Aliases for KDM4A Gene
- Lysine Demethylase 4A 2 3 5
- JmjC Domain-Containing Histone Demethylation Protein 3A 3 4
- Jumonji C Domain-Containing Histone Demethylase 3A 2 3
- Jumonji Domain-Containing Protein 2A 3 4
- Lysine (K)-Specific Demethylase 4A 2 3
- Jumonji Domain Containing 2A 2 3
- Jumonji Domain Containing 2 2 3
- Tudor Domain Containing 14A 2 3
External Ids for KDM4A Gene
Previous HGNC Symbols for KDM4A Gene
Previous GeneCards Identifiers for KDM4A Gene
This gene is a member of the Jumonji domain 2 (JMJD2) family and encodes a protein containing a JmjN domain, a JmjC domain, a JD2H domain, two TUDOR domains, and two PHD-type zinc fingers. This nuclear protein functions as a trimethylation-specific demethylase, converting specific trimethylated histone residues to the dimethylated form, and as a transcriptional repressor. [provided by RefSeq, Apr 2009]
GeneCards Summary for KDM4A Gene
KDM4A (Lysine Demethylase 4A) is a Protein Coding gene. Among its related pathways are Chromatin organization and DNA Double-Strand Break Repair. Gene Ontology (GO) annotations related to this gene include ubiquitin protein ligase binding and histone demethylase activity (H3-K36 specific). An important paralog of this gene is KDM4C.
UniProtKB/Swiss-Prot for KDM4A Gene
Histone demethylase that specifically demethylates Lys-9 and Lys-36 residues of histone H3, thereby playing a central role in histone code (PubMed:26741168). Does not demethylate histone H3 Lys-4, H3 Lys-27 nor H4 Lys-20. Demethylates trimethylated H3 Lys-9 and H3 Lys-36 residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.
Isoform 2: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain.