This gene is a member of the Jumonji domain 2 (JMJD2) family and encodes a protein containing a JmjN domain, a JmjC domain, a JD2H domain, two TUDOR domains, and two PHD-type zinc fingers. This nuclear protein functions as a trimethylation-specific demethylase, converting specific trimethylated histone residues to the dimethylated form, and as a transcriptional repressor. [provided by RefSeq, Apr 2009],
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Function:
cofactor:Binds 1 Fe(2+) ion per subunit.,Domain:The 2 Tudor domains recognize and bind methylated histone H3 'Lys-4' residue. Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails. Trimethylated H3 'Lys-4' is bound in a cage of 3 aromatic residues, 2 of which are from the Tudor domain 2, while the binding specificity is determined by side-chain interactions involving residues from the Tudor domain 1. The Tudor domains are able to bind trimethylated histone H3 'Lys-4', trimethylated histone H3 'Lys-9', di- and trimethylated H4 'Lys-20'.,Function:Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.,similarity:Belongs to the JHDM3 histone demethylase family.,similarity:Contains 1 JmjC domain.,similarity:Contains 1 JmjN domain.,similarity:Contains 2 PHD-type zinc fingers.,similarity:Contains 2 Tudor domains.,subunit:Interacts with histone deacetylase proteins HDAC1, HDAC2 and HDAC3. Interacts with RB and NCOR1. Interacts with HTLV-1 Tax protein.,tissue specificity:Ubiquitous.,