An endonuclease III-like protein 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P78549]
hNTH1;
EC 3.2.2.-;
EC 4.2.99.18;
Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase;
DNA glycosylase/AP lyase
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|---|---|
| pre-1990 | 0 (0) | 18.7374 |
| 1990's | 0 (0) | 18.2507 |
| 2000's | 0 (0) | 29.6817 |
| 2010's | 0 (0) | 24.3611 |
| 2020's | 0 (0) | 2.80 |
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| isoniazid | Homo sapiens (human) | IC50 | 50.0000 | 1 | 0 |
This protein enables 11 target(s):
| Target | Category | Definition |
|---|---|---|
| oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity | molecular function | Catalysis of the removal oxidized pyrimidine bases by cleaving the N-C1' glycosidic bond between the oxidized pyrimidine and the deoxyribose sugar. The reaction involves formation of a covalent enzyme-pyrimidine base intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apyrimidinic (AP) site. [GOC:elh, PMID:11554296] |
| damaged DNA binding | molecular function | Binding to damaged DNA. [GOC:jl] |
| double-stranded DNA binding | molecular function | Binding to double-stranded DNA. [GOC:elh, GOC:vw] |
| DNA-(apurinic or apyrimidinic site) endonuclease activity | molecular function | Catalysis of the cleavage of the C-O-P bond in the AP site created when DNA glycosylase removes a damaged base, involved in the DNA base excision repair pathway (BER). [Wikipedia:AP_endonuclease] |
| endonuclease activity | molecular function | Catalysis of the hydrolysis of ester linkages within nucleic acids by creating internal breaks. [GOC:mah, ISBN:0198547684] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| oxidized purine nucleobase lesion DNA N-glycosylase activity | molecular function | Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site. [GOC:elh, PMID:11554296] |
| DNA N-glycosylase activity | molecular function | Catalysis of the removal of damaged bases by cleaving the N-C1' glycosidic bond between the target damaged DNA base and the deoxyribose sugar. The reaction releases a free base and leaves an apurinic/apyrimidinic (AP) site. [GOC:elh, PMID:11554296] |
| metal ion binding | molecular function | Binding to a metal ion. [GOC:ai] |
| 4 iron, 4 sulfur cluster binding | molecular function | Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. [GOC:ai, PMID:15952888, Wikipedia:Iron-sulfur_cluster] |
| class I DNA-(apurinic or apyrimidinic site) endonuclease activity | molecular function | Catalysis of the cleavage of an AP site 3' of the baseless site by a beta-lyase mechanism, leaving an unsaturated aldehyde, termed a 3'-(4-hydroxy-5-phospho-2-pentenal) residue, and a 5'-phosphate. [PMID:1698278, RHEA:66592] |
This protein is located in 3 target(s):
| Target | Category | Definition |
|---|---|---|
| nucleus | cellular component | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators] |
| nucleoplasm | cellular component | That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653] |
| mitochondrion | cellular component | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. [GOC:giardia, ISBN:0198506732] |
This protein is active in 1 target(s):
| Target | Category | Definition |
|---|---|---|
| nucleus | cellular component | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators] |
This protein is involved in 3 target(s):
| Target | Category | Definition |
|---|---|---|
| base-excision repair, AP site formation | biological process | The formation of an AP site, a deoxyribose sugar with a missing base, by DNA glycosylase which recognizes an altered base in DNA and catalyzes its hydrolytic removal. This sugar phosphate is the substrate recognized by the AP endonuclease, which cuts the DNA phosphodiester backbone at the 5' side of the altered site to leave a gap which is subsequently repaired. [ISBN:0815316194] |
| nucleotide-excision repair | biological process | A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts). [PMID:10197977] |
| depyrimidination | biological process | The disruption of the bond between the sugar in the backbone and the C or T base, causing the base to be removed and leaving a depyrimidinated sugar. [GOC:ai] |