Search Results
Overview
| Uniprot ID | P46063 |
|---|---|
| Protein Name | ATP-dependent DNA helicase Q1 |
| Gene Name | RECQL |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 193 | LIYVTPEKIAKSKMF |
| 198 | PEKIAKSKMFMSRLE |
| 618 | GDKKMEEKNSGNFQK |
| 625 | KNSGNFQKKAANMLQ |
| 626 | NSGNFQKKAANMLQQ |
| 637 | MLQQSGSKNTGAKKR |
Function
DNA helicase that plays a role in DNA damage repair and genome stability (PubMed:15886194, PubMed:35025765, PubMed:7527136, PubMed:7961977, PubMed:8056767). Exhibits a Mg(2+)- and ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction (PubMed:19151156, PubMed:35025765, PubMed:7527136, PubMed:8056767). Full-length protein unwinds forked DNA substrates, resolves Holliday junctions, and has DNA strand annealing activity (PubMed:19151156, PubMed:25831490). Plays a role in restoring regressed replication forks (PubMed:35025765). Required to restart stalled replication forks induced by abortive topoisomerase 1 and 2 lesions (PubMed:35025765). Does not unwind G-quadruplex DNA (PubMed:18426915). May play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens (PubMed:15886194, PubMed:7961977)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Molecular Function | GO:1990814 | DNA/DNA annealing activity |
| Cellular Component | GO:0005694 | chromosome |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0043138 | 3'-5' DNA helicase activity |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0003678 | DNA helicase activity |
| Molecular Function | GO:0036121 | double-stranded DNA helicase activity |
| Molecular Function | GO:0009378 | four-way junction helicase activity |
| Molecular Function | GO:0046872 | metal ion binding |
| Biological Process | GO:0006281 | DNA repair |
| Biological Process | GO:0006260 | DNA replication |
| Biological Process | GO:0000724 | double-strand break repair via homologous recombination |
| Biological Process | GO:0031297 | replication fork processing |
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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[4] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.
[5] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.
[6] 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.
[7] 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.
[8] 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.
[9] 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.