Page last updated: 2024-08-07 14:42:03

N-glycosylase/DNA lyase

An N-glycosylase/DNA lyase that is encoded in the genome of human. [PRO:DNx, UniProtKB:O15527]

Synonyms

Research

Bioassay Publications (1)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's1 (100.00)24.3611
2020's0 (0.00)2.80

Compounds (5)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
hydralazineHomo sapiens (human)IC5050.000011
isocarboxazidHomo sapiens (human)IC5050.000021
isoniazidHomo sapiens (human)IC5050.000042
nialamideHomo sapiens (human)IC5050.000021
hydralazine hydrochlorideHomo sapiens (human)IC5050.000010

Enables

This protein enables 10 target(s):

TargetCategoryDefinition
RNA polymerase II cis-regulatory region sequence-specific DNA bindingmolecular functionBinding to a specific upstream regulatory DNA sequence (transcription factor recognition sequence or binding site) located in cis relative to the transcription start site (i.e., on the same strand of DNA) of a gene transcribed by RNA polymerase II. [GOC:txnOH-2018]
damaged DNA bindingmolecular functionBinding to damaged DNA. [GOC:jl]
endonuclease activitymolecular functionCatalysis of the hydrolysis of ester linkages within nucleic acids by creating internal breaks. [GOC:mah, ISBN:0198547684]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
microtubule bindingmolecular functionBinding to a microtubule, a filament composed of tubulin monomers. [GOC:krc]
oxidized purine nucleobase lesion DNA N-glycosylase activitymolecular functionCatalysis 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]
enzyme bindingmolecular functionBinding to an enzyme, a protein with catalytic activity. [GOC:jl]
oxidized purine DNA bindingmolecular functionBinding to a DNA region containing an oxidized purine residue. [GOC:vk]
8-oxo-7,8-dihydroguanine DNA N-glycosylase activitymolecular functionCatalysis of the removal of 8-oxo-7,8-dihydroguanine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. [GOC:mah, PMID:17641464]
class I DNA-(apurinic or apyrimidinic site) endonuclease activitymolecular functionCatalysis 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]

Located In

This protein is located in 6 target(s):

TargetCategoryDefinition
nucleuscellular componentA 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]
nucleoplasmcellular componentThat part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653]
mitochondrial matrixcellular componentThe gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. [GOC:as, ISBN:0198506732]
cytosolcellular componentThe part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl]
nuclear matrixcellular componentThe dense fibrillar network lying on the inner side of the nuclear membrane. [ISBN:0582227089]
nuclear speckcellular componentA discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy. [http://www.cellnucleus.com/]

Active In

This protein is active in 1 target(s):

TargetCategoryDefinition
nucleuscellular componentA 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]

Part Of

This protein is part of 1 target(s):

TargetCategoryDefinition
protein-containing complexcellular componentA stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. [GOC:dos, GOC:mah]

Involved In

This protein is involved in 17 target(s):

TargetCategoryDefinition
base-excision repairbiological processIn 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]
regulation of DNA-templated transcriptionbiological processAny process that modulates the frequency, rate or extent of cellular DNA-templated transcription. [GOC:go_curators, GOC:txnOH]
response to oxidative stressbiological processAny 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]
response to radiationbiological processAny 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 an electromagnetic radiation stimulus. Electromagnetic radiation is a propagating wave in space with electric and magnetic components. These components oscillate at right angles to each other and to the direction of propagation. [GOC:jl, Wikipedia:Electromagnetic_radiation]
response to xenobiotic stimulusbiological processAny 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 a stimulus from a xenobiotic, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical. [GOC:jl, GOC:krc]
response to light stimulusbiological processAny 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 a light stimulus, electromagnetic radiation of wavelengths classified as infrared, visible or ultraviolet light. [GOC:go_curators, ISBN:0582227089]
response to estradiolbiological processAny 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 stimulus by estradiol, a C18 steroid hormone hydroxylated at C3 and C17 that acts as a potent estrogen. [GOC:mah, ISBN:0911910123]
cellular response to reactive oxygen speciesbiological processAny process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals. [GOC:mah]
negative regulation of apoptotic processbiological processAny process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. [GOC:jl, GOC:mtg_apoptosis]
positive regulation of gene expression via chromosomal CpG island demethylationbiological processAn epigenetic gene regulation mechanism that positively regulates gene expression by demethylation of cytosine residues in chromosomal CpG islands. CpG islands are genomic regions that contain a high frequency of the CG dinucleotide and are often associated with the transcription start site of genes. [PMID:36150101, Wikipedia:Cpg_island]
depurinationbiological processThe disruption of the bond between the sugar in the backbone and the A or G base, causing the base to be removed and leaving a depurinated sugar. [GOC:ai]
depyrimidinationbiological processThe 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]
response to ethanolbiological processAny 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 an ethanol stimulus. [GOC:go_curators]
positive regulation of transcription by RNA polymerase IIbiological processAny process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter. [GOC:go_curators, GOC:txnOH]
response to folic acidbiological processAny 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 a folic acid stimulus. [GOC:ai]
cellular response to cadmium ionbiological processAny process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cadmium (Cd) ion stimulus. [GOC:mah]
base-excision repair, AP site formationbiological processThe 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]