Search Results
Overview
| Uniprot ID | Q03468 |
|---|---|
| Protein Name | DNA excision repair protein ERCC-6 |
| Gene Name | ERCC6 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1052 | GADHDVPKRKKFPAS |
| 1054 | DHDVPKRKKFPASNI |
| 297 | CNKRAARKAPAPVTP |
| 323 | KKARVLSKKEERLKK |
Function
Essential factor involved in transcription-coupled nucleotide excision repair (TC-NER), a process during which RNA polymerase II-blocking lesions are rapidly removed from the transcribed strand of active genes (PubMed:16246722, PubMed:20541997, PubMed:22483866, PubMed:26620705, PubMed:32355176, PubMed:34526721, PubMed:38316879, PubMed:38600235, PubMed:38600236). Plays a central role in the initiation of the TC-NER process: specifically recognizes and binds RNA polymerase II stalled at a lesion, and mediates recruitment of ERCC8/CSA, initiating DNA damage excision by TFIIH recruitment (PubMed:32355176, PubMed:34526721, PubMed:38600235, PubMed:38600236). Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA (PubMed:15548521). Acts as a chromatin remodeler at DSBs; DNA-dependent ATPase-dependent activity is essential for this function (PubMed:16246722, PubMed:9565609). Plays an important role in regulating the choice of the DNA double-strand breaks (DSBs) repair pathway and G2/M checkpoint activation; DNA-dependent ATPase activity is essential for this function (PubMed:25820262). Regulates the DNA repair pathway choice by inhibiting non-homologous end joining (NHEJ), thereby promoting the homologous recombination (HR)-mediated repair of DSBs during the S/G2 phases of the cell cycle (PubMed:25820262). Mediates the activation of the ATM- and CHEK2-dependent DNA damage responses thus preventing premature entry of cells into mitosis following the induction of DNA DSBs (PubMed:25820262). Remodels chromatin by evicting histones from chromatin flanking DSBs, limiting RIF1 accumulation at DSBs thereby promoting BRCA1-mediated HR (PubMed:29203878). Required for stable recruitment of ELOA and CUL5 to DNA damage sites (PubMed:28292928). Also involved in UV-induced translocation of ERCC8 to the nuclear matrix (PubMed:26620705). Essential for neuronal differentiation and neuritogenesis; regulates transcription and chromatin remodeling activities required during neurogenesis (PubMed:24874740)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0016604 | nuclear body |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0090734 | site of DNA damage |
| Cellular Component | GO:0008023 | transcription elongation factor complex |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0008094 | ATP-dependent activity, acting on DNA |
| Molecular Function | GO:0140658 | ATP-dependent chromatin remodeler activity |
| Molecular Function | GO:0140664 | ATP-dependent DNA damage sensor activity |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0140463 | chromatin-protein adaptor activity |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0004386 | helicase activity |
| Molecular Function | GO:0030296 | protein tyrosine kinase activator activity |
| Molecular Function | GO:0070063 | RNA polymerase binding |
| Biological Process | GO:0006284 | base-excision repair |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0000077 | DNA damage checkpoint signaling |
| Biological Process | GO:0042262 | DNA protection |
| Biological Process | GO:0006281 | DNA repair |
| Biological Process | GO:0097680 | double-strand break repair via classical nonhomologous end joining |
| Biological Process | GO:2001033 | negative regulation of double-strand break repair via nonhomologous end joining |
| Biological Process | GO:0022008 | neurogenesis |
| Biological Process | GO:0030182 | neuron differentiation |
| Biological Process | GO:0031175 | neuron projection development |
| Biological Process | GO:0045739 | positive regulation of DNA repair |
| Biological Process | GO:0032786 | positive regulation of DNA-templated transcription, elongation |
| Biological Process | GO:1905168 | positive regulation of double-strand break repair via homologous recombination |
| Biological Process | GO:0045943 | positive regulation of transcription by RNA polymerase I |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0045945 | positive regulation of transcription by RNA polymerase III |
| Biological Process | GO:0071168 | protein localization to chromatin |
| Biological Process | GO:0032784 | regulation of DNA-templated transcription elongation |
| Biological Process | GO:0034243 | regulation of transcription elongation by RNA polymerase II |
| Biological Process | GO:0006979 | response to oxidative stress |
| Biological Process | GO:0000012 | single strand break repair |
| Biological Process | GO:0006366 | transcription by RNA polymerase II |
| Biological Process | GO:0006283 | transcription-coupled nucleotide-excision repair |
Reference
[1] 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.
[2] 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.