Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q61164 (CTCF_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcriptional repressor CTCF
Alternative name(s):
11-zinc finger protein
CCCTC-binding factor
CTCFL paralog
Gene names
Name:Ctcf
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length736 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11

Subunit structure

Interacts with CHD8. Ref.7

Subcellular location

Nucleusnucleoplasm Probable. 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. Ref.1

Post-translational modification

Sumoylated on Lys-74 and Lys-698; sumoylation of CTCF contributes to the repressive function of CTCF on the MYC P2 promoter. Ref.12

Sequence similarities

Belongs to the CTCF zinc-finger protein family.

Contains 11 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processChromosome partition
Transcription
Transcription regulation
   Cellular componentCentromere
Chromosome
Nucleus
   DiseaseTumor suppressor
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Chromatin regulator
Repressor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA methylation

Inferred from direct assay PubMed 12461525. Source: MGI

chromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

chromosome segregation

Inferred from electronic annotation. Source: UniProtKB-KW

dosage compensation by inactivation of X chromosome

Traceable author statement Ref.4. Source: MGI

maintenance of DNA methylation

Inferred from mutant phenotype PubMed 14716017. Source: MGI

negative regulation of gene expression

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

nucleosome positioning

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression by genetic imprinting

Inferred from direct assay PubMed 12461525PubMed 15143173. Source: MGI

regulation of histone acetylation

Inferred from mutant phenotype Ref.6. Source: UniProtKB

regulation of histone methylation

Inferred from mutant phenotype Ref.6. Source: UniProtKB

regulation of molecular function, epigenetic

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15143173. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromosome, centromeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

condensed chromosome

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 12011441PubMed 15572351. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay Ref.4PubMed 12461525PubMed 15143173PubMed 15340049. Source: MGI

chromatin insulator sequence binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.7. Source: IntAct

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Chd8Q09XV53EBI-932785,EBI-1169080

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 736736Transcriptional repressor CTCF
PRO_0000047229

Regions

Zinc finger266 – 28823C2H2-type 1
Zinc finger294 – 31623C2H2-type 2
Zinc finger322 – 34524C2H2-type 3
Zinc finger351 – 37323C2H2-type 4
Zinc finger379 – 40123C2H2-type 5
Zinc finger407 – 43024C2H2-type 6
Zinc finger437 – 46024C2H2-type 7
Zinc finger467 – 48923C2H2-type 8
Zinc finger495 – 51723C2H2-type 9
Zinc finger523 – 54624C2H2-type 10
Zinc finger555 – 57723C2H2-type 11; atypical
Compositional bias635 – 67642Pro-rich

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue2891Phosphothreonine By similarity
Modified residue3171Phosphothreonine By similarity
Modified residue3741Phosphothreonine By similarity
Modified residue4021Phosphoserine By similarity
Modified residue6091Phosphoserine By similarity
Modified residue6101Phosphoserine By similarity
Modified residue6121Phosphoserine By similarity
Cross-link74Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.12
Cross-link698Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.12

Experimental info

Mutagenesis741K → R: No sumoylation. Ref.12
Mutagenesis6981K → R: No sumoylation. Ref.12
Sequence conflict381C → S in AAC52928. Ref.1
Sequence conflict2571I → K in AAH37456. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q61164 [UniParc].

Last modified April 23, 2003. Version 2.
Checksum: 7C49D4A7BDCFEFA1

FASTA73683,745
        10         20         30         40         50         60 
MEGEAVEAIV EESETFIKGK ERKTYQRRRE GGQEEDACHL PQNQTDGGEV VQDVNSSVQM 

        70         80         90        100        110        120 
VMMEQLDPTL LQMKTEVMEG TVAPEAEAAV DDTQIITLQV VNMEEQPINI GELQLVQVPV 

       130        140        150        160        170        180 
PVTVPVATTS VEELQGAYEN EVSKEGLAES EPMICHTLPL PEGFQVVKVG ANGEVETLEQ 

       190        200        210        220        230        240 
GELPPQEDSS WQKDPDYQPP AKKTKKTKKS KLRYTEEGKD VDVSVYDFEE EQQEGLLSEV 

       250        260        270        280        290        300 
NAEKVVGNMK PPKPTKIKKK GVKKTFQCEL CSYTCPRRSN LDRHMKSHTD ERPHKCHLCG 

       310        320        330        340        350        360 
RAFRTVTLLR NHLNTHTGTR PHKCPDCDMA FVTSGELVRH RRYKHTHEKP FKCSMCDYAS 

       370        380        390        400        410        420 
VEVSKLKRHI RSHTGERPFQ CSLCSYASRD TYKLKRHMRT HSGEKPYECY ICHARFTQSG 

       430        440        450        460        470        480 
TMKMHILQKH TENVAKFHCP HCDTVIARKS DLGVHLRKQH SYIEQGKKCR YCDAVFHERY 

       490        500        510        520        530        540 
ALIQHQKSHK NEKRFKCDQC DYACRQERHM IMHKRTHTGE KPYACSHCDK TFRQKQLLDM 

       550        560        570        580        590        600 
HFKRYHDPNF VPAAFVCSKC GKTFTRRNTM ARHADNCAGP DGVEGENGGE TKKSKRGRKR 

       610        620        630        640        650        660 
KMRSKKEDSS DSEENAEPDL DDNEEEEEPA VEIEPEPEPQ PQPPPPPQPV APAPPPAKKR 

       670        680        690        700        710        720 
RGRPPGRTNQ PKQNQPTAII QVEDQNTGAI ENIIVEVKKE PDAEPAEGEE EEAQAATTDA 

       730 
PNGDLTPEMI LSMMDR 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS22606.1.
RefSeqNP_851839.1. NM_181322.3.
XP_006530711.1. XM_006530648.1.
UniGeneMm.269474.

3D structure databases

ProteinModelPortalQ61164.
SMRQ61164. Positions 263-591.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198963. 21 interactions.
DIPDIP-38020N.
IntActQ61164. 14 interactions.
MINTMINT-4092474.
STRING10090.ENSMUSP00000005841.

Proteomic databases

PaxDbQ61164.
PRIDEQ61164.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005841; ENSMUSP00000005841; ENSMUSG00000005698.
GeneID13018.
KEGGmmu:13018.
UCSCuc009ndm.2. mouse.

Organism-specific databases

CTD10664.
MGIMGI:109447. Ctcf.

Phylogenomic databases

eggNOGCOG5048.
GeneTreeENSGT00530000063079.
HOGENOMHOG000276534.
HOVERGENHBG000350.
InParanoidQ61164.
OMAPPNQADG.
OrthoDBEOG71K632.
PhylomeDBQ61164.
TreeFamTF106430.

Gene expression databases

ArrayExpressQ61164.
BgeeQ61164.
CleanExMM_CTCF.
GenevestigatorQ61164.

Family and domain databases

Gene3D3.30.160.60. 9 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 11 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 8 hits.
PS50157. ZINC_FINGER_C2H2_2. 11 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTCF. mouse.
NextBio282878.
PROQ61164.
SOURCESearch...

Entry information

Entry nameCTCF_MOUSE
AccessionPrimary (citable) accession number: Q61164
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: April 23, 2003
Last modified: July 9, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot