6a3z

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==Zinc finger domain from the HRD1 Protein==
==Zinc finger domain from the HRD1 Protein==
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<StructureSection load='6a3z' size='340' side='right'caption='[[6a3z]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='6a3z' size='340' side='right'caption='[[6a3z]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6a3z]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A3Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A3Z FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6a3z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A3Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A3Z FirstGlance]. <br>
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</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>
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</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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </span></td></tr>
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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=6a3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a3z OCA], [https://pdbe.org/6a3z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a3z RCSB], [https://www.ebi.ac.uk/pdbsum/6a3z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a3z ProSAT]</span></td></tr>
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<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=6a3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a3z OCA], [http://pdbe.org/6a3z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a3z RCSB], [http://www.ebi.ac.uk/pdbsum/6a3z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a3z ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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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[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>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: RING-type E3 ubiquitin transferase]]
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[[Category: Miyamoto K]]
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[[Category: Miyamoto, K]]
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[[Category: Hrd1]]
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[[Category: Metal binding protein]]
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Current revision

Zinc finger domain from the HRD1 Protein

PDB ID 6a3z

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