RNF2

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Ring finger protein 2
PDB rendering based on 2ckl.
Available structures: 2ckl, 2h0d
Identifiers
Symbol(s) RNF2; BAP-1; BAP1; DING; HIPI3; RING1B; RING2
External IDs OMIM: 608985 MGI1101759 HomoloGene2199
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 6045 19821
Ensembl ENSG00000121481 ENSMUSG00000026484
Uniprot Q99496 Q9CQJ4
Refseq NM_007212 (mRNA)
NP_009143 (protein)
NM_011277 (mRNA)
NP_035407 (protein)
Location Chr 1: 183.28 - 183.34 Mb Chr 1: 153.23 - 153.26 Mb
Pubmed search [1] [2]

Ring finger protein 2, also known as RNF2, is a human gene.[1]

Polycomb group (PcG) of proteins form the multiprotein complexes that are important for the transcription repression of various genes involved in development and cell proliferation. The protein encoded by this gene is one of the PcG proteins. It has been shown to interact with, and suppress the activity of, transcription factor CP2 (TFCP2/CP2). Studies of the mouse counterpart suggested the involvement of this gene in the specification of anterior-posterior axis, as well as in cell proliferation in early development. This protein was also found to interact with huntingtin interacting protein 2 (HIP2), an ubiquitin-conjugating enzyme, and possess ubiquitin ligase activity.[1]

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[edit] See also

[edit] References

[edit] Further reading

  • García E, Marcos-Gutiérrez C, del Mar Lorente M, et al. (1999). "RYBP, a new repressor protein that interacts with components of the mammalian Polycomb complex, and with the transcription factor YY1.". EMBO J. 18 (12): 3404–18. doi:10.1093/emboj/18.12.3404. PMID 10369680. 
  • Lee SJ, Choi JY, Sung YM, et al. (2001). "E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme.". FEBS Lett. 503 (1): 61–4. PMID 11513855. 
  • Tuckfield A, Clouston DR, Wilanowski TM, et al. (2002). "Binding of the RING polycomb proteins to specific target genes in complex with the grainyhead-like family of developmental transcription factors.". Mol. Cell. Biol. 22 (6): 1936–46. PMID 11865070. 
  • Levine SS, Weiss A, Erdjument-Bromage H, et al. (2002). "The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans.". Mol. Cell. Biol. 22 (17): 6070–8. PMID 12167701. 
  • Suzuki M, Mizutani-Koseki Y, Fujimura Y, et al. (2002). "Involvement of the Polycomb-group gene Ring1B in the specification of the anterior-posterior axis in mice.". Development 129 (18): 4171–83. PMID 12183370. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Voncken JW, Roelen BA, Roefs M, et al. (2003). "Rnf2 (Ring1b) deficiency causes gastrulation arrest and cell cycle inhibition.". Proc. Natl. Acad. Sci. U.S.A. 100 (5): 2468–73. doi:10.1073/pnas.0434312100. PMID 12589020. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
  • Obuse C, Yang H, Nozaki N, et al. (2004). "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 Cells 9 (2): 105–20. PMID 15009096. 
  • Wang H, Wang L, Erdjument-Bromage H, et al. (2004). "Role of histone H2A ubiquitination in Polycomb silencing.". Nature 431 (7010): 873–8. doi:10.1038/nature02985. PMID 15386022. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334. 
  • Voncken JW, Niessen H, Neufeld B, et al. (2005). "MAPKAP kinase 3pK phosphorylates and regulates chromatin association of the polycomb group protein Bmi1.". J. Biol. Chem. 280 (7): 5178–87. doi:10.1074/jbc.M407155200. PMID 15563468. 
  • Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells.". Science 307 (5715): 1621–5. doi:10.1126/science.1105776. PMID 15761153. 
  • Lee SJ, Choi D, Rhim H, Kang S (2005). "E3 ubiquitin ligase RNF2 interacts with the S6' proteasomal ATPase subunit and increases the ATP hydrolysis activity of S6'.". Biochem. J. 389 (Pt 2): 457–63. doi:10.1042/BJ20041982. PMID 15773819. 
  • Glinsky GV, Berezovska O, Glinskii AB (2005). "Microarray analysis identifies a death-from-cancer signature predicting therapy failure in patients with multiple types of cancer.". J. Clin. Invest. 115 (6): 1503–21. doi:10.1172/JCI23412. PMID 15931389. 
  • Dou Y, Milne TA, Tackett AJ, et al. (2005). "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.". Cell 121 (6): 873–85. doi:10.1016/j.cell.2005.04.031. PMID 15960975. 
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
  • Cao R, Tsukada Y, Zhang Y (2006). "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing.". Mol. Cell 20 (6): 845–54. doi:10.1016/j.molcel.2005.12.002. PMID 16359901. 
  • Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414. 
  • Li Z, Cao R, Wang M, et al. (2006). "Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex.". J. Biol. Chem. 281 (29): 20643–9. doi:10.1074/jbc.M602461200. PMID 16714294. 

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