6ved - Revision history

OCA at 11:05, 14 June 2023

OCA — Wed, 14 Jun 2023 11:05:31 GMT

←Older revision		Revision as of 11:05, 14 June 2023
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	==Solution structure of the TTD and linker region of UHRF1==		==Solution structure of the TTD and linker region of UHRF1==
-	<StructureSection load='6ved' size='340' side='right'caption='[[6ved~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='6ved' size='340' side='right'caption='[[6ved]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6ved]] 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=6VED OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6VED FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6ved]] 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=6VED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VED FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UHRF1, ICBP90, NP95, RNF106 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</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=6ved FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ved OCA], [https://pdbe.org/6ved PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ved RCSB], [https://www.ebi.ac.uk/pdbsum/6ved PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ved ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </span></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6ved FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ved OCA], [~~http~~://pdbe.org/6ved PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6ved RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6ved PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6ved ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/UHRF1_HUMAN UHRF1_HUMAN]] Note=Defects in UHRF1 may be a cause of cancers. Overexpressed in many different forms of human cancers, including bladder, breast, cervical, colorectal and prostate cancers, as well as pancreatic adenocarcinomas, rhabdomyosarcomas and gliomas. Plays an important role in the correlation of histone modification and gene silencing in cancer progression. Expression is associated with a poor prognosis in patients with various cancers, suggesting that it participates in cancer progression.	+	[https://www.uniprot.org/uniprot/UHRF1_HUMAN UHRF1_HUMAN] Note=Defects in UHRF1 may be a cause of cancers. Overexpressed in many different forms of human cancers, including bladder, breast, cervical, colorectal and prostate cancers, as well as pancreatic adenocarcinomas, rhabdomyosarcomas and gliomas. Plays an important role in the correlation of histone modification and gene silencing in cancer progression. Expression is associated with a poor prognosis in patients with various cancers, suggesting that it participates in cancer progression.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/UHRF1_HUMAN UHRF1_HUMAN]] Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. May be involved in DNA repair.<ref>PMID:10646863</ref> <ref>PMID:15009091</ref> <ref>PMID:15361834</ref> <ref>PMID:17673620</ref> <ref>PMID:17967883</ref> <ref>PMID:19056828</ref> <ref>PMID:21745816</ref> <ref>PMID:22945642</ref> <ref>PMID:21777816</ref>	+	[https://www.uniprot.org/uniprot/UHRF1_HUMAN UHRF1_HUMAN] Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. May be involved in DNA repair.<ref>PMID:10646863</ref> <ref>PMID:15009091</ref> <ref>PMID:15361834</ref> <ref>PMID:17673620</ref> <ref>PMID:17967883</ref> <ref>PMID:19056828</ref> <ref>PMID:21745816</ref> <ref>PMID:22945642</ref> <ref>PMID:21777816</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 6ved" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6ved" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Ubiquitin protein ligase 3D structures\|Ubiquitin protein ligase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: RING-type E3 ubiquitin transferase]]~~	+	[[Category: Arrowsmith CH]]
-	[[Category: Arrowsmith~~, C H~~]]	+	[[Category: Duan S]]
-	[[Category: Duan, S]]	+	[[Category: Houliston S]]
-	[[Category: Houliston, S]]	+	[[Category: Lemak A]]
-	[[Category: Lemak, A]]	+	[[Category: Ong MS]]
-	[[Category: Ong~~, M S]]~~	+
-	~~[[Category: H3k9me3]]~~	+
-	~~[[Category: Histone]]~~	+
-	~~[[Category: Peptide binding protein]]~~	+
-	~~[[Category: Tandem tudor domain]]~~	+
-	~~[[Category: Uhrf1~~]]	+

OCA at 11:34, 26 August 2020

OCA — Wed, 26 Aug 2020 11:34:07 GMT

←Older revision		Revision as of 11:34, 26 August 2020
Line 1:		Line 1:

	==Solution structure of the TTD and linker region of UHRF1==		==Solution structure of the TTD and linker region of UHRF1==
-	<StructureSection load='6ved' size='340' side='right'caption='[[6ved]]' scene=''>	+	<StructureSection load='6ved' size='340' side='right'caption='[[6ved]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full ~~crystallographic~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VED OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VED FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6ved]] 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=6VED OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VED FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ved FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ved OCA], [http://pdbe.org/6ved PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ved RCSB], [http://www.ebi.ac.uk/pdbsum/6ved PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ved ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UHRF1, ICBP90, NP95, RNF106 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ved FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ved OCA], [http://pdbe.org/6ved PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ved RCSB], [http://www.ebi.ac.uk/pdbsum/6ved PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ved ProSAT]</span></td></tr>
	</table>		</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/UHRF1_HUMAN UHRF1_HUMAN]] Note=Defects in UHRF1 may be a cause of cancers. Overexpressed in many different forms of human cancers, including bladder, breast, cervical, colorectal and prostate cancers, as well as pancreatic adenocarcinomas, rhabdomyosarcomas and gliomas. Plays an important role in the correlation of histone modification and gene silencing in cancer progression. Expression is associated with a poor prognosis in patients with various cancers, suggesting that it participates in cancer progression.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/UHRF1_HUMAN UHRF1_HUMAN]] Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. May be involved in DNA repair.<ref>PMID:10646863</ref> <ref>PMID:15009091</ref> <ref>PMID:15361834</ref> <ref>PMID:17673620</ref> <ref>PMID:17967883</ref> <ref>PMID:19056828</ref> <ref>PMID:21745816</ref> <ref>PMID:22945642</ref> <ref>PMID:21777816</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	UHRF1 is an important epigenetic regulator associated with apoptosis and tumour development. It is a multidomain protein that integrates readout of different histone modification states and DNA methylation with enzymatic histone ubiquitylation activity. Emerging evidence indicates that the chromatin-binding and enzymatic modules of UHRF1 do not act in isolation but interplay in a coordinated and regulated manner. Here, we compared two splicing variants (V1, V2) of murine UHRF1 (mUHRF1) with human UHRF1 (hUHRF1). We show that insertion of nine amino acids in a linker region connecting the different TTD and PHD histone modification-binding domains causes distinct H3K9me3-binding behaviour of mUHRF1 V1. Structural analysis suggests that in mUHRF1 V1, in contrast to V2 and hUHRF1, the linker is anchored in a surface groove of the TTD domain, resulting in creation of a coupled TTD-PHD module. This establishes multivalent, synergistic H3-tail binding causing distinct cellular localization and enhanced H3K9me3-nucleosome ubiquitylation activity. In contrast to hUHRF1, H3K9me3-binding of the murine proteins is not allosterically regulated by phosphatidylinositol 5-phosphate that interacts with a separate less-conserved polybasic linker region of the protein. Our results highlight the importance of flexible linkers in regulating multidomain chromatin binding proteins and point to divergent evolution of their regulation.
		+
		+	Alternative splicing and allosteric regulation modulate the chromatin binding of UHRF1.,Tauber M, Kreuz S, Lemak A, Mandal P, Yerkesh Z, Veluchamy A, Al-Gashgari B, Aljahani A, Cortes-Medina LV, Azhibek D, Fan L, Ong MS, Duan S, Houliston S, Arrowsmith CH, Fischle W Nucleic Acids Res. 2020 Aug 20;48(14):7728-7747. doi: 10.1093/nar/gkaa520. PMID:32609811<ref>PMID:32609811</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6ved" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Arrowsmith CH]]	+	[[Category: RING-type E3 ubiquitin transferase]]
-	[[Category: Duan S]]	+	[[Category: Arrowsmith, C H]]
-	[[Category: Houliston S]]	+	[[Category: Duan, S]]
-	[[Category: Lemak A]]	+	[[Category: Houliston, S]]
-	[[Category: Ong MS]]	+	[[Category: Lemak, A]]
		+	[[Category: Ong, M S]]
		+	[[Category: H3k9me3]]
		+	[[Category: Histone]]
		+	[[Category: Peptide binding protein]]
		+	[[Category: Tandem tudor domain]]
		+	[[Category: Uhrf1]]

OCA at 10:13, 17 June 2020

OCA — Wed, 17 Jun 2020 10:13:38 GMT

←Older revision		Revision as of 10:13, 17 June 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6ved ~~is ON HOLD until Paper Publication~~	+	==Solution structure of the TTD and linker region of UHRF1==
-		+	<StructureSection load='6ved' size='340' side='right'caption='[[6ved]]' scene=''>
-	~~Authors~~: ~~Lemak~~, A., ~~Houliston, S~~., ~~Duan, S~~., ~~Ong, M~~.S., ~~Arrowsmith, C~~.H.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VED OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VED FirstGlance]. <br>
-	~~Description: Solution structure of the TTD and linker region of UHRF1~~	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ved FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ved OCA], [http://pdbe.org/6ved PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ved RCSB], [http://www.ebi.ac.uk/pdbsum/6ved PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ved ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: ~~Lemak, A~~]]	+	__TOC__
-	[[Category: ~~Arrowsmith, C.H~~]]	+	</StructureSection>
-	[[Category: Houliston, S]]	+	[[Category: Large Structures]]
-	[[Category: ~~Ong, M.S~~]]	+	[[Category: Arrowsmith CH]]
-	[[Category: ~~Duan, S~~]]	+	[[Category: Duan S]]
		+	[[Category: Houliston S]]
		+	[[Category: Lemak A]]
		+	[[Category: Ong MS]]

OCA at 05:34, 4 March 2020

OCA — Wed, 04 Mar 2020 05:34:12 GMT

←Older revision		Revision as of 05:34, 4 March 2020
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6ved is ON HOLD	+	The entry 6ved is ON HOLD until Paper Publication

	Authors: Lemak, A., Houliston, S., Duan, S., Ong, M.S., Arrowsmith, C.H.		Authors: Lemak, A., Houliston, S., Duan, S., Ong, M.S., Arrowsmith, C.H.

OCA: Protected "6ved" [edit=sysop:move=sysop]

OCA — Wed, 08 Jan 2020 06:14:02 GMT

Protected "6ved" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:14, 8 January 2020

OCA: New page: '''Unreleased structure''' The entry 6ved is ON HOLD Authors: Lemak, A., Houliston, S., Duan, S., Ong, M.S., Arrowsmith, C.H. Description: Solution structure of the TTD and linker regi...

OCA — Wed, 08 Jan 2020 06:14:00 GMT

New page: '''Unreleased structure''' The entry 6ved is ON HOLD Authors: Lemak, A., Houliston, S., Duan, S., Ong, M.S., Arrowsmith, C.H. Description: Solution structure of the TTD and linker regi...

New page

'''Unreleased structure'''

The entry 6ved is ON HOLD

Authors: Lemak, A., Houliston, S., Duan, S., Ong, M.S., Arrowsmith, C.H.

Description: Solution structure of the TTD and linker region of UHRF1
[[Category: Unreleased Structures]]
[[Category: Lemak, A]]
[[Category: Arrowsmith, C.H]]
[[Category: Houliston, S]]
[[Category: Ong, M.S]]
[[Category: Duan, S]]