NACHT, LRR and PYD domains-containing protein 3

A NACHT, LRR and PYD domains-containing protein 3 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q96P20]

Synonyms

Angiotensin/vasopressin receptor AII/AVP-like;
Caterpiller protein 1.1;
CLR1.1;
Cold-induced autoinflammatory syndrome 1 protein;
Cryopyrin;
PYRIN-containing APAF1-like protein 1

Research

Bioassay Publications (15)

Timeframe	Studies on this Protein(%)	All Drugs %
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	4 (26.67)	24.3611
2020's	11 (73.33)	2.80

Compounds (8)

Drugs with Inhibition Measurements

Drug	Taxonomy	Measurement	Average (mM)	Bioassay(s)	Publication(s)
glyburide	Homo sapiens (human)	IC50	12.0000	1	1
micheliolide	Homo sapiens (human)	IC50	5.9000	1	1
isoliquiritigenin	Homo sapiens (human)	IC50	5.8200	2	2
1,6-anhydro-3,4-dideoxy-beta-d-glycero-hex-3-enopyran-2-ulose	Homo sapiens (human)	IC50	6.6000	1	1
curcumin	Homo sapiens (human)	IC50	24.2000	1	1
3-((3-trifluoromethyl)phenyl)-5-((3-carboxyphenyl)methylene)-2-thioxo-4-thiazolidinone	Homo sapiens (human)	IC50	6.3900	1	1
apigenin	Homo sapiens (human)	IC50	10.0000	1	1
mcc-950	Homo sapiens (human)	IC50	0.0106	9	9

Enables

This protein enables 16 target(s):

Target	Category	Definition
protein binding	molecular function	Binding to a protein. [GOC:go_curators]
ATP binding	molecular function	Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. [ISBN:0198506732]
ATP hydrolysis activity	molecular function	Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. [RHEA:13065]
protein-macromolecule adaptor activity	molecular function	The binding activity of a protein that brings together two or more macromolecules in contact, permitting those molecules to function in a coordinated way. The adaptor can bring together two proteins, or a protein and another macromolecule such as a lipid or a nucleic acid. [GOC:bf, GOC:mah, GOC:vw]
signaling adaptor activity	molecular function	The binding activity of a molecule that brings together two or more molecules in a signaling pathway, permitting those molecules to function in a coordinated way. Adaptor molecules themselves do not have catalytic activity. [GOC:bf, PMID:19104498]
identical protein binding	molecular function	Binding to an identical protein or proteins. [GOC:jl]
peptidoglycan binding	molecular function	Interacting selectively and non-covalently, in a non-covalent manner, with peptidoglycan, any of a class of glycoconjugates found in bacterial cell walls. [GOC:go_curators, PMID:14698226]
ADP binding	molecular function	Binding to ADP, adenosine 5'-diphosphate. [GOC:jl]
sequence-specific DNA binding	molecular function	Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding. [GOC:jl]
molecular adaptor activity	molecular function	The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way. [GOC:mtg_MIT_16mar07, GOC:vw]
phosphatidylinositol-4-phosphate binding	molecular function	Binding to phosphatidylinositol-4-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' position. [GOC:bf, GOC:mah]
DNA-binding transcription factor binding	molecular function	Binding to a DNA-binding transcription factor, a protein that interacts with a specific DNA sequence (sometimes referred to as a motif) within the regulatory region of a gene to modulate transcription. [GOC:txnOH-2018]
small molecule sensor activity	molecular function	Binding to a small molecule and eliciting a change in the protein's activity in response to the intracellular level of that small molecule. [PMID:26328879]
cysteine-type endopeptidase activator activity	molecular function	Binds to and increases the activity of a cysteine-type endopeptidase. [PMID:32558991]
molecular condensate scaffold activity	molecular function	Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate. [PMID:28225081]
phosphatidylinositol phosphate binding	molecular function	Binding to phosphatidylinositol phosphate. [GOC:TermGenie, PMID:23445487]

Located In

This protein is located in 9 target(s):

Target	Category	Definition
Golgi membrane	cellular component	The lipid bilayer surrounding any of the compartments of the Golgi apparatus. [GOC:mah]
extracellular region	cellular component	The 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]
nucleus	cellular component	A 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]
cytoplasm	cellular component	The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]
mitochondrion	cellular component	A 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 reticulum	cellular component	The 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]
microtubule organizing center	cellular component	An intracellular structure that can catalyze gamma-tubulin-dependent microtubule nucleation and that can anchor microtubules by interacting with their minus ends, plus ends or sides. [GOC:vw, ISBN:0815316194, PMID:17072892, PMID:17245416, Wikipedia:Microtubule_organizing_center]
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]
interphase microtubule organizing center	cellular component	A microtubule organizing center found in interphase cells, which organize a longitudinal array of three to five MT bundles from the nuclear envelope during interphase. Each MT bundle is composed of two to seven MTs arranged in an antiparallel configuration, with the dynamic MT plus ends extending toward the cell tips and stable minus ends near the nucleus. [PMID:15068790]

Active In

This protein is active in 3 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]
membrane	cellular component	A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194]

Part Of

This protein is part of 1 target(s):

Target	Category	Definition
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]

Involved In

This protein is involved in 28 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]
negative regulation of acute inflammatory response	biological process	Any process that stops, prevents, or reduces the frequency, rate, or extent of an acute inflammatory response. [GOC:add]
positive regulation of type 2 immune response	biological process	Any process that activates or increases the frequency, rate, or extent of a type 2 immune response. [GOC:add]
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]
defense response	biological process	Reactions, triggered in response to the presence of a foreign body or the occurrence of an injury, which result in restriction of damage to the organism attacked or prevention/recovery from the infection caused by the attack. [GOC:go_curators]
inflammatory response	biological process	The 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]
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]
detection of biotic stimulus	biological process	The series of events in which a biotic stimulus, one caused or produced by a living organism, is received and converted into a molecular signal. [GOC:hb]
negative regulation of interleukin-1 beta production	biological process	Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-1 beta production. [GOC:mah]
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-4 production	biological process	Any process that activates or increases the frequency, rate, or extent of interleukin-4 production. [GOC:mah]
NLRP3 inflammasome complex assembly	biological process	The aggregation, arrangement and bonding together of a set of components to form the NLRP3 inflammasome complex, occurring at the level of an individual cell. [GOC:jl, PMID:21048113]
innate immune response	biological process	Innate 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]
positive regulation of T-helper 2 cell differentiation	biological process	Any process that activates or increases the frequency, rate or extent of T-helper 2 cell differentiation. [GOC:go_curators]
positive regulation of transcription by RNA polymerase II	biological process	Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter. [GOC:go_curators, GOC:txnOH]
negative regulation of inflammatory response	biological process	Any process that stops, prevents, or reduces the frequency, rate or extent of the inflammatory response. [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]
positive regulation of NF-kappaB transcription factor activity	biological process	Any process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB. [GOC:dph, GOC:tb, PMID:15087454, PMID:15170030]
protein homooligomerization	biological process	The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer. [GOC:ai]
protein maturation	biological process	Any process leading to the attainment of the full functional capacity of a protein. [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 virus	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 stimulus from a virus. [GOC:dos]
negative regulation of non-canonical NF-kappaB signal transduction	biological process	Any process that stops, prevents or reduces the frequency, rate or extent of non-canonical NF-kappaB signaling cascade. [GOC:TermGenie]
positive regulation of non-canonical NF-kappaB signal transduction	biological process	Any process that activates or increases the frequency, rate or extent of the non-canonical NF-kappaB cascade. [GOC:TermGenie]
positive regulation of T-helper 2 cell cytokine production	biological process	Any process that activates or increases the frequency, rate or extent of T-helper 2 cell cytokine production. [GOC:obol]
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]