2ea6

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==Solution Structure of the RING domain of the human ring finger protein 4==
==Solution Structure of the RING domain of the human ring finger protein 4==
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<StructureSection load='2ea6' size='340' side='right' caption='[[2ea6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2ea6' size='340' side='right'caption='[[2ea6]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ea6]] 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=2EA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EA6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ea6]] 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=2EA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EA6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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">RNF4 ([http://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>
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<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=2ea6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ea6 OCA], [http://pdbe.org/2ea6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ea6 RCSB], [http://www.ebi.ac.uk/pdbsum/2ea6 PDBsum], [http://www.topsan.org/Proteins/RSGI/2ea6 TOPSAN]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ea6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ea6 OCA], [https://pdbe.org/2ea6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ea6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ea6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ea6 ProSAT], [https://www.topsan.org/Proteins/RSGI/2ea6 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/RNF4_HUMAN RNF4_HUMAN]] E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation.<ref>PMID:12885770</ref> <ref>PMID:18408734</ref> <ref>PMID:19307308</ref> <ref>PMID:20212317</ref> <ref>PMID:20943951</ref> <ref>PMID:20026589</ref>
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[https://www.uniprot.org/uniprot/RNF4_HUMAN RNF4_HUMAN] E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation.<ref>PMID:12885770</ref> <ref>PMID:18408734</ref> <ref>PMID:19307308</ref> <ref>PMID:20212317</ref> <ref>PMID:20943951</ref> <ref>PMID:20026589</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ea/2ea6_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ea/2ea6_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ea6 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
== References ==
== References ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Harada, T]]
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[[Category: Large Structures]]
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[[Category: Kigawa, T]]
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[[Category: Harada T]]
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[[Category: Koshiba, S]]
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[[Category: Kigawa T]]
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[[Category: Miyamoto, K]]
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[[Category: Koshiba S]]
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[[Category: Structural genomic]]
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[[Category: Miyamoto K]]
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[[Category: Tomizawa, T]]
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[[Category: Tomizawa T]]
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[[Category: Watanabe, S]]
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[[Category: Watanabe S]]
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[[Category: Yokoyama, S]]
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[[Category: Yokoyama S]]
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[[Category: Yoneyama, M]]
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[[Category: Yoneyama M]]
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[[Category: National project on protein structural and functional analyse]]
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[[Category: Nppsfa]]
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[[Category: Res4-26]]
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[[Category: Ring domain]]
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[[Category: Ring finger protein 4]]
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[[Category: Rnf4]]
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[[Category: Rsgi]]
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[[Category: Transcription]]
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[[Category: Zinc-binding domain]]
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Current revision

Solution Structure of the RING domain of the human ring finger protein 4

PDB ID 2ea6

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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