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)
Timeframe | Studies on this Protein(%) | All Drugs % |
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 4 (19.05) | 18.2507 |
2000's | 8 (38.10) | 29.6817 |
2010's | 8 (38.10) | 24.3611 |
2020's | 1 (4.76) | 2.80 |
Compounds (41)
Drugs with Potency Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
p-chloromercuribenzoic acid | Homo sapiens (human) | Potency | 2.2536 | 2 | 0 |
gossypol | Homo sapiens (human) | Potency | 17.8524 | 3 | 0 |
rhein | Homo sapiens (human) | Potency | 22.0289 | 3 | 0 |
toxoflavin | Homo sapiens (human) | Potency | 2.3661 | 3 | 0 |
isoteolin | Homo sapiens (human) | Potency | 31.6228 | 1 | 0 |
nsc 663284 | Homo sapiens (human) | Potency | 2.8371 | 2 | 0 |
irl 2500 | Homo sapiens (human) | Potency | 18.9389 | 3 | 0 |
bvt.948 | Homo sapiens (human) | Potency | 6.9906 | 2 | 0 |
Drugs with Inhibition Measurements
Drugs with Activation Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
cannabidiol | Homo sapiens (human) | Kd | 0.0188 | 1 | 1 |
Drugs with Other Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
indomethacin | Homo sapiens (human) | ID50 | 30.0000 | 1 | 1 |
MK-8353 | Homo sapiens (human) | Activity | 0.1850 | 1 | 1 |
Inhibiting the Inflammasome: A Chemical Perspective.Journal of medicinal chemistry, , Mar-10, Volume: 59, Issue:5, 2016
Synthesis and evaluation of thiazepines as interleukin-1beta converting enzyme (ICE) inhibitors.Bioorganic & medicinal chemistry letters, , Sep-15, Volume: 16, Issue:18, 2006
Synthesis and evaluation of novel 1-(2-acylhydrazinocarbonyl)-cycloalkyl carboxamides as interleukin-1beta converting enzyme (ICE) inhibitors.Bioorganic & medicinal chemistry letters, , Aug-15, Volume: 16, Issue:16, 2006
Discovery of novel conformationally restricted diazocan peptidomimetics as inhibitors of interleukin-1beta synthesis.Bioorganic & medicinal chemistry letters, , Oct-01, Volume: 15, Issue:19, 2005
Synthesis and in vitro evaluation of sulfonamide isatin Michael acceptors as small molecule inhibitors of caspase-6.Journal of medicinal chemistry, , Apr-23, Volume: 52, Issue:8, 2009
N-benzylisatin sulfonamide analogues as potent caspase-3 inhibitors: synthesis, in vitro activity, and molecular modeling studies.Journal of medicinal chemistry, , Dec-01, Volume: 48, Issue:24, 2005
Discovery of novel aspartyl ketone dipeptides as potent and selective caspase-3 inhibitors.Bioorganic & medicinal chemistry letters, , Feb-09, Volume: 14, Issue:3, 2004
Inhibition of human caspases by peptide-based and macromolecular inhibitors.The Journal of biological chemistry, , Dec-04, Volume: 273, Issue:49, 1998
Peptidyl beta-homo-aspartals: specific inhibitors of interleukin-1 beta converting enzyme and its homologues (caspases).Bioorganic & medicinal chemistry letters, , Jun-16, Volume: 8, Issue:12, 1998
Synthesis and evaluation of isatin analogs as caspase-3 inhibitors: introduction of a hydrophilic group increases potency in a whole cell assay.Bioorganic & medicinal chemistry letters, , Apr-15, Volume: 21, Issue:8, 2011
Succinic acid amides as P2-P3 replacements for inhibitors of interleukin-1beta converting enzyme (ICE or caspase 1).Bioorganic & medicinal chemistry letters, , Sep-01, Volume: 20, Issue:17, 2010
Synthesis and in vitro evaluation of sulfonamide isatin Michael acceptors as small molecule inhibitors of caspase-6.Journal of medicinal chemistry, , Apr-23, Volume: 52, Issue:8, 2009
N-benzylisatin sulfonamide analogues as potent caspase-3 inhibitors: synthesis, in vitro activity, and molecular modeling studies.Journal of medicinal chemistry, , Dec-01, Volume: 48, Issue:24, 2005
Peptidyl beta-homo-aspartals: specific inhibitors of interleukin-1 beta converting enzyme and its homologues (caspases).Bioorganic & medicinal chemistry letters, , Jun-16, Volume: 8, Issue:12, 1998
Enables
This protein enables 9 target(s):
Target | Category | Definition |
endopeptidase activity | molecular function | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. [http://merops.sanger.ac.uk/about/glossary.htm#ENDOPEPTIDASE] |
cysteine-type endopeptidase activity | molecular function | Catalysis 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 binding | molecular function | Binding to a protein. [GOC:go_curators] |
cysteine-type endopeptidase activator activity involved in apoptotic process | molecular function | Binds to and increases the rate of proteolysis catalyzed by a cysteine-type endopeptidase involved in the apoptotic process. [GOC:mah, GOC:mtg_apoptosis] |
kinase binding | molecular function | Binding to a kinase, any enzyme that catalyzes the transfer of a phosphate group. [GOC:jl] |
cytokine binding | molecular function | Binding 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 binding | molecular function | Binding to an identical protein or proteins. [GOC:jl] |
CARD domain binding | molecular function | Binding 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 binding | molecular function | Binding to a caspase family protein. [GOC:dos, GOC:ha] |
Located In
This protein is located in 5 target(s):
Target | Category | Definition |
nucleolus | cellular component | A 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] |
cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
microtubule | cellular component | Any 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 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] |
Active In
This protein is active in 2 target(s):
Target | Category | Definition |
cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
cytosol | cellular component | The 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):
Target | Category | Definition |
canonical inflammasome complex | cellular component | A cytosolic protein complex that is capable of activating caspase-1. [GOC:dph, PMID:17599095] |
NLRP1 inflammasome complex | cellular component | An 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 complex | cellular component | An 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 complex | cellular component | An 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 complex | cellular component | A 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 complex | cellular component | An 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 complex | cellular component | A 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):
Target | Category | Definition |
pattern recognition receptor signaling pathway | biological process | The 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] |
proteolysis | biological process | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. [GOC:bf, GOC:mah] |
apoptotic process | biological process | A 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 transduction | biological process | The 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 pathway | biological process | The series of molecular signals initiated in response to osmotic change. [GOC:jl] |
protein autoprocessing | biological process | Processing 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 production | biological process | Any process that activates or increases the frequency, rate, or extent of interleukin-1 beta production. [GOC:mah] |
positive regulation of interleukin-18 production | biological process | Any process that activates or increases the frequency, rate, or extent of interleukin-18 production. [GOC:mah] |
defense response to bacterium | biological process | Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism. [GOC:jl] |
regulation of apoptotic process | biological process | Any 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 transduction | biological process | Any 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 process | biological process | Any process that activates or increases the activity of a cysteine-type endopeptidase involved in the apoptotic process. [GOC:jl, GOC:mtg_apoptosis] |
icosanoid biosynthetic process | biological process | The chemical reactions and pathways resulting in the formation of icosanoids, any of a group of C20 polyunsaturated fatty acids. [ISBN:0198506732] |
regulation of inflammatory response | biological process | Any 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 response | biological process | Any process that activates or increases the frequency, rate or extent of the inflammatory response. [GOC:ai] |
protein maturation | biological process | Any process leading to the attainment of the full functional capacity of a protein. [GOC:ai] |
defense response to virus | biological process | Reactions triggered in response to the presence of a virus that act to protect the cell or organism. [GOC:ai] |
pyroptosis | biological process | A 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 lipopolysaccharide | biological process | Any 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 stimulus | biological process | Any 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 interferon | biological process | Any 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 processing | biological process | The 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 processing | biological process | The 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 assembly | biological process | The 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 pathway | biological process | Any 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] |