KDM5C
Domain
The first PHD-type zinc finger domain recognizes and binds H3-K9Me3.
Both the JmjC domain and the JmjN domain are required for enzymatic activity.
Function
Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code (PubMed:28262558). Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Participates in transcriptional repression of neuronal genes by recruiting histone deacetylases and REST at neuron-restrictive silencer elements. Represses the CLOCK-BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2 (By similarity).
Involvement in disease
Intellectual developmental disorder, X-linked, syndromic, Claes-Jensen type
MRXSCJ
A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXSCJ patients manifest intellectual disability associated with variable features such as slowly progressive spastic paraplegia, seizures, facial dysmorphism.
None
The disease is caused by variants affecting the gene represented in this entry.
Sequence Similarities
Belongs to the JARID1 histone demethylase family.
Tissue Specificity
Expressed in all tissues examined. Highest levels found in brain and skeletal muscle.
Cellular localization
- Nucleus
Alternative names
DXS1272E, JARID1C, SMCX, XE169, KDM5C, Lysine-specific demethylase 5C, Histone demethylase JARID1C, Jumonji/ARID domain-containing protein 1C, Protein SmcX, Protein Xe169, [histone H3]-trimethyl-L-lysine(4) demethylase 5C