A cathepsin K that is encoded in the genome of human. [PRO:WCB, UniProtKB:P43235]
EC 3.4.22.38;
Cathepsin O;
Cathepsin O2;
Cathepsin X
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 17 (53.13) | 29.6817 |
| 2010's | 13 (40.63) | 24.3611 |
| 2020's | 2 (6.25) | 2.80 |
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| tryptamine | Homo sapiens (human) | IC50 | 15.0000 | 1 | 1 |
| leupeptin | Homo sapiens (human) | Ki | 0.0240 | 1 | 1 |
| calpeptin | Homo sapiens (human) | IC50 | 0.0001 | 2 | 2 |
| Pyrrolidine-1-carbonitrile | Homo sapiens (human) | IC50 | 2.2730 | 7 | 7 |
| Pyrrolidine-1-carbonitrile | Homo sapiens (human) | Ki | 2.1000 | 1 | 1 |
| nsc13345 | Homo sapiens (human) | IC50 | 80.0000 | 1 | 1 |
| benzyloxycarbonylleucyl-leucyl-leucine aldehyde | Homo sapiens (human) | Ki | 0.0014 | 1 | 1 |
| telaprevir | Homo sapiens (human) | IC50 | 0.6300 | 1 | 1 |
| relacatib | Homo sapiens (human) | IC50 | 0.0005 | 1 | 1 |
| relacatib | Homo sapiens (human) | Ki | 0.0029 | 3 | 8 |
| a-705253 | Homo sapiens (human) | Ki | 0.0018 | 1 | 1 |
| l 006235 | Homo sapiens (human) | IC50 | 0.0004 | 2 | 2 |
| l-873724 | Homo sapiens (human) | IC50 | 0.0002 | 7 | 7 |
| odanacatib | Homo sapiens (human) | IC50 | 0.0005 | 9 | 9 |
| odanacatib | Homo sapiens (human) | Ki | 0.0002 | 1 | 1 |
| balicatib | Homo sapiens (human) | IC50 | 0.0027 | 5 | 5 |
| balicatib | Homo sapiens (human) | Ki | 0.0014 | 1 | 1 |
| n-(3-amino-1-(cyclobutylmethyl)-2,3-dioxopropyl)-3-(2-((((1,1-dimethylethyl)amino)carbonyl)amino)-3,3-dimethyl-1-oxobutyl)-6,6-dimethyl-3-azabicyclo(3.1.0)hexan-2-carboxamide | Homo sapiens (human) | IC50 | 0.0400 | 1 | 1 |
| PF-00835231 | Homo sapiens (human) | IC50 | 0.4837 | 1 | 3 |
| mk-7009 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| vel-0230 | Homo sapiens (human) | IC50 | 0.0345 | 1 | 1 |
| 6-(3,5-difluoroanilino)-9-ethyl-2-purinecarbonitrile | Homo sapiens (human) | IC50 | 0.0234 | 1 | 1 |
| 9-(3,5-difluorophenyl)-6-(ethylamino)-2-purinecarbonitrile | Homo sapiens (human) | IC50 | 0.0501 | 1 | 1 |
| grassystatin a | Homo sapiens (human) | IC50 | 10.0000 | 2 | 2 |
| N-[(2S)-3-cyclohexyl-1-oxo-1-({(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}amino)propan-2-yl]-1H-indole-2-carboxamide | Homo sapiens (human) | IC50 | 0.0041 | 1 | 2 |
This protein enables 8 target(s):
| Target | Category | Definition |
|---|---|---|
| fibronectin binding | molecular function | Binding to a fibronectin, a group of related adhesive glycoproteins of high molecular weight found on the surface of animal cells, connective tissue matrices, and in extracellular fluids. [GOC:hjd] |
| cysteine-type endopeptidase activity | molecular function | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile. [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE, https://www.ebi.ac.uk/merops/about/glossary.shtml#ENDOPEPTIDASE] |
| serine-type endopeptidase activity | molecular function | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| collagen binding | molecular function | Binding to collagen, a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%). [GOC:ai, ISBN:0198506732] |
| cysteine-type peptidase activity | molecular function | Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile. [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE] |
| proteoglycan binding | molecular function | Binding to a proteoglycan, any glycoprotein in which the carbohydrate units are glycosaminoglycans. [ISBN:0198506732] |
| cysteine-type endopeptidase activator activity involved in apoptotic process | molecular function | Binds to and increases the rate of proteolysis catalyzed by a cysteine-type endopeptidase involved in the apoptotic process. [GOC:mah, GOC:mtg_apoptosis] |
This protein is located in 9 target(s):
| Target | Category | Definition |
|---|---|---|
| extracellular region | cellular component | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators] |
| extracellular space | cellular component | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. [ISBN:0198547684] |
| nucleoplasm | cellular component | That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653] |
| lysosome | cellular component | A small lytic vacuole that has cell cycle-independent morphology found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions. [GOC:mah, ISBN:0198506732] |
| external side of plasma membrane | cellular component | The leaflet of the plasma membrane that faces away from the cytoplasm and any proteins embedded or anchored in it or attached to its surface. [GOC:dos, GOC:tb] |
| apical plasma membrane | cellular component | The region of the plasma membrane located at the apical end of the cell. [GOC:curators] |
| endolysosome lumen | cellular component | The volume enclosed by the membrane of an endolysosome. An endolysosome is a transient hybrid organelle formed by fusion of a late endosome with a lysosome. [GOC:pde] |
| lysosomal lumen | cellular component | The volume enclosed within the lysosomal membrane. [GOC:jl, PMID:15213228] |
| intracellular membrane-bounded organelle | cellular component | Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. [GOC:go_curators] |
This protein is active in 2 target(s):
| Target | Category | Definition |
|---|---|---|
| extracellular space | cellular component | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. [ISBN:0198547684] |
| lysosome | cellular component | A small lytic vacuole that has cell cycle-independent morphology found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions. [GOC:mah, ISBN:0198506732] |
This protein is involved in 20 target(s):
| Target | Category | Definition |
|---|---|---|
| mitophagy | biological process | The selective autophagy process in which a mitochondrion is degraded by macroautophagy. [PMID:15798367] |
| intramembranous ossification | biological process | Direct ossification that occurs within mesenchyme or an accumulation of relatively unspecialized cells. [ISBN:0878932437] |
| proteolysis | biological process | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. [GOC:bf, GOC:mah] |
| thyroid hormone generation | biological process | The formation of either of the compounds secreted by the thyroid gland, mainly thyroxine and triiodothyronine. This is achieved by the iodination and joining of tyrosine molecules to form the precursor thyroglobin, proteolysis of this precursor gives rise to the thyroid hormones. [GOC:jl, ISBN:0716720094] |
| apoptotic process | biological process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. [GOC:cjm, GOC:dhl, GOC:ecd, GOC:go_curators, GOC:mtg_apoptosis, GOC:tb, ISBN:0198506732, PMID:18846107, PMID:21494263] |
| response to organic cyclic compound | 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 organic cyclic compound stimulus. [GOC:ef] |
| extracellular matrix disassembly | biological process | A process that results in the breakdown of the extracellular matrix. [GOC:jid] |
| collagen catabolic process | biological process | The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells. [GOC:mah, ISBN:0815316194] |
| response to insulin | 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 insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms. [GOC:mah, ISBN:0198506732] |
| cellular response to zinc ion starvation | 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 deprivation of zinc ions. [GOC:mah] |
| bone resorption | biological process | The process in which specialized cells known as osteoclasts degrade the organic and inorganic portions of bone, and endocytose and transport the degradation products. [GOC:mah, PMID:10968780] |
| response to ethanol | 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 ethanol stimulus. [GOC:go_curators] |
| proteolysis involved in protein catabolic process | biological process | The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells. [GOC:ai, GOC:dph, GOC:tb] |
| negative regulation of cartilage development | biological process | Any process that decreases the rate, frequency, or extent of cartilage development, the process whose specific outcome is the progression of the cartilage over time, from its formation to the mature structure. Cartilage is a connective tissue dominated by extracellular matrix containing collagen type II and large amounts of proteoglycan, particularly chondroitin sulfate. [GOC:dph] |
| cellular response to tumor necrosis factor | 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 tumor necrosis factor stimulus. [GOC:mah] |
| cellular response to transforming growth factor beta stimulus | 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 transforming growth factor beta stimulus. [GOC:ecd, PMID:15451575] |
| mononuclear cell differentiation | biological process | The process in which a relatively unspecialized cell acquires the specialized features of a mononuclear cell. [CL:0000842, GO_REF:0000086, GOC:TermGenie, PMID:24759906] |
| positive regulation of apoptotic signaling pathway | biological process | Any process that activates or increases the frequency, rate or extent of apoptotic signaling pathway. [GOC:mtg_apoptosis] |
| positive regulation of peptidase activity | biological process | Any process that increases the frequency, rate or extent of peptidase activity, the hydrolysis of peptide bonds within proteins. [GOC:dph, GOC:tb] |
| immune response | biological process | Any immune system process that functions in the calibrated response of an organism to a potential internal or invasive threat. [GO_REF:0000022, GOC:add] |