An endonuclease 8-like 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q96FI4]
EC 3.2.2.-;
EC 4.2.99.18;
DNA glycosylase/AP lyase Neil1;
DNA-(apurinic or apyrimidinic site) lyase Neil1;
Endonuclease VIII-like 1;
FPG1;
Nei homolog 1;
NEH1;
Nei-like protein 1
| 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 7 target(s):
| Target | Category | Definition |
|---|---|---|
| damaged DNA binding | molecular function | Binding to damaged DNA. [GOC:jl] |
| 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] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| zinc ion binding | molecular function | Binding to a zinc ion (Zn). [GOC:ai] |
| hydrolase activity, acting on glycosyl bonds | molecular function | Catalysis of the hydrolysis of any glycosyl bond. [GOC:jl] |
| 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] |
| 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 6 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] |
| chromosome | cellular component | A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information. [ISBN:0198547684] |
| cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
| centrosome | cellular component | A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle. [GOC:mah, ISBN:0198547684] |
| cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
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 5 target(s):
| Target | Category | Definition |
|---|---|---|
| base-excision repair | biological process | In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. [ISBN:0815316194] |
| base-excision repair, gap-filling | biological process | Repair of the damaged strand by the combined action of an apurinic endouclease that degrades a few bases on the damaged strand and a polymerase that synthesizes a 'patch' in the 5' to 3' direction, using the undamaged strand as a template. [ISBN:1550091131] |
| response to oxidative stress | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. [GOC:jl, PMID:12115731] |
| negative regulation of nuclease activity | biological process | Any process that stops or reduces the rate of nuclease activity, the hydrolysis of ester linkages within nucleic acids. [GOC:mah] |
| 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] |