View source for 8p82


==Cryo-EM structure of dimeric UBR5==
<StructureSection load='8p82' size='340' side='right'caption='[[8p82]], [[Resolution|resolution]] 3.36&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8p82]] 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=8P82 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8P82 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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8p82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8p82 OCA], [https://pdbe.org/8p82 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8p82 RCSB], [https://www.ebi.ac.uk/pdbsum/8p82 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8p82 ProSAT]</span></td></tr>
</table>
== Function ==
[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> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Aguirre JD]]
[[Category: Cavadini S]]
[[Category: Kater L]]
[[Category: Kempf G]]
[[Category: Thoma NH]]