ID:KDM5C_HUMAN DESCRIPTION: RecName: Full=Lysine-specific demethylase 5C; EC=1.14.11.-; AltName: Full=Histone demethylase JARID1C; AltName: Full=Jumonji/ARID domain-containing protein 1C; AltName: Full=Protein SmcX; AltName: Full=Protein Xe169; FUNCTION: Histone demethylase that specifically demethylates 'Lys- 4' of histone H3, thereby playing a central role in histone code. 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. COFACTOR: Alpha-ketoglutarate. COFACTOR: Binds 1 Fe(2+) ion per subunit. SUBUNIT: Part of two distinct complexes, one containing E2F6, and the other containing REST. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Expressed in all tissues examined. Highest levels found in brain and skeletal muscle. DOMAIN: The first PHD-type zinc finger domain recognizes and binds H3-K9Me3. DOMAIN: Both the JmjC domain and the JmjN domain are required for enzymatic activity. DISEASE: Defects in KDM5C are the cause of mental retardation syndromic X-linked JARID1C-related (MRXSJ) [MIM:300534]. MRXSJ is characterized by significantly sub-average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. MRXSJ patients manifest mental retardation associated with variable features such as slowly progressive spastic paraplegia, seizures, facial dysmorphism. MISCELLANEOUS: Escapes X-inactivation. SIMILARITY: Belongs to the JARID1 histone demethylase family. SIMILARITY: Contains 1 ARID domain. SIMILARITY: Contains 1 JmjC domain. SIMILARITY: Contains 1 JmjN domain. SIMILARITY: Contains 2 PHD-type zinc fingers. WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/JARID1C";
Protein Domain and Structure Information
Press "+" in the title bar above to open this section.
