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) [1] Band 1q25.3 Start 185,045,526 bp [1] End 185,102,603 bp [1]
Gene location (Mouse) Chr. Chromosome 1 (mouse) [2] Band 1|1 G1 Start 151,333,755 bp [2] End 151,376,706 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) 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 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]

See also

• RING finger domain

References

1. GRCh38: Ensembl release 89: ENSG00000121481 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026484 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: RNF2 ring finger protein 2".
7. 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.

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. 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.

External links

• RNF2+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)