2xxz
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=2xxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xxz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xxz RCSB], [http://www.ebi.ac.uk/pdbsum/2xxz 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=2xxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xxz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xxz RCSB], [http://www.ebi.ac.uk/pdbsum/2xxz PDBsum]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/KDM6B_HUMAN KDM6B_HUMAN]] Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Involved in inflammatory response by participating in macrophage differentiation in case of inflammation by regulating gene expression and macrophage differentiation.<ref>PMID:17825402</ref> <ref>PMID:17851529</ref> | ||
+ | == 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: Burgess-Brown, N | + | [[Category: Burgess-Brown, N]] |
- | [[Category: Che, K H | + | [[Category: Che, K H]] |
- | [[Category: Daniel, M | + | [[Category: Daniel, M]] |
- | [[Category: Edwards, A | + | [[Category: Edwards, A]] |
- | [[Category: Filippakopoulos, P | + | [[Category: Filippakopoulos, P]] |
- | [[Category: Krojer, T | + | [[Category: Krojer, T]] |
- | [[Category: Muniz, J R.C | + | [[Category: Muniz, J R.C]] |
- | [[Category: Ng, S S | + | [[Category: Ng, S S]] |
- | [[Category: Oppermann, U | + | [[Category: Oppermann, U]] |
- | [[Category: Savitsky, P | + | [[Category: Savitsky, P]] |
- | [[Category: Tumber, A | + | [[Category: Tumber, A]] |
- | [[Category: Ugochukwu, E | + | [[Category: Ugochukwu, E]] |
- | [[Category: Weigelt, J | + | [[Category: Weigelt, J]] |
- | [[Category: Yue, W W | + | [[Category: Yue, W W]] |
[[Category: Chromatin modification]] | [[Category: Chromatin modification]] | ||
[[Category: Histone demethylation]] | [[Category: Histone demethylation]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Oxygenase]] | [[Category: Oxygenase]] |
Revision as of 08:35, 25 December 2014
CRYSTAL STRUCTURE OF THE HUMAN JMJD3 JUMONJI DOMAIN
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Categories: Homo sapiens | Arrowsmith, C | Bountra, C | Burgess-Brown, N | Che, K H | Daniel, M | Edwards, A | Filippakopoulos, P | Krojer, T | Muniz, J R.C | Ng, S S | Oppermann, U | Savitsky, P | Tumber, A | Ugochukwu, E | Weigelt, J | Yue, W W | Chromatin modification | Histone demethylation | Oxidoreductase | Oxygenase