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3m54
From Proteopedia
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<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=3m54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m54 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m54 RCSB], [http://www.ebi.ac.uk/pdbsum/3m54 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=3m54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m54 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m54 RCSB], [http://www.ebi.ac.uk/pdbsum/3m54 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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 05:53, 25 December 2014
SET7/9 Y305F in complex with TAF10 peptide and AdoHcy
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Categories: Histone-lysine N-methyltransferase | Homo sapiens | Brunzelle, J S | Couture, J F | Dirk, L M | Houtz, R L | Rizzo, P A.Del | Roiko, M S | Strunk, B S | Trievel, R C | Chromatin regulator | Chromosomal protein | Methyltransferase | Nucleus | S-adenosyl-l-homocysteine | S-adenosyl-l-methionine | Set domain | Taf10 peptide | Ternary complex | Transcription | Transcription regulation | Transferase

