3ppa - Revision history

OCA at 09:58, 6 September 2023

OCA — Wed, 06 Sep 2023 09:58:49 GMT

←Older revision		Revision as of 09:58, 6 September 2023
Line 3:		Line 3:
	<StructureSection load='3ppa' size='340' side='right'caption='[[3ppa]], [[Resolution\|resolution]] 2.35Å' scene=''>		<StructureSection load='3ppa' size='340' side='right'caption='[[3ppa]], [[Resolution\|resolution]] 2.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ppa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PPA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ppa]] is a 1 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=3PPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PPA FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>~~, ~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.35Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[1w6v\|1w6v]], [[3lmn\|3lmn]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>KIAA0529, USP15 ([https://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~~'>~~[https://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12]~~ </~~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=3ppa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppa OCA], [https://pdbe.org/3ppa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ppa RCSB], [https://www.ebi.ac.uk/pdbsum/3ppa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppa 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=3ppa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppa OCA], [https://pdbe.org/3ppa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ppa RCSB], [https://www.ebi.ac.uk/pdbsum/3ppa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppa ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[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>	+	[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>

	==See Also==		==See Also==
Line 19:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Ubiquitinyl hydrolase 1]]~~	+	[[Category: Arrowsmith CH]]
-	[[Category: Arrowsmith~~, C H~~]]	+	[[Category: Asinas AE]]
-	[[Category: Asinas~~, A E~~]]	+	[[Category: Bountra C]]
-	[[Category: Bountra, C]]	+	[[Category: Dhe-Paganon S]]
-	[[Category: Dhe-Paganon, S]]	+	[[Category: Dong A]]
-	[[Category: Dong, A]]	+	[[Category: Edwards AM]]
-	[[Category: Edwards~~, A M]]~~	+	[[Category: Walker JR]]
-	~~[[Category: Structural genomic~~]]	+	[[Category: Weigelt J]]
-	[[Category: Walker~~, J R~~]]	+
-	[[Category: Weigelt, J]]	+
-	~~[[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 08:49, 25 May 2022

OCA — Wed, 25 May 2022 08:49:16 GMT

←Older revision		Revision as of 08:49, 25 May 2022
Line 1:		Line 1:

	==Structure of the Dusp-Ubl domains of Usp15==		==Structure of the Dusp-Ubl domains of Usp15==
-	<StructureSection load='3ppa' size='340' side='right' caption='[[3ppa]], [[Resolution\|resolution]] 2.35Å' scene=''>	+	<StructureSection load='3ppa' size='340' side='right'caption='[[3ppa]], [[Resolution\|resolution]] 2.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ppa]] is a 1 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=3PPA OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3PPA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ppa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PPA FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1w6v\|1w6v]], [[3lmn\|3lmn]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1w6v\|1w6v]], [[3lmn\|3lmn]]</div></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='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KIAA0529, USP15 ([https://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/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </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=3ppa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppa OCA], [~~http~~://pdbe.org/3ppa PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3ppa RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3ppa PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppa 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=3ppa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppa OCA], [https://pdbe.org/3ppa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ppa RCSB], [https://www.ebi.ac.uk/pdbsum/3ppa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppa 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>

	==See Also==		==See Also==
-	*[[Thioesterase\|Thioesterase]]	+	*[[Thioesterase 3D structures\|Thioesterase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 20:		Line 20:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Ubiquitinyl hydrolase 1]]		[[Category: Ubiquitinyl hydrolase 1]]
	[[Category: Arrowsmith, C H]]		[[Category: Arrowsmith, C H]]
Line 27:		Line 28:
	[[Category: Dong, A]]		[[Category: Dong, A]]
	[[Category: Edwards, A M]]		[[Category: Edwards, A M]]
		+	[[Category: Structural genomic]]
	[[Category: Walker, J R]]		[[Category: Walker, J R]]
	[[Category: Weigelt, J]]		[[Category: Weigelt, J]]

OCA at 23:36, 4 August 2016

OCA — Thu, 04 Aug 2016 23:36:09 GMT

←Older revision		Revision as of 23:36, 4 August 2016
Line 1:		Line 1:
		+
	==Structure of the Dusp-Ubl domains of Usp15==		==Structure of the Dusp-Ubl domains of Usp15==
	<StructureSection load='3ppa' size='340' side='right' caption='[[3ppa]], [[Resolution\|resolution]] 2.35Å' scene=''>		<StructureSection load='3ppa' size='340' side='right' caption='[[3ppa]], [[Resolution\|resolution]] 2.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ppa]] is a 1 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=3PPA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PPA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ppa]] is a 1 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=3PPA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PPA FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1w6v\|1w6v]], [[3lmn\|3lmn]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1w6v\|1w6v]], [[3lmn\|3lmn]]</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/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </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=3ppa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ppa RCSB], [http://www.ebi.ac.uk/pdbsum/3ppa 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=3ppa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppa OCA], [http://pdbe.org/3ppa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ppa RCSB], [http://www.ebi.ac.uk/pdbsum/3ppa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppa ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Ubiquitinyl hydrolase 1]]		[[Category: Ubiquitinyl hydrolase 1]]
	[[Category: Arrowsmith, C H]]		[[Category: Arrowsmith, C H]]

OCA at 20:45, 24 December 2014

OCA — Wed, 24 Dec 2014 20:45:46 GMT

←Older revision		Revision as of 20:45, 24 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=3ppa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ppa RCSB], [http://www.ebi.ac.uk/pdbsum/3ppa 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=3ppa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ppa RCSB], [http://www.ebi.ac.uk/pdbsum/3ppa 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>

	==See Also==		==See Also==
	*[[Thioesterase\|Thioesterase]]		*[[Thioesterase\|Thioesterase]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 10:57, 19 December 2014

OCA — Fri, 19 Dec 2014 10:57:05 GMT

←Older revision		Revision as of 10:57, 19 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3ppa\| PDB=3ppa \| SCENE= }}~~	+	==Structure of the Dusp-Ubl domains of Usp15==
-	===Structure of the Dusp-Ubl domains of Usp15===	+	<StructureSection load='3ppa' size='340' side='right' caption='[[3ppa]], [[Resolution\|resolution]] 2.35Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3ppa]] is a 1 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=3PPA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PPA FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1w6v\|1w6v]], [[3lmn\|3lmn]]</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/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </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=3ppa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ppa RCSB], [http://www.ebi.ac.uk/pdbsum/3ppa PDBsum]</span></td></tr>
		+	</table>

-	==~~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>
-	[[3ppa]] is a 1 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=3PPA OCA].	+
-		+
-	~~==Reference==~~	+
-	~~<references group="xtra"/>~~<~~references~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ubiquitinyl hydrolase 1]]		[[Category: Ubiquitinyl hydrolase 1]]
-	[[Category: Arrowsmith, C H.]]	+	[[Category: Arrowsmith, C H]]
-	[[Category: Asinas, A E.]]	+	[[Category: Asinas, A E]]
-	[[Category: Bountra, C.]]	+	[[Category: Bountra, C]]
-	[[Category: Dhe-Paganon, S.]]	+	[[Category: Dhe-Paganon, S]]
-	[[Category: Dong, A.]]	+	[[Category: Dong, A]]
-	[[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 at 08:22, 8 May 2013

OCA — Wed, 08 May 2013 08:22:46 GMT

←Older revision		Revision as of 08:22, 8 May 2013
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-	[[Image:3ppa.jpg\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3ppa", 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_3ppa\| PDB=3ppa \| SCENE= }}		{{STRUCTURE_3ppa\| PDB=3ppa \| SCENE= }}
-
	===Structure of the Dusp-Ubl domains of Usp15===		===Structure of the Dusp-Ubl domains of 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==
	[[3ppa]] is a 1 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=3PPA OCA].		[[3ppa]] is a 1 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=3PPA OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ubiquitinyl hydrolase 1]]		[[Category: Ubiquitinyl hydrolase 1]]
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	[[Category: Walker, J R.]]		[[Category: Walker, J R.]]
	[[Category: Weigelt, J.]]		[[Category: Weigelt, J.]]
		+	[[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: Protected "3ppa" [edit=sysop:move=sysop]

OCA — Wed, 19 Jan 2011 06:27:31 GMT

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

←Older revision

Revision as of 06:27, 19 January 2011

OCA at 06:27, 19 January 2011

OCA — Wed, 19 Jan 2011 06:27:30 GMT

←Older revision		Revision as of 06:27, 19 January 2011
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-	~~'''Unreleased structure'''~~	+	[[Image:3ppa.jpg\|left\|200px]]

-	The ~~entry 3ppa~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3ppa", 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_3ppa\| PDB=3ppa \| SCENE= }}

-	~~Authors: Walker, J.R., Asinas, A.E., Dong, A., Weigelt, J., Bountra, C., Edwards, A.M., Arrowsmith, C.H., Dhe~~-~~Paganon, S.~~	+	===Structure of the Dusp-Ubl domains of Usp15===

-	Description: Structure of the Dusp-Ubl domains of Usp15

-	~~''Page seeded by~~ [http://oca.weizmann.ac.il/oca OCA ] ~~on Wed Dec 8 11~~:32:~~41 2010''~~	+	==About this Structure==
		+	[[3ppa]] is a 1 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=3PPA OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: Ubiquitinyl hydrolase 1]]
		+	[[Category: Arrowsmith, C H.]]
		+	[[Category: Asinas, A E.]]
		+	[[Category: Bountra, C.]]
		+	[[Category: Dhe-Paganon, S.]]
		+	[[Category: Dong, A.]]
		+	[[Category: Edwards, A M.]]
		+	[[Category: Walker, J R.]]
		+	[[Category: Weigelt, J.]]

OCA at 08:20, 8 December 2010

OCA — Wed, 08 Dec 2010 08:20:37 GMT

←Older revision		Revision as of 08:20, 8 December 2010
Line 5:		Line 5:
	Authors: Walker, J.R., Asinas, A.E., Dong, A., Weigelt, J., Bountra, C., Edwards, A.M., Arrowsmith, C.H., Dhe-Paganon, S.		Authors: Walker, J.R., Asinas, A.E., Dong, A., Weigelt, J., Bountra, C., Edwards, A.M., Arrowsmith, C.H., Dhe-Paganon, S.

-	Description: ~~STRUCTURE OF THE DUSP~~-~~UBL DOMAINS OF USP15~~	+	Description: Structure of the Dusp-Ubl domains of Usp15

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 1 11:15:05 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 8 11:32:41 2010''

OCA: New page: '''Unreleased structure''' The entry 3ppa is ON HOLD Authors: Walker, J.R., Asinas, A.E., Dong, A., Weigelt, J., Bountra, C., Edwards, A.M., Arrowsmith, C.H., Dhe-Paganon, S. Descripti...

OCA — Wed, 01 Dec 2010 08:03:18 GMT

New page: '''Unreleased structure''' The entry 3ppa is ON HOLD Authors: Walker, J.R., Asinas, A.E., Dong, A., Weigelt, J., Bountra, C., Edwards, A.M., Arrowsmith, C.H., Dhe-Paganon, S. Descripti...

New page

'''Unreleased structure'''

The entry 3ppa is ON HOLD

Authors: Walker, J.R., Asinas, A.E., Dong, A., Weigelt, J., Bountra, C., Edwards, A.M., Arrowsmith, C.H., Dhe-Paganon, S.

Description: STRUCTURE OF THE DUSP-UBL DOMAINS OF USP15

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 1 11:15:05 2010''