Neil3
entrez
234258
canonical
uniprot
Q8K203
canonical
ensembl
ENSMUSG00000039396
resolver
ensp
ENSMUSP00000041909
resolver
genesymbol
Neil3
resolver
uniprot
Q4ADY6
resolver
uniprot
Q8CD85
resolver
uniprot
Q8R3P4
resolver
uniprot_entry
NEIL3_MOUSE
resolver
uniprot_sec
Q4ADY6
resolver
uniprot_sec
Q8CD85
resolver
uniprot_sec
Q8R3P4
resolver
amino_acid_sequence
MVEGPGCTLNGEKIRARVLPGQAVTGVRGTALQSLLGPAMSPAASLADVATSAAPMNAKDSGWKLLRLFNGYVYSGVETLGKELFMYFGPRALRIHFGMKGSILINPREGENRAGASPALAVQLTRDLICFYDSSVELRNSVESQQRVRVMEELDICSPKFSFSRAESEVKKQGDRMLCDVLLDQRVLPGVGNIIKNEALFDSGLHPAVKVCQLSDKQACHLVKMTRDFSILFYRCCKAGSAISKHCKVYKRPNCDQCHSKITVCRFGENSRMTYFCPHCQKENPQCVQVCQLPTRNTEISWTPRGEDCFTDSVARKSEEQWSCVVCTLINRPSAKACDACLTTRPLDSVLKNRENSIAFNNLVKYPCNNFENTHTEVKINRKTAFGNTTLVLTDLSNKSSALARKKRANHTIDGESQMFLPTDIGFSDSQHPSKEGINYITQPSNKVNISPTVCAQSKLFSSAHKKFKPAHTSATELKSYNSGLSNSELQTNRTRGHHSKSDGSPLCKMHHRRCVLRVVRKDGENKGRQFYACSLPRGAQCGFFEWADLSFPFCRHGKRSIMKTVLKIGPNNGKNFFVCPLEKKKQCNFFQWAENGPGMEIVPGC
uniprot
proteins
ec_number
3.2.2.-
uniprot
proteins
ec_number
4.2.99.18
uniprot
proteins
function
FUNCTION: DNA glycosylase which prefers single-stranded DNA (ssDNA), or partially ssDNA structures such as bubble and fork structures, to double-stranded DNA (dsDNA) (PubMed:20185759, PubMed:22065741, PubMed:22569481, PubMed:22959434, PubMed:23305905, PubMed:23313161). 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 (By similarity). 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 (PubMed:20185759, PubMed:22065741, PubMed:22569481, PubMed:22959434, PubMed:23305905, PubMed:23313161). No activity on 8-oxoG detected (PubMed:20185759, PubMed:22065741, PubMed:22569481, PubMed:22959434, PubMed:23305905, PubMed:23313161). Also shows weak DNA-(apurinic or apyrimidinic site) lyase activity (PubMed:20185759, PubMed:22065741, PubMed:22569481, PubMed:22959434, PubMed:23305905, PubMed:23313161). In vivo, appears to be the primary enzyme involved in removing Sp and Gh from ssDNA in neonatal tissues (PubMed:20185759, PubMed:22065741, PubMed:22569481, PubMed:22959434, PubMed:23305905, PubMed:23313161). {ECO:0000250|UniProtKB:A0A1L8HU22, ECO:0000269|PubMed:20185759, ECO:0000269|PubMed:22065741, ECO:0000269|PubMed:22569481, ECO:0000269|PubMed:22959434, ECO:0000269|PubMed:23305905, ECO:0000269|PubMed:23313161}.
uniprot
proteins
mass_dalton
67416
uniprot
proteins
protein_family
FPG family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16428305
uniprot
proteins
pubmed
19170771
uniprot
proteins
pubmed
19426544
uniprot
proteins
pubmed
20185759
uniprot
proteins
pubmed
22065741
uniprot
proteins
pubmed
22569481
uniprot
proteins
pubmed
22959434
uniprot
proteins
pubmed
23305905
uniprot
proteins
pubmed
23313161
uniprot
proteins
sequence_length
606
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16428305}. Chromosome {ECO:0000250|UniProtKB:A0A1L8HU22}. Note=Recruited to replication stress sites via interaction with ubiquitinated CMG helicase. {ECO:0000250|UniProtKB:A0A1L8HU22}.
uniprot
proteins