A DNA excision repair protein ERCC-5 that is encoded in the genome of human. [PRO:DNx]
EC 3.1.-.-;
DNA excision repair protein ERCC-5;
Xeroderma pigmentosum group G-complementing protein
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 2 (100.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| 3-hydroxy-quinazoline-2,4-dione | Homo sapiens (human) | IC50 | 0.0002 | 1 | 1 |
| 4-phenyl-4-oxo-2-hydroxybuten-2-oic acid | Homo sapiens (human) | IC50 | 75.4000 | 1 | 1 |
This protein enables 12 target(s):
| Target | Category | Definition |
|---|---|---|
| bubble DNA binding | molecular function | Binding to DNA segment that contains a bubble. A bubble occurs when DNA contains a region of unpaired, single-stranded DNA flanked on both sides by regions of paired, double-stranded DNA. [GOC:elh, GOC:vw, PMID:16781730] |
| RNA polymerase II complex binding | molecular function | Binding to an RNA polymerase II core enzyme, a multisubunit eukaryotic nuclear RNA polymerase typically composed of twelve subunits. [GOC:txnOH] |
| 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] |
| single-stranded DNA binding | molecular function | Binding to single-stranded DNA. [GOC:elh, GOC:vw, PMID:22976174] |
| 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] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| enzyme activator activity | molecular function | Binds to and increases the activity of an enzyme. [GOC:dph, GOC:mah, GOC:tb] |
| protein homodimerization activity | molecular function | Binding to an identical protein to form a homodimer. [GOC:jl] |
| protein-containing complex binding | molecular function | Binding to a macromolecular complex. [GOC:jl] |
| metal ion binding | molecular function | Binding to a metal ion. [GOC:ai] |
This protein is located in 2 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] |
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 part of 3 target(s):
| Target | Category | Definition |
|---|---|---|
| DNA replication factor A complex | cellular component | A conserved heterotrimeric complex that binds nonspecifically to single-stranded DNA and is required for multiple processes in eukaryotic DNA metabolism, including DNA replication, DNA repair, and recombination. In all eukaryotic organisms examined the complex is composed of subunits of approximately 70, 30, and 14 kDa. [PMID:9242902] |
| nucleotide-excision repair complex | cellular component | Any complex formed of proteins that act in nucleotide-excision repair. [PMID:10915862] |
| protein-containing complex | cellular component | A 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] |
This protein is involved in 7 target(s):
| Target | Category | Definition |
|---|---|---|
| double-strand break repair via homologous recombination | biological process | The error-free repair of a double-strand break in DNA in which the broken DNA molecule is repaired using homologous sequences. A strand in the broken DNA searches for a homologous region in an intact chromosome to serve as the template for DNA synthesis. The restoration of two intact DNA molecules results in the exchange, reciprocal or nonreciprocal, of genetic material between the intact DNA molecule and the broken DNA molecule. [GOC:elh, PMID:10357855] |
| transcription-coupled nucleotide-excision repair | biological process | The nucleotide-excision repair process that carries out preferential repair of DNA lesions on the actively transcribed strand of the DNA duplex. In addition, the transcription-coupled nucleotide-excision repair pathway is required for the recognition and repair of a small subset of lesions that are not recognized by the global genome nucleotide excision repair pathway. [PMID:10197977, PMID:11900249] |
| 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] |
| response to UV | 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 an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers. [GOC:hb] |
| response to UV-C | 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 a UV-C radiation stimulus. UV-C radiation (UV-C light) spans the wavelengths 100 to 280 nm. [GOC:tb] |
| negative regulation of apoptotic process | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. [GOC:jl, GOC:mtg_apoptosis] |