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Q61164

- CTCF_MOUSE

UniProt

Q61164 - CTCF_MOUSE

Protein

Transcriptional repressor CTCF

Gene

Ctcf

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (23 Apr 2003)
      Previous versions | rss
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    Functioni

    Chromatin binding factor that binds to DNA sequence specific sites. Involved in transcriptional regulation by binding to chromatin insulators and preventing interaction between promoter and nearby enhancers and silencers. Acts as transcriptional repressor binding to promoters of vertebrate MYC gene and BAG1 gene. Also binds to the PLK and PIM1 promoters. Acts as a transcriptional activator of APP. Regulates APOA1/C3/A4/A5 gene cluster and controls MHC class II gene expression. Plays an essential role in oocyte and preimplantation embryo development by activating or repressing transcription. Seems to act as tumor suppressor. Plays a critical role in the epigenetic regulation. Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus. On the maternal allele, binding within the H19 imprinting control region (ICR) mediates maternally inherited higher-order chromatin conformation to restrict enhancer access to IGF2. Plays a critical role in gene silencing over considerable distances in the genome. Preferentially interacts with unmethylated DNA, preventing spreading of CpG methylation and maintaining methylation-free zones. Inversely, binding to target sites is prevented by CpG methylation. Plays a important role in chromatin remodeling. Can dimerize when it is bound to different DNA sequences, mediating long-range chromatin looping By similarity. Mediates interchromosomal association between IGF2/H19 and WSB1/NF1 and may direct distant DNA segments to a common transcription factory. Causes local loss of histone acetylation and gain of histone methylation in the beta-globin locus, without affecting transcription. When bound to chromatin, it provides an anchor point for nucleosomes positioning. Seems to be essential for homologous X-chromosome pairing. May participate with Tsix in establishing a regulatable epigenetic switch for X chromosome inactivation. May play a role in preventing the propagation of stable methylation at the escape genes from X-inactivation. Involved in sister chromatid cohesion. Associates with both centromeres and chromosomal arms during metaphase and required for cohesin localization to CTCF sites. Regulates asynchronous replication of IGF2/H19.By similarity7 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri266 – 28823C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri294 – 31623C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri322 – 34524C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri351 – 37323C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri379 – 40123C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri407 – 43024C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri437 – 46024C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri467 – 48923C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri495 – 51723C2H2-type 9PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri523 – 54624C2H2-type 10PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri555 – 57723C2H2-type 11; atypicalPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. chromatin insulator sequence binding Source: Ensembl
    3. DNA binding Source: MGI
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: IntAct
    6. sequence-specific DNA binding Source: Ensembl
    7. sequence-specific DNA binding transcription factor activity Source: Ensembl
    8. transcription regulatory region DNA binding Source: Ensembl

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. chromosome segregation Source: UniProtKB-KW
    3. DNA methylation Source: MGI
    4. dosage compensation by inactivation of X chromosome Source: MGI
    5. maintenance of DNA methylation Source: MGI
    6. negative regulation of gene expression Source: UniProtKB
    7. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    8. nucleosome positioning Source: Ensembl
    9. positive regulation of gene expression Source: UniProtKB
    10. positive regulation of transcription, DNA-templated Source: Ensembl
    11. regulation of gene expression by genetic imprinting Source: MGI
    12. regulation of histone acetylation Source: UniProtKB
    13. regulation of histone methylation Source: UniProtKB
    14. regulation of molecular function, epigenetic Source: Ensembl
    15. regulation of transcription, DNA-templated Source: MGI
    16. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Repressor

    Keywords - Biological processi

    Chromosome partition, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcriptional repressor CTCF
    Alternative name(s):
    11-zinc finger protein
    CCCTC-binding factor
    CTCFL paralog
    Gene namesi
    Name:Ctcf
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:109447. Ctcf.

    Subcellular locationi

    Nucleusnucleoplasm 1 Publication. Chromosome By similarity. Chromosomecentromere By similarity
    Note: May translocate to the nucleolus upon cell differentiation. Associates with both centromeres and chromosomal arms during metaphase. Associates with the H19 ICR in mitotic chromosomes. May be preferentially excluded from heterochromatin during interphase By similarity.By similarity

    GO - Cellular componenti

    1. chromosome, centromeric region Source: UniProtKB-SubCell
    2. condensed chromosome Source: Ensembl
    3. nucleolus Source: Ensembl
    4. nucleoplasm Source: UniProtKB-SubCell
    5. nucleus Source: MGI

    Keywords - Cellular componenti

    Centromere, Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi74 – 741K → R: No sumoylation. 1 Publication
    Mutagenesisi698 – 6981K → R: No sumoylation. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 736736Transcriptional repressor CTCFPRO_0000047229Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Cross-linki74 – 74Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei289 – 2891PhosphothreonineBy similarity
    Modified residuei317 – 3171PhosphothreonineBy similarity
    Modified residuei374 – 3741PhosphothreonineBy similarity
    Modified residuei402 – 4021PhosphoserineBy similarity
    Modified residuei609 – 6091PhosphoserineBy similarity
    Modified residuei610 – 6101PhosphoserineBy similarity
    Modified residuei612 – 6121PhosphoserineBy similarity
    Cross-linki698 – 698Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

    Post-translational modificationi

    Sumoylated on Lys-74 and Lys-698; sumoylation of CTCF contributes to the repressive function of CTCF on the MYC P2 promoter.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ61164.
    PRIDEiQ61164.

    Expressioni

    Gene expression databases

    ArrayExpressiQ61164.
    BgeeiQ61164.
    CleanExiMM_CTCF.
    GenevestigatoriQ61164.

    Interactioni

    Subunit structurei

    Interacts with CHD8.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Chd8Q09XV53EBI-932785,EBI-1169080

    Protein-protein interaction databases

    BioGridi198963. 21 interactions.
    DIPiDIP-38020N.
    IntActiQ61164. 14 interactions.
    MINTiMINT-4092474.
    STRINGi10090.ENSMUSP00000005841.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61164.
    SMRiQ61164. Positions 263-591.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi635 – 67642Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the CTCF zinc-finger protein family.Curated
    Contains 11 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri266 – 28823C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri294 – 31623C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri322 – 34524C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri351 – 37323C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri379 – 40123C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri407 – 43024C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri437 – 46024C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri467 – 48923C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri495 – 51723C2H2-type 9PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri523 – 54624C2H2-type 10PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri555 – 57723C2H2-type 11; atypicalPROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5048.
    GeneTreeiENSGT00530000063079.
    HOGENOMiHOG000276534.
    HOVERGENiHBG000350.
    InParanoidiQ61164.
    OMAiPPNQADG.
    OrthoDBiEOG71K632.
    PhylomeDBiQ61164.
    TreeFamiTF106430.

    Family and domain databases

    Gene3Di3.30.160.60. 9 hits.
    InterProiIPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    PfamiPF00096. zf-C2H2. 1 hit.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 11 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 8 hits.
    PS50157. ZINC_FINGER_C2H2_2. 11 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q61164-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGEAVEAIV EESETFIKGK ERKTYQRRRE GGQEEDACHL PQNQTDGGEV    50
    VQDVNSSVQM VMMEQLDPTL LQMKTEVMEG TVAPEAEAAV DDTQIITLQV 100
    VNMEEQPINI GELQLVQVPV PVTVPVATTS VEELQGAYEN EVSKEGLAES 150
    EPMICHTLPL PEGFQVVKVG ANGEVETLEQ GELPPQEDSS WQKDPDYQPP 200
    AKKTKKTKKS KLRYTEEGKD VDVSVYDFEE EQQEGLLSEV NAEKVVGNMK 250
    PPKPTKIKKK GVKKTFQCEL CSYTCPRRSN LDRHMKSHTD ERPHKCHLCG 300
    RAFRTVTLLR NHLNTHTGTR PHKCPDCDMA FVTSGELVRH RRYKHTHEKP 350
    FKCSMCDYAS VEVSKLKRHI RSHTGERPFQ CSLCSYASRD TYKLKRHMRT 400
    HSGEKPYECY ICHARFTQSG TMKMHILQKH TENVAKFHCP HCDTVIARKS 450
    DLGVHLRKQH SYIEQGKKCR YCDAVFHERY ALIQHQKSHK NEKRFKCDQC 500
    DYACRQERHM IMHKRTHTGE KPYACSHCDK TFRQKQLLDM HFKRYHDPNF 550
    VPAAFVCSKC GKTFTRRNTM ARHADNCAGP DGVEGENGGE TKKSKRGRKR 600
    KMRSKKEDSS DSEENAEPDL DDNEEEEEPA VEIEPEPEPQ PQPPPPPQPV 650
    APAPPPAKKR RGRPPGRTNQ PKQNQPTAII QVEDQNTGAI ENIIVEVKKE 700
    PDAEPAEGEE EEAQAATTDA PNGDLTPEMI LSMMDR 736
    Length:736
    Mass (Da):83,745
    Last modified:April 23, 2003 - v2
    Checksum:i7C49D4A7BDCFEFA1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 381C → S in AAC52928. (PubMed:8649389)Curated
    Sequence conflicti257 – 2571I → K in AAH37456. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51037 mRNA. Translation: AAC52928.1.
    BC037456 mRNA. Translation: AAH37456.1.
    BC046398 mRNA. Translation: AAH46398.1.
    BC049131 mRNA. Translation: AAH49131.1.
    BC058240 mRNA. Translation: AAH58240.1.
    AK076192 mRNA. Translation: BAC36245.1.
    CCDSiCCDS22606.1.
    RefSeqiNP_851839.1. NM_181322.3.
    XP_006530711.1. XM_006530648.1.
    UniGeneiMm.269474.

    Genome annotation databases

    EnsembliENSMUST00000005841; ENSMUSP00000005841; ENSMUSG00000005698.
    GeneIDi13018.
    KEGGimmu:13018.
    UCSCiuc009ndm.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51037 mRNA. Translation: AAC52928.1 .
    BC037456 mRNA. Translation: AAH37456.1 .
    BC046398 mRNA. Translation: AAH46398.1 .
    BC049131 mRNA. Translation: AAH49131.1 .
    BC058240 mRNA. Translation: AAH58240.1 .
    AK076192 mRNA. Translation: BAC36245.1 .
    CCDSi CCDS22606.1.
    RefSeqi NP_851839.1. NM_181322.3.
    XP_006530711.1. XM_006530648.1.
    UniGenei Mm.269474.

    3D structure databases

    ProteinModelPortali Q61164.
    SMRi Q61164. Positions 263-591.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198963. 21 interactions.
    DIPi DIP-38020N.
    IntActi Q61164. 14 interactions.
    MINTi MINT-4092474.
    STRINGi 10090.ENSMUSP00000005841.

    Proteomic databases

    PaxDbi Q61164.
    PRIDEi Q61164.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000005841 ; ENSMUSP00000005841 ; ENSMUSG00000005698 .
    GeneIDi 13018.
    KEGGi mmu:13018.
    UCSCi uc009ndm.2. mouse.

    Organism-specific databases

    CTDi 10664.
    MGIi MGI:109447. Ctcf.

    Phylogenomic databases

    eggNOGi COG5048.
    GeneTreei ENSGT00530000063079.
    HOGENOMi HOG000276534.
    HOVERGENi HBG000350.
    InParanoidi Q61164.
    OMAi PPNQADG.
    OrthoDBi EOG71K632.
    PhylomeDBi Q61164.
    TreeFami TF106430.

    Miscellaneous databases

    ChiTaRSi CTCF. mouse.
    NextBioi 282878.
    PROi Q61164.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61164.
    Bgeei Q61164.
    CleanExi MM_CTCF.
    Genevestigatori Q61164.

    Family and domain databases

    Gene3Di 3.30.160.60. 9 hits.
    InterProi IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    Pfami PF00096. zf-C2H2. 1 hit.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 11 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 8 hits.
    PS50157. ZINC_FINGER_C2H2_2. 11 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "An exceptionally conserved transcriptional repressor, CTCF, employs different combinations of zinc fingers to bind diverged promoter sequences of avian and mammalian c-myc oncogenes."
      Filippova G.N., Fagerlie S., Klenova E.M., Myers C., Dehner Y., Goodwin G., Neiman P.E., Collins S.J., Lobanenkov V.V.
      Mol. Cell. Biol. 16:2802-2813(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
      Strain: BDF1.
    2. "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: C57BL/6J.
      Tissue: Brain, Mammary gland and Olfactory epithelium.
    3. "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] OF 1-201.
      Strain: C57BL/6J.
      Tissue: Extraembryonic tissue and Placenta.
    4. "CTCF, a candidate trans-acting factor for X-inactivation choice."
      Chao W., Huynh K.D., Spencer R.J., Davidow L.S., Lee J.T.
      Science 295:345-347(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Boundaries between chromosomal domains of X inactivation and escape bind CTCF and lack CpG methylation during early development."
      Filippova G.N., Cheng M.K., Moore J.M., Truong J.-P., Hu Y.J., Nguyen D.K., Tsuchiya K.D., Disteche C.M.
      Dev. Cell 8:31-42(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "CTCF mediates long-range chromatin looping and local histone modification in the beta-globin locus."
      Splinter E., Heath H., Kooren J., Palstra R.-J., Klous P., Grosveld F., Galjart N., de Laat W.
      Genes Dev. 20:2349-2354(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "CTCF-dependent chromatin insulator is linked to epigenetic remodeling."
      Ishihara K., Oshimura M., Nakao M.
      Mol. Cell 23:733-742(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHD8.
    8. "CTCF mediates interchromosomal colocalization between Igf2/H19 and Wsb1/Nf1."
      Ling J.Q., Li T., Hu J.F., Vu T.H., Chen H.L., Qiu X.W., Cherry A.M., Hoffman A.R.
      Science 312:269-272(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "CTCF regulates asynchronous replication of the imprinted H19/Igf2 domain."
      Bergstroem R., Whitehead J., Kurukuti S., Ohlsson R.
      Cell Cycle 6:450-454(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Evidence that homologous X-chromosome pairing requires transcription and Ctcf protein."
      Xu N., Donohoe M.E., Silva S.S., Lee J.T.
      Nat. Genet. 39:1390-1396(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Maternal depletion of CTCF reveals multiple functions during oocyte and preimplantation embryo development."
      Wan L.-B., Pan H., Hannenhalli S., Cheng Y., Ma J., Fedoriw A., Lobanenkov V., Latham K.E., Schultz R.M., Bartolomei M.S.
      Development 135:2729-2738(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "The CTCF insulator protein is posttranslationally modified by SUMO."
      MacPherson M.J., Beatty L.G., Zhou W., Du M., Sadowski P.D.
      Mol. Cell. Biol. 29:714-725(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-74 AND LYS-698, MUTAGENESIS OF LYS-74 AND LYS-698.

    Entry informationi

    Entry nameiCTCF_MOUSE
    AccessioniPrimary (citable) accession number: Q61164
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 23, 2003
    Last sequence update: April 23, 2003
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3