol. Genet. 21 1725-43 PubMed GONUTS page

[PMID:26818499-8] Rajagopalan, S et al. (2016) Regulation of ATP13A2 via PHD2-HIF1α Signaling Is Critical for Cellular Iron Homeostasis: Implications for Parkinson's Disease. J. Neurosci. 36 1086-95 PubMed GONUTS page

[PMID:22361905-9] 9.0 ^9.1 Medici, S et al. (2012) Mn(II) and Zn(II) interactions with peptide fragments from Parkinson's disease genes. Dalton Trans 41 4378-88 PubMed GONUTS page

[PMID:23202360-10] 10.0 ^10.1 ^10.2 Remelli, M et al. (2013) Interaction of divalent cations with peptide fragments from Parkinson's disease genes. Dalton Trans 42 5964-74 PubMed GONUTS page

[PMID:25392495-11] 11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 Tsunemi, T et al. (2014) ATP13A2/PARK9 regulates secretion of exosomes and α-synuclein. J. Neurosci. 34 15281-7 PubMed GONUTS page

[PMID:23499937-12] 12.0 ^12.1 ^12.2 ^12.3 Matsui, H et al. (2013) ATP13A2 deficiency induces a decrease in cathepsin D activity, fingerprint-like inclusion body formation, and selective degeneration of dopaminergic neurons. FEBS Lett. 587 1316-25 PubMed GONUTS page

[PMID:22198378-13] 13.0 ^13.1 Gusdon, AM et al. (2012) ATP13A2 regulates mitochondrial bioenergetics through macroautophagy. Neurobiol. Dis. 45 962-72 PubMed GONUTS page

[PMID:24252804-14] Dias, V et al. (2013) The role of oxidative stress in Parkinson's disease. J Parkinsons Dis 3 461-91 PubMed GONUTS page

[PMID:17897319-15] Schröder, B et al. (2007) Integral and associated lysosomal membrane proteins. Traffic 8 1676-86 PubMed GONUTS page

[PMID:21542062-16] Park, JS et al. (2011) Pathogenic effects of novel mutations in the P-type ATPase ATP13A2 (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset parkinsonism. Hum. Mutat. 32 956-64 PubMed GONUTS page

[PMID:22885599-17] 17.0 ^17.1 ^17.2 ^17.3 Dehay, B et al. (2012) Lysosomal dysfunction in Parkinson disease: ATP13A2 gets into the groove. Autophagy 8 1389-91 PubMed GONUTS page

[PMID:26392192-18] 18.0 ^18.1 ^18.2 ^18.3 Martin, S et al. (2015) Unlocking ATP13A2/PARK9 activity. Cell Cycle 14 3341-2 PubMed GONUTS page

[PMID:23628791-19] 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:25548531-20] 20.0 ^20.1 ^20.2 ^20.3 Lopes da Fonseca, T & Outeiro, TF (2014) ATP13A2 and Alpha-synuclein: a Metal Taste in Autophagy. Exp Neurobiol 23 314-23 PubMed GONUTS page

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