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| | <StructureSection load='4rt4' size='340' side='right'caption='[[4rt4]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='4rt4' size='340' side='right'caption='[[4rt4]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4rt4]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RT4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RT4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4rt4]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RT4 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DPY30 ([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">X-ray diffraction, [[Resolution|Resolution]] 1.997Å</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=4rt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rt4 OCA], [http://pdbe.org/4rt4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rt4 RCSB], [http://www.ebi.ac.uk/pdbsum/4rt4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rt4 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=4rt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rt4 OCA], [https://pdbe.org/4rt4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rt4 RCSB], [https://www.ebi.ac.uk/pdbsum/4rt4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rt4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DPY30_HUMAN DPY30_HUMAN]] As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In a teratocarcinoma cell, plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. May also play an indirect or direct role in endosomal transport.<ref>PMID:19556245</ref> <ref>PMID:19651892</ref> <ref>PMID:21335234</ref> [[http://www.uniprot.org/uniprot/BRE2_YEAST BRE2_YEAST]] The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.<ref>PMID:11742990</ref> <ref>PMID:11805083</ref> | + | [https://www.uniprot.org/uniprot/DPY30_HUMAN DPY30_HUMAN] As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In a teratocarcinoma cell, plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. May also play an indirect or direct role in endosomal transport.<ref>PMID:19556245</ref> <ref>PMID:19651892</ref> <ref>PMID:21335234</ref> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chang, W R]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Li, M]] | + | [[Category: Chang WR]] |
| - | [[Category: Zhang, H M]] | + | [[Category: Li M]] |
| - | [[Category: H3k4 methylation]] | + | [[Category: Zhang HM]] |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: X-type helix]]
| + | |
| Structural highlights
Function
DPY30_HUMAN As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In a teratocarcinoma cell, plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. May also play an indirect or direct role in endosomal transport.[1] [2] [3]
References
- ↑ Patel A, Dharmarajan V, Vought VE, Cosgrove MS. On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex. J Biol Chem. 2009 Sep 4;284(36):24242-56. Epub 2009 Jun 25. PMID:19556245 doi:M109.014498
- ↑ Xu Z, Gong Q, Xia B, Groves B, Zimmermann M, Mugler C, Mu D, Matsumoto B, Seaman M, Ma D. A role of histone H3 lysine 4 methyltransferase components in endosomal trafficking. J Cell Biol. 2009 Aug 10;186(3):343-53. doi: 10.1083/jcb.200902146. Epub 2009 Aug, 3. PMID:19651892 doi:http://dx.doi.org/10.1083/jcb.200902146
- ↑ Jiang H, Shukla A, Wang X, Chen WY, Bernstein BE, Roeder RG. Role for Dpy-30 in ES cell-fate specification by regulation of H3K4 methylation within bivalent domains. Cell. 2011 Feb 18;144(4):513-25. doi: 10.1016/j.cell.2011.01.020. PMID:21335234 doi:http://dx.doi.org/10.1016/j.cell.2011.01.020
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