Search Results

Overview

Uniprot IDQ01831
Protein NameDNA repair protein complementing XP-C cells
Gene NameXPC
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
361 LENHTKPKTSKGTKQ
364 HTKPKTSKGTKQEET
374 KQEETFAKGTCRPSA
50 PKKSLLSKVSQGKRK
73 SADGPAKKKVAKVTV
77 PAKKKVAKVTVKSEN
81 KVAKVTVKSENLKVI

Function

Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex (PubMed:10734143, PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19609301, PubMed:19941824, PubMed:20028083, PubMed:20649465, PubMed:20798892, PubMed:9734359). Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides (PubMed:10734143, PubMed:19609301, PubMed:20649465). This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity (PubMed:10734143, PubMed:19609301, PubMed:20649465). The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). The orientation of XPC complex binding appears to be crucial for inducing a productive NER (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts (PubMed:20028083). XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1 (PubMed:20028083)

Protein Sequence

10 MARKRAAGGE 20 PRGRELRSQK 30 SKAKSKARRE 40 EEEEDAFEDE 50 KPPKKSLLSK 60 VSQGKRKRGC 70 SHPGGSADGP 80 AKKKVAKVTV 90 KSENLKVIKD 100 EALSDGDDLR 110 DFPSDLKKAH 120 HLKRGATMNE 130 DSNEEEEESE 140 NDWEEVEELS 150 EPVLGDVRES 160 TAFSRSLLPV 170 KPVEIEIETP 180 EQAKTRERSE 190 KIKLEFETYL 200 RRAMKRFNKG 210 VHEDTHKVHL 220 LCLLANGFYR 230 NNICSQPDLH 240 AIGLSIIPAR 250 FTRVLPRDVD 260 TYYLSNLVKW 270 FIGTFTVNAE 280 LSASEQDNLQ 290 TTLERRFAIY 300 SARDDEELVH 310 IFLLILRALQ 320 LLTRLVLSLQ 330 PIPLKSATAK 340 GKKPSKERLT 350 ADPGGSSETS 360 SQVLENHTKP 370 KTSKGTKQEE 380 TFAKGTCRPS 390 AKGKRNKGGR 400 KKRSKPSSSE 410 EDEGPGDKQE 420 KATQRRPHGR 430 ERRVASRVSY 440 KEESGSDEAG 450 SGSDFELSSG 460 EASDPSDEDS 470 EPGPPKQRKA 480 PAPQRTKAGS 490 KSASRTHRGS 500 HRKDPSLPAA 510 SSSSSSSKRG 520 KKMCSDGEKA 530 EKRSIAGIDQ 540 WLEVFCEQEE 550 KWVCVDCVHG 560 VVGQPLTCYK 570 YATKPMTYVV 580 GIDSDGWVRD 590 VTQRYDPVWM 600 TVTRKCRVDA 610 EWWAETLRPY 620 QSPFMDREKK 630 EDLEFQAKHM 640 DQPLPTAIGL 650 YKNHPLYALK 660 RHLLKYEAIY 670 PETAAILGYC 680 RGEAVYSRDC 690 VHTLHSRDTW 700 LKKARVVRLG 710 EVPYKMVKGF 720 SNRARKARLA 730 EPQLREENDL 740 GLFGYWQTEE 750 YQPPVAVDGK 760 VPRNEFGNVY 770 LFLPSMMPIG 780 CVQLNLPNLH 790 RVARKLDIDC 800 VQAITGFDFH 810 GGYSHPVTDG 820 YIVCEEFKDV 830 LLTAWENEQA 840 VIERKEKEKK 850 EKRALGNWKL 860 LAKGLLIRER 870 LKRRYGPKSE 880 AAAPHTDAGG 890 GLSSDEEEGT 900 SSQAEAARIL 910 AASWPQNRED 920 EEKQKLKGGP 930 KKTKREKKAA 940 ASHLFPFEQL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0000109 nucleotide-excision repair complex
Cellular Component GO:0000111 nucleotide-excision repair factor 2 complex
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0090734 site of DNA damage
Cellular Component GO:0071942 XPC complex
Molecular Function GO:0000405 bubble DNA binding
Molecular Function GO:0003684 damaged DNA binding
Molecular Function GO:0140612 DNA damage sensor activity
Molecular Function GO:0000404 heteroduplex DNA loop binding
Molecular Function GO:0044877 protein-containing complex binding
Molecular Function GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding
Molecular Function GO:0003697 single-stranded DNA binding
Molecular Function GO:0003713 transcription coactivator activity
Biological Process GO:0006281 DNA repair
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0006298 mismatch repair
Biological Process GO:0006289 nucleotide-excision repair
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:1901990 regulation of mitotic cell cycle phase transition
Biological Process GO:0010996 response to auditory stimulus
Biological Process GO:0009410 response to xenobiotic stimulus
Biological Process GO:0070914 UV-damage excision repair

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] 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] 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.

[4] 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.

[5] 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.