7uv8
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7uv8]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UV8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7uv8]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UV8 FirstGlance]. <br> | ||
| - | </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=7uv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uv8 OCA], [https://pdbe.org/7uv8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uv8 RCSB], [https://www.ebi.ac.uk/pdbsum/7uv8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uv8 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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=7uv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uv8 OCA], [https://pdbe.org/7uv8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uv8 RCSB], [https://www.ebi.ac.uk/pdbsum/7uv8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uv8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/UBC2_YEAST UBC2_YEAST] Catalyzes the covalent attachment of ubiquitin to other proteins. In association with the E3 enzyme BRE1 and LGE1, it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 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 association with the E3 enzyme RAD18, it catalyzes the monoubiquitination of POL30 'Lys-164', involved in postreplication repair of UV-damaged DNA. The RAD6/UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine. In association with the E3 enzyme UBR1, is involved in N-end rule-dependent protein degradation. Also involved in sporulation.<ref>PMID:3306404</ref> <ref>PMID:7038392</ref> <ref>PMID:2157209</ref> <ref>PMID:1651502</ref> <ref>PMID:2065660</ref> <ref>PMID:8436296</ref> <ref>PMID:7926769</ref> <ref>PMID:9287349</ref> <ref>PMID:9343433</ref> <ref>PMID:10880451</ref> <ref>PMID:12077605</ref> <ref>PMID:12226657</ref> <ref>PMID:14752010</ref> <ref>PMID:15388802</ref> <ref>PMID:16307922</ref> <ref>PMID:15632065</ref> <ref>PMID:16247017</ref> | [https://www.uniprot.org/uniprot/UBC2_YEAST UBC2_YEAST] Catalyzes the covalent attachment of ubiquitin to other proteins. In association with the E3 enzyme BRE1 and LGE1, it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 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 association with the E3 enzyme RAD18, it catalyzes the monoubiquitination of POL30 'Lys-164', involved in postreplication repair of UV-damaged DNA. The RAD6/UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine. In association with the E3 enzyme UBR1, is involved in N-end rule-dependent protein degradation. Also involved in sporulation.<ref>PMID:3306404</ref> <ref>PMID:7038392</ref> <ref>PMID:2157209</ref> <ref>PMID:1651502</ref> <ref>PMID:2065660</ref> <ref>PMID:8436296</ref> <ref>PMID:7926769</ref> <ref>PMID:9287349</ref> <ref>PMID:9343433</ref> <ref>PMID:10880451</ref> <ref>PMID:12077605</ref> <ref>PMID:12226657</ref> <ref>PMID:14752010</ref> <ref>PMID:15388802</ref> <ref>PMID:16307922</ref> <ref>PMID:15632065</ref> <ref>PMID:16247017</ref> | ||
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| + | ==See Also== | ||
| + | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Rad6-Bre1 Complex
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