Page last updated: 2024-08-07 15:42:58
Cathepsin D
A cathepsin D that is encoded in the genome of human. [PRO:DNx, UniProtKB:P07339]
Synonyms
EC 3.4.23.5
Research
Bioassay Publications (34)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (5.88) | 18.2507 |
| 2000's | 11 (32.35) | 29.6817 |
| 2010's | 13 (38.24) | 24.3611 |
| 2020's | 8 (23.53) | 2.80 |
Compounds (20)
Drugs with Inhibition Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| nafamostat | Homo sapiens (human) | IC50 | 1,000.0000 | 1 | 1 |
| 1,2-diphenylhydrazine | Homo sapiens (human) | IC50 | 1.7125 | 3 | 4 |
| amprenavir | Homo sapiens (human) | IC50 | 15.2000 | 1 | 1 |
| bila 2157 bs | Homo sapiens (human) | IC50 | 0.5500 | 1 | 1 |
| resveratrol | Homo sapiens (human) | IC50 | 138.0000 | 1 | 1 |
| om99-2 | Homo sapiens (human) | IC50 | 0.0042 | 2 | 3 |
| om99-2 | Homo sapiens (human) | Ki | 0.0016 | 1 | 1 |
| pl 100 | Homo sapiens (human) | IC50 | 50.0000 | 1 | 1 |
| benzyloxycarbonyl-phe-ala-fluormethylketone | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| pepstatin | Homo sapiens (human) | IC50 | 5.8953 | 18 | 18 |
| pepstatin | Homo sapiens (human) | Ki | 0.0000 | 1 | 1 |
| ca 074 | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| kni 10006 | Homo sapiens (human) | Ki | 0.0020 | 1 | 1 |
| balicatib | Homo sapiens (human) | Ki | 0.0013 | 1 | 1 |
| tasiamide b | Homo sapiens (human) | IC50 | 0.2510 | 1 | 1 |
| calpain inhibitor iii | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| PF-00835231 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| gsk188909 | Homo sapiens (human) | IC50 | 1.0978 | 3 | 5 |
| ly2811376 | Homo sapiens (human) | IC50 | 15.4667 | 3 | 3 |
| grassystatin a | Homo sapiens (human) | IC50 | 2.3046 | 7 | 7 |
| ly2886721 | Homo sapiens (human) | IC50 | 300.0000 | 2 | 2 |
| tipranavir | Homo sapiens (human) | Ki | 15.0000 | 1 | 1 |
Drugs with Other Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| pepstatin | Homo sapiens (human) | INH | 0.0001 | 1 | 1 |
| ly2811376 | Homo sapiens (human) | INH | 15.7000 | 1 | 1 |
Enables
This protein enables 5 target(s):
| Target | Category | Definition |
|---|---|---|
| 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] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| peptidase activity | molecular function | Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. [GOC:jl, ISBN:0815332181] |
| aspartic-type peptidase activity | molecular function | Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile. [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE] |
| aspartic-type endopeptidase activity | molecular function | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile. [ISBN:0198506732] |
Located In
This protein is located in 14 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] |
| 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] |
| lysosomal membrane | cellular component | The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm. [GOC:ai] |
| endosome membrane | cellular component | The lipid bilayer surrounding an endosome. [GOC:mah] |
| endosome lumen | cellular component | The volume enclosed by the membrane of an endosome. [GOC:mah] |
| specific granule lumen | cellular component | The volume enclosed by the membrane of a specific granule, a granule with a membranous, tubular internal structure, found primarily in mature neutrophil cells. Most are released into the extracellular fluid. Specific granules contain lactoferrin, lysozyme, vitamin B12 binding protein and elastase. [GOC:bf, PMID:7334549] |
| melanosome | cellular component | A tissue-specific, membrane-bounded cytoplasmic organelle within which melanin pigments are synthesized and stored. Melanosomes are synthesized in melanocyte cells. [GOC:jl, PMID:11584301] |
| lysosomal lumen | cellular component | The volume enclosed within the lysosomal membrane. [GOC:jl, PMID:15213228] |
| membrane raft | cellular component | Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions. [PMID:16645198, PMID:20044567] |
| collagen-containing extracellular matrix | cellular component | An extracellular matrix consisting mainly of proteins (especially collagen) and glycosaminoglycans (mostly as proteoglycans) that provides not only essential physical scaffolding for the cellular constituents but can also initiate crucial biochemical and biomechanical cues required for tissue morphogenesis, differentiation and homeostasis. The components are secreted by cells in the vicinity and form a sheet underlying or overlying cells such as endothelial and epithelial cells. [GOC:BHF, GOC:rph, PMID:21123617] |
| extracellular exosome | cellular component | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894] |
| tertiary granule lumen | cellular component | Any membrane-enclosed lumen that is part of a tertiary granule. [GO_REF:0000064, GOC:TermGenie, PMID:23650620] |
| ficolin-1-rich granule lumen | cellular component | Any membrane-enclosed lumen that is part of a ficolin-1-rich granule. [GO_REF:0000064, GOC:TermGenie, PMID:23650620] |
Involved In
This protein is involved in 9 target(s):
| Target | Category | Definition |
|---|---|---|
| autophagosome assembly | biological process | The formation of a double membrane-bounded structure, the autophagosome, that occurs when a specialized membrane sac, called the isolation membrane, starts to enclose a portion of the cytoplasm. [GOC:autophagy, PMID:9412464] |
| proteolysis | biological process | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. [GOC:bf, GOC:mah] |
| antigen processing and presentation of exogenous peptide antigen via MHC class II | biological process | The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class II protein complex. The peptide antigen is typically, but not always, processed from a whole protein. [GOC:add, ISBN:0781735149, PMID:15771591] |
| insulin receptor recycling | biological process | The process that results in the return of an insulin receptor to an active state at the plasma membrane. An active state is when the receptor is ready to receive an insulin signal. Internalized insulin receptors can be recycled to the plasma membrane or sorted to lysosomes for protein degradation. [GOC:bf, GOC:signaling, PMID:3907718] |
| lipoprotein catabolic process | biological process | The chemical reactions and pathways resulting in the breakdown of any conjugated, water-soluble protein in which the covalently attached nonprotein group consists of a lipid or lipids. [ISBN:0198506732] |
| positive regulation of apoptotic process | biological process | Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process. [GOC:jl, GOC:mtg_apoptosis] |
| positive regulation of cysteine-type endopeptidase activity involved in apoptotic process | biological process | Any process that activates or increases the activity of a cysteine-type endopeptidase involved in the apoptotic process. [GOC:jl, GOC:mtg_apoptosis] |
| regulation of establishment of protein localization | biological process | Any process that modulates the frequency, rate or extent of the directed movement of a protein to a specific location. [GOC:BHF, GOC:mah] |
| insulin catabolic process | biological process | The chemical reactions and pathways resulting in the breakdown of insulin. [GOC:TermGenie] |