KDM1A: Difference between revisions
CSV import |
CSV import |
||
| Line 27: | Line 27: | ||
{{medicine-stub}} | {{medicine-stub}} | ||
{{No image}} | {{No image}} | ||
__NOINDEX__ | |||
Latest revision as of 16:22, 17 March 2025
KDM1A, also known as Lysine-specific histone demethylase 1A, is a protein that in humans is encoded by the KDM1A gene. It is a member of the amine oxidase family and plays a key role in the epigenetic regulation of gene expression.
Function[edit]
KDM1A is a histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. It demethylates mono- and dimethylated H3 'Lys-4' residues but has no activity on trimethylated H3 'Lys-4', 'Lys-9', 'Lys-27', 'Lys-36' and 'Lys-79'. It is also involved in the hormonal regulation of gene expression and is necessary for pluripotency of embryonic stem cells.
Clinical significance[edit]
Alterations in KDM1A have been associated with various forms of cancer, including breast cancer, prostate cancer, and leukemia. It is also implicated in neurodevelopmental disorders, such as autism and intellectual disability.
Structure[edit]
The KDM1A protein contains a SWIRM domain, a FAD-binding motif, and an amine oxidase domain. The SWIRM domain is involved in protein-protein interactions, while the FAD-binding motif and amine oxidase domain are necessary for the protein's catalytic activity.
See also[edit]
References[edit]
<references />

