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P49711

- CTCF_HUMAN

UniProt

P49711 - CTCF_HUMAN

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Protein
Transcriptional repressor CTCF
Gene
CTCF
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 1
Add
BLAST
Zinc fingeri294 – 31623C2H2-type 2
Add
BLAST
Zinc fingeri322 – 34524C2H2-type 3
Add
BLAST
Zinc fingeri351 – 37323C2H2-type 4
Add
BLAST
Zinc fingeri379 – 40123C2H2-type 5
Add
BLAST
Zinc fingeri407 – 43024C2H2-type 6
Add
BLAST
Zinc fingeri437 – 46024C2H2-type 7
Add
BLAST
Zinc fingeri467 – 48923C2H2-type 8
Add
BLAST
Zinc fingeri495 – 51723C2H2-type 9
Add
BLAST
Zinc fingeri523 – 54624C2H2-type 10
Add
BLAST
Zinc fingeri555 – 57723C2H2-type 11; atypical
Add
BLAST

GO - Molecular functioni

  1. chromatin insulator sequence binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. sequence-specific DNA binding Source: UniProtKB
  4. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  5. transcription corepressor activity Source: ProtInc
  6. transcription regulatory region DNA binding Source: UniProtKB
  7. zinc ion binding Source: UniProtKB
Complete GO annotation...

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. nucleosome positioning Source: UniProtKB
  6. positive regulation of gene expression Source: UniProtKB
  7. positive regulation of transcription, DNA-templated Source: UniProtKB
  8. regulation of centromeric sister chromatid cohesion Source: UniProtKB
  9. regulation of gene expression by genetic imprinting Source: Ensembl
  10. regulation of gene expression, epigenetic Source: UniProtKB
  11. regulation of histone acetylation Source: Ensembl
  12. regulation of histone methylation Source: Ensembl
  13. regulation of molecular function, epigenetic Source: UniProtKB
  14. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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.4 Publications

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 CTCF
PRO_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

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.

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

Contains 11 C2H2-type zinc fingers.

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.
VSP_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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 144 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

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