3jck - Revision history

OCA at 08:44, 7 February 2024

2024-02-07T08:44:01Z

←Older revision		Revision as of 08:44, 7 February 2024
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	<SX load='3jck' size='340' side='right' viewer='molstar' caption='[[3jck]], [[Resolution\|resolution]] 3.50Å' scene=''>		<SX load='3jck' size='340' side='right' viewer='molstar' caption='[[3jck]], [[Resolution\|resolution]] 3.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3jck]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Baker's_yeast Baker's yeast~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JCK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3jck]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JCK 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">Electron Microscopy, [[Resolution\|Resolution]] 3.5Å</td></tr>
-	~~<tr id='NonStdRes'><td class="sblockLbl"><b>~~[[~~Non-Standard_Residue~~\|~~NonStd Res:~~]]~~</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene>~~</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"~~>RPN3, SUN2, YER021W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=559292 Baker's yeast]), RPN5, NAS5, YDL147W, D1572 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN6, NAS4, YDL097C, D2381 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN7, YPR108W, P8283.8 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN8, YOR261C, O5360 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN9, NAS7, YDR427W, D9461.14 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN11, MPR1, YFR004W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN12, NIN1, YFR052W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SEM1, DSH1, YDR363W-A ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=3jck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jck OCA], [https://pdbe.org/3jck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jck RCSB], [https://www.ebi.ac.uk/pdbsum/3jck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jck 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=3jck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jck OCA], [https://pdbe.org/3jck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jck RCSB], [https://www.ebi.ac.uk/pdbsum/3jck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jck ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/RPN9_YEAST RPN9_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [[https://www.uniprot.org/uniprot/RPN6_YEAST RPN6_YEAST]] Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, RPN6 is required for proteasome assembly.<ref>PMID:9426256</ref> <ref>PMID:12486135</ref> <ref>PMID:15611133</ref> [[https://www.uniprot.org/uniprot/RPN11_YEAST RPN11_YEAST]] Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:21075847</ref> [[https://www.uniprot.org/uniprot/SEM1_YEAST SEM1_YEAST]] Versatile protein that might stabilize multiple protein complexes involved in diverse pathways. Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis. Associates also with the TREX-2 complex that is required for transcription-coupled mRNA export, and the COP9 signalosome, which is involved in deneddylation.<ref>PMID:19289793</ref> <ref>PMID:15117943</ref> [[https://www.uniprot.org/uniprot/RPN5_YEAST RPN5_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:9426256</ref> [[https://www.uniprot.org/uniprot/RPN12_YEAST RPN12_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Necessary for activation of the CDC28 kinase. [[https://www.uniprot.org/uniprot/RPN3_YEAST RPN3_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [[https://www.uniprot.org/uniprot/RPN7_YEAST RPN7_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins (By similarity). [[https://www.uniprot.org/uniprot/RPN8_YEAST RPN8_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:9584156</ref>	+	[https://www.uniprot.org/uniprot/RPN3_YEAST RPN3_YEAST] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The 26S proteasome is responsible for the selective, ATP-dependent degradation of polyubiquitinated cellular proteins. Removal of ubiquitin chains from targeted substrates at the proteasome is a prerequisite for substrate processing and is accomplished by Rpn11, a deubiquitinase within the 'lid' sub-complex. Prior to the lid's incorporation into the proteasome, Rpn11 deubiquitinase activity is inhibited to prevent unwarranted deubiquitination of polyubiquitinated proteins. Here we present the atomic model of the isolated lid sub-complex, as determined by cryo-electron microscopy at 3.5 A resolution, revealing how Rpn11 is inhibited through its interaction with a neighboring lid subunit, Rpn5. Through mutagenesis of specific residues, we describe the network of interactions that are required to stabilize this inhibited state. These results provide significant insight into the intricate mechanisms of proteasome assembly, outlining the substantial conformational rearrangements that occur during incorporation of the lid into the 26S holoenzyme, which ultimately activates the deubiquitinase for substrate degradation.	+
-		+
-	Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition.,Dambacher CM, Worden EJ, Herzik MA, Martin A, Lander GC Elife. 2016 Jan 8;5. pii: e13027. doi: 10.7554/eLife.13027. PMID:26744777<ref>PMID:26744777</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3jck" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</SX>		</SX>
-	[[Category: Baker's yeast]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Ubiquitinyl hydrolase 1~~]]	+	[[Category: Saccharomyces cerevisiae S288C]]
-	[[Category: Dambacher~~, C M~~]]	+	[[Category: Dambacher CM]]
-	[[Category: Herzik~~, M A~~]]	+	[[Category: Herzik Jr MA]]
-	[[Category: Lander~~, G C~~]]	+	[[Category: Lander GC]]
-	[[Category: Martin, A]]	+	[[Category: Martin A]]
-	[[Category: Worden~~, E J]]~~	+	[[Category: Worden EJ]]
-	~~[[Category: Deubiquitinase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Proteasome]]~~	+
-	~~[[Category: Protein homeostasis]]~~	+
-	~~[[Category: Rpn11~~]]	+

OCA at 13:32, 4 May 2022

2022-05-04T13:32:14Z

OCA at 18:34, 10 April 2020

2020-04-10T18:34:35Z

←Older revision		Revision as of 18:34, 10 April 2020
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	<SX load='3jck' size='340' side='right' viewer='molstar' caption='[[3jck]], [[Resolution\|resolution]] 3.50Å' scene=''>		<SX load='3jck' size='340' side='right' viewer='molstar' caption='[[3jck]], [[Resolution\|resolution]] 3.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3jck]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JCK OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3JCK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3jck]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JCK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3JCK 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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RPN3, SUN2, YER021W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN5, NAS5, YDL147W, D1572 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN6, NAS4, YDL097C, D2381 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN7, YPR108W, P8283.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN8, YOR261C, O5360 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN9, NAS7, YDR427W, D9461.14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN11, MPR1, YFR004W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN12, NIN1, YFR052W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SEM1, DSH1, YDR363W-A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RPN3, SUN2, YER021W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN5, NAS5, YDL147W, D1572 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN6, NAS4, YDL097C, D2381 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN7, YPR108W, P8283.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN8, YOR261C, O5360 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN9, NAS7, YDR427W, D9461.14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN11, MPR1, YFR004W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN12, NIN1, YFR052W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SEM1, DSH1, YDR363W-A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=3jck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jck OCA], [http://pdbe.org/3jck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jck RCSB], [http://www.ebi.ac.uk/pdbsum/3jck PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jck ProSAT]</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=3jck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jck OCA], [http://pdbe.org/3jck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jck RCSB], [http://www.ebi.ac.uk/pdbsum/3jck PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jck ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 17:41, 6 March 2020

2020-03-06T17:41:16Z

←Older revision		Revision as of 17:41, 6 March 2020
Line 1:		Line 1:
-	~~{{Large structure}}~~	+
	==Structure of the yeast 26S proteasome lid sub-complex==		==Structure of the yeast 26S proteasome lid sub-complex==
-	<~~StructureSection~~ load='3jck' size='340' side='right' caption='[[3jck]], [[Resolution\|resolution]] 3.50Å' scene=''>	+	<SX load='3jck' size='340' side='right' viewer='molstar' caption='[[3jck]], [[Resolution\|resolution]] 3.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3jck]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JCK FirstGlance]. <br>		<table><tr><td colspan='2'>[[3jck]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JCK FirstGlance]. <br>
Line 10:		Line 10:
	<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=3jck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jck OCA], [http://pdbe.org/3jck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jck RCSB], [http://www.ebi.ac.uk/pdbsum/3jck PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jck 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=3jck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jck OCA], [http://pdbe.org/3jck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jck RCSB], [http://www.ebi.ac.uk/pdbsum/3jck PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jck ProSAT]</span></td></tr>
	</table>		</table>
-	{{Large structure}}
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/RPN9_YEAST RPN9_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [[http://www.uniprot.org/uniprot/RPN6_YEAST RPN6_YEAST]] Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, RPN6 is required for proteasome assembly.<ref>PMID:9426256</ref> <ref>PMID:12486135</ref> <ref>PMID:15611133</ref> [[http://www.uniprot.org/uniprot/RPN11_YEAST RPN11_YEAST]] Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:21075847</ref> [[http://www.uniprot.org/uniprot/SEM1_YEAST SEM1_YEAST]] Versatile protein that might stabilize multiple protein complexes involved in diverse pathways. Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis. Associates also with the TREX-2 complex that is required for transcription-coupled mRNA export, and the COP9 signalosome, which is involved in deneddylation.<ref>PMID:19289793</ref> <ref>PMID:15117943</ref> [[http://www.uniprot.org/uniprot/RPN5_YEAST RPN5_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:9426256</ref> [[http://www.uniprot.org/uniprot/RPN12_YEAST RPN12_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Necessary for activation of the CDC28 kinase. [[http://www.uniprot.org/uniprot/RPN3_YEAST RPN3_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [[http://www.uniprot.org/uniprot/RPN7_YEAST RPN7_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins (By similarity). [[http://www.uniprot.org/uniprot/RPN8_YEAST RPN8_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:9584156</ref>		[[http://www.uniprot.org/uniprot/RPN9_YEAST RPN9_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [[http://www.uniprot.org/uniprot/RPN6_YEAST RPN6_YEAST]] Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, RPN6 is required for proteasome assembly.<ref>PMID:9426256</ref> <ref>PMID:12486135</ref> <ref>PMID:15611133</ref> [[http://www.uniprot.org/uniprot/RPN11_YEAST RPN11_YEAST]] Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:21075847</ref> [[http://www.uniprot.org/uniprot/SEM1_YEAST SEM1_YEAST]] Versatile protein that might stabilize multiple protein complexes involved in diverse pathways. Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis. Associates also with the TREX-2 complex that is required for transcription-coupled mRNA export, and the COP9 signalosome, which is involved in deneddylation.<ref>PMID:19289793</ref> <ref>PMID:15117943</ref> [[http://www.uniprot.org/uniprot/RPN5_YEAST RPN5_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:9426256</ref> [[http://www.uniprot.org/uniprot/RPN12_YEAST RPN12_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Necessary for activation of the CDC28 kinase. [[http://www.uniprot.org/uniprot/RPN3_YEAST RPN3_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [[http://www.uniprot.org/uniprot/RPN7_YEAST RPN7_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins (By similarity). [[http://www.uniprot.org/uniprot/RPN8_YEAST RPN8_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:9584156</ref>
Line 25:		Line 24:
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Baker's yeast]]		[[Category: Baker's yeast]]
		+	[[Category: Large Structures]]
	[[Category: Ubiquitinyl hydrolase 1]]		[[Category: Ubiquitinyl hydrolase 1]]
	[[Category: Dambacher, C M]]		[[Category: Dambacher, C M]]

OCA at 08:30, 18 July 2018

2018-07-18T08:30:58Z

←Older revision		Revision as of 08:30, 18 July 2018
Line 3:		Line 3:
	<StructureSection load='3jck' size='340' side='right' caption='[[3jck]], [[Resolution\|resolution]] 3.50Å' scene=''>		<StructureSection load='3jck' size='340' side='right' caption='[[3jck]], [[Resolution\|resolution]] 3.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3jck]] is a 9 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JCK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3jck]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JCK 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"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RPN3, SUN2, YER021W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN5, NAS5, YDL147W, D1572 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN6, NAS4, YDL097C, D2381 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN7, YPR108W, P8283.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN8, YOR261C, O5360 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN9, NAS7, YDR427W, D9461.14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN11, MPR1, YFR004W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN12, NIN1, YFR052W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SEM1, DSH1, YDR363W-A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=3jck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jck OCA], [http://pdbe.org/3jck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jck RCSB], [http://www.ebi.ac.uk/pdbsum/3jck PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jck 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=3jck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jck OCA], [http://pdbe.org/3jck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jck RCSB], [http://www.ebi.ac.uk/pdbsum/3jck PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jck ProSAT]</span></td></tr>
Line 25:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Baker's yeast]]
	[[Category: Ubiquitinyl hydrolase 1]]		[[Category: Ubiquitinyl hydrolase 1]]
	[[Category: Dambacher, C M]]		[[Category: Dambacher, C M]]

OCA at 17:49, 12 July 2016

2016-07-12T17:49:44Z

←Older revision		Revision as of 17:49, 12 July 2016
Line 1:		Line 1:
		+	{{Large structure}}
	==Structure of the yeast 26S proteasome lid sub-complex==		==Structure of the yeast 26S proteasome lid sub-complex==
	<StructureSection load='3jck' size='340' side='right' caption='[[3jck]], [[Resolution\|resolution]] 3.50Å' scene=''>		<StructureSection load='3jck' size='340' side='right' caption='[[3jck]], [[Resolution\|resolution]] 3.50Å' scene=''>
Line 6:		Line 7:
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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=3jck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jck OCA], [http://pdbe.org/3jck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jck RCSB], [http://www.ebi.ac.uk/pdbsum/3jck 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=3jck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jck OCA], [http://pdbe.org/3jck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jck RCSB], [http://www.ebi.ac.uk/pdbsum/3jck PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jck ProSAT]</span></td></tr>
	</table>		</table>
	{{Large structure}}		{{Large structure}}

OCA at 17:02, 20 January 2016

2016-01-20T17:02:42Z

←Older revision		Revision as of 17:02, 20 January 2016
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Structure of the yeast 26S proteasome lid sub-complex==
		+	<StructureSection load='3jck' size='340' side='right' caption='[[3jck]], [[Resolution\|resolution]] 3.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3jck]] is a 9 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JCK 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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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=3jck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jck OCA], [http://pdbe.org/3jck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jck RCSB], [http://www.ebi.ac.uk/pdbsum/3jck PDBsum]</span></td></tr>
		+	</table>
		+	{{Large structure}}
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RPN9_YEAST RPN9_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [[http://www.uniprot.org/uniprot/RPN6_YEAST RPN6_YEAST]] Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, RPN6 is required for proteasome assembly.<ref>PMID:9426256</ref> <ref>PMID:12486135</ref> <ref>PMID:15611133</ref> [[http://www.uniprot.org/uniprot/RPN11_YEAST RPN11_YEAST]] Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:21075847</ref> [[http://www.uniprot.org/uniprot/SEM1_YEAST SEM1_YEAST]] Versatile protein that might stabilize multiple protein complexes involved in diverse pathways. Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis. Associates also with the TREX-2 complex that is required for transcription-coupled mRNA export, and the COP9 signalosome, which is involved in deneddylation.<ref>PMID:19289793</ref> <ref>PMID:15117943</ref> [[http://www.uniprot.org/uniprot/RPN5_YEAST RPN5_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:9426256</ref> [[http://www.uniprot.org/uniprot/RPN12_YEAST RPN12_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Necessary for activation of the CDC28 kinase. [[http://www.uniprot.org/uniprot/RPN3_YEAST RPN3_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [[http://www.uniprot.org/uniprot/RPN7_YEAST RPN7_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins (By similarity). [[http://www.uniprot.org/uniprot/RPN8_YEAST RPN8_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:9584156</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The 26S proteasome is responsible for the selective, ATP-dependent degradation of polyubiquitinated cellular proteins. Removal of ubiquitin chains from targeted substrates at the proteasome is a prerequisite for substrate processing and is accomplished by Rpn11, a deubiquitinase within the 'lid' sub-complex. Prior to the lid's incorporation into the proteasome, Rpn11 deubiquitinase activity is inhibited to prevent unwarranted deubiquitination of polyubiquitinated proteins. Here we present the atomic model of the isolated lid sub-complex, as determined by cryo-electron microscopy at 3.5 A resolution, revealing how Rpn11 is inhibited through its interaction with a neighboring lid subunit, Rpn5. Through mutagenesis of specific residues, we describe the network of interactions that are required to stabilize this inhibited state. These results provide significant insight into the intricate mechanisms of proteasome assembly, outlining the substantial conformational rearrangements that occur during incorporation of the lid into the 26S holoenzyme, which ultimately activates the deubiquitinase for substrate degradation.

-	~~The entry 3jck is ON HOLD~~	+	Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition.,Dambacher CM, Worden EJ, Herzik MA, Martin A, Lander GC Elife. 2016 Jan 8;5. pii: e13027. doi: 10.7554/eLife.13027. PMID:26744777<ref>PMID:26744777</ref>

-	~~Authors: Herzik Jr.~~, M.A.~~, Dambacher, C.M., Worden, E.J., Martin, A., Lander, G.C~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Structure of the yeast 26S proteasome lid sub-complex~~	+	<div class="pdbe-citations 3jck" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Unreleased Structures~~]]	+	== References ==
-	[[Category: ~~Herzik Jr~~]]	+	<references/>
-	[[Category: ~~Lander~~, ~~G.C~~]]	+	__TOC__
-	[[Category: ~~Dambacher~~, C.M]]	+	</StructureSection>
		+	[[Category: Ubiquitinyl hydrolase 1]]
		+	[[Category: Dambacher, C M]]
		+	[[Category: Herzik, M A]]
		+	[[Category: Lander, G C]]
	[[Category: Martin, A]]		[[Category: Martin, A]]
-	[[Category: Worden, E.J]]	+	[[Category: Worden, E J]]
-	[[Category: ~~M.A~~]]	+	[[Category: Deubiquitinase]]
		+	[[Category: Hydrolase]]
		+	[[Category: Proteasome]]
		+	[[Category: Protein homeostasis]]
		+	[[Category: Rpn11]]

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

2015-12-30T12:11:03Z

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

←Older revision

Revision as of 12:11, 30 December 2015

OCA: New page: '''Unreleased structure''' The entry 3jck is ON HOLD Authors: Herzik Jr., M.A., Dambacher, C.M., Worden, E.J., Martin, A., Lander, G.C. Description: Structure of the yeast 26S proteaso...

2015-12-30T12:11:01Z

New page: '''Unreleased structure''' The entry 3jck is ON HOLD Authors: Herzik Jr., M.A., Dambacher, C.M., Worden, E.J., Martin, A., Lander, G.C. Description: Structure of the yeast 26S proteaso...

New page

'''Unreleased structure'''

The entry 3jck is ON HOLD

Authors: Herzik Jr., M.A., Dambacher, C.M., Worden, E.J., Martin, A., Lander, G.C.

Description: Structure of the yeast 26S proteasome lid sub-complex
[[Category: Unreleased Structures]]
[[Category: Herzik Jr]]
[[Category: Lander, G.C]]
[[Category: Dambacher, C.M]]
[[Category: Martin, A]]
[[Category: Worden, E.J]]
[[Category: M.A]]

←Older revision		Revision as of 13:32, 4 May 2022
Line 3:		Line 3:
	<SX load='3jck' size='340' side='right' viewer='molstar' caption='[[3jck]], [[Resolution\|resolution]] 3.50Å' scene=''>		<SX load='3jck' size='340' side='right' viewer='molstar' caption='[[3jck]], [[Resolution\|resolution]] 3.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3jck]] is a 9 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JCK OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=3JCK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3jck]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JCK 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='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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RPN3, SUN2, YER021W ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN5, NAS5, YDL147W, D1572 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN6, NAS4, YDL097C, D2381 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN7, YPR108W, P8283.8 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN8, YOR261C, O5360 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN9, NAS7, YDR427W, D9461.14 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN11, MPR1, YFR004W ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN12, NIN1, YFR052W ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SEM1, DSH1, YDR363W-A ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RPN3, SUN2, YER021W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN5, NAS5, YDL147W, D1572 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN6, NAS4, YDL097C, D2381 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN7, YPR108W, P8283.8 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN8, YOR261C, O5360 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN9, NAS7, YDR427W, D9461.14 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN11, MPR1, YFR004W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPN12, NIN1, YFR052W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SEM1, DSH1, YDR363W-A ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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~~://proteopedia.org/fgij/fg.htm?mol=3jck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jck OCA], [~~http~~://pdbe.org/3jck PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3jck RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3jck PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3jck 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=3jck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jck OCA], [https://pdbe.org/3jck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jck RCSB], [https://www.ebi.ac.uk/pdbsum/3jck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jck ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/RPN9_YEAST RPN9_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [[~~http~~://www.uniprot.org/uniprot/RPN6_YEAST RPN6_YEAST]] Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, RPN6 is required for proteasome assembly.<ref>PMID:9426256</ref> <ref>PMID:12486135</ref> <ref>PMID:15611133</ref> [[~~http~~://www.uniprot.org/uniprot/RPN11_YEAST RPN11_YEAST]] Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:21075847</ref> [[~~http~~://www.uniprot.org/uniprot/SEM1_YEAST SEM1_YEAST]] Versatile protein that might stabilize multiple protein complexes involved in diverse pathways. Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis. Associates also with the TREX-2 complex that is required for transcription-coupled mRNA export, and the COP9 signalosome, which is involved in deneddylation.<ref>PMID:19289793</ref> <ref>PMID:15117943</ref> [[~~http~~://www.uniprot.org/uniprot/RPN5_YEAST RPN5_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:9426256</ref> [[~~http~~://www.uniprot.org/uniprot/RPN12_YEAST RPN12_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Necessary for activation of the CDC28 kinase. [[~~http~~://www.uniprot.org/uniprot/RPN3_YEAST RPN3_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [[~~http~~://www.uniprot.org/uniprot/RPN7_YEAST RPN7_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins (By similarity). [[~~http~~://www.uniprot.org/uniprot/RPN8_YEAST RPN8_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:9584156</ref>	+	[[https://www.uniprot.org/uniprot/RPN9_YEAST RPN9_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [[https://www.uniprot.org/uniprot/RPN6_YEAST RPN6_YEAST]] Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, RPN6 is required for proteasome assembly.<ref>PMID:9426256</ref> <ref>PMID:12486135</ref> <ref>PMID:15611133</ref> [[https://www.uniprot.org/uniprot/RPN11_YEAST RPN11_YEAST]] Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:21075847</ref> [[https://www.uniprot.org/uniprot/SEM1_YEAST SEM1_YEAST]] Versatile protein that might stabilize multiple protein complexes involved in diverse pathways. Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis. Associates also with the TREX-2 complex that is required for transcription-coupled mRNA export, and the COP9 signalosome, which is involved in deneddylation.<ref>PMID:19289793</ref> <ref>PMID:15117943</ref> [[https://www.uniprot.org/uniprot/RPN5_YEAST RPN5_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:9426256</ref> [[https://www.uniprot.org/uniprot/RPN12_YEAST RPN12_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Necessary for activation of the CDC28 kinase. [[https://www.uniprot.org/uniprot/RPN3_YEAST RPN3_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [[https://www.uniprot.org/uniprot/RPN7_YEAST RPN7_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins (By similarity). [[https://www.uniprot.org/uniprot/RPN8_YEAST RPN8_YEAST]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:9584156</ref>
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	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==