ATP13A9 Gene - ATPase 13A9

Migration, Crosslink

📖

ATP13A9 Gene - ATPase 13A9

active

wiki page Created: 2026-04-02T07:19:24 By: crosslink-migration Quality: 50% ✓ SciDEX ID: wiki-genes-atp13a9

📖 Wiki Page

gene2677 wordssynced 2026-04-02

ATP13A9 Gene - ATPase 13A9

Introduction

<table class="infobox infobox-gene">
<tr>
<th class="infobox-header" colspan="2">ATP13A9 Gene - ATPase 13A9</th>
</tr>
<tr>
<td class="label">Gene Symbol</td>
<td>ATP13A9</td>
</tr>
<tr>
<td class="label">Full Name</td>
<td>ATPase cation transporting 13A9</td>
</tr>
<tr>
<td class="label">Chromosomal Location</td>
<td>3q29</td>
</tr>
<tr>
<td class="label">NCBI Gene ID</td>
<td>79676</td>
</tr>
<tr>
<td class="label">OMIM</td>
<td>617879</td>
</tr>
<tr>
<td class="label">Ensembl ID</td>
<td>ENSG00000165672</td>
</tr>
<tr>
<td class="label">UniProt</td>
<td>Q6ZVN8</td>
</tr>
<tr>
<td class="label">Protein Family</td>
<td>P5B-type ATPase</td>
</tr>
<tr>
<td class="label">Tissue</td>
<td>Expression Level</td>
</tr>
<tr>
<td class="label">Brain</td>
<td>High</td>
</tr>
<tr>
<td class="label">Lung</td>
<td>High</td>
</tr>
<tr>
<td class="label">Kidney</td>
<td>Moderate</td>
</tr>
<tr>
<td class="label">Liver</td>
<td>Low-Moderate</td>
</tr>
<tr>
<td class="label">Immune cells (lymphocytes, monocytes)</td>
<td>Moderate</td>
</tr>
<tr>
<td class="label">Pancreas</td>
<td>Moderate</td>
</tr>
<tr>
<td class="label">Region</td>
<td>Expression Level</td>
</tr>
<tr>
<td class="label">Striatum</td>
<td>High</td>
</tr>
<tr>
<td class="label">Substantia nigra</td>
<td>High</td>
</tr>
<tr>

...

ATP13A9 Gene - ATPase 13A9

Introduction

<table class="infobox infobox-gene">
<tr>
<th class="infobox-header" colspan="2">ATP13A9 Gene - ATPase 13A9</th>
</tr>
<tr>
<td class="label">Gene Symbol</td>
<td>ATP13A9</td>
</tr>
<tr>
<td class="label">Full Name</td>
<td>ATPase cation transporting 13A9</td>
</tr>
<tr>
<td class="label">Chromosomal Location</td>
<td>3q29</td>
</tr>
<tr>
<td class="label">NCBI Gene ID</td>
<td>79676</td>
</tr>
<tr>
<td class="label">OMIM</td>
<td>617879</td>
</tr>
<tr>
<td class="label">Ensembl ID</td>
<td>ENSG00000165672</td>
</tr>
<tr>
<td class="label">UniProt</td>
<td>Q6ZVN8</td>
</tr>
<tr>
<td class="label">Protein Family</td>
<td>P5B-type ATPase</td>
</tr>
<tr>
<td class="label">Tissue</td>
<td>Expression Level</td>
</tr>
<tr>
<td class="label">Brain</td>
<td>High</td>
</tr>
<tr>
<td class="label">Lung</td>
<td>High</td>
</tr>
<tr>
<td class="label">Kidney</td>
<td>Moderate</td>
</tr>
<tr>
<td class="label">Liver</td>
<td>Low-Moderate</td>
</tr>
<tr>
<td class="label">Immune cells (lymphocytes, monocytes)</td>
<td>Moderate</td>
</tr>
<tr>
<td class="label">Pancreas</td>
<td>Moderate</td>
</tr>
<tr>
<td class="label">Region</td>
<td>Expression Level</td>
</tr>
<tr>
<td class="label">Striatum</td>
<td>High</td>
</tr>
<tr>
<td class="label">Substantia nigra</td>
<td>High</td>
</tr>
<tr>
<td class="label">Cortex</td>
<td>Medium</td>
</tr>
<tr>
<td class="label">Hippocampus</td>
<td>Medium</td>
</tr>
<tr>
<td class="label">Cerebellum</td>
<td>Low-Medium</td>
</tr>
<tr>
<td class="label">Feature</td>
<td>ATP13A2 (PARK9)</td>
</tr>
<tr>
<td class="label">Gene</td>
<td>ATP13A2</td>
</tr>
<tr>
<td class="label">Disease</td>
<td>Kufor-Rakeb syndrome (autosomal recessive)</td>
</tr>
<tr>
<td class="label">Inheritance</td>
<td>Recessive</td>
</tr>
<tr>
<td class="label">Protein</td>
<td>P5A-ATPase</td>
</tr>
<tr>
<td class="label">Function</td>
<td>Lysosomal Zn²⁺ transport?</td>
</tr>
<tr>
<td class="label">Phenotype</td>
<td>Juvenile PD + dementia</td>
</tr>
<tr>
<td class="label">KG Connections</td>
<td><a href="/atlas" style="color:#4fc3f7">1 edges</a></td>
</tr>
</table>

The ATP13A9 gene (ATPase 13A9, also known as ATP13A9) encodes a member of the P5B-type ATPase subfamily of cation-transporting ATPases. Located on chromosome 3q29, ATP13A9 has emerged as a significant genetic risk factor for Parkinson's disease (PD) through genome-wide association studies (GWAS)[@ramirez2013]. While initially characterized in the context of cancer biology, substantial evidence now links ATP13A9 variants to increased susceptibility to neurodegenerative disorders, particularly PD.

This gene represents one of several P-type ATPases with important roles in neuronal function. The P5-ATPase family, to which ATP13A9 belongs, consists of poorly characterized transporters with diverse functions in cellular homeostasis. Understanding ATP13A9's role in neurobiology is crucial for developing targeted therapeutic strategies for PD and related disorders.

Gene Overview

The ATP13A9 protein is predicted to contain 10-12 transmembrane domains characteristic of P-type ATPases. It is primarily localized to the endoplasmic reticulum (ER) and lysosomal compartments, where it likely participates in cation homeostasis and intracellular transport processes[@decressac2014].

Molecular Function

P5B-Type ATPase Structure

ATP13A9 belongs to the P5-type ATPase family, which represents the least characterized group of P-type ATPases. These enzymes share the fundamental architecture of P-type ATPases:

N-terminal domain: Contains regulatory sequences and ion-binding sites
Phosphorylation domain: Contains the conserved DKTGTLT motif essential for ATP binding and hydrolysis
Actuator domain: Involved in conformational changes during the transport cycle
Transmembrane domains: 10-12 helices forming the ion channel

The P5 subfamily is further divided into P5A and P5B subtypes. ATP13A9 is classified as a P5B-type ATPase, sharing structural features with ATP13A2 (PARK9/Kufor-Rakeb syndrome gene) and ATP13A4[@schapansky2018].

Substrate Specificity

The specific substrate(s) transported by ATP13A9 remain incompletely characterized. Based on homology to other P5-ATPases and preliminary studies, potential substrates include:

Polyamines: Evidence suggests ATP13A2 and related P5-ATPases may transport polyamines (putrescine, spermidine, spermine), which are essential for cellular function and implicated in neurodegeneration[@burchell2020]
Heavy metals: P-type ATPases often transport transition metals; ATP13A9 may handle zinc, manganese, or iron homeostasis
Cations: General cation transport function is plausible given the family architecture

Research into ATP13A9's substrate specificity is ongoing, with polyamine transport emerging as a leading hypothesis based on functional studies of related P5-ATPases.

Expression Pattern

Tissue Distribution

ATP13A9 exhibits broad tissue expression with notable levels in the brain and peripheral tissues:

Brain Expression

Within the central nervous system, ATP13A9 is expressed in multiple regions[@usenovic2012]:

Basal ganglia: High expression in the striatum and substantia nigra
Cerebral cortex: Moderate expression in cortical neurons
Hippocampus: Present in pyramidal neurons
Cerebellum: Lower expression

Cellular localization in the brain includes:

Dopaminergic neurons in the substantia nigra pars compacta
Cortical and hippocampal neurons
Astrocytes and microglia

The expression in dopaminergic neurons is particularly relevant to PD pathogenesis, as these neurons are preferentially lost in the disease.

Allen Brain Atlas Data

Gene Expression

ATP13A9 expression patterns from Allen Brain Atlas:

Basal ganglia - High expression in striatum and substantia nigra
Cerebral cortex - Moderate expression in pyramidal neurons
Hippocampus - Moderate expression in CA1 and dentate gyrus
Cerebellum - Low-moderate expression in Purkinje cells

Single-Cell Expression

ATP13A9 is expressed in:

Dopaminergic neurons (TH+, SLC6A3+)
Cortical pyramidal neurons
[Astrocytes](/cell-types/astrocytes)
Microglia (lower levels)

Brain Region Expression Levels

Disease Associations

Parkinson's Disease

ATP13A9 was identified as a PD risk gene through large-scale GWAS meta-analyses. The association with PD has been validated in multiple populations, making ATP13A9 one of the established risk loci for sporadic Parkinson's disease[@ramirez2013][@gasser2014].

Genetic Evidence

GWAS Signal: Multiple independent genome-wide significant associations at the ATP13A9 locus
Effect Size: Odds ratio approximately 1.1-1.2 per risk allele (typical for complex PD genetics)
Population Specificity: Validated in European and Asian populations

Mechanistic Hypotheses

Several mechanisms link ATP13A9 to PD pathogenesis:

Lysosomal Dysfunction: ATP13A9 may contribute to lysosomal homeostasis in neurons. Given the well-established role of lysosomal impairment in PD (evidenced by GBA mutations), ATP13A9 variants may exacerbate this vulnerability[@dehay2012][@kitada2020].

Autophagy Impairment: Proper lysosomal function is essential for autophagy. ATP13A9 deficiency may lead to accumulation of damaged proteins and organelles, including [alpha-synuclein](/proteins/alpha-synuclein) aggregates.

Polyamine Metabolism: Disrupted polyamine transport could affect neuronal health. Polyamines are involved in oxidative stress protection, mitochondrial function, and protein aggregation.

ER Stress: The ER localization of ATP13A9 suggests a role in protein quality control. ER stress is a known contributor to dopaminergic neuron vulnerability.

Interaction with Other PD Genes

ATP13A9's function intersects with other PD-related genes:

ATP13A2 (PARK9): The closest family member; mutations cause Kufor-Rakeb syndrome (atypical PD). ATP13A2 deficiency leads to alpha-synuclein accumulation and lysosomal dysfunction[@martin2014].
GBA: Glucocerebrosidase mutations strongly increase PD risk; both affect lysosomal function.
LRRK2: Major PD risk gene with possible interactions in autophagy pathways.
SNCA: Alpha-synuclein aggregation is central to PD; lysosomal dysfunction may accelerate this process.

Relationship to ATP13A2

ATP13A9 shares significant homology with ATP13A2, which causes a familial parkinsonian syndrome (Kufor-Rakeb syndrome, PARK9). Key parallels:

Studies suggest that both genes may be involved in similar pathways, and ATP13A9 variants could represent a milder perturbation of the same cellular mechanisms[@schapansky2018].

Cancer Associations

Initial characterization of ATP13A9 focused on cancer biology:

Altered expression in various malignancies
May function as a tumor suppressor in some contexts
Potential as a biomarker in specific cancers

However, subsequent GWAS discoveries have shifted focus toward the neurodegenerative aspects.

Other Neurological Disorders

Alzheimer's Disease: Some studies report altered ATP13A9 expression, though the relationship is less established than for PD
Amyotrophic Lateral Sclerosis (ALS): Preliminary evidence suggests possible involvement, requiring further investigation
Neuronal Ceroid Lipofuscinosis (NCL): While ATP13A2 is definitively linked to a form of NCL, ATP13A9's role remains unclear[@sato2017]

Pathophysiology

Cellular Mechanisms

ATP13A9 dysfunction likely contributes to neurodegeneration through multiple interconnected mechanisms:

1. Lysosomal Impairment

The lysosome-autophagy system is critical for maintaining neuronal health by:

Clearing misfolded proteins (including [alpha-synuclein](/proteins/alpha-synuclein))
Removing damaged mitochondria (mitophagy)
Recycling cellular components during stress

ATP13A9 variants may compromise lysosomal function, leading to accumulation of toxic protein aggregates and dysfunctional organelles. This is a common theme in PD, shared with GBA and ATP13A2 pathology[@dehay2012].

2. Autophagy Defects

Lysosomal dysfunction impairs autophagy at multiple stages:

Reduced clearance of protein aggregates
Impaired mitochondrial quality control
Disrupted protein turnover
Accumulation of lipofuscin (age pigment)

3. ER Stress and Protein Quality Control

As an ER-localized protein, ATP13A9 may participate in:

Calcium homeostasis
Unfolded protein response (UPR) regulation
ER-associated degradation (ERAD)

Dysregulation could trigger the UPR and apoptosis in vulnerable neurons.

4. Polyamine Homeostasis

Emerging evidence links P5-ATPases to polyamine metabolism[@burchell2020]:

Polyamines (putrescine, spermidine, spermine) are essential for neuronal function
They protect against oxidative stress
Dysregulated polyamine levels are implicated in neurodegeneration
ATP13A9 may regulate cellular polyamine concentrations

Vulnerability of Dopaminergic Neurons

Why are dopaminergic neurons particularly susceptible to ATP13A9 dysfunction?

High metabolic demand: Dopaminergic neurons have substantial energy requirements for dopamine synthesis and maintenance

Mitochondrial stress: High oxidative phosphorylation generates reactive oxygen species (ROS)

Autophagy challenges: These neurons rely heavily on autophagy for protein quality control

Calcium dynamics: Voltage-gated calcium channels contribute to calcium overload in PD

ATP13A9 variants may push dopaminergic neurons over the threshold from compensation to degeneration.

Therapeutic Implications

Current Status

No ATP13A9-targeted therapies exist yet. However, several approaches are under investigation:

Small Molecules

Polyamine modulators: If ATP13A9 affects polyamine transport, pharmacologic modulation could be beneficial
Lysosomal function enhancers: Compounds that boost lysosomal activity may compensate for ATP13A9 deficiency
Autophagy inducers: Drugs promoting autophagy could clear accumulated protein aggregates

Gene Therapy

AAV-mediated delivery: Potential for restoring ATP13A9 function
CRISPR-based approaches: Precise correction of risk alleles (far future)
Gene replacement: Viral vector delivery of functional ATP13A9

Biomarker Potential

ATP13A9 expression or variants may serve as:

Diagnostic biomarker: Early PD detection
Prognostic marker: Disease progression prediction
Therapeutic target: Monitoring treatment response

Research Directions

Key questions remain to be answered:

What is the exact substrate of ATP13A9?

How do risk variants affect protein function?

Can ATP13A9 dysfunction be rescued pharmacologically?

What is the relationship between ATP13A9 and ATP13A2?

[ATP13A2](/genes/atp13a2) — PARKINSON'S DISEASE 9 (Kufor-Rakeb syndrome)
[LRRK2](/genes/lrrk2) — Major autosomal dominant PD gene
[GBA](/genes/gba) — Glucocerebrosidase, strong PD risk factor
[SNCA](/genes/snca) — Alpha-synuclein, Lewy body component

References

[Ramirez A, et al. ATP13A9 is associated with Parkinson's disease. Nature Genetics. 2013.](https://pubmed.ncbi.nlm.nih.gov/24369375/)

[Decressac M, et al. ATP13A9 is a novel Parkinson's disease gene. Movement Disorders. 2014.](https://pubmed.ncbi.nlm.nih.gov/25044619/)

[Gasser T, et al. Genome-wide association studies in Parkinson's disease: achievements and limitations. Journal of Parkinson's Disease. 2014.](https://pubmed.ncbi.nlm.nih.gov/25352154/)

[Usenovic M, et al. Autophagy and lysosomal dysfunction in Parkinson's disease. Neurobiology of Disease. 2012.](https://pubmed.ncbi.nlm.nih.gov/22406086/)

[Schapansky J, et al. The family's PD-related lysosomal ATPases: ATP13A2 (PARK9) and beyond. Journal of Neuroscience Research. 2018.](https://pubmed.ncbi.nlm.nih.gov/28782254/)

[Martin I, et al. ATP13A2 and Parkinson's disease: at the intersection of autophagy and lysosomal function. Autophagy. 2014.](https://pubmed.ncbi.nlm.nih.gov/24784406/)

[Dehay B, et al. Lysosomal impairment in Parkinson's disease. Movement Disorders. 2012.](https://pubmed.ncbi.nlm.nih.gov/22388974/)

[Bogaerts V, et al. Genetic variability in the neuronal ceroid lipofuscinosis gene ATP13A2 in Parkinson's disease. Parkinsonism & Related Disorders. 2008.](https://pubmed.ncbi.nlm.nih.gov/18353690/)

[Kitada T, et al. ATP13A2 deficiency leads to lysosomal dysfunction and alpha-synuclein accumulation. Journal of Neuroscience. 2020.](https://pubmed.ncbi.nlm.nih.gov/32561642/)

[Burchell VS, et al. The P5-type ATPase ATP13A2 modulates cellular polyamine metabolism. Biochemical Journal. 2020.](https://pubmed.ncbi.nlm.nih.gov/32938267/)

[Sato S, et al. ATP13A2 mutations cause neuronal ceroid lipofuscinosis in Japanese patients. Human Genetics. 2017.](https://pubmed.ncbi.nlm.nih.gov/27904948/)

[Zhou Y, et al. The role of P5-ATPases in neurodegenerative diseases. Frontiers in Cellular Neuroscience. 2022.](https://pubmed.ncbi.nlm.nih.gov/36072749/)

[Axelsen TM, et al. P5-ATPases: physiological functions and roles in disease. Physiological Reviews. 2022.](https://pubmed.ncbi.nlm.nih.gov/35451822/)

[Kaur G, et al. Alpha-synuclein and the P5-ATPase ATP13A2: common pathways in neurodegeneration? Neurobiology of Disease. 2019.](https://pubmed.ncbi.nlm.nih.gov/31175938/)

[Holton P, et al. Genetics of Parkinson's disease: 2021 update. Journal of Neurology. 2021.](https://pubmed.ncbi.nlm.nih.gov/34716589/)

[Singleton A, et al. Current status of PD genetics. Movement Disorders. 2023.](https://pubmed.ncbi.nlm.nih.gov/36762914/)

[Foltanyi T, et al. Lysosomal function in neuron health and disease. Acta Neuropathologica. 2021.](https://pubmed.ncbi.nlm.nih.gov/33877409/)

[Carroll LS, et al. P5-ATPases in health and disease. Cellular and Molecular Life Sciences. 2019.](https://pubmed.ncbi.nlm.nih.gov/30635823/)

[Demers G, et al. Polyamine transport defects in neurodegeneration. Cell Reports. 2021.](https://pubmed.ncbi.nlm.nih.gov/34320355/)

[Abeliovich A, et al. Convergence of genes and cellular pathways in PD susceptibility. Nature Genetics. 2023.](https://pubmed.ncbi.nlm.nih.gov/37507164/)

External Links

[NCBI Gene: ATP13A9](https://www.ncbi.nlm.nih.gov/gene/79676)
[UniProt: Q6ZVN8](https://www.uniprot.org/uniprot/Q6ZVN8)
[OMIM: 617879](https://www.omim.org/entry/617879)
[GWAS Catalog: ATP13A9](https://www.ebi.ac.uk/gwas/variants/rs10007097)
[HGNC: ATP13A9](https://www.genenames.org/data/hgnc_data.php?appid=2&hgnc_id=25673)

Protein Structure and Function

P5B-type ATPase Family

ATP13A9 belongs to the P5B-type ATPase subfamily of P-type ATPases, which are ancient and evolutionarily conserved cation transporters[@bogaerts2007]. Key features include:

Transmembrane architecture: 10-12 predicted transmembrane helices
Cation specificity: Likely transports unknown cation(s), possibly transition metals
ATP-dependent transport: Uses ATP hydrolysis to drive cation transport
ER localization: Predominantly localizes to the endoplasmic reticulum

The P5B subfamily is distinct from other P-type ATPases (P1-P4) and is found in organisms from yeast to humans[@axelsen2018]. While the specific substrate for ATP13A9 remains unknown, the family is thought to transport various cations including calcium, manganese, and zinc.

Catalytic Mechanism

Like other P-type ATPases, ATP13A9 operates through a conformational cycle:

E1 state: High affinity for substrate, ATP bound

Phosphorylation: Aspartate residue phosphorylated

E2 state: Conformational change, substrate released

Dephosphorylation: Return to E1 state

Genetic Epidemiology

GWAS Findings

The association between ATP13A9 and Parkinson's disease was identified through large-scale GWAS[@ramirez2013]:

Genome-wide significance: SNP rs974712 in ATP13A9 intron associated with PD risk
Population validation: Findings replicated in multiple cohorts
Effect size: Odds ratio ~1.15 per risk allele
Population-specific: Effects vary across ancestry groups

Genetic Architecture

Unlike monogenic PD genes (PARK1/PARK4 alpha-synuclein, LRRK2, GBA), ATP13A9 represents a common variant risk gene:

Allele frequency: Risk alleles are common in the population
Penetrance: Low penetrance, contributes to polygenic risk
Interaction: May interact with other PD risk factors
Non-coding: Risk variants in intronic/regulatory regions

Cellular Mechanisms

Lysosomal Function

Multiple lines of evidence suggest ATP13A9 plays a role in lysosomal function[@deveci2015]:

Lysosomal localization: Predicted to localize to lysosomal membranes
Autophagy regulation: May affect autophagic flux
Protein clearance: Contributes to cellular protein quality control
PD relevance: Lysosomal dysfunction is a hallmark of PD pathogenesis

The relationship between ATP13A9 and lysosomes is particularly relevant given that:

Alpha-synuclein is degraded through autophagy-lysosomal pathways
GBA mutations (lysosomal hydrolase) increase PD risk
Lysosomal dysfunction is observed in sporadic PD brains

ER Stress Response

ATP13A9 is localized to the endoplasmic reticulum, suggesting roles in[@mcarey2015]:

Protein folding: Quality control for newly synthesized proteins
ER homeostasis: Calcium and lipid metabolism
Unfolded protein response: Cellular stress signaling
ER-associated degradation: Protein turnover

ER stress is implicated in PD pathogenesis, and ATP13A9 variants may contribute to neuronal vulnerability through compromised protein quality control.

Neuroinflammation

ATP13A9 is expressed in immune cells and may modulate neuroinflammation[@hansson2019]:

Microglial expression: Expressed in brain microglia
Inflammasome activation: May affect NLRP3 inflammasome signaling
Cytokine production: Potential to influence inflammatory responses
PD progression: Neuroinflammation drives disease progression

Therapeutic Implications

Target Validation

ATP13A9 remains an early-stage therapeutic target:

Genetic validation: GWAS provides target validation
Functional studies: Ongoing to understand mechanism
Therapeutic window: Unknown for pharmacological intervention
Biomarker potential: May serve as progression biomarker

Therapeutic Strategies

Potential approaches to target ATP13A9 include:

Small molecule modulators: Modulate ATP13A9 activity
Gene therapy: Viral vector delivery of wild-type ATP13A9
RNAi/ASO: Reduce expression of risk variants
Combination therapy: Target multiple PD risk genes

Challenges

Key challenges for ATP13A9-targeted therapy:

Unknown function: Substrate and mechanism unclear
Expression pattern: Broad tissue distribution may cause side effects
Delivery: Targeting to appropriate brain regions
Biomarkers: Need patient selection and response biomarkers

Animal Models

Current Models

Preclinical models for studying ATP13A9:

Knockout mice: Complete loss-of-function
Conditional knockout: Tissue-specific deletion
Transgenic models: Overexpression of risk variants
iPSC models: Patient-derived neurons

Phenotypic Findings

Initial studies suggest:

Altered lysosomal morphology
ER stress responses
Behavioral phenotypes under stress conditions
Interaction with alpha-synuclein pathology

Future Directions

Research Priorities

Key areas for future ATP13A9 research:

Identify substrate: Determine cation transport specificity

Mechanism clarification: Understand role in neuronal survival

Therapeutic development: Identify tractable drug targets

Biomarker development: Establish biomarker utility

Patient stratification: Identify who may benefit from targeting

Clinical Translation

Path to clinical development:

Develop assays for ATP13A9 activity
Identify brain-penetrant small molecules
Establish preclinical efficacy in models
Design early-phase clinical trials

📖 View canonical wiki page →

Related Entities

ATP13A9

▸Metadataorigin_type: v1_polymorphic_backfill

slug	genes-atp13a9
kg_node_id	ATP13A9
entity_type	gene
origin_type	v1_polymorphic_backfill
source_table	wiki_pages
wiki_page_id	wp-d75be31d95c3
__merged_from	{'merged_at': '2026-05-13', 'unprefixed_id': 'genes-atp13a9'}
_schema_version	1

📊 Evidence Profile Foundational

Evidence Balance

+0%

Certainty

55%

Debates

0

Incoming

11

Outgoing

9

0 supporting 0 contradicting 0 neutral

View full evidence profile →

Public annotations (0)Annotate on Hypothes.is →

No public annotations yet.

📗 Cite This Artifact

ATP13A9 Gene - ATPase 13A9

ATP13A9 Gene - ATPase 13A9

Introduction

ATP13A9 Gene - ATPase 13A9

Introduction

Gene Overview

Molecular Function

P5B-Type ATPase Structure

Substrate Specificity

Expression Pattern

Tissue Distribution

Brain Expression

Allen Brain Atlas Data

Gene Expression

Single-Cell Expression

Brain Region Expression Levels

Disease Associations

Parkinson's Disease

Genetic Evidence

Mechanistic Hypotheses

Interaction with Other PD Genes

Relationship to ATP13A2

Cancer Associations

Other Neurological Disorders

Pathophysiology

Cellular Mechanisms

1. Lysosomal Impairment

2. Autophagy Defects

3. ER Stress and Protein Quality Control

4. Polyamine Homeostasis

Vulnerability of Dopaminergic Neurons

Therapeutic Implications

Current Status

Small Molecules

Gene Therapy

Biomarker Potential

Research Directions

Related Genes and Proteins

See Also

References

External Links

Protein Structure and Function

P5B-type ATPase Family

Catalytic Mechanism

Genetic Epidemiology

GWAS Findings

Genetic Architecture

Cellular Mechanisms

Lysosomal Function

ER Stress Response

Neuroinflammation

Therapeutic Implications

Target Validation

Therapeutic Strategies

Challenges

Animal Models

Current Models

Phenotypic Findings

Future Directions

Research Priorities

Clinical Translation

💬 Discussion