2e6s

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==Solution structure of the PHD domain in RING finger protein 107==
==Solution structure of the PHD domain in RING finger protein 107==
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<StructureSection load='2e6s' size='340' side='right'caption='[[2e6s]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2e6s' size='340' side='right'caption='[[2e6s]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2e6s]] 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=2E6S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E6S FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2e6s]] 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=2E6S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E6S FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UHRF2, NIRF, RNF107 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2e6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e6s OCA], [https://pdbe.org/2e6s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e6s RCSB], [https://www.ebi.ac.uk/pdbsum/2e6s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e6s ProSAT], [https://www.topsan.org/Proteins/RSGI/2e6s 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=2e6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e6s OCA], [https://pdbe.org/2e6s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e6s RCSB], [https://www.ebi.ac.uk/pdbsum/2e6s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e6s ProSAT], [https://www.topsan.org/Proteins/RSGI/2e6s TOPSAN]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/UHRF2_HUMAN UHRF2_HUMAN]] Associated with various cancers. DNA copy number loss is found in multiple kinds of malignancies originating from the brain, breast, stomach, kidney, hematopoietic tissue and lung.
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[https://www.uniprot.org/uniprot/UHRF2_HUMAN UHRF2_HUMAN] Associated with various cancers. DNA copy number loss is found in multiple kinds of malignancies originating from the brain, breast, stomach, kidney, hematopoietic tissue and lung.
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/UHRF2_HUMAN UHRF2_HUMAN]] E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. E3 SUMO-, but not ubiquitin-, protein ligase for ZNF131.<ref>PMID:12176013</ref> <ref>PMID:15178429</ref> <ref>PMID:14741369</ref> <ref>PMID:15361834</ref> <ref>PMID:21952639</ref> <ref>PMID:23404503</ref>
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[https://www.uniprot.org/uniprot/UHRF2_HUMAN UHRF2_HUMAN] E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. E3 SUMO-, but not ubiquitin-, protein ligase for ZNF131.<ref>PMID:12176013</ref> <ref>PMID:15178429</ref> <ref>PMID:14741369</ref> <ref>PMID:15361834</ref> <ref>PMID:21952639</ref> <ref>PMID:23404503</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>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: He, F]]
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[[Category: He F]]
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[[Category: Inoue, M]]
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[[Category: Inoue M]]
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[[Category: Kadirvel, S]]
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[[Category: Kadirvel S]]
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[[Category: Kigawa, T]]
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[[Category: Kigawa T]]
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[[Category: Muto, Y]]
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[[Category: Muto Y]]
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[[Category: Structural genomic]]
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[[Category: Shirouzu M]]
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[[Category: Shirouzu, M]]
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[[Category: Terada T]]
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[[Category: Terada, T]]
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[[Category: Yokoyama S]]
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[[Category: Yokoyama, S]]
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[[Category: Cell cycle]]
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[[Category: National project on protein structural and functional analyse]]
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[[Category: Nppsfa]]
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[[Category: Phd domain]]
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[[Category: Rsgi]]
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Current revision

Solution structure of the PHD domain in RING finger protein 107

PDB ID 2e6s

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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