Page last updated: 2024-08-07 23:48:13
Heat shock protein 75 kDa, mitochondrial
A heat shock protein 75 kDa, mitochondrial that is encoded in the genome of human. [PRO:DAN]
Synonyms
HSP 75;
TNFR-associated protein 1;
Tumor necrosis factor type 1 receptor-associated protein;
TRAP-1
Research
Bioassay Publications (13)
| 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 | 7 (53.85) | 24.3611 |
| 2020's | 6 (46.15) | 2.80 |
Compounds (11)
Drugs with Inhibition Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| adenosine diphosphate | Homo sapiens (human) | IC50 | 55.5940 | 1 | 1 |
| geldanamycin | Homo sapiens (human) | IC50 | 0.6610 | 1 | 1 |
| tanespimycin | Homo sapiens (human) | IC50 | 1.4960 | 1 | 1 |
| 9h-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-n-(1-methylethyl)- | Homo sapiens (human) | IC50 | 0.3108 | 6 | 6 |
| ec 144 | Homo sapiens (human) | Ki | 0.2550 | 1 | 1 |
| cnf 2024 | Homo sapiens (human) | IC50 | 0.3125 | 2 | 2 |
| cnf 2024 | Homo sapiens (human) | Ki | 0.0620 | 1 | 1 |
| snx 2112 | Homo sapiens (human) | IC50 | 0.7585 | 2 | 2 |
| snx 2112 | Homo sapiens (human) | Ki | 0.7910 | 1 | 1 |
| debio 0932 | Homo sapiens (human) | IC50 | 1.5860 | 1 | 1 |
| tas-116 | Homo sapiens (human) | Ki | 50.0000 | 2 | 2 |
| ver 52296 | Homo sapiens (human) | IC50 | 0.3577 | 3 | 3 |
| ver 52296 | Homo sapiens (human) | Ki | 0.0160 | 1 | 1 |
| sta 9090 | Homo sapiens (human) | IC50 | 0.0444 | 2 | 2 |
Drugs with Other Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| 9h-purine-9-propanamine, 6-amino-8-((6-iodo-1,3-benzodioxol-5-yl)thio)-n-(1-methylethyl)- | Homo sapiens (human) | Km | 1,052.1900 | 1 | 1 |
Enables
This protein enables 8 target(s):
| Target | Category | Definition |
|---|---|---|
| RNA binding | molecular function | Binding to an RNA molecule or a portion thereof. [GOC:jl, GOC:mah] |
| tumor necrosis factor receptor binding | molecular function | Binding to a tumor necrosis factor receptor. [GOC:ai] |
| 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 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] |
| protein kinase binding | molecular function | Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. [GOC:jl] |
| ATP-dependent protein folding chaperone | molecular function | Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. [PMID:27365453] |
| unfolded protein binding | molecular function | Binding to an unfolded protein. [GOC:ai] |
Located In
This protein is located in 7 target(s):
| Target | Category | Definition |
|---|---|---|
| nucleoplasm | cellular component | That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653] |
| 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] |
| mitochondrial inner membrane | cellular component | The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. [GOC:ai] |
| mitochondrial intermembrane space | cellular component | The region between the inner and outer lipid bilayers of the mitochondrial envelope. [GOC:mah] |
| mitochondrial matrix | cellular component | The 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] |
| membrane | cellular component | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194] |
| cell periphery | cellular component | The broad region around and including the plasma membrane of a cell, encompassing the cell cortex (inside the cell), the plasma membrane, and any external encapsulating structures. [GOC:pdt] |
Active In
This protein is active in 1 target(s):
| Target | Category | Definition |
|---|---|---|
| mitochondrial inner membrane | cellular component | The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. [GOC:ai] |
Involved In
This protein is involved in 6 target(s):
| Target | Category | Definition |
|---|---|---|
| translational attenuation | biological process | Translational attenuation is a regulatory mechanism analogous to ribosome-mediated transcriptional attenuation. The system requires the presence of a short ORF, called a leader peptide, encoded in the mRNA upstream of the ribosome-binding site and start codon of the gene whose translation is to be regulated. Certain conditions, such as presence of the antibiotic tetracycline in bacteria or amino acid starvation, may cause slowing or stalling of the ribosome translating the leader peptide. The stalled ribosome masks a region of the mRNA and affects which of two alternative mRNA folded structures will form, therefore controlling whether or not a ribosome will bind and initiate translation of the downstream gene. Translational attenuation is analogous to ribosome-mediated transcriptional attenuation, in which mRNA remodeling caused by ribosome stalling regulates transcriptional termination rather than translational initiation. [PMID:15694341, PMID:15805513] |
| chaperone-mediated protein folding | biological process | The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone. [GOC:dph, GOC:vw] |
| negative regulation of cellular respiration | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of cellular respiration. [GOC:TermGenie, GOC:yaf, PMID:23150719] |
| negative regulation of reactive oxygen species biosynthetic process | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of reactive oxygen species biosynthetic process. [GO_REF:0000058, GOC:bf, GOC:PARL, GOC:TermGenie, PMID:24252804] |
| negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of intrinsic apoptotic signaling pathway in response to hydrogen peroxide. [GO_REF:0000058, GOC:TermGenie, PMID:18681888] |
| protein folding | biological process | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. [GOC:go_curators, GOC:rb] |