2ybf

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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=2ybf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ybf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ybf RCSB], [http://www.ebi.ac.uk/pdbsum/2ybf 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=2ybf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ybf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ybf RCSB], [http://www.ebi.ac.uk/pdbsum/2ybf PDBsum]</span></td></tr>
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== Function ==
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[[http://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> [[http://www.uniprot.org/uniprot/RAD18_HUMAN RAD18_HUMAN]] E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity.<ref>PMID:17108083</ref> <ref>PMID:21659603</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 20:05, 24 December 2014

COMPLEX OF RAD18 (RAD6 BINDING DOMAIN) WITH RAD6B

2ybf, resolution 2.00Å

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