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Q9CQJ4

- RING2_MOUSE

UniProt

Q9CQJ4 - RING2_MOUSE

Protein

E3 ubiquitin-protein ligase RING2

Gene

Rnf2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation. H2AK119Ub 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. In resting B- and T-lymphocytes, interaction with AURKB leads to block its activity, thereby maintaining transcription in resting lymphocytes.4 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri51 – 9141RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. ligase activity Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. ubiquitin-protein transferase activity Source: MGI
    5. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. anterior/posterior axis specification Source: MGI
    2. gastrulation with mouth forming second Source: MGI
    3. histone H2A-K119 monoubiquitination Source: UniProtKB
    4. histone ubiquitination Source: MGI
    5. mitotic cell cycle Source: MGI
    6. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_188970. Oxidative Stress Induced Senescence.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase RING2 (EC:6.3.2.-)
    Alternative name(s):
    RING finger protein 1B
    Short name:
    RING1b
    RING finger protein 2
    Gene namesi
    Name:Rnf2
    Synonyms:DinG, Ring1b
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1101759. Rnf2.

    Subcellular locationi

    Nucleus. Chromosome
    Note: 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.

    GO - Cellular componenti

    1. euchromatin Source: MGI
    2. heterochromatin Source: MGI
    3. MLL1 complex Source: UniProtKB
    4. nuclear body Source: MGI
    5. nucleus Source: MGI
    6. PcG protein complex Source: MGI
    7. PRC1 complex Source: Ensembl
    8. sex chromatin Source: MGI
    9. ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 336335E3 ubiquitin-protein ligase RING2PRO_0000056039Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Cross-linki112 – 112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

    Post-translational modificationi

    Polyubiquitinated in the presence of UBE2D3 (in vitro).
    Monoubiquitinated, by auto-ubiquitination.

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ9CQJ4.
    PaxDbiQ9CQJ4.
    PRIDEiQ9CQJ4.

    PTM databases

    PhosphoSiteiQ9CQJ4.

    Expressioni

    Gene expression databases

    BgeeiQ9CQJ4.
    CleanExiMM_RNF2.
    GenevestigatoriQ9CQJ4.

    Interactioni

    Subunit structurei

    Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RNF1/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 KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, 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. Interacts with CBX4, CBX6, CBX7 and CBX8. Component of repressive BCOR complex containing Polycomb group subcomplex at least composed of RYBP, PCGF1, BCOR and RING1 By similarity. Component of chromatin-associated Polycomb (PcG) complexes. Interacts with RYBP, PCGF2, CBX2, RNF1/RING1, BMI1, PHC1 and PHC2. Interacts with CHTOP. Interacts with AURKB.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Bmi1P2591611EBI-927321,EBI-927401
    Cbx8Q9QXV15EBI-927321,EBI-1216641
    Csnk2a1Q611774EBI-927321,EBI-1216438
    Kdm1aQ6ZQ883EBI-927321,EBI-1216284
    Kdm2bQ6P1G24EBI-927321,EBI-1216214
    Pcgf2P2379815EBI-927321,EBI-926857
    Phc1Q640283EBI-927321,EBI-927346
    Phc2Q9QWH17EBI-927321,EBI-642357
    Ring1O357303EBI-927321,EBI-929310
    RybpQ8CCI58EBI-927321,EBI-929290
    Skp1Q9WTX54EBI-927321,EBI-1202363

    Protein-protein interaction databases

    BioGridi202919. 122 interactions.
    DIPiDIP-36109N.
    IntActiQ9CQJ4. 57 interactions.
    MINTiMINT-1341250.
    STRINGi10090.ENSMUSP00000075476.

    Structurei

    Secondary structure

    1
    336
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 255
    Helixi46 – 494
    Turni52 – 543
    Beta strandi55 – 573
    Beta strandi59 – 646
    Turni65 – 673
    Beta strandi70 – 723
    Helixi73 – 819
    Turni88 – 903
    Helixi97 – 993
    Beta strandi100 – 1023
    Helixi104 – 11310

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CKLX-ray2.00B1-159[»]
    ProteinModelPortaliQ9CQJ4.
    SMRiQ9CQJ4. Positions 15-114, 223-333.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9CQJ4.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 179178Interaction with HIP2By similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri51 – 9141RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG324386.
    GeneTreeiENSGT00390000016977.
    HOGENOMiHOG000273917.
    HOVERGENiHBG079942.
    InParanoidiQ9CQJ4.
    KOiK10695.
    OMAiSDCIITA.
    OrthoDBiEOG7NGQC3.
    PhylomeDBiQ9CQJ4.
    TreeFamiTF105501.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF00097. zf-C3HC4. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9CQJ4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQAVQTNGT QPLSKTWELS LYELQRTPQE AITDGLEIVV SPRSLHSELM    50
    CPICLDMLKN TMTTKECLHR FCADCIITAL RSGNKECPTC RKKLVSKRSL 100
    RPDPNFDALI SKIYPSRDEY EAHQERVLAR INKHNNQQAL SHSIEEGLKI 150
    QAMNRLQRGK KQQIENGSGA EDNGDSSHCS NASTHSNQEA GPSNKRTKTS 200
    DDSGLELDNN NAAVAIDPVM DGASEIELVF RPHPTLMEKD DSAQTRYIKT 250
    SGNATVDHLS KYLAVRLALE ELRSKGESNQ MNLDTASEKQ YTIYIATASG 300
    QFTVLNGSFS LELVSEKYWK VNKPMELYYA PTKEHK 336
    Length:336
    Mass (Da):37,623
    Last modified:June 1, 2001 - v1
    Checksum:i84BA5B3E044DB7EC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti253 – 2531N → H in BAC41075. (PubMed:16141072)Curated
    Sequence conflicti299 – 2991S → T in BAC41075. (PubMed:16141072)Curated
    Sequence conflicti304 – 3041V → L in BAC41075. (PubMed:16141072)Curated
    Sequence conflicti332 – 3365TKEHK → FTASGNVR in CAA73380. (PubMed:9312051)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12880 mRNA. Translation: CAA73380.1.
    Y12783 mRNA. Translation: CAA73321.1.
    AK145767 mRNA. Translation: BAE26638.1.
    AK012358 mRNA. Translation: BAB28186.1.
    AK013124 mRNA. Translation: BAB28663.1.
    AK030319 mRNA. Translation: BAC26898.1.
    AK090066 mRNA. Translation: BAC41075.1.
    CT010297 mRNA. Translation: CAJ18505.1.
    BC020122 mRNA. Translation: AAH20122.1.
    CCDSiCCDS15362.1.
    RefSeqiNP_035407.1. NM_011277.2.
    UniGeneiMm.474038.

    Genome annotation databases

    EnsembliENSMUST00000076110; ENSMUSP00000075476; ENSMUSG00000026484.
    GeneIDi19821.
    KEGGimmu:19821.
    UCSCiuc007cyx.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12880 mRNA. Translation: CAA73380.1 .
    Y12783 mRNA. Translation: CAA73321.1 .
    AK145767 mRNA. Translation: BAE26638.1 .
    AK012358 mRNA. Translation: BAB28186.1 .
    AK013124 mRNA. Translation: BAB28663.1 .
    AK030319 mRNA. Translation: BAC26898.1 .
    AK090066 mRNA. Translation: BAC41075.1 .
    CT010297 mRNA. Translation: CAJ18505.1 .
    BC020122 mRNA. Translation: AAH20122.1 .
    CCDSi CCDS15362.1.
    RefSeqi NP_035407.1. NM_011277.2.
    UniGenei Mm.474038.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CKL X-ray 2.00 B 1-159 [» ]
    ProteinModelPortali Q9CQJ4.
    SMRi Q9CQJ4. Positions 15-114, 223-333.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202919. 122 interactions.
    DIPi DIP-36109N.
    IntActi Q9CQJ4. 57 interactions.
    MINTi MINT-1341250.
    STRINGi 10090.ENSMUSP00000075476.

    PTM databases

    PhosphoSitei Q9CQJ4.

    Proteomic databases

    MaxQBi Q9CQJ4.
    PaxDbi Q9CQJ4.
    PRIDEi Q9CQJ4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000076110 ; ENSMUSP00000075476 ; ENSMUSG00000026484 .
    GeneIDi 19821.
    KEGGi mmu:19821.
    UCSCi uc007cyx.1. mouse.

    Organism-specific databases

    CTDi 6045.
    MGIi MGI:1101759. Rnf2.

    Phylogenomic databases

    eggNOGi NOG324386.
    GeneTreei ENSGT00390000016977.
    HOGENOMi HOG000273917.
    HOVERGENi HBG079942.
    InParanoidi Q9CQJ4.
    KOi K10695.
    OMAi SDCIITA.
    OrthoDBi EOG7NGQC3.
    PhylomeDBi Q9CQJ4.
    TreeFami TF105501.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_188970. Oxidative Stress Induced Senescence.

    Miscellaneous databases

    EvolutionaryTracei Q9CQJ4.
    NextBioi 297285.
    PROi Q9CQJ4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9CQJ4.
    CleanExi MM_RNF2.
    Genevestigatori Q9CQJ4.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF00097. zf-C3HC4. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CBX2.
      Strain: NIH Swiss.
    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.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: B-cell and Ovary.
    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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Czech II.
      Tissue: Mammary tumor.
    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]
      Cited for: INTERACTION WITH RYBP AND RING1.
    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.
      Development 129:4171-4183(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBX2; PCGF2; PHC1; PHC2; RNF1 AND BMI1, FUNCTION, SUBCELLULAR LOCATION.
    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. Cell 7:663-676(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, FUNCTION.
    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]
      Cited for: SUBCELLULAR LOCATION.
    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]
      Cited for: INTERACTION WITH PHC2.
    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.
      Biochemistry 48:1348-1360(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RYBP.
    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. Proteomics 11:1263-1273(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHTOP.
    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. Cell 51:647-661(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AURKB.
    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]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-159 IN COMPLEX WITH BMI1 AND ZINC IONS, FUNCTION, MONOUBIQUITINATION, SUBUNIT.

    Entry informationi

    Entry nameiRING2_MOUSE
    AccessioniPrimary (citable) accession number: Q9CQJ4
    Secondary accession number(s): O35699
    , O35729, Q4FJV5, Q8C1X8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 122 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3