4ppe - Revision history

OCA at 12:42, 1 March 2024

OCA — Fri, 01 Mar 2024 12:42:26 GMT

←Older revision		Revision as of 12:42, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ppe]] is a 2 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=4PPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PPE FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ppe]] is a 2 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=4PPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PPE 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">X-ray diffraction, [[Resolution\|Resolution]] 2Å</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=4ppe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ppe OCA], [https://pdbe.org/4ppe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ppe RCSB], [https://www.ebi.ac.uk/pdbsum/4ppe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ppe ProSAT]</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=4ppe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ppe OCA], [https://pdbe.org/4ppe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ppe RCSB], [https://www.ebi.ac.uk/pdbsum/4ppe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ppe ProSAT]</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>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The post-translational modification of DNA repair and checkpoint proteins by ubiquitin and small ubiquitin-like modifier (SUMO) critically orchestrates the DNA damage response (DDR). The ubiquitin ligase RNF4 integrates signaling by SUMO and ubiquitin, through its selective recognition and ubiquitination of SUMO-modified proteins. Here, we define a key new determinant for target discrimination by RNF4, in addition to interaction with SUMO. We identify a nucleosome-targeting motif within the RNF4 RING domain that can bind DNA and thereby enables RNF4 to selectively ubiquitinate nucleosomal histones. Furthermore, RNF4 nucleosome-targeting is crucially required for the repair of TRF2-depleted dysfunctional telomeres by 53BP1-mediated non-homologous end joining.
-
-	RNF4 interacts with both SUMO and nucleosomes to promote the DNA damage response.,Groocock LM, Nie M, Prudden J, Moiani D, Wang T, Cheltsov A, Rambo RP, Arvai AS, Hitomi C, Tainer JA, Luger K, Perry JJ, Lazzerini-Denchi E, Boddy MN EMBO Rep. 2014 May;15(5):601-8. doi: 10.1002/embr.201338369. Epub 2014 Apr 8. PMID:24714598<ref>PMID:24714598</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4ppe" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 07:23, 8 February 2023

OCA — Wed, 08 Feb 2023 07:23:01 GMT

←Older revision		Revision as of 07:23, 8 February 2023
Line 1:		Line 1:

	==human RNF4 RING domain==		==human RNF4 RING domain==
-	<StructureSection load='4ppe' size='340' side='right' caption='[[4ppe]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='4ppe' size='340' side='right'caption='[[4ppe]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ppe]] is a 2 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=4PPE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4PPE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ppe]] is a 2 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=4PPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PPE FirstGlance]. <br>
-	</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>~~	+	</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='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RES4-26, RNF4, SNURF ([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=4ppe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ppe OCA], [https://pdbe.org/4ppe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ppe RCSB], [https://www.ebi.ac.uk/pdbsum/4ppe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ppe 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=4ppe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ppe OCA], [~~http~~://pdbe.org/4ppe PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ppe RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ppe PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ppe ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[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>	+	[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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 20:

	==See Also==		==See Also==
-	*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]	+	*[[Ubiquitin protein ligase 3D structures\|Ubiquitin protein ligase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Arvai, A S~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Hitomi, C~~]]	+	[[Category: Arvai AS]]
-	[[Category: ~~Perry, J J~~]]	+	[[Category: Hitomi C]]
-	[[Category: ~~Tainer, J A~~]]	+	[[Category: Perry JJ]]
-	[[Category: ~~Ligase]]~~	+	[[Category: Tainer JA]]
-	~~[[Category: Ring domain]]~~	+
-	~~[[Category: Ubiquitin ligase~~]]	+

OCA at 17:04, 4 January 2017

OCA — Wed, 04 Jan 2017 17:04:55 GMT

←Older revision		Revision as of 17:04, 4 January 2017
Line 1:		Line 1:
		+
	==human RNF4 RING domain==		==human RNF4 RING domain==
	<StructureSection load='4ppe' size='340' side='right' caption='[[4ppe]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4ppe' size='340' side='right' caption='[[4ppe]], [[Resolution\|resolution]] 2.00Å' scene=''>
Line 5:		Line 6:
	</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>		</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>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RES4-26, RNF4, SNURF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RES4-26, RNF4, SNURF ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ppe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ppe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ppe RCSB], [http://www.ebi.ac.uk/pdbsum/4ppe PDBsum]</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=4ppe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ppe OCA], [http://pdbe.org/4ppe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ppe RCSB], [http://www.ebi.ac.uk/pdbsum/4ppe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ppe ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4ppe" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 08:00, 25 February 2015

OCA — Wed, 25 Feb 2015 08:00:00 GMT

←Older revision		Revision as of 08:00, 25 February 2015
Line 9:		Line 9:
	== Function ==		== Function ==
	[[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>		[[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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The post-translational modification of DNA repair and checkpoint proteins by ubiquitin and small ubiquitin-like modifier (SUMO) critically orchestrates the DNA damage response (DDR). The ubiquitin ligase RNF4 integrates signaling by SUMO and ubiquitin, through its selective recognition and ubiquitination of SUMO-modified proteins. Here, we define a key new determinant for target discrimination by RNF4, in addition to interaction with SUMO. We identify a nucleosome-targeting motif within the RNF4 RING domain that can bind DNA and thereby enables RNF4 to selectively ubiquitinate nucleosomal histones. Furthermore, RNF4 nucleosome-targeting is crucially required for the repair of TRF2-depleted dysfunctional telomeres by 53BP1-mediated non-homologous end joining.
		+
		+	RNF4 interacts with both SUMO and nucleosomes to promote the DNA damage response.,Groocock LM, Nie M, Prudden J, Moiani D, Wang T, Cheltsov A, Rambo RP, Arvai AS, Hitomi C, Tainer JA, Luger K, Perry JJ, Lazzerini-Denchi E, Boddy MN EMBO Rep. 2014 May;15(5):601-8. doi: 10.1002/embr.201338369. Epub 2014 Apr 8. PMID:24714598<ref>PMID:24714598</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==

OCA at 04:33, 25 December 2014

OCA — Thu, 25 Dec 2014 04:33:34 GMT

←Older revision		Revision as of 04:33, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4ppe~~\| ~~PDB~~=4ppe \| ~~SCENE~~= }}	+	==human RNF4 RING domain==
-	===~~human~~ RNF4 ~~RING domain~~===	+	<StructureSection load='4ppe' size='340' side='right' caption='[[4ppe]], [[Resolution\|resolution]] 2.00Å' scene=''>
-		+	== Structural highlights ==
-	==Function==	+	<table><tr><td colspan='2'>[[4ppe]] is a 2 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=4PPE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PPE FirstGlance]. <br>
		+	</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>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RES4-26, RNF4, SNURF ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ppe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ppe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ppe RCSB], [http://www.ebi.ac.uk/pdbsum/4ppe PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[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>		[[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>

-	==~~About this Structure~~==	+	==See Also==
-	[[~~4ppe~~]] ~~is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PPE OCA].~~	+	*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
-	[[Category: Arvai, A S.]]	+	</StructureSection>
-	[[Category: Hitomi, C.]]	+	[[Category: Human]]
-	[[Category: Perry, J J.]]	+	[[Category: Arvai, A S]]
-	[[Category: Tainer, J A.]]	+	[[Category: Hitomi, C]]
		+	[[Category: Perry, J J]]
		+	[[Category: Tainer, J A]]
	[[Category: Ligase]]		[[Category: Ligase]]
	[[Category: Ring domain]]		[[Category: Ring domain]]
	[[Category: Ubiquitin ligase]]		[[Category: Ubiquitin ligase]]

OCA at 09:40, 26 March 2014

OCA — Wed, 26 Mar 2014 09:40:57 GMT

←Older revision		Revision as of 09:40, 26 March 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4ppe\| PDB=4ppe \| SCENE= }}
		+	===human RNF4 RING domain===

-	~~The entry 4ppe is ON HOLD~~	+	==Function==
		+	[[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>

-	~~Authors~~: ~~Perry, J.J., Arvai, A.S~~.~~, Hitomi, C~~.~~, Tainer, J~~.A.	+	==About this Structure==
		+	[[4ppe]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PPE OCA].

-	~~Description~~: ~~human RNF4 RING~~ domain	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Arvai, A S.]]
		+	[[Category: Hitomi, C.]]
		+	[[Category: Perry, J J.]]
		+	[[Category: Tainer, J A.]]
		+	[[Category: Ligase]]
		+	[[Category: Ring domain]]
		+	[[Category: Ubiquitin ligase]]

OCA: Protected "4ppe" [edit=sysop:move=sysop]

OCA — Wed, 12 Mar 2014 12:33:44 GMT

Protected "4ppe" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:33, 12 March 2014

OCA: New page: '''Unreleased structure''' The entry 4ppe is ON HOLD Authors: Perry, J.J., Arvai, A.S., Hitomi, C., Tainer, J.A. Description: human RNF4 RING domain

OCA — Wed, 12 Mar 2014 12:33:42 GMT

New page: '''Unreleased structure''' The entry 4ppe is ON HOLD Authors: Perry, J.J., Arvai, A.S., Hitomi, C., Tainer, J.A. Description: human RNF4 RING domain

New page

'''Unreleased structure'''

The entry 4ppe is ON HOLD

Authors: Perry, J.J., Arvai, A.S., Hitomi, C., Tainer, J.A.

Description: human RNF4 RING domain