4e47
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4e47]] 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=4E47 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E47 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4e47]] 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=4E47 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E47 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0N6:(R)-(3-(3-CYANOPHENYL)-1-OXO-1-(PYRROLIDIN-1-YL)PROPAN-2-YL)-1,2,3,4-TETRAHYDROISOQUINOLINE-6-SULFONAMIDE'>0N6</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0N6:(R)-(3-(3-CYANOPHENYL)-1-OXO-1-(PYRROLIDIN-1-YL)PROPAN-2-YL)-1,2,3,4-TETRAHYDROISOQUINOLINE-6-SULFONAMIDE'>0N6</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SETD7, KIAA1717, KMT7, SET7, SET9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SETD7, KIAA1717, KMT7, SET7, SET9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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='activity'><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e47 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e47 RCSB], [http://www.ebi.ac.uk/pdbsum/4e47 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=4e47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e47 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e47 RCSB], [http://www.ebi.ac.uk/pdbsum/4e47 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SETD7_HUMAN SETD7_HUMAN]] Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.<ref>PMID:12588998</ref> <ref>PMID:15099517</ref> <ref>PMID:16141209</ref> <ref>PMID:17108971</ref> <ref>PMID:12540855</ref> <ref>PMID:15525938</ref> | ||
==See Also== | ==See Also== | ||
*[[Histone methyltransferase|Histone methyltransferase]] | *[[Histone methyltransferase|Histone methyltransferase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Histone-lysine N-methyltransferase]] | [[Category: Histone-lysine N-methyltransferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Arrowsmith, C H | + | [[Category: Arrowsmith, C H]] |
| - | [[Category: Barsyte, D | + | [[Category: Barsyte, D]] |
| - | [[Category: Bountra, C | + | [[Category: Bountra, C]] |
| - | [[Category: Brown, P J | + | [[Category: Brown, P J]] |
| - | [[Category: Bunnage, M | + | [[Category: Bunnage, M]] |
| - | [[Category: Cook, A | + | [[Category: Cook, A]] |
| - | [[Category: Dong, A | + | [[Category: Dong, A]] |
| - | [[Category: Edwards, A M | + | [[Category: Edwards, A M]] |
| - | [[Category: Fish, P | + | [[Category: Fish, P]] |
| - | [[Category: Ouyang, H | + | [[Category: Ouyang, H]] |
| - | [[Category: Owen, D | + | [[Category: Owen, D]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: Tatlock, J | + | [[Category: Tatlock, J]] |
| - | [[Category: Vedadi, M | + | [[Category: Vedadi, M]] |
| - | [[Category: Walker, J R | + | [[Category: Walker, J R]] |
| - | [[Category: Weigelt, J | + | [[Category: Weigelt, J]] |
[[Category: Chromatin regulator]] | [[Category: Chromatin regulator]] | ||
[[Category: Chromosomal protein]] | [[Category: Chromosomal protein]] | ||
| Line 39: | Line 43: | ||
[[Category: Set domain]] | [[Category: Set domain]] | ||
[[Category: Sgc]] | [[Category: Sgc]] | ||
| - | [[Category: Structural genomics consortium]] | ||
[[Category: Ternary complex]] | [[Category: Ternary complex]] | ||
[[Category: Transcription]] | [[Category: Transcription]] | ||
Revision as of 08:18, 25 December 2014
SET7/9 in complex with inhibitor (R)-(3-(3-cyanophenyl)-1-oxo-1-(pyrrolidin-1-yl)propan-2-yl)-1,2,3,4-tetrahydroisoquinoline-6- sulfonamide and S-adenosylmethionine
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Categories: Histone-lysine N-methyltransferase | Homo sapiens | Arrowsmith, C H | Barsyte, D | Bountra, C | Brown, P J | Bunnage, M | Cook, A | Dong, A | Edwards, A M | Fish, P | Ouyang, H | Owen, D | Structural genomic | Tatlock, J | Vedadi, M | Walker, J R | Weigelt, J | Chromatin regulator | Chromosomal protein | Inhibitor | Methyltransferase | Nucleus | S-adenosylmethionine | Set domain | Sgc | Ternary complex | Transcription | Transcription regulation | Transferase | Transferase-transferase inhibitor complex
