Q9EPB4

PR
Gene name
Pycard (Asc)
Protein name
Apoptosis-associated speck-like protein containing a CARD
Names
mASC, PYD and CARD domain-containing protein
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:66824
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

55-136 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

2 structures for Q9EPB4

Entry ID Method Resolution Chain Position Source
2N1F Other 400 A A/B/C/D/E/F/G/H/I/J/K/L/M/N/O 2-90 PDB
AF-Q9EPB4-F1 Predicted AlphaFoldDB

12 variants for Q9EPB4

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388950335 3 R>W No EVA
rs3388946460 47 M>L No EVA
rs3388956004 56 L>R No EVA
rs3388908201 76 M>I No EVA
rs3388931474 82 A>T No EVA
rs3388946522 97 A>T No EVA
rs226419628 99 A>T No EVA
rs3388958084 100 S>C No EVA
rs3388950583 137 S>T No EVA
rs3388950593 142 G>E No EVA
rs241319345 164 V>A No EVA
rs3388946496 165 P>A No EVA

No associated diseases with Q9EPB4

3 regional properties for Q9EPB4

Type Name Position InterPro Accession
domain CARD domain 105 - 193 IPR001315
domain DAPIN domain 1 - 91 IPR004020
domain CARD8/ASC/NALP1, CARD domain 111 - 191 IPR033516

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Inflammasome
  • Endoplasmic reticulum
  • Mitochondrion
  • Nucleus
  • Upstream of caspase activation, a redistribution from the cytoplasm to the aggregates occurs
  • These appear as hollow, perinuclear spherical, ball-like structures
  • Upon NLRP3 inflammasome activation redistributes to the perinuclear space localizing to endoplasmic reticulum and mitochondria
  • Localized primarily to the nucleus in resting monocytes/macrophages and rapidly redistributed to the cytoplasm upon pathogen infection (By similarity)
  • Localized to large cytoplasmic aggregate appearing as a speck containing AIM2, PYCARD, CASP8 and bacterial DNA after infection with Francisella tularensis (PubMed:22555457)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

18 GO annotations of cellular component

Name Definition
AIM2 inflammasome complex 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.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
endoplasmic reticulum 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).
extracellular region 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.
Golgi membrane The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
IkappaB kinase complex A trimeric protein complex that phosphorylates inhibitory-kappaB (I-kappaB) proteins. The complex is composed of two kinase subunits (alpha and beta) and a regulatory gamma subunit (also called NEMO). In a resting state, NF-kappaB dimers are bound to inhibitory IKB 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.
inflammasome complex A cytosolic protein complex that is capable of activating caspase-1.
microtubule 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.
mitochondrion 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.
neuronal cell body The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
NLRP1 inflammasome complex 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.
NLRP3 inflammasome complex 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.
NLRP6 inflammasome complex An inflammasome complex that consists of NLRP6, PYCARD/ASC and caspase-1 or caspase-4/caspase-11.
nucleolus 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.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
nucleus 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.
protein-containing complex 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.

13 GO annotations of molecular function

Name Definition
BMP receptor binding Binding to a BMP receptor.
cysteine-type endopeptidase activity involved in apoptotic process 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, and contributing to the apoptotic process.
enzyme binding Binding to an enzyme, a protein with catalytic activity.
identical protein binding Binding to an identical protein or proteins.
interleukin-6 receptor binding Binding to an interleukin-6 receptor.
myosin I binding Binding to a class I myosin; myosin I heavy chains are single-headed, possess tails of various lengths, and do not self-associate into bipolar filaments.
peptidase activator activity involved in apoptotic process Binds to and increases the activity of a peptidase that is involved in the apoptotic process.
protease binding Binding to a protease or a peptidase.
protein dimerization activity The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
protein homodimerization activity Binding to an identical protein to form a homodimer.
Pyrin domain binding Binding to a Pyrin (PAAD/DAPIN) domain, a protein-protein interaction domain that has the same fold as the Death domain.
transmembrane transporter binding Binding to a transmembrane transporter, a protein or protein complex that enables the transfer of a substance, usually a specific substance or a group of related substances, from one side of a membrane to the other.
tropomyosin binding Binding to tropomyosin, a protein associated with actin filaments both in cytoplasm and, in association with troponin, in the thin filament of striated muscle.

62 GO annotations of biological process

Name Definition
activation of cysteine-type endopeptidase activity Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase.
activation of cysteine-type endopeptidase activity involved in apoptotic process Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process.
activation of innate immune response Any process that initiates an innate immune response. Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens. Examples of this process include activation of the hypersensitive response of Arabidopsis thaliana and activation of any NOD or TLR signaling pathway in vertebrate species.
apoptotic 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.
cellular response to interleukin-1 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 interleukin-1 stimulus.
cellular response to lipopolysaccharide 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.
cellular response to tumor necrosis factor 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 tumor necrosis factor stimulus.
defense response to Gram-negative bacterium Reactions triggered in response to the presence of a Gram-negative bacterium that act to protect the cell or organism.
defense response to Gram-positive bacterium Reactions triggered in response to the presence of a Gram-positive bacterium that act to protect the cell or organism.
defense response to virus Reactions triggered in response to the presence of a virus that act to protect the cell or organism.
inflammatory response 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.
innate immune response Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens.
intrinsic apoptotic signaling pathway by p53 class mediator The series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, and ends when the execution phase of apoptosis is triggered.
intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator The series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, in response to the detection of DNA damage, and ends when the execution phase of apoptosis is triggered.
macropinocytosis An endocytosis process that results in the uptake of liquid material by cells from their external environment by the 'ruffling' of the cell membrane to form heterogeneously sized intracellular vesicles called macropinosomes, which can be up to 5 micrometers in size.
myeloid dendritic cell activation The change in morphology and behavior of a dendritic cell resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor.
myeloid dendritic cell activation involved in immune response The change in morphology and behavior of a myeloid dendritic cell resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an immune response.
negative regulation of cytokine production involved in inflammatory response Any process that stops, prevents or reduces the frequency, rate or extent of cytokine production involved in inflammatory response.
negative regulation of I-kappaB kinase/NF-kappaB signaling Any process that stops, prevents, or reduces the frequency, rate or extent of -kappaB kinase/NF-kappaB signaling.
negative regulation of interferon-beta production Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-beta production.
negative regulation of NF-kappaB transcription factor activity Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of the transcription factor NF-kappaB.
negative regulation of protein serine/threonine kinase activity Any process that decreases the rate, frequency, or extent of protein serine/threonine kinase activity.
osmosensory signaling pathway The series of molecular signals initiated in response to osmotic change.
pattern recognition receptor signaling pathway 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.
positive regulation of actin filament polymerization Any process that activates or increases the frequency, rate or extent of actin polymerization.
positive regulation of activated T cell proliferation Any process that activates or increases the rate or extent of activated T cell proliferation.
positive regulation of adaptive immune response Any process that activates or increases the frequency, rate, or extent of an adaptive immune response.
positive regulation of antigen processing and presentation of peptide antigen via MHC class II Any process that activates or increases the frequency, rate, or extent of antigen processing and presentation of peptide antigen via MHC class II.
positive regulation of apoptotic process Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
positive regulation of chemokine production Any process that activates or increases the frequency, rate, or extent of chemokine production.
positive regulation of cysteine-type endopeptidase activity Any process that activates or increases the frequency, rate or extent of cysteine-type endopeptidase activity.
positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Any process that activates or increases the activity of a cysteine-type endopeptidase involved in the apoptotic process.
positive regulation of defense response to virus by host Any host process that results in the promotion of antiviral immune response mechanisms, thereby limiting viral replication.
positive regulation of DNA-binding transcription factor activity Any process that activates or increases the frequency, rate or extent of activity of a transcription factor, any factor involved in the initiation or regulation of transcription.
positive regulation of ERK1 and ERK2 cascade Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the ERK1 and ERK2 cascade.
positive regulation of extrinsic apoptotic signaling pathway Any process that activates or increases the frequency, rate or extent of extrinsic apoptotic signaling pathway.
positive regulation of inflammatory response Any process that activates or increases the frequency, rate or extent of the inflammatory response.
positive regulation of interferon-gamma production Any process that activates or increases the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon.
positive regulation of interleukin-1 beta production Any process that activates or increases the frequency, rate, or extent of interleukin-1 beta production.
positive regulation of interleukin-10 production Any process that activates or increases the frequency, rate, or extent of interleukin-10 production.
positive regulation of interleukin-6 production Any process that activates or increases the frequency, rate, or extent of interleukin-6 production.
positive regulation of interleukin-8 production Any process that activates or increases the frequency, rate, or extent of interleukin-8 production.
positive regulation of JNK cascade Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the JNK cascade.
positive regulation of macrophage cytokine production Any process that increases the rate, frequency or extent of macrophage cytokine production. Macrophage cytokine production is the appearance of a chemokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
positive regulation of NF-kappaB transcription factor activity Any process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB.
positive regulation of phagocytosis Any process that activates or increases the frequency, rate or extent of phagocytosis.
positive regulation of release of cytochrome c from mitochondria Any process that increases the rate, frequency or extent of release of cytochrome c from mitochondria, the process in which cytochrome c is enabled to move from the mitochondrial intermembrane space into the cytosol, which is an early step in apoptosis and leads to caspase activation.
positive regulation of T cell activation Any process that activates or increases the frequency, rate or extent of T cell activation.
positive regulation of T cell migration Any process that activates or increases the frequency, rate or extent of T cell migration.
positive regulation of tumor necrosis factor production Any process that activates or increases the frequency, rate or extent of tumor necrosis factor production.
protein homooligomerization 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.
pyroptosis A caspase-1-dependent cell death subroutine that is associated with the generation of pyrogenic mediators such as IL-1beta and IL-18.
regulation of apoptotic process Any process that modulates the occurrence or rate of cell death by apoptotic process.
regulation of autophagy Any process that modulates the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.
regulation of cysteine-type endopeptidase activity involved in apoptotic process Any process that modulates the activity of a cysteine-type endopeptidase involved in apoptosis.
regulation of GTPase activity Any process that modulates the rate of GTP hydrolysis by a GTPase.
regulation of inflammatory response 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.
regulation of intrinsic apoptotic signaling pathway Any process that modulates the frequency, rate or extent of intrinsic apoptotic signaling pathway.
regulation of protein stability Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.
regulation of tumor necrosis factor-mediated signaling pathway Any process that modulates the rate or extent of the tumor necrosis factor-mediated signaling pathway. The tumor necrosis factor-mediated signaling pathway is the series of molecular signals generated as a consequence of tumor necrosis factor binding to a cell surface receptor.
response to bacterium Any 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 stimulus from a bacterium.
tumor necrosis factor-mediated signaling pathway The 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.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
A1Z198 Nlrp1b NACHT, LRR and PYD domains-containing protein 1b allele 2 Mus musculus (Mouse) SS
Q2LKU9 Nlrp1a NACHT, LRR and PYD domains-containing protein 1a Mus musculus (Mouse) SS
10 20 30 40 50 60
MGRARDAILD ALENLSGDEL KKFKMKLLTV QLREGYGRIP RGALLQMDAI DLTDKLVSYY
70 80 90 100 110 120
LESYGLELTM TVLRDMGLQE LAEQLQTTKE ESGAVAAAAS VPAQSTARTG HFVDQHRQAL
130 140 150 160 170 180
IARVTEVDGV LDALHGSVLT EGQYQAVRAE TTSQDKMRKL FSFVPSWNLT CKDSLLQALK
190
EIHPYLVMDL EQS