UniProt Summary: DNA glycosylase which prefers single-stranded DNA (ssDNA), or partially ssDNA structures such as bubble and fork structures, to double-stranded DNA (dsDNA). 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. Seems to be an important facilitator of cell proliferation in certain populations, for example neural stem/progenitor cells and tumor cells, suggesting a role in replication-associated DNA repair. {ECO:0000269|PubMed:12433996, ECO:0000269|PubMed:19170771, ECO:0000269|PubMed:22569481, ECO:0000269|PubMed:23755964}.
Pfam DomainsGO Terms
Pfam Domains
H2TH
zf-GRF
zf-RanBP
GO Terms
bubble DNA binding
DNA N-glycosylase activity
class I DNA-(apurinic or apyrimidinic site) endonuclease activity
DNA-(apurinic or apyrimidinic site) endonuclease activity
base-excision repair
damaged DNA binding
double-stranded DNA binding
single-stranded DNA binding
nucleotide-excision repair
DNA repair
DNA metabolic process
cellular response to DNA damage stimulus
zinc ion binding
cellular response to stress
CRISPR Data
Compound HitMost Correlated Genes in ChemogenomicsTissues where Essential in the Avana Dataset (DepMap 20Q1)