Biology:RING1
Generic protein structure example |
E3 ubiquitin-protein ligase RING1 is an enzyme that in humans is encoded by the RING1 gene.[1][2]
Function
This gene belongs to the RING finger family, members of which encode proteins characterized by a RING domain, a zinc-binding motif related to the zinc finger domain. The gene product can bind DNA and can act as a transcriptional repressor. It is 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 large nuclear domains. It interacts with the CBX4 protein via its glycine-rich C-terminal domain. The gene maps to the HLA class II region, where it is contiguous with the RING finger genes FABGL and HKE4.[2]
Interactions
RING1 has been shown to interact with CBX8,[3] BMI1[4][5] and RYBP.[6][7]
References
- ↑ "New genes in the class II region of the human major histocompatibility complex". Genomics 10 (2): 417–24. Jun 1991. doi:10.1016/0888-7543(91)90327-B. PMID 1906426.
- ↑ 2.0 2.1 "Entrez Gene: RING1 ring finger protein 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6015.
- ↑ "HPC3 is a new human polycomb orthologue that interacts and associates with RING1 and Bmi1 and has transcriptional repression properties". The Journal of Biological Chemistry 275 (37): 28785–92. Sep 2000. doi:10.1074/jbc.M001835200. PMID 10825164.
- ↑ "RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressor". Molecular and Cellular Biology 17 (7): 4105–13. Jul 1997. doi:10.1128/mcb.17.7.4105. PMID 9199346.
- ↑ "RING1 interacts with multiple Polycomb-group proteins and displays tumorigenic activity". Molecular and Cellular Biology 19 (1): 57–68. Jan 1999. doi:10.1128/mcb.19.1.57. PMID 9858531.
- ↑ "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. Oct 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- ↑ "RYBP, a new repressor protein that interacts with components of the mammalian Polycomb complex, and with the transcription factor YY1". The EMBO Journal 18 (12): 3404–18. Jun 1999. doi:10.1093/emboj/18.12.3404. PMID 10369680.
Further reading
- "Identification and preliminary characterization of a protein motif related to the zinc finger". Proceedings of the National Academy of Sciences of the United States of America 90 (6): 2112–6. Mar 1993. doi:10.1073/pnas.90.6.2112. PMID 7681583. Bibcode: 1993PNAS...90.2112L.
- "RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressor". Molecular and Cellular Biology 17 (7): 4105–13. Jul 1997. doi:10.1128/mcb.17.7.4105. PMID 9199346.
- "Physical mapping 220 kb centromeric of the human MHC and DNA sequence analysis of the 43-kb segment including the RING1, HKE6, and HKE4 genes". Genomics 42 (3): 422–35. Jun 1997. doi:10.1006/geno.1997.4745. PMID 9205114.
- "RING1 interacts with multiple Polycomb-group proteins and displays tumorigenic activity". Molecular and Cellular Biology 19 (1): 57–68. Jan 1999. doi:10.1128/mcb.19.1.57. PMID 9858531.
- "RYBP, a new repressor protein that interacts with components of the mammalian Polycomb complex, and with the transcription factor YY1". The EMBO Journal 18 (12): 3404–18. Jun 1999. doi:10.1093/emboj/18.12.3404. PMID 10369680.
- "HPC3 is a new human polycomb orthologue that interacts and associates with RING1 and Bmi1 and has transcriptional repression properties". The Journal of Biological Chemistry 275 (37): 28785–92. Sep 2000. doi:10.1074/jbc.M001835200. PMID 10825164.
- "The E2F6 transcription factor is a component of the mammalian Bmi1-containing polycomb complex". Proceedings of the National Academy of Sciences of the United States of America 98 (4): 1519–24. Feb 2001. doi:10.1073/pnas.041597698. PMID 11171983.
- "Linking the Rb and polycomb pathways". Molecular Cell 8 (3): 557–69. Sep 2001. doi:10.1016/S1097-2765(01)00346-X. PMID 11583618.
- "A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells". Science 296 (5570): 1132–6. May 2002. doi:10.1126/science.1069861. PMID 12004135. Bibcode: 2002Sci...296.1132O.
- "MBLR, a new RING finger protein resembling mammalian Polycomb gene products, is regulated by cell cycle-dependent phosphorylation". Genes to Cells 7 (8): 835–50. Aug 2002. doi:10.1046/j.1365-2443.2002.00565.x. PMID 12167161. https://deepblue.lib.umich.edu/bitstream/2027.42/72663/1/j.1365-2443.2002.00565.x.pdf.
- "The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans". Molecular and Cellular Biology 22 (17): 6070–8. Sep 2002. doi:10.1128/MCB.22.17.6070-6078.2002. PMID 12167701.
- "Polycomb CBX7 has a unifying role in cellular lifespan". Nature Cell Biology 6 (1): 67–72. Jan 2004. doi:10.1038/ncb1077. PMID 14647293.
- "Proteomics analysis of the centromere complex from HeLa interphase cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of the CEN-complex, while BMI-1 is transiently co-localized with the centromeric region in interphase". Genes to Cells 9 (2): 105–20. Feb 2004. doi:10.1111/j.1365-2443.2004.00705.x. PMID 15009096.
- "Role of histone H2A ubiquitination in Polycomb silencing". Nature 431 (7010): 873–8. Oct 2004. doi:10.1038/nature02985. PMID 15386022. Bibcode: 2004Natur.431..873W.
- "The PcG protein HPC2 inhibits RBP-J-mediated transcription by interacting with LIM protein KyoT2". FEBS Letters 579 (5): 1220–6. Feb 2005. doi:10.1016/j.febslet.2005.01.022. PMID 15710417.
External links
- RING1+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
Original source: https://en.wikipedia.org/wiki/RING1.
Read more |