NEIL2
entrez
252969
canonical
uniprot
Q969S2
canonical
ensembl
ENSG00000154328
resolver
ensembl
ENSG00000292286
resolver
ensp
ENSP00000284503
resolver
ensp
ENSP00000384070
resolver
ensp
ENSP00000394023
resolver
ensp
ENSP00000397538
resolver
ensp
ENSP00000435657
resolver
genesymbol
NEIL2
resolver
hgnc
HGNC:18956
resolver
uniprot
B4DFR7
resolver
uniprot
Q7Z3Q7
resolver
uniprot
Q8N842
resolver
uniprot
Q8NG52
resolver
uniprot_entry
NEIL2_HUMAN
resolver
uniprot_sec
B4DFR7
resolver
uniprot_sec
Q7Z3Q7
resolver
uniprot_sec
Q8N842
resolver
uniprot_sec
Q8NG52
resolver
activity_regulation
ACTIVITY REGULATION: Acetylation of Lys-50 leads to loss of DNA nicking activity. Acetylation of Lys-154 has no effect.
uniprot
proteins
amino_acid_sequence
MPEGPLVRKFHHLVSPFVGQQVVKTGGSSKKLQPASLQSLWLQDTQVHGKKLFLRFDLDEEMGPPGSSPTPEPPQKEVQKEGAADPKQVGEPSGQKTLDGSSRSAELVPQGEDDSEYLERDAPAGDAGRWLRVSFGLFGSVWVNDFSRAKKANKRGDWRDPSPRLVLHFGGGGFLAFYNCQLSWSSSPVVTPTCDILSEKFHRGQALEALGQAQPVCYTLLDQRYFSGLGNIIKNEALYRAGIHPLSLGSVLSASRREVLVDHVVEFSTAWLQGKFQGRPQHTQVYQKEQCPAGHQVMKEAFGPEDGLQRLTWWCPQCQPQLSEEPEQCQFS
uniprot
proteins
ec_number
3.2.2.-
uniprot
proteins
ec_number
4.2.99.18
uniprot
proteins
function
FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Has DNA glycosylase activity towards 5-hydroxyuracil and other oxidized derivatives of cytosine with a preference for mismatched double-stranded DNA (DNA bubbles). Has low or no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine, hypoxanthine and 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. {ECO:0000269|PubMed:12097317, ECO:0000269|PubMed:14522990, ECO:0000269|PubMed:15175427, ECO:0000269|PubMed:15339932}.
uniprot
proteins
mass_dalton
36826
uniprot
proteins
mutagenesis
MUTAGEN 50; /note="K->R: Loss of glycosylase and AP lyase activity."; /evidence="ECO:0000269|PubMed:14522990, ECO:0000269|PubMed:15175427"; MUTAGEN 154; /note="K->R: No effect on glycosylase and AP lyase activity."; /evidence="ECO:0000269|PubMed:15175427"; MUTAGEN 291; /note="C->S: Loss of glycosylase and AP lyase activity."; /evidence="ECO:0000269|PubMed:15339932"; MUTAGEN 295; /note="H->A: Loss of glycosylase and AP lyase activity."; /evidence="ECO:0000269|PubMed:15339932"; MUTAGEN 310; /note="R->Q: Strongly reduces strand AP lyase activity."; /evidence="ECO:0000269|PubMed:15339932"; MUTAGEN 315; /note="C->S: Loss of glycosylase and AP lyase activity."; /evidence="ECO:0000269|PubMed:15339932"; MUTAGEN 318; /note="C->S: Loss of glycosylase and AP lyase activity."; /evidence="ECO:0000269|PubMed:15339932
uniprot
proteins
protein_family
FPG family
uniprot
proteins
pubmed
12097317
uniprot
proteins
pubmed
12200441
uniprot
proteins
pubmed
14522990
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15175427
uniprot
proteins
pubmed
15339932
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
sequence_length
332
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12097317}.
uniprot
proteins