Page last updated: 2024-08-07 16:24:56

B2 bradykinin receptor

A B2 bradykinin receptor that is encoded in the genome of human. [PRO:WCB, UniProtKB:P30411]

Synonyms

B2R;
BK-2 receptor

Research

Bioassay Publications (23)

TimeframeStudies on this Protein(%)All Drugs %
pre-19901 (4.35)18.7374
1990's7 (30.43)18.2507
2000's8 (34.78)29.6817
2010's6 (26.09)24.3611
2020's1 (4.35)2.80

Compounds (13)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
amiodaroneHomo sapiens (human)IC5012.966010
amiodaroneHomo sapiens (human)Ki7.674010
arg-3-hyp-7-phe-bradykininHomo sapiens (human)IC500.011344
bradykinin, leu(8)-des-arg(9)-Homo sapiens (human)Ki0.010011
bradykininHomo sapiens (human)IC500.001811
bradykininHomo sapiens (human)Ki0.000555
tamoxifenHomo sapiens (human)IC5020.356010
tamoxifenHomo sapiens (human)Ki12.048010
fr 173657Homo sapiens (human)IC500.001433
fr 190997Homo sapiens (human)IC500.000433
bradyzideHomo sapiens (human)Ki0.772011
icatibantHomo sapiens (human)IC500.001944
icatibantHomo sapiens (human)Ki0.000144
rmp 7Homo sapiens (human)Ki0.019011
cp 195543Homo sapiens (human)IC500.280011
cp 105696Homo sapiens (human)IC5076.700011
nitd 609Homo sapiens (human)IC5030.000011

Drugs with Activation Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
bradykininHomo sapiens (human)EC500.000011
icatibantHomo sapiens (human)Kd0.000311

Drugs with Other Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
bradykininHomo sapiens (human)ED500.001611
bradykininHomo sapiens (human)pD8,780,000.000011

Enables

This protein enables 6 target(s):

TargetCategoryDefinition
protease bindingmolecular functionBinding to a protease or a peptidase. [GOC:hjd]
phosphatidylinositol phospholipase C activitymolecular functionCatalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1,2-diacylglycerol + 1D-myo-inositol 1,4,5-trisphosphate + H+. [EC:3.1.4.11, RHEA:33179]
bradykinin receptor activitymolecular functionCombining with bradykinin to initiate a change in cell activity. [GOC:ai]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
type 1 angiotensin receptor bindingmolecular functionBinding to a type 1 angiotensin receptor. [GOC:mah, GOC:nln]
protein heterodimerization activitymolecular functionBinding to a nonidentical protein to form a heterodimer. [GOC:ai]

Located In

This protein is located in 4 target(s):

TargetCategoryDefinition
endosomecellular componentA vacuole to which materials ingested by endocytosis are delivered. [ISBN:0198506732, PMID:19696797]
Golgi apparatuscellular componentA membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways. [ISBN:0198506732]
plasma membranecellular componentThe membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363]
intracellular membrane-bounded organellecellular componentOrganized 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]

Active In

This protein is active in 1 target(s):

TargetCategoryDefinition
plasma membranecellular componentThe membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363]

Involved In

This protein is involved in 16 target(s):

TargetCategoryDefinition
smooth muscle contractionbiological processA process in which force is generated within smooth muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. Smooth muscle differs from striated muscle in the much higher actin/myosin ratio, the absence of conspicuous sarcomeres and the ability to contract to a much smaller fraction of its resting length. [GOC:ef, GOC:jl, GOC:mtg_muscle, ISBN:0198506732]
inflammatory responsebiological processThe immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. [GO_REF:0000022, ISBN:0198506732]
cell surface receptor signaling pathwaybiological processThe series of molecular signals initiated by an extracellular ligand binding to a receptor located on the cell surface. The pathway ends with regulation of a downstream cellular process, e.g. transcription. [GOC:signaling]
cell surface receptor protein tyrosine kinase signaling pathwaybiological processThe series of molecular signals initiated by an extracellular ligand binding to a receptor on the surface of the target cell where the receptor possesses tyrosine kinase activity, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:ceb, GOC:signaling]
positive regulation of cytosolic calcium ion concentrationbiological processAny process that increases the concentration of calcium ions in the cytosol. [GOC:ai]
blood circulationbiological processThe flow of blood through the body of an animal, enabling the transport of nutrients to the tissues and the removal of waste products. [GOC:mtg_heart, ISBN:0192800825]
response to salt stressbiological processAny 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 a stimulus indicating an increase or decrease in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment. [GOC:jl]
regulation of vasoconstrictionbiological processAny process that modulates the frequency, rate or extent of reductions in the diameter of blood vessels. [GOC:jl]
negative regulation of peptidyl-serine phosphorylationbiological processAny process that stops, prevents, or reduces the frequency, rate or extent of the phosphorylation of peptidyl-serine. [GOC:mah]
vasoconstrictionbiological processA decrease in the diameter of blood vessels, especially arteries, due to constriction of smooth muscle cells that line the vessels, and usually causing an increase in blood pressure. [GOC:pr, ISBN:0192800752]
vasodilationbiological processAn increase in the internal diameter of blood vessels, especially arterioles or capillaries, due to relaxation of smooth muscle cells that line the vessels, and usually resulting in a decrease in blood pressure. [GOC:pr, ISBN:0192800981]
regulation of vascular permeabilitybiological processAny process that modulates the extent to which blood vessels can be pervaded by fluid. [GOC:jl]
arachidonic acid secretionbiological processThe controlled release of arachidonic acid from a cell or a tissue. [GOC:ai]
negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress by p53 class mediatorbiological processAny process that stops, prevents or reduces the frequency, rate or extent of intrinsic apoptotic signaling pathway in response to osmotic stress by p53 class mediator. [GOC:krc, GOC:mtg_apoptosis, GOC:TermGenie, PMID:16571598]
intrinsic apoptotic signaling pathway in response to osmotic stress by p53 class mediatorbiological processThe series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, in response to the detection of osmotic stress, and ends when the execution phase of apoptosis is triggered. [GOC:krc, GOC:mtg_apoptosis, PMID:16571598]
G protein-coupled receptor signaling pathwaybiological processThe series of molecular signals initiated by a ligand binding to its receptor, in which the activated receptor promotes the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, and ends with regulation of a downstream cellular process. The pathway can start from the plasma membrane, Golgi or nuclear membrane. [GOC:bf, GOC:mah, PMID:16902576, PMID:24568158, Wikipedia:G_protein-coupled_receptor]