2y4w

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<StructureSection load='2y4w' size='340' side='right' caption='[[2y4w]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2y4w' size='340' side='right' caption='[[2y4w]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2y4w]] is a 1 chain structure with sequence from [http://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]. <br>
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<table><tr><td colspan='2'>[[2y4w]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y4W FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nxa|1nxa]], [[1jas|1jas]], [[2y43|2y43]]</td></tr>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nxa|1nxa]], [[1jas|1jas]], [[2y43|2y43]]</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2y4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y4w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y4w RCSB], [http://www.ebi.ac.uk/pdbsum/2y4w PDBsum]</span></td></tr>
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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=2y4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y4w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y4w RCSB], [http://www.ebi.ac.uk/pdbsum/2y4w PDBsum]</span></td></tr>
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<table>
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</table>
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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>
<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>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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==See Also==
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*[[Ubiquitin conjugating enzyme|Ubiquitin conjugating enzyme]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Ubiquitin--protein ligase]]
[[Category: Ubiquitin--protein ligase]]
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[[Category: Boelens, R.]]
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[[Category: Boelens, R]]
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[[Category: Das, D.]]
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[[Category: Das, D]]
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[[Category: Dejong, R N.]]
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[[Category: Dejong, R N]]
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[[Category: Hibbert, R G.]]
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[[Category: Hibbert, R G]]
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[[Category: Huang, A.]]
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[[Category: Huang, A]]
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[[Category: Sixma, T K.]]
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[[Category: Sixma, T K]]
[[Category: Dna damage]]
[[Category: Dna damage]]
[[Category: Dna repair]]
[[Category: Dna repair]]
[[Category: Ligase]]
[[Category: Ligase]]
[[Category: Ubiquitination]]
[[Category: Ubiquitination]]

Revision as of 00:27, 25 December 2014

Solution structure of human ubiquitin conjugating enzyme Rad6b

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