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RNF2

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{{Short description|Protein-coding gene in the species Homo sapiens}}

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E3 ubiquitin-protein ligase RING2 is an enzyme that in humans is encoded by the RNF2 gene.{{cite journal |vauthors=Lee SJ, Choi JY, Sung YM, Park H, Rhim H, Kang S | title = E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme | journal = FEBS Lett | volume = 503 | issue = 1 | pages = 61–4 |date=August 2001 | pmid = 11513855 | doi =10.1016/S0014-5793(01)02689-8 | s2cid = 42977319 | doi-access = }}{{cite web | title = Entrez Gene: RNF2 ring finger protein 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6045}}

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.

Interactions

RNF2 has been shown to interact with TFCP2{{cite journal |last=Tuckfield |first=Annabel |author2=Clouston David R |author3=Wilanowski Tomasz M |author4=Zhao Lin-Lin |author5=Cunningham John M |author6=Jane Stephen M |date=March 2002 |title=Binding of the RING polycomb proteins to specific target genes in complex with the grainyhead-like family of developmental transcription factors |journal=Mol. Cell. Biol. |volume=22 |issue=6 |pages=1936–46 | issn = 0270-7306| pmid = 11865070 |doi=10.1128/MCB.22.6.1936-1946.2002 |pmc=135618 }} and HIP2.

See also

References

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Further reading

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  • {{cite journal |vauthors=García E, Marcos-Gutiérrez C, del Mar Lorente M, etal |title=RYBP, a new repressor protein that interacts with components of the mammalian Polycomb complex, and with the transcription factor YY1 |journal=EMBO J. |volume=18 |issue= 12 |pages= 3404–18 |year= 1999 |pmid= 10369680 |doi= 10.1093/emboj/18.12.3404 | pmc=1171420 }}
  • {{cite journal |vauthors=Tuckfield A, Clouston DR, Wilanowski TM, etal |title=Binding of the RING polycomb proteins to specific target genes in complex with the grainyhead-like family of developmental transcription factors |journal=Mol. Cell. Biol. |volume=22 |issue= 6 |pages= 1936–46 |year= 2002 |pmid= 11865070 |doi=10.1128/MCB.22.6.1936-1946.2002 | pmc=135618 }}
  • {{cite journal |vauthors=Levine SS, Weiss A, Erdjument-Bromage H, etal |title=The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans |journal=Mol. Cell. Biol. |volume=22 |issue= 17 |pages= 6070–8 |year= 2002 |pmid= 12167701 |doi=10.1128/MCB.22.17.6070-6078.2002 | pmc=134016 }}
  • {{cite journal |vauthors=Suzuki M, Mizutani-Koseki Y, Fujimura Y, etal |title=Involvement of the Polycomb-group gene Ring1B in the specification of the anterior-posterior axis in mice |journal=Development |volume=129 |issue= 18 |pages= 4171–83 |year= 2002 |doi=10.1242/dev.129.18.4171 |pmid= 12183370 }}
  • {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
  • {{cite journal |vauthors=Voncken JW, Roelen BA, Roefs M, etal |title=Rnf2 (Ring1b) deficiency causes gastrulation arrest and cell cycle inhibition |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 5 |pages= 2468–73 |year= 2003 |pmid= 12589020 |doi= 10.1073/pnas.0434312100 | pmc=151364 |bibcode=2003PNAS..100.2468V |doi-access=free }}
  • {{cite journal |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |doi-access= free }}
  • {{cite journal |vauthors=Obuse C, Yang H, Nozaki N, etal |title=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 |journal=Genes Cells |volume=9 |issue= 2 |pages= 105–20 |year= 2004 |pmid= 15009096 |doi=10.1111/j.1365-2443.2004.00705.x |s2cid=21813024 |doi-access=free }}
  • {{cite journal |vauthors=Wang H, Wang L, Erdjument-Bromage H, etal |title=Role of histone H2A ubiquitination in Polycomb silencing |journal=Nature |volume=431 |issue= 7010 |pages= 873–8 |year= 2004 |pmid= 15386022 |doi= 10.1038/nature02985 |bibcode=2004Natur.431..873W |s2cid=4344378 }}
  • {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
  • {{cite journal |vauthors=Voncken JW, Niessen H, Neufeld B, etal |title=MAPKAP kinase 3pK phosphorylates and regulates chromatin association of the polycomb group protein Bmi1 |journal=J. Biol. Chem. |volume=280 |issue= 7 |pages= 5178–87 |year= 2005 |pmid= 15563468 |doi= 10.1074/jbc.M407155200 |doi-access= free }}
  • {{cite journal |vauthors=Barrios-Rodiles M, Brown KR, Ozdamar B, etal |title=High-throughput mapping of a dynamic signaling network in mammalian cells |journal=Science |volume=307 |issue= 5715 |pages= 1621–5 |year= 2005 |pmid= 15761153 |doi= 10.1126/science.1105776 |bibcode=2005Sci...307.1621B |s2cid=39457788 }}
  • {{cite journal |vauthors=Lee SJ, Choi D, Rhim H, Kang S |title=E3 ubiquitin ligase RNF2 interacts with the S6' proteasomal ATPase subunit and increases the ATP hydrolysis activity of S6' |journal=Biochem. J. |volume=389 |issue= Pt 2 |pages= 457–63 |year= 2005 |pmid= 15773819 |doi= 10.1042/BJ20041982 | pmc=1175123 }}
  • {{cite journal |vauthors=Glinsky GV, Berezovska O, Glinskii AB |title=Microarray analysis identifies a death-from-cancer signature predicting therapy failure in patients with multiple types of cancer |journal=J. Clin. Invest. |volume=115 |issue= 6 |pages= 1503–21 |year= 2005 |pmid= 15931389 |doi= 10.1172/JCI23412 | pmc=1136989 }}
  • {{cite journal |vauthors=Dou Y, Milne TA, Tackett AJ, etal |title=Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF |journal=Cell |volume=121 |issue= 6 |pages= 873–85 |year= 2005 |pmid= 15960975 |doi= 10.1016/j.cell.2005.04.031 |s2cid=14717470 |doi-access=free }}
  • {{cite journal |vauthors=Rual JF, Venkatesan K, Hao T, etal |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |bibcode=2005Natur.437.1173R |s2cid=4427026 }}
  • {{cite journal |vauthors=Cao R, Tsukada Y, Zhang Y |title=Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing |journal=Mol. Cell |volume=20 |issue= 6 |pages= 845–54 |year= 2006 |pmid= 16359901 |doi= 10.1016/j.molcel.2005.12.002 |doi-access= free }}
  • {{cite journal |vauthors=Gregory SG, Barlow KF, McLay KE, etal |title=The DNA sequence and biological annotation of human chromosome 1 |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 |bibcode=2006Natur.441..315G |doi-access=free }}
  • {{cite journal |vauthors=Li Z, Cao R, Wang M, etal |title=Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex |journal=J. Biol. Chem. |volume=281 |issue= 29 |pages= 20643–9 |year= 2006 |pmid= 16714294 |doi= 10.1074/jbc.M602461200 |doi-access= free }}

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{{PDB Gallery|geneid=6045}}

External links

  • {{MeshName|RNF2+protein,+human}}

Category:RING finger proteins

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