Search Results
Overview
| Uniprot ID | Q15554 |
|---|---|
| Protein Name | Telomeric repeat-binding factor 2 |
| Gene Name | TERF2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 375 | LKNKRPRKDENESSA |
| 452 | NPKVPKGKWNSSNGV |
Function
Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes (PubMed:15608617, PubMed:16166375, PubMed:20655466, PubMed:28216226, PubMed:31595153, PubMed:9326950, PubMed:9326951, PubMed:9476899). In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo (PubMed:16166375, PubMed:20655466). Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection (PubMed:16166375). Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways (PubMed:16166375). Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair (PubMed:20655466). Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo (PubMed:20655466, PubMed:28216226). Preferentially binds to positive supercoiled DNA (PubMed:15608617, PubMed:20655466). Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology (PubMed:20655466). Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0030424 | axon |
| Cellular Component | GO:0000781 | chromosome, telomeric region |
| Cellular Component | GO:0001673 | male germ cell nucleus |
| Cellular Component | GO:0016604 | nuclear body |
| 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:0003691 | double-stranded telomeric DNA binding |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0098505 | G-rich strand telomeric DNA binding |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Molecular Function | GO:0042162 | telomeric DNA binding |
| Biological Process | GO:0099088 | axonal transport of messenger ribonucleoprotein complex |
| Biological Process | GO:0090398 | cellular senescence |
| Biological Process | GO:2000773 | negative regulation of cellular senescence |
| Biological Process | GO:1904430 | negative regulation of t-circle formation |
| Biological Process | GO:1904354 | negative regulation of telomere capping |
| Biological Process | GO:0032205 | negative regulation of telomere maintenance |
| Biological Process | GO:0032208 | negative regulation of telomere maintenance via recombination |
| Biological Process | GO:0032214 | negative regulation of telomere maintenance via semi-conservative replication |
| Biological Process | GO:0032211 | negative regulation of telomere maintenance via telomerase |
| Biological Process | GO:1904357 | negative regulation of telomere maintenance via telomere lengthening |
| Biological Process | GO:1903824 | negative regulation of telomere single strand break repair |
| Biological Process | GO:1905839 | negative regulation of telomeric D-loop disassembly |
| 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:0032204 | regulation of telomere maintenance |
| Biological Process | GO:0032210 | regulation of telomere maintenance via telomerase |
| Biological Process | GO:0006278 | RNA-templated DNA biosynthetic process |
| Biological Process | GO:0016233 | telomere capping |
| Biological Process | GO:0000723 | telomere maintenance |
| Biological Process | GO:0061820 | telomeric D-loop disassembly |
| Biological Process | GO:0031627 | telomeric loop formation |
Reference
[1] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[2] 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.
[3] 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.