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6mm1
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the cysteine-rich region from human EHMT2== | |
| - | + | <StructureSection load='6mm1' size='340' side='right'caption='[[6mm1]], [[Resolution|resolution]] 1.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6mm1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MM1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MM1 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | [[Category: | + | <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=6mm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mm1 OCA], [http://pdbe.org/6mm1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mm1 RCSB], [http://www.ebi.ac.uk/pdbsum/6mm1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mm1 ProSAT]</span></td></tr> |
| + | </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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Briknarova, K]] | [[Category: Briknarova, K]] | ||
| - | [[Category: | + | [[Category: Kerchner, K M]] |
| - | [[Category: | + | [[Category: Mou, T C]] |
| - | [[Category: Sprang, S | + | [[Category: Sprang, S R]] |
| + | [[Category: Cysteine-rich region]] | ||
| + | [[Category: Ring-like]] | ||
| + | [[Category: Transferase]] | ||
| + | [[Category: Zinc-binding]] | ||
Revision as of 10:26, 2 October 2019
Structure of the cysteine-rich region from human EHMT2
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