KDM4B
Domain
The 2 Tudor domains recognize and bind methylated histones. Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails (By similarity).
Function
Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Only able to demethylate trimethylated H3 'Lys-9', with a weaker activity than KDM4A, KDM4C and KDM4D. Demethylation of Lys residue generates formaldehyde and succinate (PubMed:16603238, PubMed:28262558). Plays a critical role in the development of the central nervous system (CNS).
Involvement in disease
Intellectual developmental disorder, autosomal dominant 65
MRD65
An autosomal dominant form of intellectual disability, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD65 is characterized by delayed motor and speech acquisition, variably impaired intellectual development, behavioral abnormalities, and dysmorphic facial features. Additional variable features include feeding difficulties, hypotonia, and seizures.
None
The disease is caused by variants affecting the gene represented in this entry.
Sequence Similarities
Belongs to the JHDM3 histone demethylase family.
Cellular localization
- Nucleus
Alternative names
JHDM3B, JMJD2B, KIAA0876, KDM4B, Lysine-specific demethylase 4B, JmjC domain-containing histone demethylation protein 3B, Jumonji domain-containing protein 2B, [histone H3]-trimethyl-L-lysine(9) demethylase 4B