A cytosol aminopeptidase that is encoded in the genome of human. [PRO:DNx, UniProtKB:P28838]
EC 3.4.11.1;
Cysteinylglycine-S-conjugate dipeptidase;
3.4.13.23;
Leucine aminopeptidase 3;
LAP-3;
Leucyl aminopeptidase;
Peptidase S;
Proline aminopeptidase;
3.4.11.5;
Prolyl aminopeptidase
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|---|---|
| pre-1990 | 3 (37.50) | 18.7374 |
| 1990's | 1 (12.50) | 18.2507 |
| 2000's | 2 (25.00) | 29.6817 |
| 2010's | 2 (25.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| isoamylamine | Homo sapiens (human) | Ki | 50,000.0000 | 1 | 1 |
| 1-aminomethylphosphonic acid | Homo sapiens (human) | Ki | 1,040.0000 | 1 | 1 |
| ubenimex | Homo sapiens (human) | IC50 | 11.2000 | 1 | 1 |
| ubenimex | Homo sapiens (human) | Ki | 0.0103 | 2 | 2 |
| 1-(aminoethyl)phosphonic acid | Homo sapiens (human) | Ki | 240.0000 | 1 | 1 |
| 1-amino-2-phenylethylphosphonic acid | Homo sapiens (human) | Ki | 0.4200 | 1 | 1 |
| jtp 4819 | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| amastatin | Homo sapiens (human) | Ki | 5.1125 | 4 | 4 |
| leucine phosphonic acid | Homo sapiens (human) | Ki | 0.2300 | 1 | 1 |
| apstatin | Homo sapiens (human) | IC50 | 0.3000 | 1 | 1 |
| ubenimex | Homo sapiens (human) | Ki | 20.0000 | 1 | 1 |
This protein enables 7 target(s):
| Target | Category | Definition |
|---|---|---|
| aminopeptidase activity | molecular function | Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain. [https://www.ebi.ac.uk/merops/about/glossary.shtml#AMINOPEPTIDASE, PMID:24157837] |
| carboxypeptidase activity | molecular function | Catalysis of the hydrolysis of a single C-terminal amino acid residue from a polypeptide chain. [https://www.ebi.ac.uk/merops/about/glossary.shtml#CARBOXYPEPTIDASE] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| metalloexopeptidase activity | molecular function | Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml] |
| manganese ion binding | molecular function | Binding to a manganese ion (Mn). [GOC:ai] |
| metalloaminopeptidase activity | molecular function | Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. [https://www.ebi.ac.uk/merops/about/glossary.shtml#AMINOPEPTIDASE] |
| 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] |
This protein is located in 4 target(s):
| Target | Category | Definition |
|---|---|---|
| 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] |
| trans-Golgi network | cellular component | The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination. [GOC:vw, ISBN:0815316194] |
| focal adhesion | cellular component | A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). [GOC:aruk, GOC:bc, ISBN:0124325653, ISBN:0815316208, PMID:10419689, PMID:12191915, PMID:15246682, PMID:1643657, PMID:16805308, PMID:19197329, PMID:23033047, PMID:26923917, PMID:28796323, PMID:8314002] |
| 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 1 target(s):
| Target | Category | Definition |
|---|---|---|
| cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
This protein is involved in 1 target(s):
| Target | Category | Definition |
|---|---|---|
| proteolysis | biological process | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. [GOC:bf, GOC:mah] |