Search Results

Overview

Uniprot IDP39748
Protein NameFlap endonuclease 1
Gene NameFEN1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
109 ERRAEAEKQLQQAQA
125 GAEQEVEKFTKRLVK
128 QEVEKFTKRLVKVTK
200 HLTASEAKKLPIQEF
201 LTASEAKKLPIQEFH
252 RAVDLIQKHKSIEEI
345 GRLDDFFKVTGSLSS
354 TGSLSSAKRKEPEPK
361 KRKEPEPKGSTKKKA
375 AKTGAAGKFKRGK**
99 LKSGELAKRSERRAE

Function

Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA

Protein Sequence

10 MGIQGLAKLI 20 ADVAPSAIRE 30 NDIKSYFGRK 40 VAIDASMSIY 50 QFLIAVRQGG 60 DVLQNEEGET 70 TSHLMGMFYR 80 TIRMMENGIK 90 PVYVFDGKPP 100 QLKSGELAKR 110 SERRAEAEKQ 120 LQQAQAAGAE 130 QEVEKFTKRL 140 VKVTKQHNDE 150 CKHLLSLMGI 160 PYLDAPSEAE 170 ASCAALVKAG 180 KVYAAATEDM 190 DCLTFGSPVL 200 MRHLTASEAK 210 KLPIQEFHLS 220 RILQELGLNQ 230 EQFVDLCILL 240 GSDYCESIRG 250 IGPKRAVDLI 260 QKHKSIEEIV 270 RRLDPNKYPV 280 PENWLHKEAH 290 QLFLEPEVLD 300 PESVELKWSE 310 PNEEELIKFM 320 CGEKQFSEER 330 IRSGVKRLSK 340 SRQGSTQGRL 350 DDFFKVTGSL 360 SSAKRKEPEP 370 KGSTKKKAKT 380 GAAGKFKRGK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000781 chromosome, telomeric region
Cellular Component GO:0016020 membrane
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0032991 protein-containing complex
Molecular Function GO:0008409 5'-3' exonuclease activity
Molecular Function GO:0017108 5'-flap endonuclease activity
Molecular Function GO:0003684 damaged DNA binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0003690 double-stranded DNA binding
Molecular Function GO:0008309 double-stranded DNA exodeoxyribonuclease activity
Molecular Function GO:0004519 endonuclease activity
Molecular Function GO:0004527 exonuclease activity
Molecular Function GO:0048256 flap endonuclease activity
Molecular Function GO:0000287 magnesium ion binding
Molecular Function GO:0030145 manganese ion binding
Molecular Function GO:0004523 RNA-DNA hybrid ribonuclease activity
Biological Process GO:0006287 base-excision repair, gap-filling
Biological Process GO:0006281 DNA repair
Biological Process GO:0006260 DNA replication
Biological Process GO:0043137 DNA replication, removal of RNA primer
Biological Process GO:0006302 double-strand break repair
Biological Process GO:0000724 double-strand break repair via homologous recombination
Biological Process GO:0007613 memory
Biological Process GO:0045876 positive regulation of sister chromatid cohesion
Biological Process GO:0032201 telomere maintenance via semi-conservative replication
Biological Process GO:0009650 UV protection

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] 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.

[4] 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.

[5] 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.

[6] 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.

[7] 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.

[8] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[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.