Function | DNA glycosylase which prefers single-stranded DNA (ssDNA), or partially ssDNA structures such as bubble and fork structures, to double-stranded DNA (dsDNA). Mediates interstrand cross-link repair in response to replication stress: acts by mediating DNA glycosylase activity, cleaving one of the two N-glycosyl bonds comprising the interstrand cross-link, which avoids the formation of a double-strand break but generates an abasic site that is bypassed by translesion synthesis polymerases. In vitro, displays strong glycosylase activity towards the hydantoin lesions spiroiminodihydantoin (Sp) and guanidinohydantoin (Gh) in both ssDNA and dsDNA.also recognizes FapyA, FapyG, 5-OHU, 5-OHC, 5-OHMH, Tg and 8-oxoA lesions in ssDNA. No activity on 8-oxoG detected. Also shows weak DNA-(apurinic or apyrimidinic site) lyase activity. In vivo, appears to be the primary enzyme involved in removing Sp and Gh from ssDNA in neonatal tissues. |
Protein Name | Endonuclease 8-Like 3Dna Glycosylase Fpg2Dna Glycosylase/Ap Lyase Neil3Endonuclease Viii-Like 3Nei-Like Protein 3 |
Database Links | Reactome: R-HSA-110328Reactome: R-HSA-110329Reactome: R-HSA-110330Reactome: R-HSA-110331Reactome: R-HSA-9629232Reactome: R-HSA-9636003 |
Cellular Localisation | NucleusChromosomeRecruited To Replication Stress Sites Via Interaction With Ubiquitinated Cmg Helicase |
Alternative Protein Names | Endonuclease 8-Like 3 proteinDna Glycosylase Fpg2 proteinDna Glycosylase/Ap Lyase Neil3 proteinEndonuclease Viii-Like 3 proteinNei-Like Protein 3 proteinNEIL3 protein |
Information sourced from Uniprot.org