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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== |
| - | <StructureSection load='2ea6' size='340' side='right'caption='[[2ea6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2ea6' size='340' side='right'caption='[[2ea6]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ea6]] 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=2EA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EA6 FirstGlance]. <br> | + | <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> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RNF4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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> |
| | <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> | | <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 == |
| - | [[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>
| + | [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]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Harada, T]] | + | [[Category: Harada T]] |
| - | [[Category: Kigawa, T]] | + | [[Category: Kigawa T]] |
| - | [[Category: Koshiba, S]] | + | [[Category: Koshiba S]] |
| - | [[Category: Miyamoto, K]] | + | [[Category: Miyamoto K]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Tomizawa T]] |
| - | [[Category: Tomizawa, T]] | + | [[Category: Watanabe S]] |
| - | [[Category: Watanabe, S]] | + | [[Category: Yokoyama S]] |
| - | [[Category: Yokoyama, S]] | + | [[Category: Yoneyama M]] |
| - | [[Category: Yoneyama, M]] | + | |
| - | [[Category: National project on protein structural and functional analyse]]
| + | |
| - | [[Category: Nppsfa]]
| + | |
| - | [[Category: Res4-26]]
| + | |
| - | [[Category: Ring domain]]
| + | |
| - | [[Category: Ring finger protein 4]]
| + | |
| - | [[Category: Rnf4]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Zinc-binding domain]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4] [5] [6]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Kaiser FJ, Moroy T, Chang GT, Horsthemke B, Ludecke HJ. The RING finger protein RNF4, a co-regulator of transcription, interacts with the TRPS1 transcription factor. J Biol Chem. 2003 Oct 3;278(40):38780-5. Epub 2003 Jul 28. PMID:12885770 doi:http://dx.doi.org/10.1074/jbc.M306259200
- ↑ Tatham MH, Geoffroy MC, Shen L, Plechanovova A, Hattersley N, Jaffray EG, Palvimo JJ, Hay RT. RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat Cell Biol. 2008 May;10(5):538-46. doi: 10.1038/ncb1716. Epub 2008 Apr 13. PMID:18408734 doi:10.1038/ncb1716
- ↑ Guo B, Sharrocks AD. Extracellular signal-regulated kinase mitogen-activated protein kinase signaling initiates a dynamic interplay between sumoylation and ubiquitination to regulate the activity of the transcriptional activator PEA3. Mol Cell Biol. 2009 Jun;29(11):3204-18. doi: 10.1128/MCB.01128-08. Epub 2009 Mar , 23. PMID:19307308 doi:http://dx.doi.org/10.1128/MCB.01128-08
- ↑ Mukhopadhyay D, Arnaoutov A, Dasso M. The SUMO protease SENP6 is essential for inner kinetochore assembly. J Cell Biol. 2010 Mar 8;188(5):681-92. doi: 10.1083/jcb.200909008. PMID:20212317 doi:http://dx.doi.org/10.1083/jcb.200909008
- ↑ Geoffroy MC, Jaffray EG, Walker KJ, Hay RT. Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies. Mol Biol Cell. 2010 Dec;21(23):4227-39. doi: 10.1091/mbc.E10-05-0449. Epub 2010, Oct 13. PMID:20943951 doi:10.1091/mbc.E10-05-0449
- ↑ van Hagen M, Overmeer RM, Abolvardi SS, Vertegaal AC. RNF4 and VHL regulate the proteasomal degradation of SUMO-conjugated Hypoxia-Inducible Factor-2alpha. Nucleic Acids Res. 2010 Apr;38(6):1922-31. doi: 10.1093/nar/gkp1157. Epub 2009, Dec 21. PMID:20026589 doi:http://dx.doi.org/10.1093/nar/gkp1157
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