4l1m

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m (Protected "4l1m" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4l1m| PDB=4l1m | SCENE= }}
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===Structure of the first RCC1-like domain of HERC2===
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The entry 4l1m is ON HOLD
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==Function==
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[[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>
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Authors: Tempel, W., Khan, M.B., Dong, A., Hu, J., Li, Y., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Tong, Y., Structural Genomics Consortium (SGC)
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==About this Structure==
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[[4l1m]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L1M OCA].
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Description: Structure of the first RCC1-like domain of HERC2
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Bountra, C.]]
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[[Category: Dong, A.]]
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[[Category: Edwards, A M.]]
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[[Category: Hu, J.]]
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[[Category: Khan, M B.]]
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[[Category: Li, Y.]]
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[[Category: SGC, Structural Genomics Consortium.]]
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[[Category: Tempel, W.]]
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[[Category: Tong, Y.]]
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[[Category: Beta-propeller]]
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[[Category: Herc2]]
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[[Category: Ligase]]
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[[Category: Rcc1]]
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[[Category: Rld]]
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[[Category: Sgc]]
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[[Category: Structural genomics consortium]]

Revision as of 14:20, 3 July 2013

Template:STRUCTURE 4l1m

Contents

Structure of the first RCC1-like domain of HERC2

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]

About this Structure

4l1m is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  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

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