2y4w: Difference between revisions
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==Solution structure of human ubiquitin conjugating enzyme Rad6b== | ==Solution structure of human ubiquitin conjugating enzyme Rad6b== | ||
<StructureSection load='2y4w' size='340' side='right' caption='[[2y4w | <StructureSection load='2y4w' size='340' side='right'caption='[[2y4w]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2y4w]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2y4w]] 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=2Y4W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y4W FirstGlance]. <br> | ||
</ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<tr><td class="sblockLbl"><b> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y4w OCA], [https://pdbe.org/2y4w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y4w RCSB], [https://www.ebi.ac.uk/pdbsum/2y4w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y4w ProSAT]</span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </table> | ||
<table> | == Function == | ||
[https://www.uniprot.org/uniprot/UBE2B_HUMAN UBE2B_HUMAN] Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'- and 'Lys-63'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA. Associates to the E3 ligase RAD18 to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. May be involved in neurite outgrowth.<ref>PMID:1717990</ref> <ref>PMID:16337599</ref> <ref>PMID:17130289</ref> <ref>PMID:17108083</ref> <ref>PMID:20061386</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Symmetry and Asymmetry of the RING-RING Dimer of Rad18.,Huang A, Hibbert RG, de Jong RN, Das D, Sixma TK, Boelens R J Mol Biol. 2011 Jul 15;410(3):424-35. Epub 2011 Apr 27. PMID:21549715<ref>PMID:21549715</ref> | Symmetry and Asymmetry of the RING-RING Dimer of Rad18.,Huang A, Hibbert RG, de Jong RN, Das D, Sixma TK, Boelens R J Mol Biol. 2011 Jul 15;410(3):424-35. Epub 2011 Apr 27. PMID:21549715<ref>PMID:21549715</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2y4w" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Boelens | [[Category: Boelens R]] | ||
[[Category: Das | [[Category: Das D]] | ||
[[Category: Hibbert RG]] | |||
[[Category: Hibbert | [[Category: Huang A]] | ||
[[Category: Huang | [[Category: Sixma TK]] | ||
[[Category: Sixma | [[Category: DeJong RN]] | ||
[[Category: | |||