EC 1.14.11.67 - [histone H3]-trimethyl-L-lysine4 demethylase

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IntEnz Enzyme Nomenclature
EC 1.14.11.67

Names

Accepted name:
[histone H3]-trimethyl-L-lysine4 demethylase
Systematic name:
[histone H3]-N6,N6,N6-trimethyl-L-lysine4,2-oxoglutarate:oxygen oxidoreductase

Reaction

Comments:

Requires iron(II). This entry describes a group of enzymes that demethylate N-methylated L-lysine residues at position 4 of histone H3 (H3K4). The enzymes are dioxygenases and act by hydroxylating the methyl group, forming an unstable hemiaminal that leaves as formaldehyde. They can act on tri-, di-, and mono-methylated forms.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0034647
UniProtKB/Swiss-Prot: (34) [show] [UniProt]

References

  1. Seward, D. J., Cubberley, G., Kim, S., Schonewald, M., Zhang, L., Tripet, B., Bentley, D. L.
    Demethylation of trimethylated histone H3 Lys4 in vivo by JARID1 JmjC proteins.
    Nat. Struct. Mol. Biol. 14 : 240-242 (2007). [PMID: 17310255]
  2. Klose, R. J., Yan, Q., Tothova, Z., Yamane, K., Erdjument-Bromage, H., Tempst, P., Gilliland, D. G., Zhang, Y., Kaelin, W. G.
    The retinoblastoma binding protein RBP2 is an H3K4 demethylase.
    Cell 128 : 889-900 (2007). [PMID: 17320163]
  3. Iwase, S., Lan, F., Bayliss, P., de la Torre-Ubieta, L., Huarte, M., Qi, H. H., Whetstine, J. R., Bonni, A., Roberts, T. M., Shi, Y.
    The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases.
    Cell 128 : 1077-1088 (2007). [PMID: 17320160]
  4. Christensen, J., Agger, K., Cloos, P. A., Pasini, D., Rose, S., Sennels, L., Rappsilber, J., Hansen, K. H., Salcini, A. E., Helin, K.
    RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3.
    Cell 128 : 1063-1076 (2007). [PMID: 17320161]

[EC 1.14.11.67 created 2019]