Page last updated: 2024-08-07 16:46:10

Caspase-4

A caspase-4 that is encoded in the genome of human. [PRO:WCB, UniProtKB:P49662]

Synonyms

CASP-4;
EC 3.4.22.57;
ICE and Ced-3 homolog 2;
ICH-2;
ICE(rel)-II;
Mih1;
Protease TX

Research

Bioassay Publications (5)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's2 (40.00)29.6817
2010's3 (60.00)24.3611
2020's0 (0.00)2.80

Compounds (13)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
4-biphenylylacetic acidHomo sapiens (human)IC5011.080015
fenbufenHomo sapiens (human)IC501.560015
ibuprofenHomo sapiens (human)IC5021.950014
indoprofenHomo sapiens (human)IC501.292015
ketoprofenHomo sapiens (human)IC5029.200015
ketorolacHomo sapiens (human)IC504.642015
tiaprofenic acidHomo sapiens (human)IC501.092015
n-methylisatinHomo sapiens (human)IC5050.000011
naproxenHomo sapiens (human)IC5028.666716
5-NitroisatinHomo sapiens (human)IC503.000011
6-(3,5-difluoroanilino)-9-ethyl-2-purinecarbonitrileHomo sapiens (human)IC5033.113111
grassystatin aHomo sapiens (human)IC505.000011

Drugs with Other Measurements

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

Enables

This protein enables 5 target(s):

TargetCategoryDefinition
lipopolysaccharide bindingmolecular functionBinding to a lipopolysaccharide. [PMID:11079463]
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]
lipid bindingmolecular functionBinding to a lipid. [GOC:ai]
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]

Located In

This protein is located in 6 target(s):

TargetCategoryDefinition
extracellular regioncellular componentThe space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators]
mitochondrioncellular componentA semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. [GOC:giardia, ISBN:0198506732]
endoplasmic reticulumcellular componentThe irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). [ISBN:0198506732]
endoplasmic reticulum membranecellular componentThe lipid bilayer surrounding the endoplasmic reticulum. [GOC:mah]
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
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]
cytoplasmcellular componentThe contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]

Part Of

This protein is part of 3 target(s):

TargetCategoryDefinition
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]
non-canonical inflammasome complexcellular componentAn inflammasome complex containing CASP4, known as caspase-11 (Casp11) in mouse, which assembles upon cytosolic lipopolysaccharide-binding and directly activates Gasdermin-D (GSDMD). [PMID:33187725]
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]

Involved In

This protein is involved in 17 target(s):

TargetCategoryDefinition
proteolysisbiological processThe hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. [GOC:bf, GOC:mah]
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]
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]
defense response to bacteriumbiological processReactions triggered in response to the presence of a bacterium that act to protect the cell or organism. [GOC:jl]
innate immune responsebiological processInnate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens. [GO_REF:0000022, GOC:add, GOC:ebc, GOC:mtg_sensu]
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]
defense response to Gram-positive bacteriumbiological processReactions triggered in response to the presence of a Gram-positive bacterium that act to protect the cell or organism. [GOC:ai]
protein maturationbiological processAny process leading to the attainment of the full functional capacity of a protein. [GOC:ai]
intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stressbiological processThe series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced in response to a stimulus indicating endoplasmic reticulum (ER) stress, and ends when the execution phase of apoptosis is triggered. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen. [GOC:mah, GOC:mtg_apoptosis, PMID:18701708]
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]
intrinsic apoptotic signaling pathwaybiological processThe series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway starts with reception of an intracellular signal (e.g. DNA damage, endoplasmic reticulum stress, oxidative stress etc.), and ends when the execution phase of apoptosis is triggered. The intrinsic apoptotic signaling pathway is crucially regulated by permeabilization of the mitochondrial outer membrane (MOMP). [GOC:mtg_apoptosis, GOC:yaf, PMID:11919192, PMID:17340152, PMID:18852119]
non-canonical inflammasome complex assemblybiological processThe aggregation, arrangement and bonding together of a set of components to form a non-canonical inflammasome complex. [PMID:27291964]
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]
cellular response to amyloid-betabiological 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 amyloid-beta stimulus. [GO_REF:0000071, GOC:TermGenie, PMID:23555824]
positive regulation of interleukin-18-mediated signaling pathwaybiological processAny process that activates or increases the frequency, rate or extent of interleukin-18-mediated signaling pathway. [GOC:obol]
positive regulation of neuron apoptotic processbiological processAny process that activates or increases the frequency, rate or extent of cell death of neurons by apoptotic process. [GOC:go_curators, GOC:mtg_apoptosis]