| KDM5A | |
|---|---|
| Gene Symbol | KDM5A |
| Full Name | Lysine Specific Demethylase 5A |
| Chromosomal Location | 12p13.33 |
| NCBI Gene ID | 8248 |
| Ensembl ID | ENSG000000150109 |
| OMIM ID | 180388 |
| UniProt ID | Q9UMM3 |
| Associated Diseases | Intellectual Disability, Neurodevelopmental Disorders, Cancer |
| Protein Family | JARID1 family (Jumonji C domain demethylase) |
Kdm5A Lysine Specific Demethylase 5A is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
KDM5A encodes a jarid1 family (jumonji c domain demethylase) that catalyzes the removal of methyl groups from histone lysine residues. This epigenetic enzyme plays critical roles in chromatin remodeling and gene expression regulation in the nervous system. Histone methylation is a key post-translational modification that regulates neuronal gene expression programs involved in development, synaptic plasticity, and memory formation.
The KDM5A gene product is a histone demethylase that specifically removes methyl groups from lysine residues on histone H3 and H4. This enzyme belongs to the JARID1 family (Jumonji C domain demethylase) and functions as a transcriptional regulator by modulating chromatin accessibility. In neurons, KDM5A regulates genes involved in synaptic plasticity, neuronal survival, and stress responses. The enzyme requires iron and 2-oxoglutarate as cofactors for its demethylase activity.
Pathogenic variants in KDM5A are associated with Intellectual Disability, Neurodevelopmental Disorders, Cancer. These conditions involve dysregulation of epigenetic processes critical for proper neuronal development and function. Altered KDM5A activity affects the expression of genes essential for cognitive function, and its dysregulation is implicated in neurodegenerative processes.
KDM5A is expressed throughout the brain, with high expression in the hippocampus, cerebral cortex, and cerebellum. The gene shows cell-type specific expression in neurons and glial cells, with activity-dependent regulation in response to neuronal stimulation.
The study of Kdm5A Lysine Specific Demethylase 5A has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.