Page last updated: 2024-08-07 16:23:07

Caspase-1

A caspase-1 that is encoded in the genome of human. [PRO:WCB, UniProtKB:P29466]

Synonyms

CASP-1;
EC 3.4.22.36;
Interleukin-1 beta convertase;
IL-1BC;
Interleukin-1 beta-converting enzyme;
ICE;
IL-1 beta-converting enzyme;
p45

Research

Bioassay Publications (21)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's4 (19.05)18.2507
2000's8 (38.10)29.6817
2010's8 (38.10)24.3611
2020's1 (4.76)2.80

Compounds (41)

Drugs with Potency Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
p-chloromercuribenzoic acidHomo sapiens (human)Potency2.253620
gossypolHomo sapiens (human)Potency17.852430
rheinHomo sapiens (human)Potency22.028930
toxoflavinHomo sapiens (human)Potency2.366130
isoteolinHomo sapiens (human)Potency31.622810
nsc 663284Homo sapiens (human)Potency2.837120
irl 2500Homo sapiens (human)Potency18.938930
bvt.948Homo sapiens (human)Potency6.990620

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
5,8,11,14-eicosatetraynoic acidHomo sapiens (human)IC5010.000011
disulfiramHomo sapiens (human)IC501.800011
ebselenHomo sapiens (human)IC504.040011
4-biphenylylacetic acidHomo sapiens (human)IC5011.080015
fenbufenHomo sapiens (human)IC501.560015
gossypolHomo sapiens (human)IC501.230011
ibuprofenHomo sapiens (human)IC5021.950014
indoprofenHomo sapiens (human)IC501.292015
ketoprofenHomo sapiens (human)IC5029.200015
ketorolacHomo sapiens (human)IC504.642015
beta-lapachoneHomo sapiens (human)IC501.690011
masoprocolHomo sapiens (human)IC5010.000011
quinoneHomo sapiens (human)IC503.000011
sulfasalazineHomo sapiens (human)IC5028.812010
tiaprofenic acidHomo sapiens (human)IC501.092015
triamtereneHomo sapiens (human)IC503.663010
thymoquinoneHomo sapiens (human)IC501.080011
n-methylisatinHomo sapiens (human)IC5050.000011
parthenolideHomo sapiens (human)Ki10.600011
pralnacasanHomo sapiens (human)IC500.107344
naproxenHomo sapiens (human)IC5028.666716
docosahexaenoateHomo sapiens (human)IC506.760011
acetyl-aspartyl-glutamyl-valyl-aspartalHomo sapiens (human)IC507.0641510
acetyl-aspartyl-glutamyl-valyl-aspartalHomo sapiens (human)Ki0.009112
5-NitroisatinHomo sapiens (human)IC503.000011
n-acetyltyrosyl-valyl-alanyl-aspartyl aldehydeHomo sapiens (human)IC5011.341766
n-acetyltyrosyl-valyl-alanyl-aspartyl aldehydeHomo sapiens (human)Ki0.000711
octyl caffeateHomo sapiens (human)IC500.840011
6-(3,5-difluoroanilino)-9-(2,2-difluoroethyl)-2-purinecarbonitrileHomo sapiens (human)IC5016.218111
9-(3,5-difluorophenyl)-6-(ethylamino)-2-purinecarbonitrileHomo sapiens (human)IC5070.794611
grassystatin aHomo sapiens (human)IC505.000011
6-o-palmitoylascorbic acidHomo sapiens (human)IC500.600011
rifampinHomo sapiens (human)IC508.319010

Drugs with Activation Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
cannabidiolHomo sapiens (human)Kd0.018811

Drugs with Other Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
indomethacinHomo sapiens (human)ID5030.000011
MK-8353Homo sapiens (human)Activity0.185011

Enables

This protein enables 9 target(s):

TargetCategoryDefinition
endopeptidase activitymolecular functionCatalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. [http://merops.sanger.ac.uk/about/glossary.htm#ENDOPEPTIDASE]
cysteine-type endopeptidase activitymolecular functionCatalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile. [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE, https://www.ebi.ac.uk/merops/about/glossary.shtml#ENDOPEPTIDASE]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
cysteine-type endopeptidase activator activity involved in apoptotic processmolecular functionBinds to and increases the rate of proteolysis catalyzed by a cysteine-type endopeptidase involved in the apoptotic process. [GOC:mah, GOC:mtg_apoptosis]
kinase bindingmolecular functionBinding to a kinase, any enzyme that catalyzes the transfer of a phosphate group. [GOC:jl]
cytokine bindingmolecular functionBinding to a cytokine, any of a group of proteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity. [GOC:ai, GOC:bf, ISBN:0198599471]
identical protein bindingmolecular functionBinding to an identical protein or proteins. [GOC:jl]
CARD domain bindingmolecular functionBinding to a CARD (N-terminal caspase recruitment) domain, a protein-protein interaction domain that belongs to the death domain-fold superfamily. These protein molecule families are similar in structure with each consisting of six or seven anti-parallel alpha-helices that form highly specific homophilic interactions between signaling partners. CARD exists in the N-terminal prodomains of several caspases and in apoptosis-regulatory proteins and mediates the assembly of CARD-containing proteins that participate in activation or suppression of CARD carrying members of the caspase family. [PMID:12054670]
caspase bindingmolecular functionBinding to a caspase family protein. [GOC:dos, GOC:ha]

Located In

This protein is located in 5 target(s):

TargetCategoryDefinition
nucleoluscellular componentA small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. [ISBN:0198506732]
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]
microtubulecellular componentAny of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle. [ISBN:0879693568]
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 7 target(s):

TargetCategoryDefinition
canonical inflammasome complexcellular componentA cytosolic protein complex that is capable of activating caspase-1. [GOC:dph, PMID:17599095]
NLRP1 inflammasome complexcellular componentAn inflammasome complex that consists of two components, NLRP1 (NALP1) and caspase-1 or caspase-5. The exact mechanisms of NLRP1 activation remain obscure, but potassium ion efflux appears to be essential. [GOC:add, GOC:BHF, GOC:vp, PMID:20303873]
NLRP3 inflammasome complexcellular componentAn inflammasome complex that consists of three components, NLRP3 (NALP3), PYCARD and caspase-1. It is activated upon exposure to whole pathogens, as well as a number of structurally diverse pathogen- and danger-associated molecular patterns (PAMPs and DAMPs) and environmental irritants. Whole pathogens demonstrated to activate the NLRP3 inflammasome complex include the fungi Candida albicans and Saccharomyces cerevisiae, bacteria that produce pore-forming toxins, including Listeria monocytogenes and Staphylococcus aureus, and viruses such as Sendai virus, adenovirus, and influenza virus. [GOC:add, GOC:BHF, GOC:vp, PMID:20303873]
AIM2 inflammasome complexcellular componentAn inflammasome complex that consists of AIM2, ASC, and caspase-1. AIM2 is a member of the HN-200 protein family that appears to be the sensor of cytosolic double-stranded DNA. [GOC:vp, PMID:20303873]
protein-containing complexcellular componentA stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. [GOC:dos, GOC:mah]
IPAF inflammasome complexcellular componentAn inflammasome complex that consists of three components, IPAF, NAIP and caspase-1, and includes among its functions the sensing of flagellin derived from Legionella pneumophila, Salmonella typhimurium, Pseudomonas aeruginosa and Shigella flexneri. [GOC:add, GOC:BHF, GOC:vp, PMID:20303873]
protease inhibitor complexcellular componentA heterodimeric protein complex that contains a protease inhibitor and a protease; formation of the complex inhibits protease activity. [GOC:ans, PMID:6323392]

Involved In

This protein is involved in 25 target(s):

TargetCategoryDefinition
pattern recognition receptor signaling pathwaybiological processThe series of molecular signals initiated by a ligand binding to a pattern recognition receptor (PRR), and ending with the regulation of a downstream cellular process, e.g. transcription. PRRs bind pathogen-associated molecular pattern (PAMPs), structures conserved among microbial species, or damage-associated molecular pattern (DAMPs), endogenous molecules released from damaged cells. [GOC:add, GOC:ar, ISBN:0781735149, PMID:15199967]
proteolysisbiological processThe hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. [GOC:bf, GOC:mah]
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]
signal transductionbiological processThe cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. [GOC:go_curators, GOC:mtg_signaling_feb11]
osmosensory signaling pathwaybiological processThe series of molecular signals initiated in response to osmotic change. [GOC:jl]
protein autoprocessingbiological processProcessing which a protein carries out itself. This involves actions such as the autolytic removal of residues to generate the mature form of the protein. [GOC:ai, PMID:9335337]
positive regulation of interleukin-1 beta productionbiological processAny process that activates or increases the frequency, rate, or extent of interleukin-1 beta production. [GOC:mah]
positive regulation of interleukin-18 productionbiological processAny process that activates or increases the frequency, rate, or extent of interleukin-18 production. [GOC:mah]
defense response to bacteriumbiological processReactions triggered in response to the presence of a bacterium that act to protect the cell or organism. [GOC:jl]
regulation of apoptotic processbiological processAny process that modulates the occurrence or rate of cell death by apoptotic process. [GOC:jl, GOC:mtg_apoptosis]
positive regulation of canonical NF-kappaB signal transductionbiological processAny process that activates or increases the frequency, rate or extent of a canonical NF-kappaB signaling cascade. [GOC:jl]
positive regulation of cysteine-type endopeptidase activity involved in apoptotic processbiological processAny process that activates or increases the activity of a cysteine-type endopeptidase involved in the apoptotic process. [GOC:jl, GOC:mtg_apoptosis]
icosanoid biosynthetic processbiological processThe chemical reactions and pathways resulting in the formation of icosanoids, any of a group of C20 polyunsaturated fatty acids. [ISBN:0198506732]
regulation of inflammatory responsebiological processAny process that modulates the frequency, rate or extent of the inflammatory response, the immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. [GOC:ai]
positive regulation of inflammatory responsebiological processAny process that activates or increases the frequency, rate or extent of the inflammatory response. [GOC:ai]
protein maturationbiological processAny process leading to the attainment of the full functional capacity of a protein. [GOC:ai]
defense response to virusbiological processReactions triggered in response to the presence of a virus that act to protect the cell or organism. [GOC:ai]
pyroptosisbiological processA caspase-1-dependent cell death subroutine that is associated with the generation of pyrogenic mediators such as IL-1beta and IL-18. [GOC:mtg_apoptosis, PMID:18846107, PMID:21760595]
cellular response to lipopolysaccharidebiological 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 lipopolysaccharide stimulus; lipopolysaccharide is a major component of the cell wall of gram-negative bacteria. [GOC:mah]
cellular response to mechanical 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 mechanical stimulus. [GOC:mah]
cellular response to type II interferonbiological 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 an interferon-gamma stimulus. Interferon gamma is the only member of the type II interferon found so far. [GOC:mah]
cytokine precursor processingbiological processThe cleavage of a peptide bond in a precursor form of a cytokine, resulting in the mature (active) form of the cytokine. [PMID:29247995]
signaling receptor ligand precursor processingbiological processThe cleavage of a peptide bond in a precursor form of a signaling receptor ligand, resulting in the mature (active) form of the ligand. [PMID:29247995]
AIM2 inflammasome complex assemblybiological processThe aggregation, arrangement and bonding together of a set of components to form the AIM2 inflammasome complex. [PMID:33467177]
positive regulation of tumor necrosis factor-mediated signaling pathwaybiological processAny process that activates or increases the frequency, rate or extent of tumor necrosis factor-mediated signaling pathway. [GO_REF:0000058, GOC:bf, GOC:PARL, GOC:TermGenie, PMID:23453807]