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4qn1

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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=4qn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qn1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qn1 RCSB], [http://www.ebi.ac.uk/pdbsum/4qn1 PDBsum]</span></td></tr>
<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=4qn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qn1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qn1 RCSB], [http://www.ebi.ac.uk/pdbsum/4qn1 PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/SHPRH_HUMAN SHPRH_HUMAN]] E3 ubiquitin-protein ligase involved in DNA repair. Upon genotoxic stress, accepts ubiquitin from the UBE2N-UBE2V2 E2 complex and transfers it to 'Lys-164' of PCNA which had been monoubiquitinated by UBE2A/B-RAD18, promoting the formation of non-canonical poly-ubiquitin chains linked through 'Lys-63'.<ref>PMID:17130289</ref> <ref>PMID:17108083</ref> <ref>PMID:18719106</ref>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 15:32, 25 December 2014

Crystal Structure of a Functionally Uncharacterized Domain of E3 Ubiquitin Ligase SHPRH

4qn1, resolution 2.48Å

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