Search Results
Overview
| Uniprot ID | Q9NYB0 |
|---|---|
| Protein Name | Telomeric repeat-binding factor 2-interacting protein 1 |
| Gene Name | TERF2IP |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 208 | PVSPSSQKLKRKAEE |
| 384 | TREALVKKFGAQNVA |
Function
Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'-TTAGGG-3' sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B signaling by promoting IKK-mediated phosphorylation of RELA/p65, leading to activate expression of NF-kappa-B target genes
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000781 | chromosome, telomeric region |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0000228 | nuclear chromosome |
| Cellular Component | GO:0000783 | nuclear telomere cap complex |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0070187 | shelterin complex |
| Molecular Function | GO:0098505 | G-rich strand telomeric DNA binding |
| Molecular Function | GO:0019902 | phosphatase binding |
| Molecular Function | GO:0042162 | telomeric DNA binding |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0035556 | intracellular signal transduction |
| Biological Process | GO:0048239 | negative regulation of DNA recombination at telomere |
| Biological Process | GO:0032205 | negative regulation of telomere maintenance |
| Biological Process | GO:0043123 | positive regulation of canonical NF-kappaB signal transduction |
| Biological Process | GO:0032206 | positive regulation of telomere maintenance |
| Biological Process | GO:0031848 | protection from non-homologous end joining at telomere |
| Biological Process | GO:0070198 | protein localization to chromosome, telomeric region |
| Biological Process | GO:0006355 | regulation of DNA-templated transcription |
| Biological Process | GO:0010569 | regulation of double-strand break repair via homologous recombination |
| Biological Process | GO:0032204 | regulation of telomere maintenance |
| Biological Process | GO:0016233 | telomere capping |
| Biological Process | GO:0000723 | telomere maintenance |
| Biological Process | GO:0007004 | telomere maintenance via telomerase |
| Biological Process | GO:0010833 | telomere maintenance via telomere lengthening |
Reference
[1] 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.
[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[3] 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.