RNF2

Ring finger protein 2
PDB rendering based on 2ckl.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2H0D​, 3GS2​, 3H8H​, 3IXS​, 3RPG​, 4R8P​
Identifiers
Symbols	RNF2 ; BAP-1; BAP1; DING; HIPI3; RING1B; RING2
External IDs	OMIM: 608985 MGI: 1101759 HomoloGene: 2199 GeneCards: RNF2 Gene
EC number	6.3.2.-
Gene ontology Molecular function • chromatin binding • ubiquitin-protein transferase activity • protein binding • zinc ion binding • ligase activity • ubiquitin protein ligase activity • RING-like zinc finger domain binding Cellular component • ubiquitin ligase complex • euchromatin • sex chromatin • nucleus • nucleoplasm • nuclear body • PcG protein complex • PRC1 complex • MLL1 complex Biological process • negative regulation of transcription from RNA polymerase II promoter • mitotic cell cycle • gastrulation with mouth forming second • transcription, DNA-templated • germ cell development • anterior/posterior axis specification • protein sumoylation • histone H2A monoubiquitination • histone H2A-K119 monoubiquitination • negative regulation of sequence-specific DNA binding transcription factor activity • post-translational protein modification • cellular protein metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6045	19821
Ensembl	ENSG00000121481	ENSMUSG00000026484
UniProt	Q99496	Q9CQJ4
RefSeq (mRNA)	NM_007212	NM_011277
RefSeq (protein)	NP_009143	NP_035407
Location (UCSC)	Chr 1: 185.05 – 185.1 Mb	Chr 1: 151.46 – 151.5 Mb
PubMed search

E3 ubiquitin-protein ligase RING2 is an enzyme that in humans is encoded by the RNF2 gene.^[1][2]

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.^[2]

Interactions

RNF2 has been shown to interact with TFCP2^[3] and HIP2.^[1]

See also

• RING finger domain

References

1. Lee SJ, Choi JY, Sung YM, Park H, Rhim H, Kang S (August 2001). "E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme". FEBS Lett 503 (1): 61–4. doi:10.1016/S0014-5793(01)02689-8. PMID 11513855.
2. "Entrez Gene: RNF2 ring finger protein 2".
3. Tuckfield, Annabel; Clouston David R; Wilanowski Tomasz M; Zhao Lin-Lin; Cunningham John M; Jane Stephen M (March 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. (United States) 22 (6): 1936–46. doi:10.1128/MCB.22.6.1936-1946.2002. ISSN 0270-7306. PMC 135618. PMID 11865070.

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. PMC 1171420. PMID 10369680.
• 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. doi:10.1128/MCB.22.6.1936-1946.2002. PMC 135618. 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. doi:10.1128/MCB.22.17.6070-6078.2002. PMC 134016. 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. PMC 139241. 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. PMC 151364. 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. doi:10.1111/j.1365-2443.2004.00705.x. 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. PMC 528928. 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. PMC 1175123. 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. PMC 1136989. 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.

External links

• RNF2 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)