2l4e

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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=2l4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l4e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l4e RCSB], [http://www.ebi.ac.uk/pdbsum/2l4e 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=2l4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l4e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l4e RCSB], [http://www.ebi.ac.uk/pdbsum/2l4e PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/DCN1_YEAST DCN1_YEAST]] Required for neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity. Does not act by preventing deneddylation, but rather facilitates neddylation, possibly by acting with HRT1/RBX1 to recruit the Nedd8-charged E2 UBC12 to the cullin component of SCF-type complexes.<ref>PMID:15988528</ref>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 21:13, 25 December 2014

NMR structure of the UBA domain of S. cerevisiae Dcn1

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