4nvq
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4nvq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NVQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NVQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[4nvq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NVQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NVQ FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2OD:5-METHOXY-6-[3-(PYRROLIDIN-1-YL)PROPOXY]SPIRO[CYCLOBUTANE-1,3-INDOL]-2-AMINE'>2OD</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2OD:5-METHOXY-6-[3-(PYRROLIDIN-1-YL)PROPOXY]SPIRO[CYCLOBUTANE-1,3-INDOL]-2-AMINE'>2OD</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EHMT2, BAT8, C6orf30, G9A, KMT1C, NG36 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EHMT2, BAT8, C6orf30, G9A, KMT1C, NG36 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nvq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nvq RCSB], [http://www.ebi.ac.uk/pdbsum/4nvq PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nvq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nvq RCSB], [http://www.ebi.ac.uk/pdbsum/4nvq PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/EHMT2_HUMAN EHMT2_HUMAN]] Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself.<ref>PMID:8457211</ref> <ref>PMID:11316813</ref> <ref>PMID:18438403</ref> <ref>PMID:20118233</ref> <ref>PMID:22387026</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| - | [[Category: Brown, P J | + | [[Category: Brown, P J]] |
| - | [[Category: Chiang, G G | + | [[Category: Chiang, G G]] |
| - | [[Category: Guo, J | + | [[Category: Guo, J]] |
| - | [[Category: Li, F | + | [[Category: Li, F]] |
| - | [[Category: Maag, D | + | [[Category: Maag, D]] |
| - | [[Category: Michaelides, M R | + | [[Category: Michaelides, M R]] |
| - | [[Category: Pappano, W N | + | [[Category: Pappano, W N]] |
| - | [[Category: Petros, A M | + | [[Category: Petros, A M]] |
| - | [[Category: Pliushchev, M | + | [[Category: Pliushchev, M]] |
| - | [[Category: Soni, N B | + | [[Category: Soni, N B]] |
| - | [[Category: Sweis, R F | + | [[Category: Sweis, R F]] |
| - | [[Category: Tse, C | + | [[Category: Tse, C]] |
| - | [[Category: Vedadi, M | + | [[Category: Vedadi, M]] |
[[Category: Lysine methyl transferase]] | [[Category: Lysine methyl transferase]] | ||
[[Category: Transferase-transferase inhibitor complex]] | [[Category: Transferase-transferase inhibitor complex]] | ||
Revision as of 08:21, 24 December 2014
Human G9a in Complex with Inhibitor A-366
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