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| ==Solution structure of the Bright/ARID domain from the human JARID1C protein.== | | ==Solution structure of the Bright/ARID domain from the human JARID1C protein.== |
- | <StructureSection load='2jrz' size='340' side='right'caption='[[2jrz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2jrz' size='340' side='right'caption='[[2jrz]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2jrz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JRZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JRZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jrz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JRZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JRZ FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">JARID1C, DXS1272E, SMCX, XE169 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2jrz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jrz OCA], [http://pdbe.org/2jrz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jrz RCSB], [http://www.ebi.ac.uk/pdbsum/2jrz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jrz ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jrz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jrz OCA], [https://pdbe.org/2jrz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jrz RCSB], [https://www.ebi.ac.uk/pdbsum/2jrz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jrz ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Disease == | | == Disease == |
- | [[http://www.uniprot.org/uniprot/KDM5C_HUMAN KDM5C_HUMAN]] Syndromic X-linked intellectual disability due to JARID1C mutation. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/KDM5C_HUMAN KDM5C_HUMAN] Syndromic X-linked intellectual disability due to JARID1C mutation. The disease is caused by mutations affecting the gene represented in this entry. |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/KDM5C_HUMAN KDM5C_HUMAN]] Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Participates in transcriptional repression of neuronal genes by recruiting histone deacetylases and REST at neuron-restrictive silencer elements. Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2 (By similarity).[UniProtKB:P41230]<ref>PMID:17320160</ref> <ref>PMID:17320161</ref> <ref>PMID:17468742</ref> | + | [https://www.uniprot.org/uniprot/KDM5C_HUMAN KDM5C_HUMAN] Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Participates in transcriptional repression of neuronal genes by recruiting histone deacetylases and REST at neuron-restrictive silencer elements. Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2 (By similarity).[UniProtKB:P41230]<ref>PMID:17320160</ref> <ref>PMID:17320161</ref> <ref>PMID:17468742</ref> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Arrowsmith, C H]] | + | [[Category: Arrowsmith CH]] |
- | [[Category: Ball, L J]] | + | [[Category: Ball LJ]] |
- | [[Category: Bishop, S]] | + | [[Category: Bishop S]] |
- | [[Category: Diehl, A]] | + | [[Category: Diehl A]] |
- | [[Category: Dowler, E F]] | + | [[Category: Dowler EF]] |
- | [[Category: Edwards, A]] | + | [[Category: Edwards A]] |
- | [[Category: Koehler, C]] | + | [[Category: Koehler C]] |
- | [[Category: Leidert, M]] | + | [[Category: Leidert M]] |
- | [[Category: Oschkinat, H]] | + | [[Category: Oschkinat H]] |
- | [[Category: Structural genomic]]
| + | [[Category: Schmieder P]] |
- | [[Category: Schmieder, P]] | + | [[Category: Sundstrom M]] |
- | [[Category: Sundstrom, M]] | + | [[Category: Wiegelt J]] |
- | [[Category: Wiegelt, J]] | + | |
- | [[Category: Bright/arid domain]]
| + | |
- | [[Category: Helical]]
| + | |
- | [[Category: Jarid1c]]
| + | |
- | [[Category: Oxidoreductase]]
| + | |
- | [[Category: Sgc]]
| + | |
| Structural highlights
Disease
KDM5C_HUMAN Syndromic X-linked intellectual disability due to JARID1C mutation. The disease is caused by mutations affecting the gene represented in this entry.
Function
KDM5C_HUMAN Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Participates in transcriptional repression of neuronal genes by recruiting histone deacetylases and REST at neuron-restrictive silencer elements. Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2 (By similarity).[UniProtKB:P41230][1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
We have assigned 1H, 13C and 15N resonances of the Bright/ARID DNA-binding domain from the human JARID1C protein, a newly discovered histone demethylase belonging to the JmjC domain-containing protein family.
Backbone and sidechain 1H, 13C and 15N resonance assignments of the Bright/ARID domain from the human JARID1C (SMCX) protein.,Koehler C, Bishop S, Dowler EF, Schmieder P, Diehl A, Oschkinat H, Ball LJ Biomol NMR Assign. 2008 Jun;2(1):9-11. Epub 2007 Dec 8. PMID:19636912[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Iwase S, Lan F, Bayliss P, de la Torre-Ubieta L, Huarte M, Qi HH, Whetstine JR, Bonni A, Roberts TM, Shi Y. The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases. Cell. 2007 Mar 23;128(6):1077-88. Epub 2007 Feb 22. PMID:17320160 doi:10.1016/j.cell.2007.02.017
- ↑ Christensen J, Agger K, Cloos PA, Pasini D, Rose S, Sennels L, Rappsilber J, Hansen KH, Salcini AE, Helin K. RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3. Cell. 2007 Mar 23;128(6):1063-76. Epub 2007 Feb 22. PMID:17320161 doi:S0092-8674(07)00182-1
- ↑ Tahiliani M, Mei P, Fang R, Leonor T, Rutenberg M, Shimizu F, Li J, Rao A, Shi Y. The histone H3K4 demethylase SMCX links REST target genes to X-linked mental retardation. Nature. 2007 May 31;447(7144):601-5. Epub 2007 Apr 29. PMID:17468742 doi:nature05823
- ↑ Koehler C, Bishop S, Dowler EF, Schmieder P, Diehl A, Oschkinat H, Ball LJ. Backbone and sidechain 1H, 13C and 15N resonance assignments of the Bright/ARID domain from the human JARID1C (SMCX) protein. Biomol NMR Assign. 2008 Jun;2(1):9-11. Epub 2007 Dec 8. PMID:19636912 doi:10.1007/s12104-007-9071-7
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