|Other Names||E3 ubiquitin-protein ligase RING1, 632-, Polycomb complex protein RING1, RING finger protein 1, Really interesting new gene 1 protein, RING1, RNF1|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Constitutes one of the E3 ubiquitin-protein ligases that mediate monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. Compared to RNF2/RING2, it does not have the main E3 ubiquitin ligase activity on histone H2A, and it may rather act as a modulator of RNF2/RING2 activity.|
|Cellular Location||Nucleus. Nucleus speckle|
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This gene belongs to the RING finger family, members ofwhich encode proteins characterized by a RING domain, azinc-binding motif related to the zinc finger domain. The geneproduct can bind DNA and can act as a transcriptional repressor. Itis associated with the multimeric polycomb group protein complex.The gene product interacts with the polycomb group proteins BMI1,EDR1, and CBX4, and colocalizes with these proteins in largenuclear domains. It interacts with the CBX4 protein via itsglycine-rich C-terminal domain. The gene maps to the HLA class IIregion, where it is contiguous with the RING finger genes FABGL andHKE4.
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)de Bie, P., et al. Biochem. Biophys. Res. Commun. 400(3):389-395(2010)Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)Barcellos, L.F., et al. PLoS Genet. 5 (10), E1000696 (2009) :Vidal, M. Int. J. Dev. Biol. 53 (2-3), 355-370 (2009) :
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