Search Results

Overview

Uniprot ID	P19447
Protein Name	General transcription and DNA repair factor IIH helicase/translocase subunit XPB
Gene Name	ERCC3
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
222	TSKSAISKTAESSGG
778	KHVHPLFKRFRK***

Function

ATP-dependent 3'-5' DNA helicase/translocase (PubMed:17466626, PubMed:27193682, PubMed:33902107, PubMed:8465201, PubMed:8663148). Binds dsDNA rather than ssDNA, unzipping it in a translocase rather than classical helicase activity (PubMed:27193682, PubMed:33902107). Component of the general transcription and DNA repair factor IIH (TFIIH) core complex (PubMed:10024882, PubMed:17466626, PubMed:8157004, PubMed:8465201). When complexed to CDK-activating kinase (CAK), involved in RNA transcription by RNA polymerase II. The ATPase activity of XPB/ERCC3, but not its helicase activity, is required for DNA opening; it may wrap around the damaged DNA wedging it open, causing localized melting that allows XPD/ERCC2 helicase to anchor (PubMed:10024882, PubMed:17466626). In transcription, TFIIH has an essential role in transcription initiation (PubMed:30894545, PubMed:8157004). When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape (PubMed:8157004). The ATP-dependent helicase activity of XPB/ERCC3 is required for promoter opening and promoter escape (PubMed:10024882). In transcription pre-initiation complexes induces and propagates a DNA twist to open DNA (PubMed:27193682, PubMed:33902107). Also involved in transcription-coupled nucleotide excision repair (NER) of damaged DNA (PubMed:17466626, PubMed:2111438, PubMed:8157004). In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The structure of the TFIIH transcription complex differs from the NER-TFIIH complex; large movements by XPD/ERCC2 and XPB/ERCC3 are stabilized by XPA (PubMed:31253769, PubMed:33902107). XPA retains XPB/ERCC3 at the 5' end of a DNA bubble (mimicking DNA damage) (PubMed:31253769)

Protein Sequence

10 MGKRDRADRD 20 KKKSRKRHYE 30 DEEDDEEDAP 40 GNDPQEAVPS 50 AAGKQVDESG 60 TKVDEYGAKD 70 YRLQMPLKDD 80 HTSRPLWVAP 90 DGHIFLEAFS 100 PVYKYAQDFL 110 VAIAEPVCRP 120 THVHEYKLTA 130 YSLYAAVSVG 140 LQTSDITEYL 150 RKLSKTGVPD 160 GIMQFIKLCT 170 VSYGKVKLVL 180 KHNRYFVESC 190 HPDVIQHLLQ 200 DPVIRECRLR 210 NSEGEATELI 220 TETFTSKSAI 230 SKTAESSGGP 240 STSRVTDPQG 250 KSDIPMDLFD 260 FYEQMDKDEE 270 EEEETQTVSF 280 EVKQEMIEEL 290 QKRCIHLEYP 300 LLAEYDFRND 310 SVNPDINIDL 320 KPTAVLRPYQ 330 EKSLRKMFGN 340 GRARSGVIVL 350 PCGAGKSLVG 360 VTAACTVRKR 370 CLVLGNSAVS 380 VEQWKAQFKM 390 WSTIDDSQIC 400 RFTSDAKDKP 410 IGCSVAISTY 420 SMLGHTTKRS 430 WEAERVMEWL 440 KTQEWGLMIL 450 DEVHTIPAKM 460 FRRVLTIVQA 470 HCKLGLTATL 480 VREDDKIVDL 490 NFLIGPKLYE 500 ANWMELQNNG 510 YIAKVQCAEV 520 WCPMSPEFYR 530 EYVAIKTKKR 540 ILLYTMNPNK 550 FRACQFLIKF 560 HERRNDKIIV 570 FADNVFALKE 580 YAIRLNKPYI 590 YGPTSQGERM 600 QILQNFKHNP 610 KINTIFISKV 620 GDTSFDLPEA 630 NVLIQISSHG 640 GSRRQEAQRL 650 GRVLRAKKGM 660 VAEEYNAFFY 670 SLVSQDTQEM 680 AYSTKRQRFL 690 VDQGYSFKVI 700 TKLAGMEEED 710 LAFSTKEEQQ 720 QLLQKVLAAT 730 DLDAEEEVVA 740 GEFGSRSSQA 750 SRRFGTMSSM 760 SGADDTVYME 770 YHSSRSKAPS 780 KHVHPLFKRF RK

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005675	transcription factor TFIIH holo complex
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0000112	nucleotide-excision repair factor 3 complex
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0005669	transcription factor TFIID complex
Cellular Component	GO:0000439	transcription factor TFIIH core complex
Cellular Component	GO:0097550	transcription preinitiation complex
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:0003684	damaged DNA binding
Molecular Function	GO:0003677	DNA binding
Molecular Function	GO:1990841	promoter-specific chromatin binding
Biological Process	GO:0006915	apoptotic process
Biological Process	GO:0006281	DNA repair
Biological Process	GO:0006265	DNA topological change
Biological Process	GO:0048568	embryonic organ development
Biological Process	GO:0035315	hair cell differentiation
Biological Process	GO:0008104	intracellular protein localization
Biological Process	GO:0006289	nucleotide-excision repair
Biological Process	GO:0043065	positive regulation of apoptotic process
Biological Process	GO:1901990	regulation of mitotic cell cycle phase transition
Biological Process	GO:0006979	response to oxidative stress
Biological Process	GO:0009411	response to UV
Biological Process	GO:0006366	transcription by RNA polymerase II
Biological Process	GO:0006368	transcription elongation by RNA polymerase II
Biological Process	GO:0006367	transcription initiation at RNA polymerase II promoter
Biological Process	GO:0006283	transcription-coupled nucleotide-excision repair

Reference

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[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] 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.

[5] 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.

[6] 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.