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| | <StructureSection load='4riq' size='340' side='right'caption='[[4riq]], [[Resolution|resolution]] 2.23Å' scene=''> | | <StructureSection load='4riq' size='340' side='right'caption='[[4riq]], [[Resolution|resolution]] 2.23Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4riq]] is a 24 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=4RIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RIQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4riq]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RIQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]), ASH2L, ASH2L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4riq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4riq OCA], [https://pdbe.org/4riq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4riq RCSB], [https://www.ebi.ac.uk/pdbsum/4riq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4riq ProSAT]</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=4riq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4riq OCA], [http://pdbe.org/4riq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4riq RCSB], [http://www.ebi.ac.uk/pdbsum/4riq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4riq 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/ASH2L_HUMAN ASH2L_HUMAN]] Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis.<ref>PMID:12670868</ref> <ref>PMID:19556245</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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Couture, J F]] | + | [[Category: Couture J-F]] |
| - | [[Category: Tremblay, V]] | + | [[Category: Tremblay V]] |
| - | [[Category: Allosteric regulator]]
| + | |
| - | [[Category: Ash2l]]
| + | |
| - | [[Category: Chromatin]]
| + | |
| - | [[Category: Dimerization/docking module]]
| + | |
| - | [[Category: Histone]]
| + | |
| - | [[Category: Methylation]]
| + | |
| - | [[Category: Mll1]]
| + | |
| - | [[Category: Mll2]]
| + | |
| - | [[Category: Mll3]]
| + | |
| - | [[Category: Mll4]]
| + | |
| - | [[Category: Rbbp5]]
| + | |
| - | [[Category: Set1a]]
| + | |
| - | [[Category: Set1b]]
| + | |
| - | [[Category: Transferase-protein binding complex]]
| + | |
| - | [[Category: Wdr5]]
| + | |
| 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]
Publication Abstract from PubMed
DPY-30 is a subunit of mammalian COMPASS-like complexes (complex of proteins associated with Set1) and regulates global histone H3 Lys-4 trimethylation. Here we report structural evidence showing that the incorporation of DPY-30 into COMPASS-like complexes is mediated by several hydrophobic interactions between an amphipathic alpha helix located on the C terminus of COMPASS subunit ASH2L and the inner surface of the DPY-30 dimerization/docking (D/D) module. Mutations impairing the interaction between ASH2L and DPY-30 result in a loss of histone H3K4me3 at the beta locus control region and cause a delay in erythroid cell terminal differentiation. Using overlay assays, we defined a consensus sequence for DPY-30 binding proteins and found that DPY-30 interacts with BAP18, a subunit of the nucleosome remodeling factor complex. Overall, our results indicate that the ASH2L/DPY-30 complex is important for cell differentiation and provide insights into the ability of DPY-30 to associate with functionally divergent multisubunit complexes.
Molecular Basis for DPY-30 Association to COMPASS-like and NURF Complexes.,Tremblay V, Zhang P, Chaturvedi CP, Thornton J, Brunzelle JS, Skiniotis G, Shilatifard A, Brand M, Couture JF Structure. 2014 Dec 2;22(12):1821-30. doi: 10.1016/j.str.2014.10.002. Epub 2014, Nov 20. PMID:25456412[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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
- ↑ Tremblay V, Zhang P, Chaturvedi CP, Thornton J, Brunzelle JS, Skiniotis G, Shilatifard A, Brand M, Couture JF. Molecular Basis for DPY-30 Association to COMPASS-like and NURF Complexes. Structure. 2014 Dec 2;22(12):1821-30. doi: 10.1016/j.str.2014.10.002. Epub 2014, Nov 20. PMID:25456412 doi:http://dx.doi.org/10.1016/j.str.2014.10.002
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