RNF2

RNF2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2H0D, 3GS2, 3H8H, 3IXS, 3RPG, 4R8P, 4S3O
Identifiers
Aliases	RNF2, BAP-1, BAP1, DING, HIPI3, RING1B, RING2, ring finger protein 2, ring1B, LUSYAM
External IDs	OMIM: 608985 MGI: 1101759 HomoloGene: 2199 GeneCards: RNF2
Gene location (Human)
Chr.	Chromosome 1 (human)
End	185,102,603 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	151,376,706 bp
RNA expression pattern
	Top expressed in
	ganglionic eminence; ; islet of Langerhans; ; stromal cell of endometrium; ; monocyte; ; Achilles tendon; ; rectum; ; gallbladder; ; prefrontal cortex; ; bone marrow cells; ; left adrenal gland;
	Top expressed in
	medial ganglionic eminence; ; secondary oocyte; ; atrioventricular valve; ; maxillary prominence; ; barrel cortex; ; primitive streak; ; abdominal wall; ; left lung lobe; ; endocardial cushion; ; dermis;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	ubiquitin protein ligase activity; chromatin binding; RING-like zinc finger domain binding; metal ion binding; ubiquitin-protein transferase activity; protein binding; transferase activity; zinc ion binding;
Cellular component	euchromatin; sex chromatin; ubiquitin ligase complex; nucleoplasm; chromosome; heterochromatin; MLL1 complex; PRC1 complex; PcG protein complex; nucleus; nuclear body;
Biological process	germ cell development; histone H2A-K119 monoubiquitination; regulation of transcription, DNA-templated; gastrulation with mouth forming second; histone H2A monoubiquitination; negative regulation of transcription by RNA polymerase II; negative regulation of DNA-binding transcription factor activity; transcription, DNA-templated; protein ubiquitination; mitotic cell cycle; anterior/posterior axis specification; histone ubiquitination; negative regulation of G0 to G1 transition;
	Sources:Amigo / QuickGO
Orthologs
	6045
	19821
	ENSG00000121481
	ENSMUSG00000026484
	Q99496
	Q9CQJ4
	NM_007212
	NM_011277; NM_001360844; NM_001360845; NM_001360847
	NP_009143
	NP_035407; NP_001347773; NP_001347774; NP_001347776
	Wikidata
View/Edit Human	View/Edit Mouse

E3 ubiquitin-protein ligase RING2 is an enzyme that in humans is encoded by the RNF2 gene.^[5]^[6]

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.^[6]

Interactions

RNF2 has been shown to interact with TFCP2^[7] and HIP2.^[5]

References

^ a b c GRCh38: Ensembl release 89: ENSG00000121481 – Ensembl, May 2017
^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026484 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ a b 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. S2CID 42977319.
^ a b "Entrez Gene: RNF2 ring finger protein 2".
^ Tuckfield A, 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. 22 (6): 1936–46. doi:10.1128/MCB.22.6.1936-1946.2002. ISSN 0270-7306. PMC 135618. PMID 11865070.

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. doi:10.1242/dev.129.18.4171. 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2003PNAS..100.2468V. doi:10.1073/pnas.0434312100. PMC 151364. PMID 12589020.
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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.
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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.
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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.
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