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. Part of two distinct complexes, one containing E2F6, and the other containing REST. Expressed in all tissues examined. Highest levels found in brain and skeletal muscle. Belongs to the JARID1 histone demethylase family. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 1.14.11.-; Demethylase; Oxidoreductase
Cellular Component: nucleus
Molecular Function: histone demethylase activity (H3-K4 specific); DNA binding; zinc ion binding; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Biological Process: transcription, DNA-dependent; regulation of transcription, DNA-dependent
SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.