JMJD2C tudor domain (human recombinant)

Tudor domains are small protein structural motifs of ~50 amino acids related to the “royal family” of methyl readers, which also includes chromo, MBT, PWWP, and Agenet-like domains. Tudor domains occur either alone, in tandem, or with other domains and are found in many proteins that are involved in RNA metabolism, germ cell development, transposon silencing, DNA damage response, histone modification, and chromatin remodeling. The tudor domains recognize symmetric methylated arginine or methylated lysine residues. JMJD2C is an α-ketoglutarate-dependent Fe (II) oxygenase that catalyzes the demethylation of trimethylated histone H3 at lysine residues 9 and 36 (H3K9me3 and H3K36me3). This protein product contains the tandem tudor domains of JMJD2C.

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[6] MARIANNE TERNDRUP PEDERSEN. The demethylase JMJD2C localizes to H3K4me3-positive transcription start sites and is dispensable for embryonic development.[J]. Molecular and Cellular Biology, 2014, 34 6: 1031-1045. DOI: 10.1128/mcb.00864-13