A coagulation factor XI that is encoded in the genome of human. [PRO:DNx, UniProtKB:P03951]
FXI;
EC 3.4.21.27;
Plasma thromboplastin antecedent;
PTA
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (30.00) | 29.6817 |
| 2010's | 7 (70.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| 5-(n,n-hexamethylene)amiloride | Homo sapiens (human) | IC50 | 50.0000 | 1 | 1 |
| amiloride | Homo sapiens (human) | IC50 | 50.0000 | 1 | 1 |
| benzamidine hydrochloride | Homo sapiens (human) | IC50 | 120.0000 | 1 | 1 |
| melagatran | Homo sapiens (human) | IC50 | 20.0000 | 1 | 1 |
| razaxaban | Homo sapiens (human) | Ki | 12.0000 | 1 | 1 |
| bms-262084 | Homo sapiens (human) | IC50 | 0.0028 | 2 | 2 |
| anabaenopeptin b | Homo sapiens (human) | IC50 | 24.0000 | 1 | 1 |
| grassystatin a | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| sulfated pentagalloylglucoside | Homo sapiens (human) | IC50 | 0.5510 | 1 | 1 |
This protein enables 4 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] |
| 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] |
| serine-type aminopeptidase activity | molecular function | Catalysis of the hydrolysis of a single N-terminal amino acid residue from 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). [https://www.ebi.ac.uk/merops/about/glossary.shtml#AMINOPEPTIDASE, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE] |
This protein is located in 5 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] |
| 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] |
| 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] |
| 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 involved in 3 target(s):
| Target | Category | Definition |
|---|---|---|
| blood coagulation | biological process | The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers. [PMID:30700128] |
| plasminogen activation | biological process | The process in which inactive plasminogen is processed to active plasmin. This process includes cleavage at an internal Arg-Val site to form an N-terminal A-chain and C-terminal B-chain held together by a disulfide bond, and can include further proteolytic cleavage events to remove the preactivation peptide. [PMID:9548733] |
| positive regulation of fibrinolysis | biological process | Any process that activates, maintains or increases the frequency, rate or extent of fibrinolysis, an ongoing process that solubilizes fibrin, resulting in the removal of small blood clots. [GOC:ai] |