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| | ==Solution structure of the TUDOR domain of PHD finger protein 19, isoform b [Homo sapiens]== | | ==Solution structure of the TUDOR domain of PHD finger protein 19, isoform b [Homo sapiens]== |
| - | <StructureSection load='2e5q' size='340' side='right' caption='[[2e5q]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2e5q' size='340' side='right'caption='[[2e5q]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2e5q]] 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=2E5Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E5Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2e5q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E5Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E5Q FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHF19 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHF19 ([https://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e5q OCA], [http://pdbe.org/2e5q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2e5q RCSB], [http://www.ebi.ac.uk/pdbsum/2e5q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2e5q ProSAT], [http://www.topsan.org/Proteins/RSGI/2e5q TOPSAN]</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=2e5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e5q OCA], [https://pdbe.org/2e5q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e5q RCSB], [https://www.ebi.ac.uk/pdbsum/2e5q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e5q ProSAT], [https://www.topsan.org/Proteins/RSGI/2e5q TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PHF19_HUMAN PHF19_HUMAN]] Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Probably involved in the transition from an active state to a repressed state in embryonic stem cells: acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting H3K36me3 histone demethylases NO66 or KDM2B, leading to demethylation of H3K36 and recruitment of the PRC2 complex that mediates H3K27me3 methylation, followed by de novo silencing. Recruits the PRC2 complex to CpG islands and contributes to embryonic stem cell self-renewal. Also binds dimethylated at 'Lys-36' (H3K36me2). Isoform 1 and isoform 2 inhibit transcription from an HSV-tk promoter.<ref>PMID:15563832</ref> <ref>PMID:21143197</ref> <ref>PMID:23104054</ref> <ref>PMID:23160351</ref> | + | [[https://www.uniprot.org/uniprot/PHF19_HUMAN PHF19_HUMAN]] Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Probably involved in the transition from an active state to a repressed state in embryonic stem cells: acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting H3K36me3 histone demethylases NO66 or KDM2B, leading to demethylation of H3K36 and recruitment of the PRC2 complex that mediates H3K27me3 methylation, followed by de novo silencing. Recruits the PRC2 complex to CpG islands and contributes to embryonic stem cell self-renewal. Also binds dimethylated at 'Lys-36' (H3K36me2). Isoform 1 and isoform 2 inhibit transcription from an HSV-tk promoter.<ref>PMID:15563832</ref> <ref>PMID:21143197</ref> <ref>PMID:23104054</ref> <ref>PMID:23160351</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Human]] | | [[Category: Human]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Dang, W]] | | [[Category: Dang, W]] |
| | [[Category: Inoue, M]] | | [[Category: Inoue, M]] |
| Structural highlights
Function
[PHF19_HUMAN] Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Probably involved in the transition from an active state to a repressed state in embryonic stem cells: acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting H3K36me3 histone demethylases NO66 or KDM2B, leading to demethylation of H3K36 and recruitment of the PRC2 complex that mediates H3K27me3 methylation, followed by de novo silencing. Recruits the PRC2 complex to CpG islands and contributes to embryonic stem cell self-renewal. Also binds dimethylated at 'Lys-36' (H3K36me2). Isoform 1 and isoform 2 inhibit transcription from an HSV-tk promoter.[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Wang S, Robertson GP, Zhu J. A novel human homologue of Drosophila polycomblike gene is up-regulated in multiple cancers. Gene. 2004 Dec 8;343(1):69-78. PMID:15563832 doi:http://dx.doi.org/10.1016/j.gene.2004.09.006
- ↑ Boulay G, Rosnoblet C, Guerardel C, Angrand PO, Leprince D. Functional characterization of human Polycomb-like 3 isoforms identifies them as components of distinct EZH2 protein complexes. Biochem J. 2011 Mar 1;434(2):333-42. doi: 10.1042/BJ20100944. PMID:21143197 doi:http://dx.doi.org/10.1042/BJ20100944
- ↑ Ballare C, Lange M, Lapinaite A, Martin GM, Morey L, Pascual G, Liefke R, Simon B, Shi Y, Gozani O, Carlomagno T, Benitah SA, Di Croce L. Phf19 links methylated Lys36 of histone H3 to regulation of Polycomb activity. Nat Struct Mol Biol. 2012 Oct 28. doi: 10.1038/nsmb.2434. PMID:23104054 doi:http://dx.doi.org/10.1038/nsmb.2434
- ↑ Brien GL, Gambero G, O'Connell DJ, Jerman E, Turner SA, Egan CM, Dunne EJ, Jurgens MC, Wynne K, Piao L, Lohan AJ, Ferguson N, Shi X, Sinha KM, Loftus BJ, Cagney G, Bracken AP. Polycomb PHF19 binds H3K36me3 and recruits PRC2 and demethylase NO66 to embryonic stem cell genes during differentiation. Nat Struct Mol Biol. 2012 Dec;19(12):1273-81. doi: 10.1038/nsmb.2449. Epub 2012, Nov 18. PMID:23160351 doi:http://dx.doi.org/10.1038/nsmb.2449
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