JmjC domain-containing histone demethylation protein 3A; Jumonji domain-containing protein 2A (MJD2A, JHDM3, JMJD2, KDM4A, KIAA0677)

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Function

histone demethylase
specifically demethylates Lys-9 & Lys-36 residues of histone H3, thus plays a role in histone code
does not demethylate histone H3 Lys-4, H3 Lys-27 nor histone H4 Lys-20
demethylates trimethylated histone H3 Lys-9 & H3 Lys-36, while it has no activity on mono- & dimethylated residues
demethylation of Lys generates formaldehyde & succinate
role in transcriptional repression of ASCL2 & E2F-responsive promoters via recruitment of histone deacetylases & NCOR1, respectively
interacts with histone deacetylase proteins HDAC1, HDAC2 & HDAC3
interacts with RB & NCOR1

Cofactor: binds 1 Fe+2 per subunit

belongs to the JHDM3 histone demethylase family
contains 1 JmjC domain
contains 1 JmjN domain
contains 2 PHD-type zinc fingers
contains 2 Tudor domains Tudor domains recognize & bind methylated histone H3 Lys-4 Double Tudor domain has an interdigitated structure & 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 Tudor domains are able to bind trimethylated histone H3 Lys-4, trimethylated histone H3 Lys-9, di- & trimethylated H4 Lys-20