JMJD2A

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Jumonji domain containing 2A
PDB rendering based on 2gf7.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols JMJD2A ; JHDM3A; JMJD2; KIAA0677
External IDs Template:OMIM5 Template:MGI HomoloGene27780
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Jumonji domain containing 2A, also known as JMJD2A, is a human gene.[1]

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.[1]

References

  1. 1.0 1.1 "Entrez Gene: JMJD2A jumonji domain containing 2A".

Further reading

  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. PMID 8889548.
  • Ishikawa K, Nagase T, Suyama M; et al. (1998). "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 5 (3): 169–76. PMID 9734811.
  • 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): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • 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): 723–34. PMID 14527417.
  • Katoh M, Katoh M (2004). "Identification and characterization of JMJD2 family genes in silico". Int. J. Oncol. 24 (6): 1623–8. PMID 15138608.
  • 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): 707–16. 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): 1711–8. doi:10.1101/gr.2435604. PMID 15342556.
  • 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): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • 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): 28507–18. 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): 6404–14. doi:10.1128/MCB.25.15.6404-6414.2005. PMID 16024779.
  • 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): 591–8. 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. PMID 16415788.
  • 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): 748–51. 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): 467–81. 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): 315–21. 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): 312–6. 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): 742–6. doi:10.1016/j.bbrc.2007.05.179. PMID 17555712.
  • Chen Z, Zang J, Kappler J; et al. "Structural basis of the recognition of a methylated histone tail by JMJD2A". Proc. Natl. Acad. Sci. U.S.A. 104 (26): 10818–23. doi:10.1073/pnas.0704525104. PMID 17567753.
  • 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. PMID 18084306.

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