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Gene Review

KDM4A  -  lysine (K)-specific demethylase 4A

Homo sapiens

Synonyms: JHDM3A, JMJD2, JMJD2A, JmjC domain-containing histone demethylation protein 3A, Jumonji domain-containing protein 2A, ...
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Disease relevance of JMJD2A

  • Because JMJD2C gene (also known as GASC1 gene) is amplified in esophageal squamous cell carcinoma (ESCC), JMJD2 family genes are cancer-associated genes [1].
  • In HTLV-1 virus-infected cells, we find that JMJD2A binds to the viral Tax protein [2].
  • In this paper we describe the molecular characterization of a member of the Jumonji domain 2 (JMJD2) family of proteins, and demonstrate its binding to both class I HDACs and the retinoblastoma protein (pRb) [2].

High impact information on JMJD2A

  • For example, the JmjC-containing protein JMJD2A has been characterized as a H3-K9me3- and H3-K36me3-specific demethylase [3].
  • Here, structures of the catalytic-core domain of JMJD2A with and without alpha-ketoglutarate in the presence of Fe2+ have been determined by X-ray crystallography [3].
  • X-ray crystal structures of JMJD2A have solved in complex with the substrate peptides H3-K9me3/me2/me1 and H3-K36me3 [4].
  • Overexpression of JMJD2A but not a catalytically inactive mutant reduced H3-K9/K36 trimethylation levels in cultured cells [5].
  • In contrast, RNAi depletion of the C. elegans JMJD2A homolog resulted in an increase in general H3-K9Me3 and localized H3-K36Me3 levels on meiotic chromosomes and triggered p53-dependent germline apoptosis [5].
  • Reversal of Histone Lysine Trimethylation by the JMJD2 Family of Histone Demethylases [5].

Biological context of JMJD2A

  • Antibodies to JMJD2A recognize the native protein but also a half-sized protein fragment, the latter up-regulated in THP-1 cells during the G(2)/M phase of the cell cycle [2].
  • The ability of JMJD2A to associate with pRb and HDACs and potentiate pRb-mediated repression of E2F-regulated promoters implies an important role for this protein in cell proliferation and oncogenesis [2].
  • Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A [6].
  • Sited-directed mutagenesis in conjunction with demethylase activity assays allowed us to propose a molecular model for substrate selection by the JMJD2 histone demethylase family [3].

Anatomical context of JMJD2A

  • The first member of this group, JMJD2A, is widely expressed in human tissues and cell lines, and high endogenous expression of JMJD2A mRNA was found in several cell types, including human T-cell lymphotropic virus 1 (HTLV-1)-infected cell lines [2].

Associations of JMJD2A with chemical compounds

  • Here we demonstrate that JHDM3A (jumonji C (JmjC)-domain-containing histone demethylase 3A; also known as JMJD2A) is capable of removing the me3 group from modified H3 lysine 9 (H3K9) and H3 lysine 36 (H3K36) [7].

Other interactions of JMJD2A


  1. Identification and characterization of JMJD2 family genes in silico. Katoh, M., Katoh, M. Int. J. Oncol. (2004) [Pubmed]
  2. Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein. Gray, S.G., Iglesias, A.H., Lizcano, F., Villanueva, R., Camelo, S., Jingu, H., Teh, B.T., Koibuchi, N., Chin, W.W., Kokkotou, E., Dangond, F. J. Biol. Chem. (2005) [Pubmed]
  3. Structural insights into histone demethylation by JMJD2 family members. Chen, Z., Zang, J., Whetstine, J., Hong, X., Davrazou, F., Kutateladze, T.G., Simpson, M., Mao, Q., Pan, C.H., Dai, S., Hagman, J., Hansen, K., Shi, Y., Zhang, G. Cell (2006) [Pubmed]
  4. Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Ng, S.S., Kavanagh, K.L., McDonough, M.A., Butler, D., Pilka, E.S., Lienard, B.M., Bray, J.E., Savitsky, P., Gileadi, O., von Delft, F., Rose, N.R., Offer, J., Scheinost, J.C., Borowski, T., Sundstrom, M., Schofield, C.J., Oppermann, U. Nature. (2007) [Pubmed]
  5. Reversal of Histone Lysine Trimethylation by the JMJD2 Family of Histone Demethylases. Whetstine, J.R., Nottke, A., Lan, F., Huarte, M., Smolikov, S., Chen, Z., Spooner, E., Li, E., Zhang, G., Colaiacovo, M., Shi, Y. Cell (2006) [Pubmed]
  6. Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Huang, Y., Fang, J., Bedford, M.T., Zhang, Y., Xu, R.M. Science (2006) [Pubmed]
  7. The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36. Klose, R.J., Yamane, K., Bae, Y., Zhang, D., Erdjument-Bromage, H., Tempst, P., Wong, J., Zhang, Y. Nature (2006) [Pubmed]
  8. JMJD2A is a novel N-CoR-interacting protein and is involved in repression of the human transcription factor achaete scute-like homologue 2 (ASCL2/Hash2). Zhang, D., Yoon, H.G., Wong, J. Mol. Cell. Biol. (2005) [Pubmed]
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