Search Results

Overview

Uniprot IDP18887
Protein NameDNA repair protein XRCC1
Gene NameXRCC1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
169 SQKVTVTKLGQFRVK
197 LFFSRINKTSPVTAS
245 PQESPKGKRKLDLNQ
247 ESPKGKRKLDLNQEE
271 QLSPSVPKRPKLPAP
298 AQGAVTGKPRGEGTE
431 EAPKLPQKQPQTKTK

Function

Scaffold protein involved in DNA single-strand break repair by mediating the assembly of DNA break repair protein complexes (PubMed:11163244, PubMed:28002403). Negatively regulates ADP-ribosyltransferase activity of PARP1 during base-excision repair in order to prevent excessive PARP1 activity (PubMed:28002403, PubMed:34102106, PubMed:34811483). Recognizes and binds poly-ADP-ribose chains: specifically binds auto-poly-ADP-ribosylated PARP1, limiting its activity (PubMed:14500814, PubMed:34102106, PubMed:34811483)

Protein Sequence

10 MPEIRLRHVV 20 SCSSQDSTHC 30 AENLLKADTY 40 RKWRAAKAGE 50 KTISVVLQLE 60 KEEQIHSVDI 70 GNDGSAFVEV 80 LVGSSAGGAG 90 EQDYEVLLVT 100 SSFMSPSESR 110 SGSNPNRVRM 120 FGPDKLVRAA 130 AEKRWDRVKI 140 VCSQPYSKDS 150 PFGLSFVRFH 160 SPPDKDEAEA 170 PSQKVTVTKL 180 GQFRVKEEDE 190 SANSLRPGAL 200 FFSRINKTSP 210 VTASDPAGPS 220 YAAATLQASS 230 AASSASPVSR 240 AIGSTSKPQE 250 SPKGKRKLDL 260 NQEEKKTPSK 270 PPAQLSPSVP 280 KRPKLPAPTR 290 TPATAPVPAR 300 AQGAVTGKPR 310 GEGTEPRRPR 320 AGPEELGKIL 330 QGVVVVLSGF 340 QNPFRSELRD 350 KALELGAKYR 360 PDWTRDSTHL 370 ICAFANTPKY 380 SQVLGLGGRI 390 VRKEWVLDCH 400 RMRRRLPSQR 410 YLMAGPGSSS 420 EEDEASHSGG 430 SGDEAPKLPQ 440 KQPQTKTKPT 450 QAAGPSSPQK 460 PPTPEETKAA 470 SPVLQEDIDI 480 EGVQSEGQDN 490 GAEDSGDTED 500 ELRRVAEQKE 510 HRLPPGQEEN 520 GEDPYAGSTD 530 ENTDSEEHQE 540 PPDLPVPELP 550 DFFQGKHFFL 560 YGEFPGDERR 570 KLIRYVTAFN 580 GELEDYMSDR 590 VQFVITAQEW 600 DPSFEEALMD 610 NPSLAFVRPR 620 WIYSCNEKQK 630 LLPHQLYGVV PQA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0000781 chromosome, telomeric region
Cellular Component GO:0070522 ERCC4-ERCC1 complex
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0090734 site of DNA damage
Molecular Function GO:1990599 3' overhang single-stranded DNA endodeoxyribonuclease activity
Molecular Function GO:0160002 ADP-D-ribose modification-dependent protein binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0032356 oxidized DNA binding
Molecular Function GO:0072572 poly-ADP-D-ribose binding
Molecular Function GO:1990165 single-strand break-containing DNA binding
Biological Process GO:0006284 base-excision repair
Biological Process GO:0006302 double-strand break repair
Biological Process GO:0006303 double-strand break repair via nonhomologous end joining
Biological Process GO:1905765 negative regulation of protection from non-homologous end joining at telomere
Biological Process GO:0010836 negative regulation of protein ADP-ribosylation
Biological Process GO:1905051 regulation of base-excision repair
Biological Process GO:0006282 regulation of DNA repair
Biological Process GO:0033194 response to hydroperoxide
Biological Process GO:0000012 single strand break repair
Biological Process GO:0061819 telomeric DNA-containing double minutes formation

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] 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.

[5] 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.

[6] 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.

[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.