| 释义 |
- Function
- References
- Further reading
{{Infobox_gene}}Lysine-specific demethylase 4A is an enzyme that in humans is encoded by the KDM4A gene.[1][2][3] Function 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 belongs to the alpha-ketoglutarate-dependent hydroxylase superfamily. It functions as a trimethylation-specific demethylase, converting specific trimethylated histone on histone H3 lysine 9 and 36 residues to the dimethylated form and lysine 9 dimethylated residues to monomethyl, and as a transcriptional repressor.[3] Alterations in this gene have been found associated with chromosomal instability that leads to cancer.({{PMID|23871696}}) References 1. ^{{cite journal | vauthors = Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O | title = 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 | journal = DNA Research | volume = 5 | issue = 3 | pages = 169–76 | date = June 1998 | pmid = 9734811 | pmc = | doi = 10.1093/dnares/5.3.169 }}
2. ^{{cite journal | vauthors = Katoh M, Katoh M | title = Identification and characterization of JMJD2 family genes in silico | journal = International Journal of Oncology | volume = 24 | issue = 6 | pages = 1623–8 | date = June 2004 | pmid = 15138608 | pmc = | doi = 10.3892/ijo.25.3.759 }}
3. ^1 {{cite web | title = Entrez Gene: JMJD2A jumonji domain containing 2A| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9682| accessdate = }}
Further reading {{refbegin | 2}}- {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Research | volume = 6 | issue = 9 | pages = 791–806 | date = September 1996 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
- {{cite journal | vauthors = Yoon HG, Chan DW, Reynolds AB, Qin J, Wong J | title = N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso | journal = Molecular Cell | volume = 12 | issue = 3 | pages = 723–34 | date = September 2003 | pmid = 14527417 | doi = 10.1016/j.molcel.2003.08.008 }}
- {{cite journal | vauthors = Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW | title = Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation | journal = Nature Biotechnology | volume = 22 | issue = 6 | pages = 707–16 | date = June 2004 | pmid = 15146197 | doi = 10.1038/nbt971 }}
- {{cite journal | vauthors = Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S | title = Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions | journal = Genome Research | volume = 14 | issue = 9 | pages = 1711–8 | date = September 2004 | pmid = 15342556 | pmc = 515316 | doi = 10.1101/gr.2435604 }}
- {{cite journal | vauthors = Gray SG, Iglesias AH, Lizcano F, Villanueva R, Camelo S, Jingu H, Teh BT, Koibuchi N, Chin WW, Kokkotou E, Dangond F | title = Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein | journal = The Journal of Biological Chemistry | volume = 280 | issue = 31 | pages = 28507–18 | date = August 2005 | pmid = 15927959 | doi = 10.1074/jbc.M413687200 }}
- {{cite journal | vauthors = Zhang D, Yoon HG, Wong J | title = 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) | journal = Molecular and Cellular Biology | volume = 25 | issue = 15 | pages = 6404–14 | date = August 2005 | pmid = 16024779 | pmc = 1190321 | doi = 10.1128/MCB.25.15.6404-6414.2005 }}
- {{cite journal | vauthors = Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R | title = Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry | journal = Nature Methods | volume = 2 | issue = 8 | pages = 591–8 | date = August 2005 | pmid = 16094384 | doi = 10.1038/nmeth776 }}
- {{cite journal | vauthors = Kim J, Daniel J, Espejo A, Lake A, Krishna M, Xia L, Zhang Y, Bedford MT | title = Tudor, MBT and chromo domains gauge the degree of lysine methylation | journal = EMBO Reports | volume = 7 | issue = 4 | pages = 397–403 | date = April 2006 | pmid = 16415788 | pmc = 1456902 | doi = 10.1038/sj.embor.7400625 }}
- {{cite journal | vauthors = Huang Y, Fang J, Bedford MT, Zhang Y, Xu RM | title = Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A | journal = Science | volume = 312 | issue = 5774 | pages = 748–51 | date = May 2006 | pmid = 16601153 | doi = 10.1126/science.1125162 }}
- {{cite journal | vauthors = Whetstine JR, Nottke A, Lan F, Huarte M, Smolikov S, Chen Z, Spooner E, Li E, Zhang G, Colaiacovo M, Shi Y | title = Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases | journal = Cell | volume = 125 | issue = 3 | pages = 467–81 | date = May 2006 | pmid = 16603238 | doi = 10.1016/j.cell.2006.03.028 }}
- {{cite journal | vauthors = Chen Z, Zang J, Whetstine J, Hong X, Davrazou F, Kutateladze TG, Simpson M, Mao Q, Pan CH, Dai S, Hagman J, Hansen K, Shi Y, Zhang G | title = Structural insights into histone demethylation by JMJD2 family members | journal = Cell | volume = 125 | issue = 4 | pages = 691–702 | date = May 2006 | pmid = 16677698 | doi = 10.1016/j.cell.2006.04.024 }}
- {{cite journal | vauthors = Klose RJ, Yamane K, Bae Y, Zhang D, Erdjument-Bromage H, Tempst P, Wong J, Zhang Y | title = The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36 | journal = Nature | volume = 442 | issue = 7100 | pages = 312–6 | date = July 2006 | pmid = 16732292 | doi = 10.1038/nature04853 }}
- {{cite journal | vauthors = Shin S, Janknecht R | title = Activation of androgen receptor by histone demethylases JMJD2A and JMJD2D | journal = Biochemical and Biophysical Research Communications | volume = 359 | issue = 3 | pages = 742–6 | date = August 2007 | pmid = 17555712 | doi = 10.1016/j.bbrc.2007.05.179 }}
- {{cite journal | vauthors = Chen Z, Zang J, Kappler J, Hong X, Crawford F, Wang Q, Lan F, Jiang C, Whetstine J, Dai S, Hansen K, Shi Y, Zhang G | title = Structural basis of the recognition of a methylated histone tail by JMJD2A | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 104 | issue = 26 | pages = 10818–23 | date = June 2007 | pmid = 17567753 | pmc = 1891149 | doi = 10.1073/pnas.0704525104 }}
- {{cite journal | vauthors = Ng SS, Kavanagh KL, McDonough MA, Butler D, Pilka ES, Lienard BM, Bray JE, Savitsky P, Gileadi O, von Delft F, Rose NR, Offer J, Scheinost JC, Borowski T, Sundstrom M, Schofield CJ, Oppermann U | title = Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity | journal = Nature | volume = 448 | issue = 7149 | pages = 87–91 | date = July 2007 | pmid = 17589501 | doi = 10.1038/nature05971 }}
- {{cite journal | vauthors = Lee J, Thompson JR, Botuyan MV, Mer G | title = Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor | journal = Nature Structural & Molecular Biology | volume = 15 | issue = 1 | pages = 109–11 | date = January 2008 | pmid = 18084306 | pmc = 2211384 | doi = 10.1038/nsmb1326 }}
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