2myx: Difference between revisions

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 ==Structure of the CUE domain of yeast Cue1==
-<StructureSection load='2myx' size='340' side='right'caption='[[2myx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2myx' size='340' side='right'caption='[[2myx]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2myx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MYX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2myx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MYX FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CUE1, KIS4, YM8156.06, YMR264W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2myx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myx OCA], [https://pdbe.org/2myx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2myx RCSB], [https://www.ebi.ac.uk/pdbsum/2myx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2myx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CUE1_YEAST CUE1_YEAST]] Component of the endoplasmic reticulum-associated protein degradation (ERAD) pathway. Recruits the soluble ubiquitin-conjugating enzyme UBC7 to the cytoplasmic face of the endoplasmic reticulum membrane where it functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Targets the E2 conjugating enzyme UBC7 to the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains, and to the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). Has also a role in cold adaptation, perhaps through effects on sterol biosynthesis.<ref>PMID:9388185</ref> <ref>PMID:9335582</ref> <ref>PMID:10991948</ref> <ref>PMID:10982838</ref> <ref>PMID:10878801</ref> <ref>PMID:11406589</ref> <ref>PMID:11390656</ref> <ref>PMID:12399372</ref> <ref>PMID:16873066</ref> <ref>PMID:16607018</ref> <ref>PMID:16556771</ref>
+[https://www.uniprot.org/uniprot/CUE1_YEAST CUE1_YEAST] Component of the endoplasmic reticulum-associated protein degradation (ERAD) pathway. Recruits the soluble ubiquitin-conjugating enzyme UBC7 to the cytoplasmic face of the endoplasmic reticulum membrane where it functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Targets the E2 conjugating enzyme UBC7 to the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains, and to the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). Has also a role in cold adaptation, perhaps through effects on sterol biosynthesis.<ref>PMID:9388185</ref> <ref>PMID:9335582</ref> <ref>PMID:10991948</ref> <ref>PMID:10982838</ref> <ref>PMID:10878801</ref> <ref>PMID:11406589</ref> <ref>PMID:11390656</ref> <ref>PMID:12399372</ref> <ref>PMID:16873066</ref> <ref>PMID:16607018</ref> <ref>PMID:16556771</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Baker's yeast]]
 [[Category: Large Structures]]
-[[Category: Doetsch, V]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Guentert, P]]
+[[Category: Doetsch V]]
-[[Category: Kniss, A]]
+[[Category: Guentert P]]
-[[Category: Loehr, F]]
+[[Category: Kniss A]]
-[[Category: Rogov, V V]]
+[[Category: Loehr F]]
-[[Category: Cue domain]]
+[[Category: Rogov VV]]
-[[Category: Erad]]
-[[Category: Ubiquitin-binding protein]]
-[[Category: Ubiquitination]]