其他名稱: KDM5C; DXS1272E; JARID1C; SMCX; XE169; Lysine-specific demethylase 5C; Histone demethylase JARID1C; Jumonji/ARID domain-containing protein 1C; Protein SmcX; Protein Xe169
功能: cofactor:Alpha-ketoglutarate.,cofactor:Fe(2+).,disease:Defects in KDM5C are a cause of X-linked mental retardation (XLMR) [MIM:300534]. Mental retardation is usually defined as cognitive impairment with an IQ less than 70. Etiologically, mental retardation is a very heterogeneous condition that involves environmental, stochastic and/or genetic factors.,domain:Both the JmjC domain and the JmjN domain are required for enzymatic activity.,domain:The first PHD-type zinc finger domain recognizes and binds H3-K9Me3.,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.,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.,subunit:Part of two distinct complexes, one containing E2F6, and the other containing REST.,tissue specificity:Expressed in all tissues examined. Highest levels found in brain and skeletal muscle.,
其他名稱: KDM5C; DXS1272E; JARID1C; SMCX; XE169; Lysine-specific demethylase 5C; Histone demethylase JARID1C; Jumonji/ARID domain-containing protein 1C; Protein SmcX; Protein Xe169
功能: cofactor:Alpha-ketoglutarate.,cofactor:Fe(2+).,disease:Defects in KDM5C are a cause of X-linked mental retardation (XLMR) [MIM:300534]. Mental retardation is usually defined as cognitive impairment with an IQ less than 70. Etiologically, mental retardation is a very heterogeneous condition that involves environmental, stochastic and/or genetic factors.,domain:Both the JmjC domain and the JmjN domain are required for enzymatic activity.,domain:The first PHD-type zinc finger domain recognizes and binds H3-K9Me3.,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.,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.,subunit:Part of two distinct complexes, one containing E2F6, and the other containing REST.,tissue specificity:Expressed in all tissues examined. Highest levels found in brain and skeletal muscle.,