9og0

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Current revision (05:48, 30 July 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9og0 is ON HOLD until 2027-04-30
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==Cryo-EM structure of OS9-SEL1L-HRD1 dimer==
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<StructureSection load='9og0' size='340' side='right'caption='[[9og0]], [[Resolution|resolution]] 3.64&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9og0]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9OG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9OG0 FirstGlance]. <br>
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Description:
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.64&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9og0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9og0 OCA], [https://pdbe.org/9og0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9og0 RCSB], [https://www.ebi.ac.uk/pdbsum/9og0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9og0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYVN1_HUMAN SYVN1_HUMAN] Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation (PubMed:12459480, PubMed:12646171, PubMed:12975321, PubMed:14593114, PubMed:16289116, PubMed:16847254, PubMed:17059562, PubMed:17141218, PubMed:17170702, PubMed:22607976, PubMed:26471130). Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (PubMed:12459480, PubMed:12646171, PubMed:12975321, PubMed:14593114, PubMed:16289116, PubMed:16847254, PubMed:17059562, PubMed:17141218, PubMed:17170702, PubMed:22607976, PubMed:26471130). Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation (PubMed:17141218). Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis (PubMed:17170702). Mediates the ubiquitination and subsequent degradation of cytoplasmic NFE2L1 (By similarity).[UniProtKB:Q9DBY1]<ref>PMID:12459480</ref> <ref>PMID:12646171</ref> <ref>PMID:12975321</ref> <ref>PMID:14593114</ref> <ref>PMID:16289116</ref> <ref>PMID:16847254</ref> <ref>PMID:17059562</ref> <ref>PMID:17141218</ref> <ref>PMID:17170702</ref> <ref>PMID:22607976</ref> <ref>PMID:26471130</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Jomaa A]]
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[[Category: Lin L]]
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[[Category: Maldosevic E]]
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[[Category: Qi L]]

Current revision

Cryo-EM structure of OS9-SEL1L-HRD1 dimer

PDB ID 9og0

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