NTHL1
entrez
4913
canonical
uniprot
P78549
canonical
ensembl
ENSG00000065057
resolver
ensp
ENSP00000498290
resolver
ensp
ENSP00000498421
resolver
ensp
ENSP00000498821
resolver
genesymbol
NTHL1
resolver
genesymbol_syn
NTH1
resolver
genesymbol_syn
OCTS3
resolver
hgnc
HGNC:8028
resolver
uniprot
E5KTI5
resolver
uniprot
Q1MVR1
resolver
uniprot
Q99566
resolver
uniprot
Q99794
resolver
uniprot
Q9BPX2
resolver
uniprot_entry
E5KTI5_HUMAN
resolver
uniprot_entry
NTH_HUMAN
resolver
uniprot_sec
Q1MVR1
resolver
uniprot_sec
Q99566
resolver
uniprot_sec
Q99794
resolver
uniprot_sec
Q9BPX2
resolver
activity_regulation
ACTIVITY REGULATION: APE1 displaces NTHL1 from the N-glycosylase-generated AP site in DNA, thereby increasing the turnover of the DNA N-glycosylase activity (PubMed:11287425, PubMed:12519758). AP lyase activity is stimulated by YBX1 (PubMed:11287425). ERCC5/XPG stimulates NTHL1 activity and NTHL1 binding to its DNA substrate (PubMed:9927729). {ECO:0000269|PubMed:11287425, ECO:0000269|PubMed:12519758, ECO:0000269|PubMed:9927729}.
uniprot
proteins
amino_acid_sequence
MTALSARMLTRSRSLGPGAGPRGCREEPGPLRRREAAAEARKSHSPVKRPRKAQRLRVAYEGSDSEKGEGAEPLKVPVWEPQDWQQQLVNIRAMRNKKDAPVDHLGTEHCYDSSAPPKVRRYQVLLSLMLSSQTKDQVTAGAMQRLRARGLTVDSILQTDDATLGKLIYPVGFWRSKVKYIKQTSAILQQHYGGDIPASVAELVALPGVGPKMAHLAMAVAWGTVSGIAVDTHVHRIANRLRWTKKATKSPEETRAALEEWLPRELWHEINGLLVGFGQQTCLPVHPRCHACLNQALCPAAQGL
uniprot
proteins
disease_involvement
DISEASE: Familial adenomatous polyposis 3 (FAP3) [MIM:616415]: A form of familial adenomatous polyposis, a condition characterized by the development of multiple colorectal adenomatous polyps, benign neoplasms derived from glandular epithelium. Some affected individuals may develop colorectal carcinoma. {ECO:0000269|PubMed:25938944}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.2.2.-
uniprot
proteins
ec_number
4.2.99.18
uniprot
proteins
function
FUNCTION: Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage (PubMed:29610152, PubMed:9927729). The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines. Also has 8-oxo-7,8-dihydroguanine (8-oxoG) DNA glycosylase activity. Acts preferentially on DNA damage opposite guanine residues in DNA. Is able to process lesions in nucleosomes without requiring or inducing nucleosome disruption. {ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:10882850, ECO:0000269|PubMed:11328882, ECO:0000269|PubMed:11380260, ECO:0000269|PubMed:11695910, ECO:0000269|PubMed:12140329, ECO:0000269|PubMed:12144783, ECO:0000269|PubMed:12519758, ECO:0000269|PubMed:14734554, ECO:0000269|PubMed:15533839, ECO:0000269|PubMed:17923696, ECO:0000269|PubMed:20005182, ECO:0000269|PubMed:20110254, ECO:0000269|PubMed:21930793, ECO:0000269|PubMed:29610152, ECO:0000269|PubMed:8990169, ECO:0000269|PubMed:9045706, ECO:0000269|PubMed:9705289, ECO:0000269|PubMed:9890904, ECO:0000269|PubMed:9927729}.
uniprot
proteins
mass_dalton
33570
uniprot
proteins
mutagenesis
MUTAGEN 32..34; /note="Missing: Sorted to the cytoplasm."; /evidence="ECO:0000269|PubMed:12531031"; MUTAGEN 34; /note="R->A: Sorted to both nuclei and mitochondria."; /evidence="ECO:0000269|PubMed:12531031"; MUTAGEN 34; /note="R->D: Sorted to the cytoplasm."; /evidence="ECO:0000269|PubMed:12531031"; MUTAGEN 49; /note="R->A,D: Sorted to both nuclei and mitochondria."; /evidence="ECO:0000269|PubMed:12531031"; MUTAGEN 212; /note="K->Q: Inactivates enzyme."; /evidence="ECO:0000269|PubMed:11695910, ECO:0000269|PubMed:9705289"; MUTAGEN 212; /note="K->R: 85-fold reduction in activity. Uncouples the glycosylase activity from the lyase activity. Shows glycosylase activity without any detectable AP-lyase activity during the first 10 minutes of the reaction."; /evidence="ECO:0000269|PubMed:11695910, ECO:0000269|PubMed:9705289
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by TRIM26; leading to proteasomal degradation. {ECO:0000269|PubMed:29610152}.
uniprot
proteins
protein_family
Nth/MutY family
uniprot
proteins
pubmed
10882850
uniprot
proteins
pubmed
11287425
uniprot
proteins
pubmed
11328882
uniprot
proteins
pubmed
11380260
uniprot
proteins
pubmed
11695910
uniprot
proteins
pubmed
12140329
uniprot
proteins
pubmed
12144783
uniprot
proteins
pubmed
12519758
uniprot
proteins
pubmed
12531031
uniprot
proteins
pubmed
14734554
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15533839
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
17923696
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20005182
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20110254
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21930793
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25938944
uniprot
proteins
pubmed
29610152
uniprot
proteins
pubmed
8990169
uniprot
proteins
pubmed
9045706
uniprot
proteins
pubmed
9611236
uniprot
proteins
pubmed
9705289
uniprot
proteins
pubmed
9831664
uniprot
proteins
pubmed
9890904
uniprot
proteins
pubmed
9927729
uniprot
proteins
sequence_length
304
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:10882850, ECO:0000269|PubMed:12531031, ECO:0000269|PubMed:9611236}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:9611236}.
uniprot
proteins