A DNA repair endonuclease XPF that is encoded in the genome of human. [PRO:DNx]
EC 3.1.-.-;
DNA excision repair protein ERCC-4;
DNA repair protein complementing XP-F cells;
Xeroderma pigmentosum group F-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 | 0 (0.00) | 29.6817 |
| 2010's | 1 (100.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| n-hydroxynaphthalimide | Homo sapiens (human) | IC50 | 30.0000 | 1 | 1 |
| 3-hydroxy-quinazoline-2,4-dione | Homo sapiens (human) | IC50 | 18.1000 | 1 | 1 |
This protein enables 8 target(s):
| Target | Category | Definition |
|---|---|---|
| TFIID-class transcription factor complex binding | molecular function | Binding to a general RNA polymerase II transcription factor belonging to the TFIID complex, one of the factors involved in formation of the preinitiation complex (PIC) by RNA polymerase II. [GOC:krc, PMID:16858867] |
| damaged DNA binding | molecular function | Binding to damaged DNA. [GOC:jl] |
| single-stranded DNA binding | molecular function | Binding to single-stranded DNA. [GOC:elh, GOC:vw, PMID:22976174] |
| 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] |
| identical protein binding | molecular function | Binding to an identical protein or proteins. [GOC:jl] |
| promoter-specific chromatin binding | molecular function | Binding to a section of chromatin that is associated with gene promoter sequences of DNA. [PMID:19948729] |
| single-stranded DNA endodeoxyribonuclease activity | molecular function | Catalysis of the hydrolysis of ester linkages within a single-stranded deoxyribonucleic acid molecule by creating internal breaks. [GOC:mah] |
This protein is located in 3 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] |
This protein is part of 3 target(s):
| Target | Category | Definition |
|---|---|---|
| ERCC4-ERCC1 complex | cellular component | A heterodimeric nucleotide-excision repair complex that has endonuclease activity specific for bubble structures characteristic of certain DNA lesions. The subunits are known as XPF/ERCC4 and ERCC1 in mammals, and Rad1p and Rad10p in S. cerevisiae. [PMID:14734547] |
| nucleotide-excision repair complex | cellular component | Any complex formed of proteins that act in nucleotide-excision repair. [PMID:10915862] |
| nucleotide-excision repair factor 1 complex | cellular component | One of several protein complexes involved in nucleotide-excision repair; possesses DNA damage recognition and endodeoxynuclease activities. In S. cerevisiae, it is composed of Rad1p, Rad10p, and Rad14p; in human the subunits are ERCC4/XPF, ERCC1 and XPA, respectively. [PMID:10915862] |
This protein is involved in 16 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] |
| 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] |
| 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] |
| 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] |
| double-strand break repair via nonhomologous end joining | biological process | The repair of a double-strand break in DNA in which the two broken ends are rejoined with little or no sequence complementarity. Information at the DNA ends may be lost due to the modification of broken DNA ends. This term covers instances of separate pathways, called classical (or canonical) and alternative nonhomologous end joining (C-NHEJ and A-NHEJ). These in turn may further branch into sub-pathways, but evidence is still unclear. [GOC:rph, PMID:10827453, PMID:24837021] |
| 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] |
| UV protection | biological process | Any process in which an organism or cell protects itself from ultraviolet radiation (UV), which may also result in resistance to repeated exposure to UV. [GOC:jl, GOC:ml] |
| regulation of autophagy | biological process | Any process that modulates the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. [GOC:dph, GOC:tb] |
| negative regulation of telomere maintenance | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of a process that affects and monitors the activity of telomeric proteins and the length of telomeric DNA. [GOC:mah] |
| cellular response to UV | biological process | Any 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 an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers. [GOC:mah] |
| telomeric DNA-containing double minutes formation | biological process | A telomere maintenance process that results in the formation of small fragments of circular extrachromosomal DNA elements which contain telomeric DNA. It is speculated that telomeric DNA-containing double minutes are formed through a recombination event between the telomere and chromosome-internal TTAGGG-like sequences. Telomeric DNA-containing double minutes appear as two closely positioned dots in metaphase. [GOC:BHF, GOC:BHF_telomere, GOC:nc, PMID:14690602, PMID:2397458] |
| nucleotide-excision repair involved in interstrand cross-link repair | biological process | Any nucleotide-excision repair that is involved in interstrand cross-link repair. [GOC:TermGenie, PMID:22064477] |
| negative regulation of telomere maintenance via telomere lengthening | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of telomere maintenance via telomere lengthening. [GO_REF:0000058, GOC:BHF, GOC:BHF_telomere, GOC:nc, GOC:TermGenie, PMID:23959892] |
| negative regulation of protection from non-homologous end joining at telomere | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of protection from non-homologous end joining at telomere. [GO_REF:0000058, GOC:BHF, GOC:BHF_telomere, GOC:nc, GOC:TermGenie, PMID:14690602] |
| negative regulation of double-stranded telomeric DNA binding | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of double-stranded telomeric DNA binding. [GO_REF:0000059, GOC:BHF, GOC:BHF_telomere, GOC:nc, GOC:TermGenie, PMID:18812185] |
| resolution of meiotic recombination intermediates | biological process | The cleavage and rejoining of intermediates, such as Holliday junctions, formed during meiotic recombination to produce two intact molecules in which genetic material has been exchanged. [GOC:elh, PMID:11733053] |