A matrix metalloproteinase-16 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P51512]
MMP-16;
EC 3.4.24.-;
MMP-X2;
Membrane-type matrix metalloproteinase 3;
MT-MMP 3;
MTMMP3;
Membrane-type-3 matrix metalloproteinase;
MT3-MMP;
MT3MMP
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 7 (87.50) | 29.6817 |
| 2010's | 1 (12.50) | 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 | 0.0080 | 2 | 2 |
| ik 682 | Homo sapiens (human) | Ki | 1.5990 | 2 | 2 |
| arp-100 | Homo sapiens (human) | IC50 | 0.9000 | 1 | 1 |
| N(2)-([biphenyl]-4-ylsulfonyl)-N-hydroxy-N(2)-isopropoxy-D-valinamide | Homo sapiens (human) | IC50 | 0.0510 | 1 | 1 |
| bms-566394 | Homo sapiens (human) | Ki | 10.0000 | 2 | 2 |
This protein enables 4 target(s):
| Target | Category | Definition |
|---|---|---|
| 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] |
| enzyme activator activity | molecular function | Binds to and increases the activity of an enzyme. [GOC:dph, GOC:mah, GOC:tb] |
| zinc ion binding | molecular function | Binding to a zinc ion (Zn). [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] |
This protein is located in 4 target(s):
| Target | Category | Definition |
|---|---|---|
| Golgi lumen | cellular component | The volume enclosed by the membranes of any cisterna or subcompartment of the Golgi apparatus, including the cis- and trans-Golgi networks. [GOC:mah] |
| plasma membrane | cellular component | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363] |
| cell surface | cellular component | The external part of the cell wall and/or plasma membrane. [GOC:jl, GOC:mtg_sensu, GOC:sm] |
| 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 active in 2 target(s):
| Target | Category | Definition |
|---|---|---|
| plasma membrane | cellular component | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363] |
| 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 9 target(s):
| Target | Category | Definition |
|---|---|---|
| endochondral ossification | biological process | Replacement ossification wherein bone tissue replaces cartilage. [GO_REF:0000034, 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] |
| protein processing | biological process | Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein. [GOC:curators, GOC:jl, GOC:jsg] |
| chondrocyte proliferation | biological process | The multiplication or reproduction of chondrocytes by cell division, resulting in the expansion of their population. A chondrocyte is a polymorphic cell that forms cartilage. [CL:0000138, GOC:yaf, PMID:21484705] |
| embryonic cranial skeleton morphogenesis | biological process | The process in which the anatomical structures of the cranial skeleton are generated and organized during the embryonic phase. [GOC:dsf, GOC:jid, PMID:16049113] |
| craniofacial suture morphogenesis | biological process | The process in which any suture between cranial and/or facial bones is generated and organized. [GOC:pr, GOC:sl, Wikipedia:Cranial_sutures, Wikipedia:Head_and_neck_anatomy#Musculoskeletal_system] |
| skeletal system development | biological process | The process whose specific outcome is the progression of the skeleton over time, from its formation to the mature structure. The skeleton is the bony framework of the body in vertebrates (endoskeleton) or the hard outer envelope of insects (exoskeleton or dermoskeleton). [GOC:dph, GOC:jid, GOC:tb] |
| 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] |
| 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] |