An a disintegrin and metalloproteinase with thrombospondin motifs 5 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9UNA0]
ADAM-TS 5;
ADAM-TS5;
ADAMTS-5;
EC 3.4.24.-;
A disintegrin and metalloproteinase with thrombospondin motifs 11;
ADAM-TS 11;
ADAMTS-11;
ADMP-2;
Aggrecanase-2
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (60.00) | 29.6817 |
| 2010's | 2 (40.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| marimastat | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| ilomastat | Homo sapiens (human) | IC50 | 0.5000 | 1 | 1 |
| 5'-(4-methylphenyl)-2-spiro[1H-indole-3,2'-3H-1,3,4-thiadiazole]one | Homo sapiens (human) | IC50 | 3.7000 | 2 | 2 |
| bms-566394 | Homo sapiens (human) | Ki | 1.4500 | 2 | 2 |
This protein enables 10 target(s):
| Target | Category | Definition |
|---|---|---|
| endopeptidase activity | molecular function | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. [http://merops.sanger.ac.uk/about/glossary.htm#ENDOPEPTIDASE] |
| metalloendopeptidase activity | molecular function | Catalysis of the hydrolysis of internal, alpha-peptide bonds in 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#CATTYPE, https://www.ebi.ac.uk/merops/about/glossary.shtml#ENDOPEPTIDASE] |
| integrin binding | molecular function | Binding to an integrin. [GOC:ceb] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| heparin binding | molecular function | Binding to heparin, a member of a group of glycosaminoglycans found mainly as an intracellular component of mast cells and which consist predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues. [GOC:jl, ISBN:0198506732] |
| 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] |
| metallopeptidase activity | molecular function | Catalysis of the hydrolysis of peptide bonds 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#CATTYPE] |
| zinc ion binding | molecular function | Binding to a zinc ion (Zn). [GOC:ai] |
| identical protein binding | molecular function | Binding to an identical protein or proteins. [GOC:jl] |
| extracellular matrix binding | molecular function | Binding to a component of the extracellular matrix. [GOC:ai] |
This protein is located in 4 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] |
| endoplasmic reticulum lumen | cellular component | The volume enclosed by the membranes of the endoplasmic reticulum. [ISBN:0198547684] |
| 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] |
This protein is active in 1 target(s):
| Target | Category | Definition |
|---|---|---|
| extracellular matrix | cellular component | A structure lying external to one or more cells, which provides structural support, biochemical or biomechanical cues for cells or tissues. [GOC:BHF, GOC:mah, GOC:rph, NIF_Subcellular:nlx_subcell_20090513, PMID:21123617, PMID:28089324] |
This protein is involved in 9 target(s):
| Target | Category | Definition |
|---|---|---|
| aortic valve morphogenesis | biological process | The process in which the structure of the aortic valve is generated and organized. [GOC:mtg_heart] |
| pulmonary valve morphogenesis | biological process | The process in which the structure of the pulmonary valve is generated and organized. [GOC:mtg_heart] |
| endocardial cushion morphogenesis | biological process | The process in which the anatomical structure of the endocardial cushion is generated and organized. The endocardial cushion is a specialized region of mesenchymal cells that will give rise to the heart septa and valves. [GOC:mtg_heart] |
| proteolysis | biological process | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. [GOC:bf, GOC:mah] |
| myoblast fusion | biological process | A process in which non-proliferating myoblasts fuse to existing fibers or to myotubes to form new fibers. A myoblast is a mononucleate cell type that, by fusion with other myoblasts, gives rise to the myotubes that eventually develop into skeletal muscle fibers. [CL:0000056, GOC:mtg_muscle] |
| extracellular matrix disassembly | biological process | A process that results in the breakdown of the extracellular matrix. [GOC:jid] |
| defense response to bacterium | biological process | Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism. [GOC:jl] |
| negative regulation of cold-induced thermogenesis | biological process | Any process that stops, prevents, or reduces the rate of cold-induced thermogenesis. [PMID:27876809] |
| extracellular matrix organization | biological process | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an extracellular matrix. [GOC:mah] |