RNF2

Protein-coding gene in the species Homo sapiens

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; OMA:RNF2 - orthologs

Gene location (Human)

Chr.	Chromosome 1 (human)^[1]

Band	1q25.3	Start	185,045,526 bp^[1]
Band	1q25.3	End	185,102,603 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 1 (mouse)^[2]

Band	1\|1 G1	Start	151,333,755 bp^[2]
Band	1\|1 G1	End	151,376,706 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

gonad

ganglionic eminence

ventricular zone

islet of Langerhans

stromal cell of endometrium

testicle

monocyte

Achilles tendon

epithelium of colon

buccal mucosa cell

Top expressed in

genital tubercle

zygote

tail of embryo

medial ganglionic eminence

secondary oocyte

Gonadal ridge

mandibular prominence

atrioventricular valve

maxillary prominence

primary oocyte

More reference expression data

BioGPS


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

Species

Human

Mouse

Entrez


6045


19821

Ensembl


ENSG00000121481


ENSMUSG00000026484

UniProt


Q99496


Q9CQJ4

RefSeq (mRNA)


NM_007212


NM_011277 NM_001360844 NM_001360845 NM_001360847

RefSeq (protein)


NP_009143


NP_035407 NP_001347773 NP_001347774 NP_001347776

Location (UCSC)

Chr 1: 185.05 – 185.1 Mb

Chr 1: 151.33 – 151.38 Mb

PubMed search

^[3]

^[4]

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.
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. S2CID 21813024.
Wang H, Wang L, Erdjument-Bromage H, et al. (2004). "Role of histone H2A ubiquitination in Polycomb silencing". Nature. 431 (7010): 873–8. Bibcode:2004Natur.431..873W. doi:10.1038/nature02985. PMID 15386022. S2CID 4344378.
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. Bibcode:2005Sci...307.1621B. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.
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. S2CID 14717470.
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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
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. Bibcode:2006Natur.441..315G. 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.