8bja

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'''Unreleased structure'''
 
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The entry 8bja is ON HOLD until 2024-11-03
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==Structure of the human UBR5 Dimer==
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<StructureSection load='8bja' size='340' side='right'caption='[[8bja]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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Authors: Hodakova, Z., Grishkovskaya, I., Haselbach, D.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8bja]] is a 2 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=8BJA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BJA FirstGlance]. <br>
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Description: Structure of the human UBR5 Dimer
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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&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<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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[[Category: Haselbach, D]]
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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=8bja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bja OCA], [https://pdbe.org/8bja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bja RCSB], [https://www.ebi.ac.uk/pdbsum/8bja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bja ProSAT]</span></td></tr>
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[[Category: Hodakova, Z]]
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</table>
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[[Category: Grishkovskaya, I]]
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== Function ==
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[https://www.uniprot.org/uniprot/UBR5_HUMAN UBR5_HUMAN] E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity). Involved in maturation and/or transcriptional regulation of mRNA by activating CDK9 by polyubiquitination. May play a role in control of cell cycle progression. May have tumor suppressor function. Regulates DNA topoisomerase II binding protein (TopBP1) in the DNA damage response. Plays an essential role in extraembryonic development. Ubiquitinates acetylated PCK1. Also acts as a regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes.<ref>PMID:21127351</ref> <ref>PMID:21726808</ref> <ref>PMID:22884692</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: Grishkovskaya I]]
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[[Category: Haselbach D]]
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[[Category: Hodakova Z]]

Revision as of 07:16, 12 July 2023

Structure of the human UBR5 Dimer

PDB ID 8bja

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