Page last updated: 2024-08-07 23:23:48

NF-kappa-B inhibitor alpha

An NF-kappa-B inhibitor alpha that is encoded in the genome of human. [TLR:AMM, UniProtKB:P25963]

Synonyms

I-kappa-B-alpha;
IkB-alpha;
IkappaBalpha;
Major histocompatibility complex enhancer-binding protein MAD3

Research

Bioassay Publications (2)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's1 (50.00)29.6817
2010's1 (50.00)24.3611
2020's0 (0.00)2.80

Compounds (6)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
nsc-287088Homo sapiens (human)IC5037.500011
physalin aHomo sapiens (human)IC5050.000011
physalin fHomo sapiens (human)IC5027.100011

Drugs with Activation Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
8-(4-benzenesulfonylamino)quinolineHomo sapiens (human)EC5018.500022
benzyloxycarbonylleucyl-leucyl-leucine aldehydeHomo sapiens (human)EC503.100022
5H-quinolino[8,7-c][1,2]benzothiazine 6,6-dioxideHomo sapiens (human)EC502.400022

Enables

This protein enables 9 target(s):

TargetCategoryDefinition
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
nuclear localization sequence bindingmolecular functionBinding to a nuclear localization sequence, a specific peptide sequence that acts as a signal to localize the protein within the nucleus. [GOC:ai]
enzyme bindingmolecular functionBinding to an enzyme, a protein with catalytic activity. [GOC:jl]
ubiquitin protein ligase bindingmolecular functionBinding to a ubiquitin protein ligase enzyme, any of the E3 proteins. [GOC:vp]
identical protein bindingmolecular functionBinding to an identical protein or proteins. [GOC:jl]
NF-kappaB bindingmolecular functionBinding to NF-kappaB, a transcription factor for eukaryotic RNA polymerase II promoters. [GOC:ai]
protein sequestering activitymolecular functionBinding to a protein to prevent it from interacting with other partners or to inhibit its localization to the area of the cell or complex where it is active. [PMID:1493333]
molecular sequestering activitymolecular functionBinding to a specific molecule to prevent it from interacting with other partners or to inhibit its localization to the area of the cell or complex where it is active. [PMID:13130076]
transcription regulator inhibitor activitymolecular functionA molecular function regulator that inhibits the activity of a transcription regulator via direct binding and/or post-translational modification. [PMID:10652346]

Located In

This protein is located in 5 target(s):

TargetCategoryDefinition
nucleuscellular componentA membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators]
nucleoplasmcellular componentThat part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653]
cytoplasmcellular componentThe contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]
cytosolcellular componentThe part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl]
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]

Active In

This protein is active in 2 target(s):

TargetCategoryDefinition
cytoplasmcellular componentThe contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]
cytosolcellular componentThe part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl]

Part Of

This protein is part of 1 target(s):

TargetCategoryDefinition
I-kappaB/NF-kappaB complexcellular componentA protein complex containing an inhibitory-kappaB (I-kappaB/IKB) protein and one or more copies of an NF-kappaB protein. In the resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. [GOC:bf, GOC:mah, PMID:9407099]

Involved In

This protein is involved in 28 target(s):

TargetCategoryDefinition
protein import into nucleusbiological processThe directed movement of a protein from the cytoplasm to the nucleus. [GOC:jl]
Notch signaling pathwaybiological processThe series of molecular signals initiated by an extracellular ligand binding to the receptor Notch on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:go_curators, GOC:signaling]
canonical NF-kappaB signal transductionbiological processAn intracellular signaling cassette characterized by the I-kappaB-kinase (IKK)-dependent activation of NF-kappaB, also known as the canonical NF-kappaB signaling cascade. The cascade begins with activation of a trimeric IKK complex (consisting of catalytic kinase subunits IKKalpha and/or IKKbeta, and the regulatory scaffold protein NEMO) and ends with the regulation of transcription of target genes by NF-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription. The canonical NF-kappaB pathway is mainly stimulated by proinflammatory cytokines such as IL-1beta, tumor necrosis factor (TNF)-alpha, antigen ligands, and toll-like receptors (TLRs). [GOC:bf, PMID:12773372, PMID:34659217]
cytoplasmic sequestering of NF-kappaBbiological processThe selective interaction of the transcription factor NF-kappaB with specific molecules in the cytoplasm, thereby inhibiting its translocation into the nucleus. [GOC:jl]
negative regulation of macrophage derived foam cell differentiationbiological processAny process that decreases the rate, frequency or extent of macrophage derived foam cell differentiation. Macrophage derived foam cell differentiation is the process in which a macrophage acquires the specialized features of a foam cell. A foam cell is a type of cell containing lipids in small vacuoles and typically seen in atherosclerotic lesions, as well as other conditions. [GOC:add, GOC:BHF, GOC:dph, GOC:tb]
positive regulation of cholesterol effluxbiological processAny process that increases the frequency, rate or extent of cholesterol efflux. Cholesterol efflux is the directed movement of cholesterol, cholest-5-en-3-beta-ol, out of a cell or organelle. [GOC:BHF, GOC:dph, GOC:tb]
negative regulation of lipid storagebiological processAny process that decreases the rate, frequency or extent of lipid storage. Lipid storage is the accumulation and maintenance in cells or tissues of lipids, compounds soluble in organic solvents but insoluble or sparingly soluble in aqueous solvents. Lipid reserves can be accumulated during early developmental stages for mobilization and utilization at later stages of development. [GOC:BHF, GOC:dph, GOC:tb]
lipopolysaccharide-mediated signaling pathwaybiological processThe series of molecular signals initiated by the binding of a lipopolysaccharide (LPS) to a receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. Lipopolysaccharides are major components of the outer membrane of Gram-negative bacteria, making them prime targets for recognition by the immune system. [GOC:mah, GOC:signaling, PMID:15379975]
response to muramyl dipeptidebiological processAny process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a muramyl dipeptide stimulus. Muramyl dipeptide is derived from peptidoglycan. [GOC:add]
tumor necrosis factor-mediated signaling pathwaybiological processThe series of molecular signals initiated by tumor necrosis factor binding to its receptor on the surface of a cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:mah, GOC:signaling]
toll-like receptor 4 signaling pathwaybiological processThe series of molecular signals initiated by a ligand binding to toll-like receptor 4. [GOC:add, PMID:16551253, PMID:17328678]
response to muscle stretchbiological 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 myofibril being extended beyond its slack length. [GOC:BHF, GOC:vk, PMID:14583192]
non-canonical NF-kappaB signal transductionbiological processAn intracellular signaling cassette characterized by the NIK-dependent processing and activation of NF-kappaB. Begins with activation of the NF-kappaB-inducing kinase (NIK), which in turn phosphorylates and activates IkappaB kinase alpha (IKKalpha). IKKalpha phosphorylates the NF-kappa B2 protein (p100) leading to p100 processing and release of an active NF-kappaB (p52). The non-canonical NF-kappaB signaling pathway is generally activated by ligands of the TNF receptor superfamily, including lymphotoxin beta (LTB), CD40, OX40, RANK, TWEAK and B cell-activating factor (BAFF). [GOC:bf, GOC:mg2, GOC:signaling, GOC:vs, PMID:11239468, PMID:15140882, PMID:34659217]
regulation of cell population proliferationbiological processAny process that modulates the frequency, rate or extent of cell proliferation. [GOC:jl]
negative regulation of canonical NF-kappaB signal transductionbiological processAny process that stops, prevents, or reduces the frequency, rate or extent of a canonical NF-kappaB signaling cascade. [GOC:jl]
response to exogenous dsRNAbiological 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 an exogenous double-stranded RNA stimulus. [GOC:go_curators]
negative regulation of myeloid cell differentiationbiological processAny process that stops, prevents, or reduces the frequency, rate or extent of myeloid cell differentiation. [GOC:go_curators]
negative regulation of Notch signaling pathwaybiological processAny process that stops, prevents, or reduces the frequency, rate or extent of the Notch signaling pathway. [GOC:go_curators]
positive regulation of transcription by RNA polymerase IIbiological processAny process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter. [GOC:go_curators, GOC:txnOH]
positive regulation of inflammatory responsebiological processAny process that activates or increases the frequency, rate or extent of the inflammatory response. [GOC:ai]
B cell receptor signaling pathwaybiological processThe series of molecular signals initiated by the cross-linking of an antigen receptor on a B cell. [GOC:add]
positive regulation of protein metabolic processbiological processAny process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving a protein. [GOC:ai]
positive regulation of transcription initiation by RNA polymerase IIbiological processAny process that increases the rate, frequency or extent of a process involved in starting transcription from an RNA polymerase II promoter. [GOC:dph, GOC:tb, GOC:txnOH]
cellular response to coldbiological 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 cold stimulus, a temperature stimulus below the optimal temperature for that organism. [GOC:jp]
nucleotide-binding oligomerization domain containing 1 signaling pathwaybiological processThe series of molecular signals initiated by the binding of a ligand (such as a bacterial peptidoglycan) to a cytoplasmic nucleotide-binding oligomerization domain containing 1 (NOD1) protein receptor, and ending with regulation of a downstream cellular process. [GOC:add, PMID:17944960, PMID:18585455]
nucleotide-binding oligomerization domain containing 2 signaling pathwaybiological processThe series of molecular signals initiated by the binding of a ligand (such as a bacterial peptidoglycan) to a cytoplasmic nucleotide-binding oligomerization domain containing 2 (NOD2) protein receptor, and ending with regulation of a downstream cellular process. [GOC:add, PMID:17944960, PMID:18585455]
interleukin-1-mediated signaling pathwaybiological processThe series of molecular signals initiated by interleukin-1 binding to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:BHF, GOC:mah, GOC:signaling]
cellular response to tumor necrosis factorbiological 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 tumor necrosis factor stimulus. [GOC:mah]