3mek: Difference between revisions
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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=3mek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mek OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mek RCSB], [http://www.ebi.ac.uk/pdbsum/3mek 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=3mek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mek OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mek RCSB], [http://www.ebi.ac.uk/pdbsum/3mek PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/SMYD3_HUMAN SMYD3_HUMAN]] Histone methyltransferase. Specifically methylates 'Lys-4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.<ref>PMID:15235609</ref> <ref>PMID:22419068</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 04:13, 25 December 2014
Crystal Structure of Human Histone-Lysine N-methyltransferase SMYD3 in Complex with S-adenosyl-L-methionine
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Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Histone-lysine N-methyltransferase
- Homo sapiens
- Arrowsmith, C H
- Bochkarev, A
- Bountra, C
- Dombrovski, L
- Edwards, A M
- Lam, R
- Li, Y
- Min, J
- Structural genomic
- Weigelt, J
- Wu, H
- Chromatin modification
- Chromatin regulator
- Di-methylation
- Dna-binding
- Histone h3
- Histone methyltransferase
- Metal-binding
- Methyltransferase
- Mynd-type zinc finger
- Nucleus
- S-adenosyl-l-methionine
- Set and mynd domain-containing protein 3
- Set domain
- Sgc
- Transcriptional activation
- Transferase
- Tri-methylation
- Zinc finger mynd domain-containing protein 1
- Zinc-finger
