6by9: Difference between revisions

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<StructureSection load='6by9' size='340' side='right' caption='[[6by9]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='6by9' size='340' side='right' caption='[[6by9]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6by9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BY9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BY9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6by9]] is a 1 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=6BY9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BY9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EHMT1, EUHMTASE1, GLP, KIAA1876, KMT1D ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6by9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6by9 OCA], [http://pdbe.org/6by9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6by9 RCSB], [http://www.ebi.ac.uk/pdbsum/6by9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6by9 ProSAT]</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=6by9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6by9 OCA], [http://pdbe.org/6by9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6by9 RCSB], [http://www.ebi.ac.uk/pdbsum/6by9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6by9 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/EHMT1_HUMAN EHMT1_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 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. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53.<ref>PMID:12004135</ref> <ref>PMID:20118233</ref>   
[[http://www.uniprot.org/uniprot/EHMT1_HUMAN EHMT1_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 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. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53.<ref>PMID:12004135</ref> <ref>PMID:20118233</ref>   
==See Also==
*[[Histone methyltransferase|Histone methyltransferase]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith, C H]]
[[Category: Bountra, C]]
[[Category: Bountra, C]]
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[[Category: Edwards, A M]]
[[Category: Edwards, A M]]
[[Category: Han, S]]
[[Category: Han, S]]
[[Category: Li, A]]
[[Category: Penn, L]]
[[Category: Penn, L]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]

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