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Index > Protein center > Rnf2(Gene name) > Mouse
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  • Rnf2 (Gene name),
  • E3 ubiquitin-protein ligase RING2 (Protein name ),  RING2_MOUSE from NCBI database.
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  • General Annotation
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  • Gene name:
    Rnf2(DinG;Ring1b);
    Protein name:
    E3 ubiquitin-protein ligase RING2;
    Alternative:
    RING finger protein 2;RING finger protein 1B(RING1b);
    Organism:
    Mouse (Mus musculus). 
    General Annotation
    Sub Unit:
    Component of chromatin-associated Polycomb (PcG) complexes. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2/RING2, MBLR, L3MBTL2 and YAF2. Component of a PRC1-like complex. Component of some MLL1/MLL complex, at least composed of the core components MLL, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components C17orf49, CHD8, E2F6, HSP70, IN80C, KIAA1267, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with RYBP, HIP2 and TFCP2. Association to the chromosomal DNA is cell-cycle dependent. Component of repressive BCOR complex containing Polycomb group subcomplex at least composed of RYBP, PCGF1, BCOR and RING1. Interacts with Interacts with PCGF2, CBX4, CBX6, CBX7 and CBX8. Interacts with CBX2, BMI and PHC2. Interacts with RYBP, HIP2 and TFCP2.
    Function:
    E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. Association to the chromosomal DNA is cell-cycle dependent.
    Subcellular Location:
    Nucleus Chromosome Enriched on inactive X chromosome (Xi) in female trophoblast stem (TS) cells as well as differentiating embryonic stem (ES) cells. The enrichment on Xi is transient during TS and ES cell differentiation. The association with Xi is mitotically stable in non-differentiated TS cells.
    Protein Attributes:
    Sequence length:
    336
    Sequence:
    50:
    MSQAVQTNGT | QPLSKTWELS | LYELQRTPQE | AITDGLEIVV | SPRSLHSELM | 
    100:
    CPICLDMLKN | TMTTKECLHR | FCADCIITAL | RSGNKECPTC | RKKLVSKRSL | 
    150:
    RPDPNFDALI | SKIYPSRDEY | EAHQERVLAR | INKHNNQQAL | SHSIEEGLKI | 
    200:
    QAMNRLQRGK | KQQIENGSGA | EDNGDSSHCS | NASTHSNQEA | GPSNKRTKTS | 
    250:
    DDSGLELDNN | NAAVAIDPVM | DGASEIELVF | RPHPTLMEKD | DSAQTRYIKT | 
    300:
    SGNATVDHLS | KYLAVRLALE | ELRSKGESNQ | MNLDTASEKQ | YTIYIATASG | 
    336:
    QFTVLNGSFS | LELVSEKYWK | VNKPMELYYA | PTKEHK
    3D Structure:
    N/A
    Predicted Eptitope:
    Please Sign in.
    EIAab Sequence  Vaild Sequence:
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    Related Databases
    String:
    UniGene:
    SMR:
    KEGG:
    UniGene:
    Pfam:
    Uniprot:
     
    FOR
    ELISA Kit for Mouse E3 ubiquitin-protein ligase RING2
    ELISA Kit for Mouse E3 ubiquitin-protein ligase RING2
    ELISA Kit for Mouse E3 ubiquitin-protein ligase RING2
    CLIA Kit for Mouse E3 ubiquitin-protein ligase RING2
    CLIA Kit for Mouse E3 ubiquitin-protein ligase RING2
    CLIA Kit for Mouse E3 ubiquitin-protein ligase RING2
    Polyclonal Antibody for Mouse E3 ubiquitin-protein ligase RING2
    Polyclonal Antibody for Mouse E3 ubiquitin-protein ligase RING2
    Polyclonal Antibody for Mouse E3 ubiquitin-protein ligase RING2
    Monoclonal Antibody for Mouse E3 ubiquitin-protein ligase RING2
    Monoclonal Antibody for Mouse E3 ubiquitin-protein ligase RING2
    Monoclonal Antibody for Mouse E3 ubiquitin-protein ligase RING2
    Protein for Mouse E3 ubiquitin-protein ligase RING2
    Protein for Mouse E3 ubiquitin-protein ligase RING2
    Protein for Mouse E3 ubiquitin-protein ligase RING2

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    Precision
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    Recovery
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    Linearity
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    References
    1. 1.
      "Ring1A is a transcriptional repressor that interacts with the Polycomb-M33 protein and is expressed at rhombomere boundaries in the mouse hindbrain."
      Schoorlemmer J. , Marcos-Gutierrez C. , Were F. , Martinez R. , Garcia E. , Satijn D.P.E. , Otte A.P. , Vidal M.
      EMBO J.16:5930-5942(1997) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];INTERACTION WITH CBX2
      strain: NIH Swiss.
    2. 2.
      "The transcriptional landscape of the mammalian genome."
      Carninci P. , Kasukawa T. , Katayama S. , Gough J. , Frith M.C. , Maeda N. , Oyama R. , Ravasi T. , Lenhard B. , Wells C. , Kodzius R. , Shimokawa K. , Bajic V.B. , Brenner S.E. , Batalov S. , Forrest A.R. , Zavolan M. , Davis M.J. , more...
      Science309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
      strain: C57BL/6J.
      tissue: B-cell.
      tissue: Ovary.
    3. 3.
      "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
      Ebert L. , Muenstermann E. , Schatten R. , Henze S. , Bohn E. , Mollenhauer J. , Wiemann S. , Schick M. , Korn B.
      Submitted (2005-07) to the EMBL/GenBank/DDBJ databases
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
    4. 4.
      "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res.14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
      strain: Czech II.
      tissue: Mammary tumor.
    5. 5.
      "RYBP, a new repressor protein that interacts with components of the mammalian Polycomb complex, and with the transcription factor YY1."
      Garcia E. , Marcos-Gutierrez C. , del Mar Lorente M. , Moreno J.C. , Vidal M.
      EMBO J.18:3404-3418(1999) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH RYBP AND RING1
    6. 6.
      "Involvement of the Polycomb-group gene Ring1B in the specification of the anterior-posterior axis in mice."
      Suzuki M. , Mizutani-Koseki Y. , Fujimura Y. , Miyagishima H. , Kaneko T. , Takada Y. , Akasaka T. , Tanzawa H. , Takihara Y. , Nakano M. , Masumoto H. , Vidal M. , Isono K. , Koseki H.
      Development129:4171-4183(2002) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH CBX2; PCGF2; PHC1; PHC2; RNF1 AND BMI1;FUNCTION;SUBCELLULAR LOCATION
    7. 7.
      "Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation."
      de Napoles M. , Mermoud J.E. , Wakao R. , Tang Y.A. , Endoh M. , Appanah R. , Nesterova T.B. , Silva J. , Otte A.P. , Vidal M. , Koseki H. , Brockdorff N.
      Dev. Cell7:663-676(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: ENZYME ACTIVITY;FUNCTION
    8. 8.
      "Ring1b-mediated H2A ubiquitination associates with inactive X chromosomes and is involved in initiation of X inactivation."
      Fang J. , Chen T. , Chadwick B. , Li E. , Zhang Y.
      J. Biol. Chem.279:52812-52815(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: SUBCELLULAR LOCATION
    9. 9.
      "Mammalian polyhomeotic homologues Phc2 and Phc1 act in synergy to mediate polycomb repression of Hox genes."
      Isono K. , Fujimura Y. , Shinga J. , Yamaki M. , O-Wang J. , Takihara Y. , Murahashi Y. , Takada Y. , Mizutani-Koseki Y. , Koseki H.
      Mol. Cell. Biol.25:6694-6706(2005) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH PHC2
    10. 10.
      "The transcriptional repressor RYBP is a natively unfolded protein which folds upon binding to DNA."
      Neira J.L. , Roman-Trufero M. , Contreras L.M. , Prieto J. , Singh G. , Barrera F.N. , Renart M.L. , Vidal M.
      Biochemistry48:1348-1360(2009) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH RYBP
    11. 11.
      "Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation."
      Fanis P. , Gillemans N. , Aghajanirefah A. , Pourfarzad F. , Demmers J. , Esteghamat F. , Vadlamudi R.K. , Grosveld F. , Philipsen S. , van Dijk T.B.
      Mol. Cell. Proteomics11:1263-1273(2012) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH CHTOP
    12. 12.
      "The Aurora B kinase and the Polycomb protein Ring1B combine to regulate active promoters in quiescent lymphocytes."
      Frangini A. , Sjoberg M. , Roman-Trufero M. , Dharmalingam G. , Haberle V. , Bartke T. , Lenhard B. , Malumbres M. , Vidal M. , Dillon N.
      Mol. Cell51:647-661(2013) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;INTERACTION WITH AURKB
    13. 13.
      "Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b."
      Buchwald G. , van der Stoop P. , Weichenrieder O. , Perrakis A. , van Lohuizen M. , Sixma T.K.
      EMBO J.25:2465-2474(2006) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-159 IN COMPLEX WITH BMI1 AND ZINC IONS;FUNCTION;MONOUBIQUITINATION;SUBUNIT
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