3lmn - Revision history

OCA at 08:40, 6 September 2023

OCA — Wed, 06 Sep 2023 08:40:52 GMT

←Older revision		Revision as of 08:40, 6 September 2023
Line 1:		Line 1:

	==Oligomeric structure of the DUSP domain of human USP15==		==Oligomeric structure of the DUSP domain of human USP15==
-	<StructureSection load='3lmn' size='340' side='right' caption='[[3lmn]], [[Resolution\|resolution]] 2.15Å' scene=''>	+	<StructureSection load='3lmn' size='340' side='right'caption='[[3lmn]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3lmn]] 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=3LMN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3LMN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3lmn]] 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=3LMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LMN FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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]] 2.15Å</td></tr>
-	~~<tr~~ id~~='related'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Related_structure~~\|~~Related:]]</b></td><td class="sblockDat">[[1w6v\|1w6v~~]]</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>KIAA0529, USP15 ([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=3lmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lmn OCA], [https://pdbe.org/3lmn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lmn RCSB], [https://www.ebi.ac.uk/pdbsum/3lmn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lmn 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/Ubiquitin_thiolesterase Ubiquitin thiolesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15]~~ </~~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=3lmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lmn OCA], [~~http~~://pdbe.org/3lmn PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3lmn RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3lmn PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3lmn ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/UBP15_HUMAN UBP15_HUMAN]] Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal (PubMed:22344298). Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway.<ref>PMID:16005295</ref> <ref>PMID:17318178</ref> <ref>PMID:19826004</ref> <ref>PMID:19576224</ref> <ref>PMID:19553310</ref> <ref>PMID:21947082</ref> <ref>PMID:22344298</ref>	+	[https://www.uniprot.org/uniprot/UBP15_HUMAN UBP15_HUMAN] Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal (PubMed:22344298). Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway.<ref>PMID:16005295</ref> <ref>PMID:17318178</ref> <ref>PMID:19826004</ref> <ref>PMID:19576224</ref> <ref>PMID:19553310</ref> <ref>PMID:21947082</ref> <ref>PMID:22344298</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 24:		Line 22:

	==See Also==		==See Also==
-	*[[Thioesterase\|Thioesterase]]	+	*[[Thioesterase 3D structures\|Thioesterase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Ubiquitin thiolesterase~~]]	+	[[Category: Large Structures]]
-	[[Category: Alenkin, D]]	+	[[Category: Alenkin D]]
-	[[Category: Arrowsmith~~, C H~~]]	+	[[Category: Arrowsmith CH]]
-	[[Category: Asinas, A]]	+	[[Category: Asinas A]]
-	[[Category: Avvakumov~~, G V~~]]	+	[[Category: Avvakumov GV]]
-	[[Category: Bochkarev, A]]	+	[[Category: Bochkarev A]]
-	[[Category: Bountra, C]]	+	[[Category: Bountra C]]
-	[[Category: Dhe-Paganon, S]]	+	[[Category: Dhe-Paganon S]]
-	[[Category: Edwards~~, A M~~]]	+	[[Category: Edwards AM]]
-	[[Category: Walker~~, J R~~]]	+	[[Category: Walker JR]]
-	[[Category: Weigelt, J]]	+	[[Category: Weigelt J]]
-	~~[[Category: Acetylation]]~~	+
-	~~[[Category: Alternative splicing]]~~	+
-	~~[[Category: Cleavage]]~~	+
-	~~[[Category: Deubiquitinating enzyme]]~~	+
-	~~[[Category: Deubiquitylation]]~~	+
-	~~[[Category: Domain-swapping]]~~	+
-	~~[[Category: Dub]]~~	+
-	~~[[Category: Dub15]]~~	+
-	~~[[Category: Dusp]]~~	+
-	~~[[Category: Endopeptidase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Protease]]~~	+
-	~~[[Category: Thiol protease]]~~	+
-	~~[[Category: Thiolesterase]]~~	+
-	~~[[Category: Ubiquitin]]~~	+
-	~~[[Category: Ubiquitin carboxyterminal hydrolase]]~~	+
-	~~[[Category: Ubiquitin specific protease]]~~	+
-	~~[[Category: Ubl conjugation pathway]]~~	+
-	~~[[Category: Ubp15]]~~	+
-	~~[[Category: Uch]]~~	+
-	~~[[Category: Usp]]~~	+
-	~~[[Category: Usp15~~]]	+

OCA at 06:31, 2 January 2019

OCA — Wed, 02 Jan 2019 06:31:35 GMT

←Older revision		Revision as of 06:31, 2 January 2019
Line 16:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lm/3lmn_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lm/3lmn_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>
Line 41:		Line 41:
	[[Category: Walker, J R]]		[[Category: Walker, J R]]
	[[Category: Weigelt, J]]		[[Category: Weigelt, J]]
		+	[[Category: Acetylation]]
		+	[[Category: Alternative splicing]]
	[[Category: Cleavage]]		[[Category: Cleavage]]
	[[Category: Deubiquitinating enzyme]]		[[Category: Deubiquitinating enzyme]]

OCA at 15:39, 5 August 2016

OCA — Fri, 05 Aug 2016 15:39:21 GMT

←Older revision		Revision as of 15:39, 5 August 2016
Line 1:		Line 1:
		+
	==Oligomeric structure of the DUSP domain of human USP15==		==Oligomeric structure of the DUSP domain of human USP15==
	<StructureSection load='3lmn' size='340' side='right' caption='[[3lmn]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='3lmn' size='340' side='right' caption='[[3lmn]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3lmn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LMN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LMN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3lmn]] 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=3LMN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LMN FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1w6v\|1w6v]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1w6v\|1w6v]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KIAA0529, USP15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KIAA0529, USP15 ([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/Ubiquitin_thiolesterase Ubiquitin thiolesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin_thiolesterase Ubiquitin thiolesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15] </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=3lmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lmn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lmn RCSB], [http://www.ebi.ac.uk/pdbsum/3lmn 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=3lmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lmn OCA], [http://pdbe.org/3lmn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lmn RCSB], [http://www.ebi.ac.uk/pdbsum/3lmn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lmn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</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].	+	</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=3lmn ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>

Line 28:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Ubiquitin thiolesterase]]		[[Category: Ubiquitin thiolesterase]]
	[[Category: Alenkin, D]]		[[Category: Alenkin, D]]

OCA at 19:58, 25 December 2014

OCA — Thu, 25 Dec 2014 19:58:41 GMT

←Older revision		Revision as of 19:58, 25 December 2014
Line 9:		Line 9:
	<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=3lmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lmn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lmn RCSB], [http://www.ebi.ac.uk/pdbsum/3lmn 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=3lmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lmn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lmn RCSB], [http://www.ebi.ac.uk/pdbsum/3lmn PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/UBP15_HUMAN UBP15_HUMAN]] Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal (PubMed:22344298). Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway.<ref>PMID:16005295</ref> <ref>PMID:17318178</ref> <ref>PMID:19826004</ref> <ref>PMID:19576224</ref> <ref>PMID:19553310</ref> <ref>PMID:21947082</ref> <ref>PMID:22344298</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 22:		Line 24:
	==See Also==		==See Also==
	*[[Thioesterase\|Thioesterase]]		*[[Thioesterase\|Thioesterase]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 16:34, 18 December 2014

OCA — Thu, 18 Dec 2014 16:34:49 GMT

←Older revision		Revision as of 16:34, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3lmn\| PDB=3lmn \| SCENE= }}~~	+	==Oligomeric structure of the DUSP domain of human USP15==
-	===Oligomeric structure of the DUSP domain of human USP15===	+	<StructureSection load='3lmn' size='340' side='right' caption='[[3lmn]], [[Resolution\|resolution]] 2.15Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3lmn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LMN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LMN FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1w6v\|1w6v]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KIAA0529, USP15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin_thiolesterase Ubiquitin thiolesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15] </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=3lmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lmn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lmn RCSB], [http://www.ebi.ac.uk/pdbsum/3lmn PDBsum]</span></td></tr>
		+	</table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lm/3lmn_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</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].
		+	<div style="clear:both"></div>

-	==~~Function~~==	+	==See Also==
-	[[~~http://www.uniprot.org/uniprot/UBP15_HUMAN UBP15_HUMAN~~]] Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal (PubMed:22344298). Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway.<ref>PMID:16005295</ref> <ref>PMID:17318178</ref> <ref>PMID:19826004</ref> <ref>PMID:19576224</ref> <ref>PMID:19553310</ref> <ref>PMID:21947082</ref> <ref>PMID:22344298</ref>	+	*[[Thioesterase\|Thioesterase]]
-		+	__TOC__
-	~~==About this Structure==~~	+	</StructureSection>
-	[[3lmn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LMN OCA].	+
-		+
-	~~==Reference==~~	+
-	~~<references group="xtra"/>~~<~~references~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ubiquitin thiolesterase]]		[[Category: Ubiquitin thiolesterase]]
-	[[Category: Alenkin, D.]]	+	[[Category: Alenkin, D]]
-	[[Category: Arrowsmith, C H.]]	+	[[Category: Arrowsmith, C H]]
-	[[Category: Asinas, A.]]	+	[[Category: Asinas, A]]
-	[[Category: Avvakumov, G V.]]	+	[[Category: Avvakumov, G V]]
-	[[Category: Bochkarev, A.]]	+	[[Category: Bochkarev, A]]
-	[[Category: Bountra, C.]]	+	[[Category: Bountra, C]]
-	[[Category: Dhe-Paganon, S.]]	+	[[Category: Dhe-Paganon, S]]
-	[[Category: Edwards, A M.]]	+	[[Category: Edwards, A M]]
-	[[Category: Walker, J R.]]	+	[[Category: Walker, J R]]
-	[[Category: Weigelt, J.]]	+	[[Category: Weigelt, J]]
	[[Category: Cleavage]]		[[Category: Cleavage]]
	[[Category: Deubiquitinating enzyme]]		[[Category: Deubiquitinating enzyme]]

OCA: Protected "3lmn" [edit=sysop:move=sysop]

OCA — Wed, 10 Apr 2013 23:03:14 GMT

Protected "3lmn" [edit=sysop:move=sysop]

←Older revision

Revision as of 23:03, 10 April 2013

OCA at 23:03, 10 April 2013

OCA — Wed, 10 Apr 2013 23:03:06 GMT

←Older revision		Revision as of 23:03, 10 April 2013
Line 1:		Line 1:
-	{{Seed}}
-	[[Image:3lmn.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3lmn", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3lmn\| PDB=3lmn \| SCENE= }}		{{STRUCTURE_3lmn\| PDB=3lmn \| SCENE= }}
-
	===Oligomeric structure of the DUSP domain of human USP15===		===Oligomeric structure of the DUSP domain of human USP15===

		+	==Function==
		+	[[http://www.uniprot.org/uniprot/UBP15_HUMAN UBP15_HUMAN]] Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal (PubMed:22344298). Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway.<ref>PMID:16005295</ref> <ref>PMID:17318178</ref> <ref>PMID:19826004</ref> <ref>PMID:19576224</ref> <ref>PMID:19553310</ref> <ref>PMID:21947082</ref> <ref>PMID:22344298</ref>

	==About this Structure==		==About this Structure==
-	~~3LMN~~ is a 2 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LMN OCA].	+	[[3lmn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LMN OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ubiquitin thiolesterase]]		[[Category: Ubiquitin thiolesterase]]
Line 27:		Line 22:
	[[Category: Walker, J R.]]		[[Category: Walker, J R.]]
	[[Category: Weigelt, J.]]		[[Category: Weigelt, J.]]
-	[[Category: Acetylation]]
-	[[Category: Alternative splicing]]
	[[Category: Cleavage]]		[[Category: Cleavage]]
	[[Category: Deubiquitinating enzyme]]		[[Category: Deubiquitinating enzyme]]
Line 50:		Line 43:
	[[Category: Usp]]		[[Category: Usp]]
	[[Category: Usp15]]		[[Category: Usp15]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 21 08:35:33 2010''

OCA at 05:35, 21 April 2010

OCA — Wed, 21 Apr 2010 05:35:34 GMT

←Older revision		Revision as of 05:35, 21 April 2010
Line 1:		Line 1:
	{{Seed}}		{{Seed}}
-	[[Image:3lmn.~~jpg~~\|left\|200px]]	+	[[Image:3lmn.png\|left\|200px]]

	<!--		<!--
Line 10:		Line 10:
	{{STRUCTURE_3lmn\| PDB=3lmn \| SCENE= }}		{{STRUCTURE_3lmn\| PDB=3lmn \| SCENE= }}

-	===Oligomeric structure of the ~~dusp~~ domain of ~~husp15~~===	+	===Oligomeric structure of the DUSP domain of human USP15===


Line 51:		Line 51:
	[[Category: Usp15]]		[[Category: Usp15]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Mar 24 09~~:06:07 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 21 08:35:33 2010''

OCA at 07:06, 24 March 2010

OCA — Wed, 24 Mar 2010 07:06:09 GMT

←Older revision		Revision as of 07:06, 24 March 2010
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3lmn.jpg\|left\|200px]]

-	The ~~entry 3lmn~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3lmn", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3lmn\| PDB=3lmn \| SCENE= }}

-	~~Authors: Walker, J.R., Asinas, A., Avvakumov, G.V., Alenkin, D., Weigelt, J., Bountra, C., Edwards, A.M., Arrowsmith, C.H., Bochkarev, A., Dhe-Paganon, S.~~	+	===Oligomeric structure of the dusp domain of husp15===

-	Description: Oligomeric structure of the dusp domain of husp15

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Feb 10 16~~:59:43 2010''	+	==About this Structure==
		+	3LMN is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LMN OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: Ubiquitin thiolesterase]]
		+	[[Category: Alenkin, D.]]
		+	[[Category: Arrowsmith, C H.]]
		+	[[Category: Asinas, A.]]
		+	[[Category: Avvakumov, G V.]]
		+	[[Category: Bochkarev, A.]]
		+	[[Category: Bountra, C.]]
		+	[[Category: Dhe-Paganon, S.]]
		+	[[Category: Edwards, A M.]]
		+	[[Category: Walker, J R.]]
		+	[[Category: Weigelt, J.]]
		+	[[Category: Acetylation]]
		+	[[Category: Alternative splicing]]
		+	[[Category: Cleavage]]
		+	[[Category: Deubiquitinating enzyme]]
		+	[[Category: Deubiquitylation]]
		+	[[Category: Domain-swapping]]
		+	[[Category: Dub]]
		+	[[Category: Dub15]]
		+	[[Category: Dusp]]
		+	[[Category: Endopeptidase]]
		+	[[Category: Hydrolase]]
		+	[[Category: Phosphoprotein]]
		+	[[Category: Protease]]
		+	[[Category: Thiol protease]]
		+	[[Category: Thiolesterase]]
		+	[[Category: Ubiquitin]]
		+	[[Category: Ubiquitin carboxyterminal hydrolase]]
		+	[[Category: Ubiquitin specific protease]]
		+	[[Category: Ubl conjugation pathway]]
		+	[[Category: Ubp15]]
		+	[[Category: Uch]]
		+	[[Category: Usp]]
		+	[[Category: Usp15]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 24 09:06:07 2010''

OCA: New page: '''Unreleased structure''' The entry 3lmn is ON HOLD Authors: Walker, J.R., Asinas, A., Avvakumov, G.V., Alenkin, D., Weigelt, J., Bountra, C., Edwards, A.M., Arrowsmith, C.H., Bochkare...

OCA — Wed, 10 Feb 2010 14:59:43 GMT

New page: '''Unreleased structure''' The entry 3lmn is ON HOLD Authors: Walker, J.R., Asinas, A., Avvakumov, G.V., Alenkin, D., Weigelt, J., Bountra, C., Edwards, A.M., Arrowsmith, C.H., Bochkare...

New page

'''Unreleased structure'''

The entry 3lmn is ON HOLD

Authors: Walker, J.R., Asinas, A., Avvakumov, G.V., Alenkin, D., Weigelt, J., Bountra, C., Edwards, A.M., Arrowsmith, C.H., Bochkarev, A., Dhe-Paganon, S.

Description: Oligomeric structure of the dusp domain of husp15

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 10 16:59:43 2010''