Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Combined Automated Annotation using Multiple IEA Methods
Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase.
Integral and associated lysosomal membrane proteins.
Pathogenic effects of novel mutations in the P-type ATPase ATP13A2 (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset parkinsonism.
PARK9-associated ATP13A2 localizes to intracellular acidic vesicles and regulates cation homeostasis and neuronal integrity.
ATP13A2 regulates mitochondrial bioenergetics through macroautophagy.
ATP13A2 (PARK9) polymorphisms influence the neurotoxic effects of manganese.
Mn(II) and Zn(II) interactions with peptide fragments from Parkinson's disease genes.
Identification of novel ATP13A2 interactors and their role in α-synuclein misfolding and toxicity.
Common pathogenic effects of missense mutations in the P-type ATPase ATP13A2 (PARK9) associated with early-onset parkinsonism.
Lysosomal dysfunction in Parkinson disease: ATP13A2 gets into the groove.
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This commentary summarizes impaired lysosomal degradation after ATP13A2 loss in patient fibroblasts and human BE-M17 cells, with wild-type rescue; it supports a positive homeostatic effect, not ATP13A2 protease activity.
"reduced degradation of lysosomal substrates"
Interaction of divalent cations with peptide fragments from Parkinson's disease genes.
Parkinson's disease-associated human P5B-ATPase ATP13A2 increases spermidine uptake.
ATP13A2 deficiency induces a decrease in cathepsin D activity, fingerprint-like inclusion body formation, and selective degeneration of dopaminergic neurons.
Down-regulation of LRRK2 in control and DAT transfected HEK cells increases manganese-induced oxidative stress and cell toxicity.
The role of oxidative stress in Parkinson's disease.
Zn²⁺ dyshomeostasis caused by loss of ATP13A2/PARK9 leads to lysosomal dysfunction and alpha-synuclein accumulation.
Parkinson's disease-linked human PARK9/ATP13A2 maintains zinc homeostasis and promotes α-Synuclein externalization via exosomes.
ATP13A2/PARK9 regulates secretion of exosomes and α-synuclein.
ATP13A2 and Alpha-synuclein: a Metal Taste in Autophagy.
A lipid switch unlocks Parkinson's disease-associated ATP13A2.
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Terminal GFP-fusion protection assays in transfected HeLa cells place both ATP13A2 termini on the cytosolic side. This is topology evidence, not a measurement of polyamine transport.
"ATP13A2 contains an even number of TM helices"
Unlocking ATP13A2/PARK9 activity.
Regulation of ATP13A2 via PHD2-HIF1α Signaling Is Critical for Cellular Iron Homeostasis: Implications for Parkinson's Disease.
The Parkinson's disease-associated genes ATP13A2 and SYT11 regulate autophagy via a common pathway.
Loss-of-function mutations in the ATP13A2/PARK9 gene cause complicated hereditary spastic paraplegia (SPG78).
Parkinson disease related ATP13A2 evolved early in animal evolution.
ATP13A2 facilitates HDAC6 recruitment to lysosome to promote autophagosome-lysosome fusion.
The Parkinson-associated human P5B-ATPase ATP13A2 modifies lipid homeostasis.
ATP13A2 deficiency disrupts lysosomal polyamine export.
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ATP13A2 is identified as a lysosomal polyamine exporter. The cached abstract supports the transport core; it does not by itself resolve the separate purified-protein ATPase and membrane-reconstitution assay details.
"establish ATP13A2 as a lysosomal polyamine exporter"
ATP13A2 transports cations from cytosol to lysosomal lumen
Ion transport by P-type ATPases
Parkinson's disease-associated ATP13A2/PARK9 functions as a lysosomal H(+),K(+)-ATPase.