E3 ubiquitin-protein ligase RING2
Definition:
References:
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[1]. Asad M Taherbhoy, et al. BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase. Nat Commun. 2015 Jul 7;6:7621. [Content Brief]
[2]. Hengbin Wang, et al. Role of histone H2A ubiquitination in Polycomb silencing. Nature. 2004 Oct 14;431(7010):873-8. [Content Brief]
[3]. Ru Cao, et al. Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing. Mol Cell. 2005 Dec 22;20(6):845-54. [Content Brief]
[4]. Zhonghua Gao, et al. An AUTS2-Polycomb complex activates gene expression in the CNS. Nature. 2014 Dec 18;516(7531):349-54. [Content Brief]
[5]. Zhizhong Li, et al. Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex. J Biol Chem. 2006 Jul 21;281(29):20643-9. [Content Brief]
[6]. Robert K McGinty, et al. Crystal structure of the PRC1 ubiquitylation module bound to the nucleosome. Nature. 2014 Oct 30;514(7524):591-6. [Content Brief]
[7]. Renjing Wang, et al. Polycomb group targeting through different binding partners of RING1B C-terminal domain. Structure. 2010 Aug 11;18(8):966-75. [Content Brief]
[8]. Matthew L Bentley, et al. Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin ligase complex. EMBO J. 2011 Jul 19;30(16):3285-97. [Content Brief]
[9]. S J Lee, et al. E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme. FEBS Lett. 2001 Aug 10;503(1):61-4. [Content Brief]
[10]. Xi Luo, et al. Rare deleterious de novo missense variants in Rnf2/Ring2 are associated with a neurodevelopmental disorder with unique clinical features. Hum Mol Genet. 2021 Jun 26;30(14):1283-1292. [Content Brief]