Page last updated: 2024-08-07 23:36:24
Bloom syndrome protein
A RecQ-like DNA helicase BLM that is encoded in the genome of human. [PRO:DNx, UniProtKB:P54132]
Synonyms
EC 3.6.4.12;
DNA helicase, RecQ-like type 2;
RecQ2;
RecQ protein-like 3
Research
Bioassay Publications (3)
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 | 3 (100.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Compounds (2)
Drugs with Inhibition Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
---|---|---|---|---|---|
1-(3,4-dichlorophenyl)-3-(5-pyridin-4-yl-1,3,4-thiadiazol-2-yl)urea | Homo sapiens (human) | IC50 | 1.4000 | 1 | 1 |
1-[4-fluoro-3-(trifluoromethyl)phenyl]-3-(5-pyridin-4-yl-1,3,4-thiadiazol-2-yl)urea | Homo sapiens (human) | IC50 | 18.3540 | 5 | 5 |
Drugs with Other Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
---|---|---|---|---|---|
1-[4-fluoro-3-(trifluoromethyl)phenyl]-3-(5-pyridin-4-yl-1,3,4-thiadiazol-2-yl)urea | Homo sapiens (human) | EC | 50.0000 | 1 | 1 |
Enables
This protein enables 25 target(s):
Target | Category | Definition |
---|---|---|
four-way junction DNA binding | molecular function | Binding to a DNA segment containing four-way junctions, also known as Holliday junctions, a structure where two DNA double strands are held together by reciprocal exchange of two of the four strands, one strand each from the two original helices. [GOC:krc, ISBN:0815332181, PMID:15563464] |
Y-form DNA binding | molecular function | Binding to a DNA segment shaped like a Y. This shape occurs when DNA contains a region of paired double-stranded DNA on one end and a region of unpaired DNA strands on the opposite end. [GOC:elh, PMID:16781730] |
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] |
p53 binding | molecular function | Binding to one of the p53 family of proteins. [GOC:hjd] |
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] |
DNA helicase activity | molecular function | Unwinding of a DNA helix, driven by ATP hydrolysis. [GOC:jl] |
single-stranded DNA binding | molecular function | Binding to single-stranded DNA. [GOC:elh, GOC:vw, PMID:22976174] |
helicase activity | molecular function | Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the unwinding of a DNA or RNA helix. [GOC:jl] |
protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
ATP binding | molecular function | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. [ISBN:0198506732] |
ATP-dependent activity, acting on DNA | molecular function | Catalytic activity that acts to modify DNA, driven by ATP hydrolysis. [GOC:pdt] |
zinc ion binding | molecular function | Binding to a zinc ion (Zn). [GOC:ai] |
four-way junction helicase activity | molecular function | Unwinding a DNA helix of DNA containing four-way junctions, including Holliday junctions, driven by ATP hydrolysis. [GOC:al, PMID:22723423, PMID:9442895] |
isomerase activity | molecular function | Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5. [ISBN:0198506732] |
ATP hydrolysis activity | molecular function | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. [RHEA:13065] |
identical protein binding | molecular function | Binding to an identical protein or proteins. [GOC:jl] |
protein homodimerization activity | molecular function | Binding to an identical protein to form a homodimer. [GOC:jl] |
3'-5' DNA helicase activity | molecular function | Unwinding a DNA helix in the direction 5' to 3', driven by ATP hydrolysis. [EC:5.6.2.4, GOC:jl] |
G-quadruplex DNA binding | molecular function | Binding to G-quadruplex DNA structures, in which groups of four guanines adopt a flat, cyclic Hoogsteen hydrogen-bonding arrangement known as a guanine tetrad. The stacking of guanine tetrads results in G-quadruplex DNA structures. G-quadruplex DNA can form under physiological conditions from some G-rich sequences, such as those found in telomeres, immunoglobulin switch regions, gene promoters, fragile X repeats, and the dimerization domain in the human immunodeficiency virus (HIV) genome. [PMID:16142245, PMID:9512530] |
forked DNA-dependent helicase activity | molecular function | Unwinding a DNA helix containing forked DNA, driven by ATP hydrolysis. [GOC:dph, PMID:26277776] |
telomeric D-loop binding | molecular function | Binding to a telomeric D-loop. A telomeric D-loop is a three-stranded DNA displacement loop that forms at the site where the telomeric 3' single-stranded DNA overhang (formed of the repeat sequence TTAGGG in mammals) is tucked back inside the double-stranded component of telomeric DNA molecule, thus forming a t-loop or telomeric-loop and protecting the chromosome terminus. [GOC:BHF, GOC:BHF_telomere, GOC:nc, PMID:19734539] |
telomeric G-quadruplex DNA binding | molecular function | Binding to telomeric G-quadruplex DNA structures, in which groups of four guanines adopt a flat, cyclic Hoogsteen hydrogen-bonding arrangement known as a guanine tetrad. The stacking of guanine tetrads results in G-quadruplex DNA structures in telomeres. [GOC:BHF, GOC:BHF_telomere, GOC:nc, PMID:16142245, PMID:9512530] |
molecular function activator activity | molecular function | A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target. [GOC:curators] |
8-hydroxy-2'-deoxyguanosine DNA binding | molecular function | Binding to 8-hydroxy-2'-deoxyguanosine an oxidized purine residue found in damaged DNA. [GO_REF:0000067, GOC:BHF, GOC:BHF_telomere, GOC:nc, GOC:TermGenie, PMID:19734539] |
DNA/DNA annealing activity | molecular function | An activity that faciliates the formation of a complementary double-stranded DNA molecule. [PMID:22888405, PMID:25520186] |
Located In
This protein is located in 9 target(s):
Target | Category | Definition |
---|---|---|
nuclear chromosome | cellular component | A chromosome that encodes the nuclear genome and is found in the nucleus of a eukaryotic cell during the cell cycle phases when the nucleus is intact. [GOC:dph, GOC:mah] |
lateral element | cellular component | A proteinaceous core found between sister chromatids during meiotic prophase. [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] |
replication fork | cellular component | The Y-shaped region of a replicating DNA molecule, resulting from the separation of the DNA strands and in which the synthesis of new strands takes place. Also includes associated protein complexes. [GOC:mah, ISBN:0198547684] |
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] |
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] |
nuclear matrix | cellular component | The dense fibrillar network lying on the inner side of the nuclear membrane. [ISBN:0582227089] |
PML body | cellular component | A class of nuclear body; they react against SP100 auto-antibodies (PML, promyelocytic leukemia); cells typically contain 10-30 PML bodies per nucleus; alterations in the localization of PML bodies occurs after viral infection. [GOC:ma, PMID:10944585] |
Active In
This protein is active in 3 target(s):
Target | Category | Definition |
---|---|---|
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] |
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] |
Part Of
This protein is part of 2 target(s):
Target | Category | Definition |
---|---|---|
RecQ family helicase-topoisomerase III complex | cellular component | A complex containing a RecQ family helicase and a topoisomerase III homologue (a member of the topoisomerase type IA subfamily); may also include one or more additional proteins; conserved from E. coli to human. [GOC:bhm, GOC:krc, PMID:15889139] |
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] |
Involved In
This protein is involved in 27 target(s):
Target | Category | Definition |
---|---|---|
regulation of cyclin-dependent protein serine/threonine kinase activity | biological process | Any process that modulates the frequency, rate or extent of cyclin-dependent protein serine/threonine kinase activity. [GOC:go_curators, GOC:pr] |
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 double-strand break processing | biological process | The 5' to 3' exonucleolytic resection of the DNA at the site of the break to form a 3' single-strand DNA overhang. [PMID:10357855] |
DNA replication | biological process | The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA. [GOC:mah] |
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] |
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] |
DNA damage response | 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 a stimulus indicating damage to its DNA from environmental insults or errors during metabolism. [GOC:go_curators] |
mitotic G2 DNA damage checkpoint signaling | biological process | A mitotic cell cycle checkpoint that detects and negatively regulates progression through the G2/M transition of the cell cycle in response to DNA damage. [GOC:mtg_cell_cycle, PMID:16299494] |
response to X-ray | 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 X-ray radiation. An X-ray is a form of electromagnetic radiation with a wavelength in the range of 10 nanometers to 100 picometers (corresponding to frequencies in the range 30 PHz to 3 EHz). [GOC:sm, Wikipedia:X-ray] |
replication fork processing | biological process | The process in which a DNA replication fork that has stalled is restored to a functional state and replication is restarted. The stalling may be due to DNA damage, DNA secondary structure, bound proteins, dNTP shortage, or other causes. [GOC:vw, PMID:11459955, PMID:15367656, PMID:17660542] |
telomere maintenance via semi-conservative replication | biological process | The process in which telomeric DNA is synthesized semi-conservatively by the conventional replication machinery and telomeric accessory factors as part of cell cycle DNA replication. [GOC:BHF, GOC:BHF_telomere, GOC:rl, GOC:vw, PMID:16598261] |
DNA duplex unwinding | biological process | The process in which interchain hydrogen bonds between two strands of DNA are broken or 'melted', generating a region of unpaired single strands. [GOC:isa_complete, GOC:mah] |
G-quadruplex DNA unwinding | biological process | The process by which G-quadruplex (also known as G4) DNA, which is a four-stranded DNA structure held together by guanine base pairing, is unwound or 'melted'. [GOC:jl, GOC:se, PMID:23657261] |
positive regulation of DNA-templated transcription | biological process | Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription. [GOC:go_curators, GOC:txnOH] |
negative regulation of DNA recombination | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of DNA recombination. [GOC:go_curators] |
protein complex oligomerization | biological process | The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers; protein oligomers may be composed of different or identical monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer. [GOC:ai, PMID:18293929] |
protein homooligomerization | biological process | The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer. [GOC:ai] |
negative regulation of cell division | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of cell division. [GOC:ai] |
telomeric D-loop disassembly | biological process | A telomere loop disassembly process that results in the disassembly of telomeric D-loops. A telomeric D-loop is a three-stranded DNA displacement loop that forms at the site where the telomeric 3' single-stranded DNA overhang (formed of the repeat sequence TTAGGG in mammals) is tucked back inside the double-stranded component of telomeric DNA molecule, thus forming a t-loop or telomeric-loop and protecting the chromosome terminus. [GOC:BHF, GOC:BHF_telomere, GOC:nc, PMID:10338204, PMID:24012755] |
resolution of DNA recombination intermediates | biological process | The cleavage and rejoining of intermediates, such as Holliday junctions, formed during DNA recombination to produce two intact molecules in which genetic material has been exchanged. [GOC:elh, GOC:mah, GOC:vw] |
cellular response to ionizing radiation | 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 a ionizing radiation stimulus. Ionizing radiation is radiation with sufficient energy to remove electrons from atoms and may arise from spontaneous decay of unstable isotopes, resulting in alpha and beta particles and gamma rays. Ionizing radiation also includes X-rays. [GOC:mah] |
cellular response to hydroxyurea | 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 a hydroxyurea stimulus. [GOC:mah] |
cellular response to camptothecin | 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 a camptothecin stimulus. [GOC:mah] |
regulation of DNA-templated DNA replication | biological process | Any process that modulates the rate, frequency, or extent of DNA-templated DNA replication, the process in which new strands of DNA are synthesized. [GOC:dph, GOC:tb] |
t-circle formation | biological process | A telomere maintenance process that results in the formation of a telomeric circle, or t-circle. A t-circle is an extrachromosomal duplex or single-stranded circular DNA molecule composed of t-arrays. T-circles are involved in the control of telomere length via alternative-lengthening of telomeres (ALT) pathway and telomere rapid deletion (TRD). [GOC:BHF, GOC:BHF_telomere, GOC:nc, PMID:19214183, PMID:19581589, PMID:19809492, PMID:19858100] |
DNA unwinding involved in DNA replication | biological process | The process in which interchain hydrogen bonds between two strands of DNA are broken or 'melted', generating unpaired template strands for DNA replication. [ISBN:071673706X, ISBN:0815316194] |
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] |