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P49711

- CTCF_HUMAN

UniProt

P49711 - CTCF_HUMAN

Protein

Transcriptional repressor CTCF

Gene

CTCF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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. 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/H19.10 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 insulator sequence binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    4. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB
    5. sequence-specific DNA binding Source: UniProtKB
    6. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    7. transcription corepressor activity Source: ProtInc
    8. transcription regulatory region DNA binding Source: UniProtKB
    9. zinc ion binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Repressor

    Keywords - Biological processi

    Chromosome partition, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiP49711.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:13723. CTCF.

    Subcellular locationi

    Nucleusnucleoplasm. Chromosome. Chromosomecentromere
    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.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Centromere, Chromosome, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, autosomal dominant 21 (MRD21) [MIM:615502]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Additional MRD21 features include short stature, microcephaly, and developmental delay.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti567 – 5671R → W in MRD21. 1 Publication
    VAR_070776

    Keywords - Diseasei

    Disease mutation, Mental retardation, Tumor suppressor

    Organism-specific databases

    MIMi615502. phenotype.
    Orphaneti363611. Intellectual disability-feeding difficulties-developmental delay-microcephaly syndrome.
    PharmGKBiPA26998.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 727727Transcriptional repressor CTCFPRO_0000047228Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Cross-linki74 – 74Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei289 – 2891Phosphothreonine1 Publication
    Modified residuei317 – 3171Phosphothreonine1 Publication
    Modified residuei374 – 3741Phosphothreonine1 Publication
    Modified residuei402 – 4021Phosphoserine1 Publication
    Modified residuei609 – 6091Phosphoserine3 Publications
    Modified residuei610 – 6101Phosphoserine3 Publications
    Modified residuei612 – 6121Phosphoserine3 Publications
    Cross-linki689 – 689Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

    Post-translational modificationi

    Sumoylated on Lys-74 and Lys-689; sumoylation of CTCF contributes to the repressive function of CTCF on the MYC P2 promoter.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP49711.
    PaxDbiP49711.
    PRIDEiP49711.

    PTM databases

    PhosphoSiteiP49711.

    Expressioni

    Tissue specificityi

    Ubiquitous. Absent in primary spermatocytes.1 Publication

    Gene expression databases

    BgeeiP49711.
    CleanExiHS_CTCF.
    GenevestigatoriP49711.

    Organism-specific databases

    HPAiCAB062550.
    HPA004122.

    Interactioni

    Subunit structurei

    Interacts with CHD8.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HDLBPQ003414EBI-932887,EBI-1049478

    Protein-protein interaction databases

    BioGridi115906. 37 interactions.
    DIPiDIP-35252N.
    IntActiP49711. 15 interactions.
    STRINGi9606.ENSP00000264010.

    Structurei

    Secondary structure

    1
    727
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi406 – 4083
    Turni410 – 4123
    Beta strandi415 – 4173
    Helixi419 – 42911
    Beta strandi430 – 4334
    Beta strandi435 – 4384
    Beta strandi440 – 4434
    Beta strandi445 – 4484
    Helixi449 – 45810
    Beta strandi526 – 5294
    Beta strandi531 – 5344
    Helixi535 – 54410
    Beta strandi558 – 5603
    Beta strandi563 – 5653
    Helixi567 – 57610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X6HNMR-A515-587[»]
    2CT1NMR-A399-462[»]
    ProteinModelPortaliP49711.
    SMRiP49711. Positions 263-591.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49711.

    Family & Domainsi

    Domaini

    The 11 zinc fingers are highly conserved among vertebrates, exhibiting almost identical amino acid sequences. Different subsets or combination of individual zinc fingers gives the ability to CTCF to recognize multiple DNA target sites.

    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.
    HOGENOMiHOG000276534.
    HOVERGENiHBG000350.
    InParanoidiP49711.
    OMAiPPNQADG.
    OrthoDBiEOG71K632.
    PhylomeDBiP49711.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49711-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEGDAVEAIV EESETFIKGK ERKTYQRRRE GGQEEDACHL PQNQTDGGEV    50
    VQDVNSSVQM VMMEQLDPTL LQMKTEVMEG TVAPEAEAAV DDTQIITLQV 100
    VNMEEQPINI GELQLVQVPV PVTVPVATTS VEELQGAYEN EVSKEGLAES 150
    EPMICHTLPL PEGFQVVKVG ANGEVETLEQ GELPPQEDPS 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 DSENAEPDLD DNEDEEEPAV EIEPEPEPQP VTPAPPPAKK 650
    RRGRPPGRTN QPKQNQPTAI IQVEDQNTGA IENIIVEVKK EPDAEPAEGE 700
    EEEAQPAATD APNGDLTPEM ILSMMDR 727
    Length:727
    Mass (Da):82,785
    Last modified:October 1, 1996 - v1
    Checksum:i2110538B65DC5706
    GO
    Isoform 2 (identifier: P49711-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-328: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:399
    Mass (Da):45,998
    Checksum:iFEB74DFBADCF586A
    GO

    Sequence cautioni

    The sequence BAD93030.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti339 – 3391R → W in a Wilms' tumor. 1 Publication
    VAR_013141
    Natural varianti344 – 3441K → E in a breast tumor. 1 Publication
    VAR_013142
    Natural varianti345 – 3451H → R in a prostate tumor. 1 Publication
    VAR_013143
    Natural varianti448 – 4481R → Q in a Wilms' tumor. 1 Publication
    VAR_013144
    Natural varianti567 – 5671R → W in MRD21. 1 Publication
    VAR_070776

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 328328Missing in isoform 2. 1 PublicationVSP_045350Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U25435 mRNA. Translation: AAB07788.1.
    AF145477
    , AF145468, AF145469, AF145470, AF145471, AF145472, AF145473, AF145474, AF145475, AF145476 Genomic DNA. Translation: AAF31318.1.
    BT009915 mRNA. Translation: AAP88917.1.
    AB209793 mRNA. Translation: BAD93030.1. Different initiation.
    AC009095 Genomic DNA. No translation available.
    AC027682 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW83142.1.
    BC014267 mRNA. Translation: AAH14267.1.
    CCDSiCCDS10841.1. [P49711-1]
    CCDS54029.1. [P49711-2]
    PIRiG01792.
    RefSeqiNP_001177951.1. NM_001191022.1. [P49711-2]
    NP_006556.1. NM_006565.3. [P49711-1]
    UniGeneiHs.368367.

    Genome annotation databases

    EnsembliENST00000264010; ENSP00000264010; ENSG00000102974. [P49711-1]
    ENST00000401394; ENSP00000384707; ENSG00000102974. [P49711-2]
    GeneIDi10664.
    KEGGihsa:10664.
    UCSCiuc002etl.3. human. [P49711-1]
    uc002etm.1. human.

    Polymorphism databases

    DMDMi1706179.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U25435 mRNA. Translation: AAB07788.1 .
    AF145477
    , AF145468 , AF145469 , AF145470 , AF145471 , AF145472 , AF145473 , AF145474 , AF145475 , AF145476 Genomic DNA. Translation: AAF31318.1 .
    BT009915 mRNA. Translation: AAP88917.1 .
    AB209793 mRNA. Translation: BAD93030.1 . Different initiation.
    AC009095 Genomic DNA. No translation available.
    AC027682 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW83142.1 .
    BC014267 mRNA. Translation: AAH14267.1 .
    CCDSi CCDS10841.1. [P49711-1 ]
    CCDS54029.1. [P49711-2 ]
    PIRi G01792.
    RefSeqi NP_001177951.1. NM_001191022.1. [P49711-2 ]
    NP_006556.1. NM_006565.3. [P49711-1 ]
    UniGenei Hs.368367.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X6H NMR - A 515-587 [» ]
    2CT1 NMR - A 399-462 [» ]
    ProteinModelPortali P49711.
    SMRi P49711. Positions 263-591.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115906. 37 interactions.
    DIPi DIP-35252N.
    IntActi P49711. 15 interactions.
    STRINGi 9606.ENSP00000264010.

    PTM databases

    PhosphoSitei P49711.

    Polymorphism databases

    DMDMi 1706179.

    Proteomic databases

    MaxQBi P49711.
    PaxDbi P49711.
    PRIDEi P49711.

    Protocols and materials databases

    DNASUi 10664.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264010 ; ENSP00000264010 ; ENSG00000102974 . [P49711-1 ]
    ENST00000401394 ; ENSP00000384707 ; ENSG00000102974 . [P49711-2 ]
    GeneIDi 10664.
    KEGGi hsa:10664.
    UCSCi uc002etl.3. human. [P49711-1 ]
    uc002etm.1. human.

    Organism-specific databases

    CTDi 10664.
    GeneCardsi GC16P067596.
    HGNCi HGNC:13723. CTCF.
    HPAi CAB062550.
    HPA004122.
    MIMi 604167. gene.
    615502. phenotype.
    neXtProti NX_P49711.
    Orphaneti 363611. Intellectual disability-feeding difficulties-developmental delay-microcephaly syndrome.
    PharmGKBi PA26998.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5048.
    HOGENOMi HOG000276534.
    HOVERGENi HBG000350.
    InParanoidi P49711.
    OMAi PPNQADG.
    OrthoDBi EOG71K632.
    PhylomeDBi P49711.
    TreeFami TF106430.

    Enzyme and pathway databases

    SignaLinki P49711.

    Miscellaneous databases

    EvolutionaryTracei P49711.
    GeneWikii CTCF.
    GenomeRNAii 10664.
    NextBioi 40551.
    PROi P49711.
    SOURCEi Search...

    Gene expression databases

    Bgeei P49711.
    CleanExi HS_CTCF.
    Genevestigatori P49711.

    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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
    2. "A widely expressed transcription factor with multiple DNA sequence specificity, CTCF, is localized at chromosome segment 16q22.1 within one of the smallest regions of overlap for common deletions in breast and prostate cancers."
      Filippova G.N., Lindblom A., Meincke L.J., Klenova E.M., Neiman P.E., Collins S.J., Doggett N.A., Lobanenkov V.V.
      Genes Chromosomes Cancer 22:26-36(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY.
    3. "Tumor-associated zinc finger mutations in the CTCF transcription factor selectively alter its DNA-binding specificity."
      Filippova G.N., Qi C.-F., Ulmer J.E., Moore J.M., Ward M.D., Hu Y.J., Loukinov D.I., Pugacheva E.M., Klenova E.M., Grundy P.E., Feinberg A.P., Cleton-Jansen A.-M., Moerland E.W., Cornelisse C.J., Suzuki H., Komiya A., Lindblom A., Dorion-Bonnet F.
      , Neiman P.E., Morse H.C. III, Collins S.J., Lobanenkov V.V.
      Cancer Res. 62:48-52(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS WILMS TUMOR TRP-339 AND GLN-448, VARIANT BREAST TUMOR GLU-344, VARIANT PROSTATE TUMOR ARG-345.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "Homo sapiens protein coding cDNA."
      Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    6. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1).
      Tissue: Placenta.
    9. "The zinc finger protein CTCF binds to the APBbeta domain of the amyloid beta-protein precursor promoter. Evidence for a role in transcriptional activation."
      Vostrov A.A., Quitschke W.W.
      J. Biol. Chem. 272:33353-33359(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 471-479 AND 483-487, TRANSCRIPTIONAL ACTIVATION OF APP.
    10. "The novel BORIS + CTCF gene family is uniquely involved in the epigenetics of normal biology and cancer."
      Klenova E.M., Morse H.C. III, Ohlsson R., Lobanenkov V.V.
      Semin. Cancer Biol. 12:399-414(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    11. "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.
    12. "CTCF binding and higher order chromatin structure of the H19 locus are maintained in mitotic chromatin."
      Burke L.J., Zhang R., Bartkuhn M., Tiwari V.K., Tavoosidana G., Kurukuti S., Weth C., Leers J., Galjart N., Ohlsson R., Renkawitz R.
      EMBO J. 24:3291-3300(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH H19 ICR.
    13. "Targeting of CTCF to the nucleolus inhibits nucleolar transcription through a poly(ADP-ribosyl)ation-dependent mechanism."
      Torrano V., Navascues J., Docquier F., Zhang R., Burke L.J., Chernukhin I., Farrar D., Leon J., Berciano M.T., Renkawitz R., Klenova E., Lafarga M., Delgado M.D.
      J. Cell Sci. 119:1746-1759(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "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.
    15. "CTCF binding at the H19 imprinting control region mediates maternally inherited higher-order chromatin conformation to restrict enhancer access to Igf2."
      Kurukuti S., Tiwari V.K., Tavoosidana G., Pugacheva E., Murrell A., Zhao Z., Lobanenkov V., Reik W., Ohlsson R.
      Proc. Natl. Acad. Sci. U.S.A. 103:10684-10689(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Critical DNA binding interactions of the insulator protein CTCF: a small number of zinc fingers mediate strong binding, and a single finger-DNA interaction controls binding at imprinted loci."
      Renda M., Baglivo I., Burgess-Beusse B., Esposito S., Fattorusso R., Felsenfeld G., Pedone P.V.
      J. Biol. Chem. 282:33336-33345(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "DNA methyltransferase 1 and 3B activate BAG-1 expression via recruitment of CTCFL/BORIS and modulation of promoter histone methylation."
      Sun L., Huang L., Nguyen P., Bisht K.S., Bar-Sela G., Ho A.S., Bradbury C.M., Yu W., Cui H., Lee S., Trepel J.B., Feinberg A.P., Gius D.
      Cancer Res. 68:2726-2735(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "The insulator factor CTCF controls MHC class II gene expression and is required for the formation of long-distance chromatin interactions."
      Majumder P., Gomez J.A., Chadwick B.P., Boss J.M.
      J. Exp. Med. 205:785-798(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "The insulator binding protein CTCF positions 20 nucleosomes around its binding sites across the human genome."
      Fu Y., Sinha M., Peterson C.L., Weng Z.
      PLoS Genet. 4:E1000138-E1000138(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-374; SER-402; SER-609; SER-610 AND SER-612, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    22. "Architectural roles of multiple chromatin insulators at the human apolipoprotein gene cluster."
      Mishiro T., Ishihara K., Hino S., Tsutsumi S., Aburatani H., Shirahige K., Kinoshita Y., Nakao M.
      EMBO J. 28:1234-1245(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    24. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-289; THR-317; SER-609; SER-610 AND SER-612, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-609; SER-610 AND SER-612, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Solution structure of zinc finger domains of transcriptional repressor CTCF protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 399-589.
    30. Cited for: VARIANT MRD21 TRP-567.

    Entry informationi

    Entry nameiCTCF_HUMAN
    AccessioniPrimary (citable) accession number: P49711
    Secondary accession number(s): B5MC38, Q53XI7, Q59EL8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 145 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    More than 13'00 CTCF-binding sites in potential insulators were identified in the human genome.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3