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==The third RLD domain of HERC2==
==The third RLD domain of HERC2==
<StructureSection load='3kci' size='340' side='right' caption='[[3kci]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3kci' size='340' side='right'caption='[[3kci]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3kci]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KCI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KCI FirstGlance]. <br>
<table><tr><td colspan='2'>[[3kci]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KCI FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">D15F37S1, DKFZP547P028, HERC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 1.8&#8491;</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=3kci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kci OCA], [http://pdbe.org/3kci PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kci RCSB], [http://www.ebi.ac.uk/pdbsum/3kci PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kci ProSAT]</span></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=3kci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kci OCA], [https://pdbe.org/3kci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kci RCSB], [https://www.ebi.ac.uk/pdbsum/3kci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kci ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/HERC2_HUMAN HERC2_HUMAN]] E3 ubiquitin-protein ligase that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. Recruited to sites of DNA damage in response to ionizing radiation (IR) and facilitates the assembly of UBE2N and RNF8 promoting DNA damage-induced formation of 'Lys-63'-linked ubiquitin chains. Acts as a mediator of binding specificity between UBE2N and RNF8. Involved in the maintenance of RNF168 levels. E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of XPA which influences the circadian oscillation of DNA excision repair activity.<ref>PMID:20023648</ref> <ref>PMID:20304803</ref> <ref>PMID:22508508</ref>
[https://www.uniprot.org/uniprot/HERC2_HUMAN HERC2_HUMAN] E3 ubiquitin-protein ligase that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. Recruited to sites of DNA damage in response to ionizing radiation (IR) and facilitates the assembly of UBE2N and RNF8 promoting DNA damage-induced formation of 'Lys-63'-linked ubiquitin chains. Acts as a mediator of binding specificity between UBE2N and RNF8. Involved in the maintenance of RNF168 levels. E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of XPA which influences the circadian oscillation of DNA excision repair activity.<ref>PMID:20023648</ref> <ref>PMID:20304803</ref> <ref>PMID:22508508</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Arrowsmith, C H]]
[[Category: Large Structures]]
[[Category: Bochkarev, A]]
[[Category: Arrowsmith CH]]
[[Category: Bountra, C]]
[[Category: Bochkarev A]]
[[Category: Dhe-Paganon, S]]
[[Category: Bountra C]]
[[Category: Edwards, A M]]
[[Category: Dhe-Paganon S]]
[[Category: Qiu, L]]
[[Category: Edwards AM]]
[[Category: Vesterberg, A]]
[[Category: Qiu L]]
[[Category: Walker, J R]]
[[Category: Vesterberg A]]
[[Category: Weigelt, J]]
[[Category: Walker JR]]
[[Category: Coiled coil]]
[[Category: Weigelt J]]
[[Category: Ligase]]
[[Category: Metal-binding]]
[[Category: Phosphoprotein]]
[[Category: Rcc1]]
[[Category: Sgc]]
[[Category: Structural genomic]]
[[Category: Ubl conjugation pathway]]
[[Category: Wd repeat]]
[[Category: Wd40]]
[[Category: Zinc]]
[[Category: Zinc-finger]]

Latest revision as of 11:13, 6 September 2023

The third RLD domain of HERC2The third RLD domain of HERC2

Structural highlights

3kci is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HERC2_HUMAN E3 ubiquitin-protein ligase that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. Recruited to sites of DNA damage in response to ionizing radiation (IR) and facilitates the assembly of UBE2N and RNF8 promoting DNA damage-induced formation of 'Lys-63'-linked ubiquitin chains. Acts as a mediator of binding specificity between UBE2N and RNF8. Involved in the maintenance of RNF168 levels. E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of XPA which influences the circadian oscillation of DNA excision repair activity.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Bekker-Jensen S, Danielsen JR, Fugger K, Gromova I, Nerstedt A, Bartek J, Lukas J, Mailand N. HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Nat Cell Biol. 2010 Jan;12(1):80-6; sup pp 1-12. Epub 2009 Dec 20. PMID:20023648 doi:ncb2008
  2. ↑ Kang TH, Lindsey-Boltz LA, Reardon JT, Sancar A. Circadian control of XPA and excision repair of cisplatin-DNA damage by cryptochrome and HERC2 ubiquitin ligase. Proc Natl Acad Sci U S A. 2010 Mar 16;107(11):4890-5. doi:, 10.1073/pnas.0915085107. PMID:20304803 doi:10.1073/pnas.0915085107
  3. ↑ Danielsen JR, Povlsen LK, Villumsen BH, Streicher W, Nilsson J, Wikstrom M, Bekker-Jensen S, Mailand N. DNA damage-inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding Zinc finger. J Cell Biol. 2012 Apr 16;197(2):179-87. doi: 10.1083/jcb.201106152. PMID:22508508 doi:10.1083/jcb.201106152

3kci, resolution 1.80Å

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OCA
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