JMJD2A

Lysine (K)-specific demethylase 4A
PDB rendering based on 2gf7.
Available structures PDB 2GF7, 2GFA, 2GP3, 2GP5, 2OQ6, 2OQ7, 2OS2, 2OT7, 2OX0, 2P5B, 2PXJ, 2Q8C, 2Q8D, 2Q8E, 2QQR, 2QQS, 2VD7, 2WWJ
Identifiers
Symbols	KDM4A; JHDM3A; JMJD2; JMJD2A; KIAA0677
External IDs	OMIM: 609764 MGI: 2446210 HomoloGene: 27780 GeneCards: KDM4A Gene
EC number	1.14.11.-
Gene Ontology Molecular function • nucleic acid binding • protein binding • zinc ion binding • oxidoreductase activity • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen • metal ion binding • histone demethylase activity (H3-K36 specific) Cellular component • nucleus • nucleolus • cytoplasm • centrosome Biological process • chromatin modification • histone demethylation • interspecies interaction between organisms • negative regulation of transcription, DNA-dependent • histone H3-K36 demethylation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9682	230674
Ensembl	ENSG00000066135	ENSMUSG00000033326
UniProt	O75164	Q8BW72
RefSeq (mRNA)	NM_014663	NM_172382
RefSeq (protein)	NP_055478	NP_759014
Location (UCSC)	Chr 1: 44.12 – 44.17 Mb	Chr 4: 117.81 – 117.85 Mb
PubMed search	[1]	[2]

Lysine-specific demethylase 4A is an enzyme that in humans is encoded by the KDM4A gene.

This gene is a member of the Jumonji domain 2 (JMJD2) family and encodes a protein with 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.

Further reading

• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548. 
• Strausberg RL, Feingold EA, Grouse LH et al (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Yoon HG, Chan DW, Reynolds AB et al (2003). "N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso". Mol. Cell 12 (3): 723–734. doi:10.1016/j.molcel.2003.08.008. PMID 14527417. 
• Brandenberger R, Wei H, Zhang S et al (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–716. doi:10.1038/nbt971. PMID 15146197. 
• Suzuki Y, Yamashita R, Shirota M et al (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–1718. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=515316. 
• Gerhard DS, Wagner L, Feingold EA et al (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–2127. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Gray SG, Iglesias AH, Lizcano F et al (2005). "Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein". J. Biol. Chem. 280 (31): 28507–28518. doi:10.1074/jbc.M413687200. PMID 15927959. 
• Zhang D, Yoon HG, Wong J (2005). "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)". Mol. Cell. Biol. 25 (15): 6404–6414. doi:10.1128/MCB.25.15.6404-6414.2005. PMC 1190321. PMID 16024779. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1190321. 
• Tao WA, Wollscheid B, O'Brien R et al (2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry". Nat. Methods 2 (8): 591–598. doi:10.1038/nmeth776. PMID 16094384. 
• Kim J, Daniel J, Espejo A et al (2006). "Tudor, MBT and chromo domains gauge the degree of lysine methylation". EMBO Rep. 7 (4): 397–403. doi:10.1038/sj.embor.7400625. PMC 1456902. PMID 16415788. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1456902. 
• Huang Y, Fang J, Bedford MT et al (2006). "Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A". Science 312 (5774): 748–751. doi:10.1126/science.1125162. PMID 16601153. 
• Whetstine JR, Nottke A, Lan F et al (2006). "Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases". Cell 125 (3): 467–481. doi:10.1016/j.cell.2006.03.028. PMID 16603238. 
• Chen Z, Zang J, Whetstine J et al (2006). "Structural insights into histone demethylation by JMJD2 family members". Cell 125 (4): 691–702. doi:10.1016/j.cell.2006.04.024. PMID 16677698. 
• Gregory SG, Barlow KF, McLay KE et al (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature 441 (7091): 315–321. doi:10.1038/nature04727. PMID 16710414. 
• Klose RJ, Yamane K, Bae Y et al (2006). "The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36". Nature 442 (7100): 312–316. doi:10.1038/nature04853. PMID 16732292. 
• Shin S, Janknecht R (2007). "Activation of androgen receptor by histone demethylases JMJD2A and JMJD2D". Biochem. Biophys. Res. Commun. 359 (3): 742–746. doi:10.1016/j.bbrc.2007.05.179. PMID 17555712. 
• Chen Z, Zang J, Kappler J et al (2007). "Structural basis of the recognition of a methylated histone tail by JMJD2A". Proc. Natl. Acad. Sci. U.S.A. 104 (26): 10818–10823. doi:10.1073/pnas.0704525104. PMC 1891149. PMID 17567753. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1891149. 
• Ng SS, Kavanagh KL, McDonough MA et al (2007). "Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity". Nature 448 (7149): 87–91. doi:10.1038/nature05971. PMID 17589501. 
• Lee J, Thompson JR, Botuyan MV et al (2008). "Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor". Nat. Struct. Mol. Biol. 15 (q): 109–111. doi:10.1038/nsmb1326. PMC 2211384. PMID 18084306. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2211384.