Search Results
Overview
| Uniprot ID | P49711 |
|---|---|
| Protein Name | Transcriptional repressor CTCF |
| Gene Name | CTCF |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 202 | PDYQPPAKKTKKTKK |
| 264 | IKKKGVKKTFQCELC |
| 592 | GENGGETKKSKRGRK |
Function
Chromatin binding factor that binds to DNA sequence specific sites and regulates the 3D structure of chromatin (PubMed:16949368, PubMed:18347100, PubMed:18654629, PubMed:19322193). Binds together strands of DNA, thus forming chromatin loops, and anchors DNA to cellular structures, such as the nuclear lamina (PubMed:18347100, PubMed:18654629, PubMed:19322193). Defines the boundaries between active and heterochromatic DNA via binding to chromatin insulators, thereby preventing interaction between promoter and nearby enhancers and silencers (PubMed:18347100, PubMed:18654629, PubMed:19322193). Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus (PubMed:16107875, PubMed:16815976, PubMed:17827499). 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 (By similarity). Mediates interchromosomal association between IGF2/H19 and WSB1/NF1 and may direct distant DNA segments to a common transcription factory (By similarity). Regulates asynchronous replication of IGF2/H19 (By similarity). Plays a critical role in gene silencing over considerable distances in the genome (By similarity). Preferentially interacts with unmethylated DNA, preventing spreading of CpG methylation and maintaining methylation-free zones (PubMed:18413740). Inversely, binding to target sites is prevented by CpG methylation (PubMed:18413740). Plays an important role in chromatin remodeling (PubMed:18413740). Can dimerize when it is bound to different DNA sequences, mediating long-range chromatin looping (PubMed:12191639). Causes local loss of histone acetylation and gain of histone methylation in the beta-globin locus, without affecting transcription (PubMed:12191639). When bound to chromatin, it provides an anchor point for nucleosomes positioning (PubMed:12191639). Seems to be essential for homologous X-chromosome pairing (By similarity). May participate with Tsix in establishing a regulatable epigenetic switch for X chromosome inactivation (PubMed:11743158). May play a role in preventing the propagation of stable methylation at the escape genes from X-inactivation (PubMed:11743158). Involved in sister chromatid cohesion (PubMed:12191639). Associates with both centromeres and chromosomal arms during metaphase and required for cohesin localization to CTCF sites (PubMed:18550811). Plays a role in the recruitment of CENPE to the pericentromeric/centromeric regions of the chromosome during mitosis (PubMed:26321640). Acts as a transcriptional repressor binding to promoters of vertebrate MYC gene and BAG1 gene (PubMed:18413740, PubMed:8649389, PubMed:9591631). Also binds to the PLK and PIM1 promoters (PubMed:12191639). Acts as a transcriptional activator of APP (PubMed:9407128). Regulates APOA1/C3/A4/A5 gene cluster and controls MHC class II gene expression (PubMed:18347100, PubMed:19322193). Plays an essential role in oocyte and preimplantation embryo development by activating or repressing transcription (By similarity). Seems to act as tumor suppressor (PubMed:12191639)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000775 | chromosome, centromeric region |
| Cellular Component | GO:0000793 | condensed chromosome |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0043035 | chromatin insulator sequence binding |
| Molecular Function | GO:0140587 | chromatin loop anchoring activity |
| Molecular Function | GO:0003700 | DNA-binding transcription factor activity |
| Molecular Function | GO:0001227 | DNA-binding transcription repressor activity, RNA polymerase II-specific |
| Molecular Function | GO:0000978 | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
| Molecular Function | GO:0043565 | sequence-specific DNA binding |
| Molecular Function | GO:0000976 | transcription cis-regulatory region binding |
| Molecular Function | GO:0001221 | transcription coregulator binding |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0140588 | chromatin looping |
| Biological Process | GO:0007059 | chromosome segregation |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0040029 | epigenetic regulation of gene expression |
| Biological Process | GO:0071514 | genomic imprinting |
| Biological Process | GO:0008285 | negative regulation of cell population proliferation |
| Biological Process | GO:0045892 | negative regulation of DNA-templated transcription |
| Biological Process | GO:0010629 | negative regulation of gene expression |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:0010628 | positive regulation of gene expression |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0071459 | protein localization to chromosome, centromeric region |
| Biological Process | GO:0070602 | regulation of centromeric sister chromatid cohesion |
| Biological Process | GO:0006357 | regulation of transcription by RNA polymerase II |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[3] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.