NEIL3
entrez
55247
canonical
uniprot
Q8TAT5
canonical
ensembl
ENSG00000109674
resolver
ensp
ENSP00000264596
resolver
enst
ENST00000264596
resolver
genesymbol
NEIL3
resolver
hgnc
HGNC:24573
resolver
uniprot
Q2PPJ3
resolver
uniprot
Q8NG51
resolver
uniprot
Q9NV95
resolver
uniprot_entry
NEIL3_HUMAN
resolver
uniprot_sec
Q2PPJ3
resolver
uniprot_sec
Q8NG51
resolver
uniprot_sec
Q9NV95
resolver
amino_acid_sequence
MVEGPGCTLNGEKIRARVLPGQAVTGVRGSALRSLQGRALRLAASTVVVSPQAAALNNDSSQNVLSLFNGYVYSGVETLGKELFMYFGPKALRIHFGMKGFIMINPLEYKYKNGASPVLEVQLTKDLICFFDSSVELRNSMESQQRIRMMKELDVCSPEFSFLRAESEVKKQKGRMLGDVLMDQNVLPGVGNIIKNEALFDSGLHPAVKVCQLTDEQIHHLMKMIRDFSILFYRCRKAGLALSKHYKVYKRPNCGQCHCRITVCRFGDNNRMTYFCPHCQKENPQHVDICKLPTRNTIISWTSSRVDHVMDSVARKSEEHWTCVVCTLINKPSSKACDACLTSRPIDSVLKSEENSTVFSHLMKYPCNTFGKPHTEVKINRKTAFGTTTLVLTDFSNKSSTLERKTKQNQILDEEFQNSPPASVCLNDIQHPSKKTTNDITQPSSKVNISPTISSESKLFSPAHKKPKTAQYSSPELKSCNPGYSNSELQINMTDGPRTLNPDSPRCSKHNRLCILRVVGKDGENKGRQFYACPLPREAQCGFFEWADLSFPFCNHGKRSTMKTVLKIGPNNGKNFFVCPLGKEKQCNFFQWAENGPGIKIIPGC
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:12433996, PubMed:19170771, PubMed:22569481, PubMed:23755964). 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:12433996, PubMed:19170771, PubMed:22569481, PubMed:23755964). No activity on 8-oxoG detected (PubMed:12433996, PubMed:19170771, PubMed:22569481, PubMed:23755964). Also shows weak DNA-(apurinic or apyrimidinic site) lyase activity (PubMed:12433996, PubMed:19170771, PubMed:22569481, PubMed:23755964). In vivo, appears to be the primary enzyme involved in removing Sp and Gh from ssDNA in neonatal tissues (PubMed:12433996, PubMed:19170771, PubMed:22569481, PubMed:23755964). {ECO:0000250|UniProtKB:A0A1L8HU22, ECO:0000269|PubMed:12433996, ECO:0000269|PubMed:19170771, ECO:0000269|PubMed:22569481, ECO:0000269|PubMed:23755964}.
uniprot
proteins
mass_dalton
67769
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="V->P: No effect on AP lyase activity. Impairs monofunctional glycosylase activity."; /evidence="ECO:0000269|PubMed:19170771, ECO:0000269|PubMed:23755964"; MUTAGEN 3; /note="E->A: No effect on AP lyase activity."; /evidence="ECO:0000269|PubMed:19170771"; MUTAGEN 81; /note="K->A: Loss of glycosylase and lyase activities."; /evidence="ECO:0000269|PubMed:23755964"; MUTAGEN 276; /note="C->S: Abolishes AP lyase activity."; /evidence="ECO:0000269|PubMed:19170771"; MUTAGEN 279; /note="C->S: Abolishes AP lyase activity."; /evidence="ECO:0000269|PubMed:19170771
uniprot
proteins
protein_family
FPG family
uniprot
proteins
pubmed
12200441
uniprot
proteins
pubmed
12433996
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16428305
uniprot
proteins
pubmed
19121397
uniprot
proteins
pubmed
19170771
uniprot
proteins
pubmed
19426544
uniprot
proteins
pubmed
22365498
uniprot
proteins
pubmed
22569481
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23755964
uniprot
proteins
sequence_length
605
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12433996}. Chromosome {ECO:0000250|UniProtKB:A0A1L8HU22}. Note=Recruited to replication stress sites via interaction with ubiquitinated CMG helicase. {ECO:0000250|UniProtKB:A0A1L8HU22}.
uniprot
proteins