2xml
From Proteopedia
(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=2xml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xml OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xml RCSB], [http://www.ebi.ac.uk/pdbsum/2xml 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=2xml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xml OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xml RCSB], [http://www.ebi.ac.uk/pdbsum/2xml PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/KDM4C_HUMAN KDM4C_HUMAN]] Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.<ref>PMID:16603238</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> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Arrowsmith, C | + | [[Category: Arrowsmith, C]] |
| - | [[Category: Bountra, C | + | [[Category: Bountra, C]] |
| - | [[Category: Carpenter, L | + | [[Category: Carpenter, L]] |
| - | [[Category: Delft, F Von | + | [[Category: Delft, F Von]] |
| - | [[Category: Edwards, A | + | [[Category: Edwards, A]] |
| - | [[Category: Gileadi, C | + | [[Category: Gileadi, C]] |
| - | [[Category: Krojer, T | + | [[Category: Krojer, T]] |
| - | [[Category: Ng, S | + | [[Category: Ng, S]] |
| - | [[Category: Oppermann, U | + | [[Category: Oppermann, U]] |
| - | [[Category: Pike, A C.W | + | [[Category: Pike, A C.W]] |
| - | [[Category: Weigelt, J | + | [[Category: Weigelt, J]] |
| - | [[Category: Yue, W W | + | [[Category: Yue, W W]] |
[[Category: Metal binding]] | [[Category: Metal binding]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Transcription regulation]] | [[Category: Transcription regulation]] | ||
Revision as of 16:29, 25 December 2014
Crystal structure of human JMJD2C catalytic domain
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