Proteins > DNA-(apurinic or apyrimidinic site) endonuclease
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DNA-(apurinic or apyrimidinic site) endonuclease
A DNA-(apurinic or apyrimidinic site) endonuclease that is encoded in the genome of human. [PRO:DNx, UniProtKB:P27695]
Synonyms
EC 3.1.-.-;
APEX nuclease;
APEN;
Apurinic-apyrimidinic endonuclease 1;
AP endonuclease 1;
APE-1;
REF-1;
Redox factor-1
Research
Bioassay Publications (7)
Timeframe | Studies on this Protein(%) | All Drugs % |
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 1 (14.29) | 29.6817 |
2010's | 6 (85.71) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Compounds (17)
Drugs with Inhibition Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
aurintricarboxylic acid | Homo sapiens (human) | IC50 | 3.3700 | 3 | 3 |
hycanthone | Homo sapiens (human) | IC50 | 0.0800 | 1 | 1 |
lucanthone | Homo sapiens (human) | IC50 | 5.0000 | 2 | 2 |
mitoxantrone hydrochloride | Homo sapiens (human) | IC50 | 2.0000 | 1 | 1 |
7-nitro-1h-indole-2-carboxylic acid | Homo sapiens (human) | IC50 | 3.0300 | 2 | 2 |
3,3',4,4',5,5'-hexabromobiphenyl | Homo sapiens (human) | IC50 | 0.2000 | 1 | 1 |
6-hydroxydopa | Homo sapiens (human) | IC50 | 0.1100 | 2 | 2 |
1,3,6-trimethylpyrimido[5,4-e][1,2,4]triazine-5,7-dione | Homo sapiens (human) | IC50 | 200.0000 | 1 | 1 |
2-[[5-(dimethylsulfamoyl)-1H-indol-3-yl]methylidene]propanedioic acid diethyl ester | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
1,6-dimethyl-3-propylpyrimido[5,4-e][1,2,4]triazine-5,7-dione | Homo sapiens (human) | IC50 | 200.0000 | 1 | 1 |
myricetin | Homo sapiens (human) | IC50 | 0.3200 | 2 | 2 |
ag 538 | Homo sapiens (human) | IC50 | 0.2800 | 1 | 1 |
e 3330 | Homo sapiens (human) | IC50 | 12.5000 | 4 | 4 |
N-[3-(1,3-benzothiazol-2-yl)-5,6-dihydro-4H-thieno[2,3-c]pyrrol-2-yl]acetamide | Homo sapiens (human) | IC50 | 2.1500 | 2 | 2 |
thiolactomycin | Homo sapiens (human) | IC50 | 1.0000 | 1 | 1 |
galloflavin | Homo sapiens (human) | IC50 | 0.4000 | 1 | 1 |
Drugs with Activation Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
hycanthone | Homo sapiens (human) | Kd | 0.0100 | 1 | 1 |
lucanthone | Homo sapiens (human) | Kd | 0.0890 | 1 | 1 |
tanshinone ii a | Homo sapiens (human) | Kd | 0.0009 | 1 | 1 |
e 3330 | Homo sapiens (human) | Kd | 0.0016 | 1 | 1 |
Inhibitors of nuclease and redox activity of apurinic/apyrimidinic endonuclease 1/redox effector factor 1 (APE1/Ref-1).Bioorganic & medicinal chemistry, , 05-01, Volume: 25, Issue:9, 2017
DNA repair and redox activities and inhibitors of apurinic/apyrimidinic endonuclease 1/redox effector factor 1 (APE1/Ref-1): a comparative analysis and their scope and limitations toward anticancer drug development.Journal of medicinal chemistry, , Dec-26, Volume: 57, Issue:24, 2014
Inhibitors of nuclease and redox activity of apurinic/apyrimidinic endonuclease 1/redox effector factor 1 (APE1/Ref-1).Bioorganic & medicinal chemistry, , 05-01, Volume: 25, Issue:9, 2017
DNA repair and redox activities and inhibitors of apurinic/apyrimidinic endonuclease 1/redox effector factor 1 (APE1/Ref-1): a comparative analysis and their scope and limitations toward anticancer drug development.Journal of medicinal chemistry, , Dec-26, Volume: 57, Issue:24, 2014
Inhibitors of nuclease and redox activity of apurinic/apyrimidinic endonuclease 1/redox effector factor 1 (APE1/Ref-1).Bioorganic & medicinal chemistry, , 05-01, Volume: 25, Issue:9, 2017
DNA repair and redox activities and inhibitors of apurinic/apyrimidinic endonuclease 1/redox effector factor 1 (APE1/Ref-1): a comparative analysis and their scope and limitations toward anticancer drug development.Journal of medicinal chemistry, , Dec-26, Volume: 57, Issue:24, 2014
Inhibitors of nuclease and redox activity of apurinic/apyrimidinic endonuclease 1/redox effector factor 1 (APE1/Ref-1).Bioorganic & medicinal chemistry, , 05-01, Volume: 25, Issue:9, 2017
DNA repair and redox activities and inhibitors of apurinic/apyrimidinic endonuclease 1/redox effector factor 1 (APE1/Ref-1): a comparative analysis and their scope and limitations toward anticancer drug development.Journal of medicinal chemistry, , Dec-26, Volume: 57, Issue:24, 2014
Inhibitors of nuclease and redox activity of apurinic/apyrimidinic endonuclease 1/redox effector factor 1 (APE1/Ref-1).Bioorganic & medicinal chemistry, , 05-01, Volume: 25, Issue:9, 2017
DNA repair and redox activities and inhibitors of apurinic/apyrimidinic endonuclease 1/redox effector factor 1 (APE1/Ref-1): a comparative analysis and their scope and limitations toward anticancer drug development.Journal of medicinal chemistry, , Dec-26, Volume: 57, Issue:24, 2014
Inhibitors of nuclease and redox activity of apurinic/apyrimidinic endonuclease 1/redox effector factor 1 (APE1/Ref-1).Bioorganic & medicinal chemistry, , 05-01, Volume: 25, Issue:9, 2017
DNA repair and redox activities and inhibitors of apurinic/apyrimidinic endonuclease 1/redox effector factor 1 (APE1/Ref-1): a comparative analysis and their scope and limitations toward anticancer drug development.Journal of medicinal chemistry, , Dec-26, Volume: 57, Issue:24, 2014
Inhibition of apurinic/apyrimidinic endonuclease I's redox activity revisited.Biochemistry, , Apr-30, Volume: 52, Issue:17, 2013
Design and synthesis of novel quinone inhibitors targeted to the redox function of apurinic/apyrimidinic endonuclease 1/redox enhancing factor-1 (Ape1/ref-1).Journal of medicinal chemistry, , Feb-11, Volume: 53, Issue:3, 2010
Enables
This protein enables 25 target(s):
Target | Category | Definition |
DNA binding | molecular function | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). [GOC:dph, GOC:jl, GOC:tb, GOC:vw] |
damaged DNA binding | molecular function | Binding to damaged DNA. [GOC:jl] |
double-stranded telomeric DNA binding | molecular function | Binding to double-stranded telomere-associated DNA. [GOC:jl, ISBN:0321000382] |
transcription coactivator activity | molecular function | A transcription coregulator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coactivators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator. [GOC:txnOH-2018, PMID:10213677, PMID:16858867] |
transcription corepressor activity | molecular function | A transcription coregulator activity that represses or decreases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Corepressors often act by altering chromatin structure and modifications. For example, one class of transcription corepressors modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. [GOC:txnOH-2018, PMID:10213677, PMID:16858867] |
RNA binding | molecular function | Binding to an RNA molecule or a portion thereof. [GOC:jl, GOC:mah] |
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] |
DNA endonuclease activity | molecular function | Catalysis of the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks. [GOC:mah, ISBN:0198547684] |
RNA-DNA hybrid ribonuclease activity | molecular function | Catalysis of the endonucleolytic cleavage of RNA in RNA-DNA hybrids to 5'-phosphomonoesters. [EC:3.1.26.4] |
phosphodiesterase I activity | molecular function | Catalysis of the sequential hydrolytic removal of 5'-nucleotides from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides. [EC:3.1.4.1] |
uracil DNA N-glycosylase activity | molecular function | Catalysis of the cleavage of the N-C1' glycosidic bond between the damaged DNA base and the deoxyribose sugar, releasing a free base and leaving an apyrimidinic (AP) site. Enzymes with this activity recognize and remove uracil bases in DNA that result from the deamination of cytosine or the misincorporation of dUTP opposite an adenine. [GOC:elh, GOC:pr, PMID:9224623] |
protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
phosphoric diester hydrolase activity | molecular function | Catalysis of the hydrolysis of a phosphodiester to give a phosphomonoester and a free hydroxyl group. [EC:3.1.4.-] |
3'-5'-DNA exonuclease activity | molecular function | Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of a DNA molecule. [GOC:mah] |
double-stranded DNA exodeoxyribonuclease activity | molecular function | Catalysis of the sequential cleavage of mononucleotides from a free 5' or 3' terminus of a double-stranded DNA molecule. [GOC:mah] |
3'-5' exonuclease activity | molecular function | Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end. [GOC:ai] |
oxidoreductase activity | molecular function | Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. [GOC:go_curators] |
site-specific endodeoxyribonuclease activity, specific for altered base | molecular function | Catalysis of the hydrolysis of ester linkages at specific sites within a deoxyribonucleic acid molecule by creating internal breaks. [GOC:jl] |
chromatin DNA binding | molecular function | Binding to DNA that is assembled into chromatin. [GOC:mah] |
metal ion binding | molecular function | Binding to a metal ion. [GOC:ai] |
class II DNA-(apurinic or apyrimidinic site) endonuclease activity | molecular function | Catalysis of the hydrolysis of ester linkages immediately 5' to an apurinic/apyrimidinic (AP; also called abasic) site within a deoxyribonucleic acid molecule by creating internal breaks, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. [PMID:19401441] |
phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands | molecular function | Catalysis of the hydrolytic removal of phosphoglycolate from the 3'-terminus of a 3'-phosphoglycolate-terminated DNA strand. [GOC:pde, GOC:rb, PMID:11238902] |
DNA-(abasic site) binding | molecular function | Binding to a DNA site that has neither a purine nor a pyrimidine base. Apurinic sites can form spontaneously or when DNA glycosylase removes a damaged base. [PMID:23245849] |
double-stranded DNA 3'-5' DNA exonuclease activity | molecular function | Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of a double-stranded DNA molecule. [GOC:mah, PMID:22562358] |
Located In
This protein is located in 11 target(s):
Target | Category | Definition |
chromosome, telomeric region | cellular component | The end of a linear chromosome, required for the integrity and maintenance of the end. A chromosome telomere usually includes a region of telomerase-encoded repeats the length of which rarely exceeds 20 bp each and that permits the formation of a telomeric loop (T-loop). The telomeric repeat region is usually preceded by a sub-telomeric region that is gene-poor but rich in repetitive elements. Some telomeres only consist of the latter part (for eg. D. melanogaster telomeres). [GOC:elh] |
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] |
nucleolus | cellular component | A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. [ISBN:0198506732] |
cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
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] |
endoplasmic reticulum | cellular component | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). [ISBN:0198506732] |
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] |
ribosome | cellular component | An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins. [ISBN:0198506732] |
nuclear speck | cellular component | A 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/] |
perinuclear region of cytoplasm | cellular component | Cytoplasm situated near, or occurring around, the nucleus. [GOC:jid] |
Active In
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] |
Involved In
This protein is involved in 13 target(s):
Target | Category | Definition |
telomere maintenance | biological process | Any process that contributes to the maintenance of proper telomeric length and structure by affecting and monitoring the activity of telomeric proteins, the length of telomeric DNA and the replication and repair of the DNA. These processes includes those that shorten, lengthen, replicate and repair the telomeric DNA sequences. [GOC:BHF, GOC:BHF_telomere, GOC:elh, GOC:rl, PMID:11092831] |
DNA repair | biological process | The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. [PMID:11563486] |
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] |
DNA catabolic process | biological process | The cellular DNA metabolic process resulting in the breakdown of DNA, deoxyribonucleic acid, one of the two main types of nucleic acid, consisting of a long unbranched macromolecule formed from one or two strands of linked deoxyribonucleotides, the 3'-phosphate group of each constituent deoxyribonucleotide being joined in 3',5'-phosphodiester linkage to the 5'-hydroxyl group of the deoxyribose moiety of the next one. [GOC:go_curators, ISBN:0198506732] |
DNA recombination | biological process | Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction. [ISBN:0198506732] |
regulation of apoptotic process | biological process | Any process that modulates the occurrence or rate of cell death by apoptotic process. [GOC:jl, GOC:mtg_apoptosis] |
regulation of mRNA stability | biological process | Any process that modulates the propensity of mRNA molecules to degradation. Includes processes that both stabilize and destabilize mRNAs. [GOC:jl] |
positive regulation of gene expression via chromosomal CpG island demethylation | biological process | An 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] |
cell redox homeostasis | biological process | Any process that maintains the redox environment of a cell or compartment within a cell. [GOC:ai, GOC:dph, GOC:tb] |
negative regulation of DNA-templated transcription | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription. [GOC:go_curators, GOC:txnOH] |
positive regulation of transcription by RNA polymerase II | biological process | Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter. [GOC:go_curators, GOC:txnOH] |
telomere maintenance via base-excision repair | biological process | A telomere maintenance process that occurs by base-excision repair of telomeric DNA in response to DNA damage. Telomeric sequences are particularly susceptible to oxidative DNA damage, due to their G-rich nature. [GOC:BHF, GOC:BHF_telomere, GOC:jbu, PMID:24703901] |