A dipeptidyl peptidase 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P53634]
EC 3.4.14.1;
Cathepsin C;
Cathepsin J;
Dipeptidyl peptidase I;
DPP-I;
DPPI;
Dipeptidyl transferase
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (50.00) | 29.6817 |
| 2010's | 3 (50.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| Pyrrolidine-1-carbonitrile | Homo sapiens (human) | IC50 | 25.1189 | 1 | 1 |
| e 64 | Homo sapiens (human) | IC50 | 0.7700 | 1 | 1 |
| canertinib | Homo sapiens (human) | IC50 | 2.7000 | 1 | 1 |
| odanacatib | Homo sapiens (human) | IC50 | 0.0100 | 1 | 1 |
| bibw 2992 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| 6-(3,5-difluoroanilino)-9-ethyl-2-purinecarbonitrile | Homo sapiens (human) | IC50 | 0.0347 | 1 | 1 |
| 6-(3,5-difluoroanilino)-9-(2,2-difluoroethyl)-2-purinecarbonitrile | Homo sapiens (human) | IC50 | 6.9183 | 1 | 1 |
| 9-(3,5-difluorophenyl)-6-(ethylamino)-2-purinecarbonitrile | Homo sapiens (human) | IC50 | 0.5888 | 1 | 1 |
| grassystatin a | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| thiopental sodium | Homo sapiens (human) | IC50 | 2.1000 | 2 | 2 |
| osimertinib | Homo sapiens (human) | IC50 | 32.9000 | 1 | 1 |
This protein enables 10 target(s):
| Target | Category | Definition |
|---|---|---|
| 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] |
| 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] |
| dipeptidyl-peptidase activity | molecular function | Catalysis of the hydrolysis of N-terminal dipeptides from a polypeptide chain. [GOC:mb, https://www.ebi.ac.uk/merops/about/glossary.shtml#DIPEPTIDYL-PEPTIDASE] |
| peptidase activator activity involved in apoptotic process | molecular function | Binds to and increases the activity of a peptidase that is involved in the apoptotic process. [GOC:BHF, GOC:mah, GOC:mtg_apoptosis, GOC:rl] |
| phosphatase binding | molecular function | Binding to a phosphatase. [GOC:jl] |
| chloride ion binding | molecular function | Binding to a chloride ion (Cl-). [GOC:mah] |
| identical protein binding | molecular function | Binding to an identical protein or proteins. [GOC:jl] |
| protein-folding chaperone binding | molecular function | Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport. [PMID:10585443] |
| 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] |
This protein is located in 13 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] |
| endoplasmic reticulum lumen | cellular component | The volume enclosed by the membranes of the endoplasmic reticulum. [ISBN:0198547684] |
| centrosome | cellular component | A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle. [GOC:mah, ISBN:0198547684] |
| 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] |
| COPII-coated ER to Golgi transport vesicle | cellular component | A vesicle with a coat formed of the COPII coat complex proteins. The COPII coat complex is formed by the Sec23p/Sec24p and the Sec13p/Sec31p heterodimers. COPII-associated vesicles transport proteins from the rough endoplasmic reticulum to the Golgi apparatus (anterograde transport). [PMID:11252894, PMID:17499046, PMID:22160157, PMID:8004676, Wikipedia:COPII] |
| endoplasmic reticulum-Golgi intermediate compartment membrane | cellular component | The lipid bilayer surrounding any of the compartments of the endoplasmic reticulum (ER)-Golgi intermediate compartment system. [GOC:mah, GOC:pr, PMID:16723730] |
| azurophil granule lumen | cellular component | The volume enclosed by the membrane of an azurophil granule, a primary lysosomal granule found in neutrophil granulocytes that contains a wide range of hydrolytic enzymes and is released into the extracellular fluid. [GOC:bf, PMID:17152095] |
| 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] |
| 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] |
This protein is active in 2 target(s):
| Target | Category | Definition |
|---|---|---|
| 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] |
| 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] |
This protein is involved in 10 target(s):
| Target | Category | Definition |
|---|---|---|
| T cell mediated cytotoxicity | biological process | The directed killing of a target cell by a T cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors. [GOC:add, GOC:pr, ISBN:0781735149, PMID:11911826] |
| proteolysis | biological process | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. [GOC:bf, GOC:mah] |
| 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] |
| 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] |
| response to organic substance | 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 substance stimulus. [GOC:sm, PMID:23356676] |
| negative regulation of myelination | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of the formation of a myelin sheath around nerve axons. [GOC:mah] |
| positive regulation of proteolysis involved in protein catabolic process | biological process | Any process that activates or increases the frequency, rate or extent of proteolysis involved in protein catabolic process. [GO_REF:0000058, GOC:BHF, GOC:rl, GOC:TermGenie, PMID:18307834] |
| positive regulation of microglial cell activation | biological process | Any process that activates or increases the frequency, rate or extent of microglial cell activation. [GO_REF:0000058, GOC:BHF, GOC:nc, GOC:TermGenie, PMID:19100238] |
| 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] |
| 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] |