2o8j

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:33, 30 August 2023) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Human euchromatic histone methyltransferase 2==
==Human euchromatic histone methyltransferase 2==
-
<StructureSection load='2o8j' size='340' side='right' caption='[[2o8j]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+
<StructureSection load='2o8j' size='340' side='right'caption='[[2o8j]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2o8j]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O8J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O8J FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2o8j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O8J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O8J FirstGlance]. <br>
-
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EHMT2, BAT8, G9A, NG36 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o8j OCA], [https://pdbe.org/2o8j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o8j RCSB], [https://www.ebi.ac.uk/pdbsum/2o8j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o8j ProSAT]</span></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=2o8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o8j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o8j RCSB], [http://www.ebi.ac.uk/pdbsum/2o8j PDBsum]</span></td></tr>
+
</table>
-
<table>
+
== Function ==
 +
[https://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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
-
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o8/2o8j_consurf.spt"</scriptWhenChecked>
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o8/2o8j_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
-
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2o8j ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
Line 26: Line 28:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
 +
<div class="pdbe-citations 2o8j" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
-
*[[Histone methyltransferase|Histone methyltransferase]]
+
*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Histone-lysine N-methyltransferase]]
 
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Antoshenko, T.]]
+
[[Category: Large Structures]]
-
[[Category: Arrowsmith, C H.]]
+
[[Category: Antoshenko T]]
-
[[Category: Bochkarev, A.]]
+
[[Category: Arrowsmith CH]]
-
[[Category: Edwards, A M.]]
+
[[Category: Bochkarev A]]
-
[[Category: Loppnau, P.]]
+
[[Category: Edwards AM]]
-
[[Category: Min, J.]]
+
[[Category: Loppnau P]]
-
[[Category: Plotnikov, A N.]]
+
[[Category: Min J]]
-
[[Category: SGC, Structural Genomics Consortium.]]
+
[[Category: Plotnikov AN]]
-
[[Category: Sundstrom, M.]]
+
[[Category: Sundstrom M]]
-
[[Category: Weigelt, J.]]
+
[[Category: Weigelt J]]
-
[[Category: Wu, H.]]
+
[[Category: Wu H]]
-
[[Category: Bat8]]
+
-
[[Category: G9a]]
+
-
[[Category: Hla-b-associated transcript 8]]
+
-
[[Category: Ng36/g9a]]
+
-
[[Category: Sgc]]
+
-
[[Category: Structural genomic]]
+
-
[[Category: Structural genomics consortium]]
+
-
[[Category: Transferase]]
+

Current revision

Human euchromatic histone methyltransferase 2

PDB ID 2o8j

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2o8j"
Personal tools