Page last updated: 2024-08-07 15:39:15

Integrin beta-2

An integrin beta-2 that is encoded in the genome of human. [PRO:WCB, UniProtKB:P05107]

Synonyms

Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta;
Complement receptor C3 subunit beta

Research

Bioassay Publications (15)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's1 (6.67)18.2507
2000's10 (66.67)29.6817
2010's3 (20.00)24.3611
2020's1 (6.67)2.80

Compounds (11)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
lovastatinHomo sapiens (human)IC503.090022
chlorfenethazineHomo sapiens (human)IC5028.000011
2-bromohippuric acidHomo sapiens (human)IC50313.500011
benzotriptHomo sapiens (human)IC50169.000011
birt 377Homo sapiens (human)IC500.026011
a 286982Homo sapiens (human)IC500.041255
bio 1211Homo sapiens (human)IC5050.000422
sar 1118Homo sapiens (human)IC500.041522

Drugs with Activation Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
indoleHomo sapiens (human)Kd300.000022
1,4-benzodioxanHomo sapiens (human)Kd10,000.000022
1-methylindoleHomo sapiens (human)Kd1,400.000011
birt 377Homo sapiens (human)Kd0.020011

Enables

This protein enables 9 target(s):

TargetCategoryDefinition
amyloid-beta bindingmolecular functionBinding to an amyloid-beta peptide/protein. [GOC:hjd]
complement component C3b bindingmolecular functionBinding to a C3b product of the complement cascade. [GOC:add, ISBN:0781735149]
integrin bindingmolecular functionBinding to an integrin. [GOC:ceb]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
protein kinase bindingmolecular functionBinding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. [GOC:jl]
ICAM-3 receptor activitymolecular functionCombining with ICAM-3, intercellular adhesion molecule 3, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity. ICAM-3, or CD50, are constitutively expressed on monocytes, granulocytes and lymphocytes; on physiological stimulation, they become transiently phosphorylated on serine residues. [GOC:ai, GOC:signaling, ISBN:0198506732, PMID:7515813]
heat shock protein bindingmolecular functionBinding to a heat shock protein, a protein synthesized or activated in response to heat shock. [GOC:mah, GOC:vw]
metal ion bindingmolecular functionBinding to a metal ion. [GOC:ai]
cell adhesion molecule bindingmolecular functionBinding to a cell adhesion molecule. [GOC:ai]

Located In

This protein is located in 10 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]
external side of plasma membranecellular componentThe leaflet of the plasma membrane that faces away from the cytoplasm and any proteins embedded or anchored in it or attached to its surface. [GOC:dos, GOC:tb]
cell surfacecellular componentThe external part of the cell wall and/or plasma membrane. [GOC:jl, GOC:mtg_sensu, GOC:sm]
membranecellular componentA lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194]
specific granule membranecellular componentThe lipid bilayer surrounding a specific granule, a granule with a membranous, tubular internal structure, found primarily in mature neutrophil cells. Most are released into the extracellular fluid. Specific granules contain lactoferrin, lysozyme, vitamin B12 binding protein and elastase. [GOC:bf, PMID:7334549]
plasma membrane raftcellular componentA membrane raft that is part of the plasma membrane. [GOC:jl]
extracellular exosomecellular componentA 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]
tertiary granule membranecellular componentThe lipid bilayer surrounding a tertiary granule. [GOC:BHF, GOC:mah, GOC:rl, PMID:12070036]
ficolin-1-rich granule membranecellular componentThe lipid bilayer surrounding a ficolin-1-rich granule. [GOC:mec, PMID:23650620]
extracellular vesiclecellular componentAny vesicle that is part of the extracellular region. [GO_REF:0000064, GOC:pm, GOC:TermGenie, PMID:24769233]

Active In

This protein is active in 2 target(s):

TargetCategoryDefinition
focal adhesioncellular componentA 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]
cell surfacecellular componentThe external part of the cell wall and/or plasma membrane. [GOC:jl, GOC:mtg_sensu, GOC:sm]

Part Of

This protein is part of 5 target(s):

TargetCategoryDefinition
integrin alphaL-beta2 complexcellular componentAn integrin complex that comprises one alphaL subunit and one beta2 subunit. [PMID:12297042]
integrin alphaM-beta2 complexcellular componentAn integrin complex that comprises one alphaM subunit and one beta2 subunit. [PMID:12297042]
integrin alphaX-beta2 complexcellular componentAn integrin complex that comprises one alphaX subunit and one beta2 subunit. [PMID:12297042]
integrin complexcellular componentA protein complex that is composed of one alpha subunit and one beta subunit, both of which are members of the integrin superfamily of cell adhesion receptors; the complex spans the plasma membrane and binds to extracellular matrix ligands, cell-surface ligands, and soluble ligands. [PMID:17543136]
receptor complexcellular componentAny protein complex that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function. [GOC:go_curators]

Involved In

This protein is involved in 29 target(s):

TargetCategoryDefinition
microglial cell activationbiological processThe change in morphology and behavior of a microglial cell resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor. [GOC:mgi_curators, PMID:10626665, PMID:10695728, PMID:12580336, PMID:9893949]
receptor-mediated endocytosisbiological processAn endocytosis process in which cell surface receptors ensure specificity of transport. A specific receptor on the cell surface binds tightly to the extracellular macromolecule (the ligand) that it recognizes; the plasma-membrane region containing the receptor-ligand complex then undergoes endocytosis, forming a transport vesicle containing the receptor-ligand complex and excluding most other plasma-membrane proteins. Receptor-mediated endocytosis generally occurs via clathrin-coated pits and vesicles. [GOC:mah, ISBN:0716731363]
phagocytosis, engulfmentbiological processThe internalization of bacteria, immune complexes and other particulate matter or of an apoptotic cell by phagocytosis, including the membrane and cytoskeletal processes required, which involves one of three mechanisms: zippering of pseudopods around a target via repeated receptor-ligand interactions, sinking of the target directly into plasma membrane of the phagocytosing cell, or induced uptake via an enhanced membrane ruffling of the phagocytosing cell similar to macropinocytosis. [GOC:curators, ISBN:0781735149]
apoptotic processbiological processA programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. [GOC:cjm, GOC:dhl, GOC:ecd, GOC:go_curators, GOC:mtg_apoptosis, GOC:tb, ISBN:0198506732, PMID:18846107, PMID:21494263]
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 adhesionbiological processThe attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules. [GOC:hb, GOC:pf]
leukocyte cell-cell adhesionbiological processThe attachment of a leukocyte to another cell via adhesion molecules. [GOC:go_curators]
cell-matrix adhesionbiological processThe binding of a cell to the extracellular matrix via adhesion molecules. [GOC:hb]
integrin-mediated signaling pathwaybiological processThe series of molecular signals initiated by an extracellular ligand binding to an integrin on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:mah, GOC:signaling]
cell-cell signalingbiological processAny process that mediates the transfer of information from one cell to another. This process includes signal transduction in the receiving cell and, where applicable, release of a ligand and any processes that actively facilitate its transport and presentation to the receiving cell. Examples include signaling via soluble ligands, via cell adhesion molecules and via gap junctions. [GOC:dos, GOC:mah]
regulation of cell shapebiological processAny process that modulates the surface configuration of a cell. [GOC:dph, GOC:go_curators, GOC:tb]
neutrophil chemotaxisbiological processThe directed movement of a neutrophil cell, the most numerous polymorphonuclear leukocyte found in the blood, in response to an external stimulus, usually an infection or wounding. [GOC:jl, ISBN:0198506732]
receptor internalizationbiological processA receptor-mediated endocytosis process that results in the movement of receptors from the plasma membrane to the inside of the cell. The process begins when cell surface receptors are monoubiquitinated following ligand-induced activation. Receptors are subsequently taken up into endocytic vesicles from where they are either targeted to the lysosome or vacuole for degradation or recycled back to the plasma membrane. [GOC:bf, GOC:mah, GOC:signaling, PMID:15006537, PMID:19643732]
positive regulation of superoxide anion generationbiological processAny process that activates or increases the frequency, rate or extent of enzymatic generation of superoxide by a cell. [GOC:mah]
heterotypic cell-cell adhesionbiological processThe attachment of a cell to a cell of a different type via adhesion molecules. [GOC:add]
endodermal cell differentiationbiological processThe process in which a relatively unspecialized cell acquires the specialized features of an endoderm cell, a cell of the inner of the three germ layers of the embryo. [CL:0000223, GOC:yaf, PMID:17624332]
receptor clusteringbiological processThe receptor metabolic process that results in grouping of a set of receptors at a cellular location, often to amplify the sensitivity of a signaling response. [GOC:bf, GOC:jl, GOC:pr, PMID:19747931, PMID:21453460]
positive regulation of neutrophil degranulationbiological processAny process that activates or increases the frequency, rate or extent of neutrophil degranulation. [ISBN:0781735149]
negative regulation of dopamine metabolic processbiological processAny process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving dopamine. [GOC:go_curators]
regulation of peptidyl-tyrosine phosphorylationbiological processAny process that modulates the frequency, rate or extent of the phosphorylation of peptidyl-tyrosine. [GOC:ai]
cellular response to low-density lipoprotein particle stimulusbiological processAny process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a low-density lipoprotein particle stimulus. [GOC:mah]
positive regulation of protein targeting to membranebiological processAny process that increases the frequency, rate or extent of the process of directing proteins towards a membrane, usually using signals contained within the protein. [GOC:tb]
amyloid-beta clearancebiological processThe process in which amyloid-beta is removed from extracellular brain regions by mechanisms involving cell surface receptors. [GOC:aruk, GOC:bc, GOC:BHF, PMID:18289866, PMID:19098903, PMID:26005850]
cell-cell adhesionbiological processThe attachment of one cell to another cell via adhesion molecules. [GOC:dos]
cell-cell adhesion via plasma-membrane adhesion moleculesbiological processThe attachment of one cell to another cell via adhesion molecules that are at least partially embedded in the plasma membrane. [GOC:dos]
positive regulation of leukocyte adhesion to vascular endothelial cellbiological processAny process that activates or increases the frequency, rate or extent of leukocyte adhesion to vascular endothelial cell. [GO_REF:0000058, GOC:bc, GOC:BHF, GOC:BHF_miRNA, GOC:TermGenie, PMID:23897866]
neutrophil migrationbiological processThe movement of a neutrophil within or between different tissues and organs of the body. [PMID:1826836]
positive regulation of prostaglandin-E synthase activitybiological processAny process that activates or increases the frequency, rate or extent of prostaglandin-E synthase activity. [GOC:BHF]
cell adhesion mediated by integrinbiological processThe attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via an integrin, a heterodimeric adhesion receptor formed by the non-covalent association of particular alpha and beta subunits. [GOC:add, PMID:12213832, PMID:14754902]