The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Death Domain, Fas
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 31: Caspase 1, isoform CRA_b

Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

There are 20 GO terms relating to "molecular function"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
6 P29452 (/IPI) P29466 (/IPI) P43527 (/IPI) P57730 (/IPI) Q5EG05 (/IPI) Q5XLA6 (/IPI)
CARD domain binding GO:0050700
Interacting selectively and non-covalently with 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.
3 P29466 (/IPI) P57730 (/IPI) Q5EG05 (/IPI)
Caspase binding GO:0089720
Interacting selectively and non-covalently with a caspase family protein.
3 P57730 (/IPI) Q5EG05 (/IPI) Q5XLA6 (/IPI)
Cysteine-type endopeptidase activity GO:0004197
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.
2 P29452 (/IDA) P29466 (/IDA)
Kinase binding GO:0019900
Interacting selectively and non-covalently with a kinase, any enzyme that catalyzes the transfer of a phosphate group.
2 P29466 (/IPI) Q5EG05 (/IPI)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
2 Q5EG05 (/IDA) Q5XLA6 (/IDA)
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
1 P29466 (/IDA)
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
1 P29452 (/ISO)
Cysteine-type endopeptidase activity GO:0004197
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.
1 P29452 (/ISO)
Cysteine-type endopeptidase activity GO:0004197
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.
1 P29466 (/TAS)
Cysteine-type endopeptidase inhibitor activity GO:0004869
Stops, prevents or reduces the activity of a cysteine-type endopeptidase, any enzyme that hydrolyzes peptide bonds in polypeptides by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile.
1 Q5EG05 (/IDA)
Peptidase activity GO:0008233
Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
1 P29452 (/IDA)
Cysteine-type endopeptidase activator activity involved in apoptotic process GO:0008656
Increases the rate of proteolysis catalyzed by a cysteine-type endopeptidase involved in the apoptotic process.
1 P29466 (/TAS)
Kinase binding GO:0019900
Interacting selectively and non-covalently with a kinase, any enzyme that catalyzes the transfer of a phosphate group.
1 P29452 (/ISO)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
1 P29466 (/IMP)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
1 P29466 (/IPI)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
1 P29452 (/ISO)
CARD domain binding GO:0050700
Interacting selectively and non-covalently with 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.
1 P29452 (/ISO)
Scaffold protein binding GO:0097110
Interacting selectively and non-covalently with a scaffold protein. Scaffold proteins are crucial regulators of many key signaling pathways. Although not strictly defined in function, they are known to interact and/or bind with multiple members of a signaling pathway, tethering them into complexes.
1 P43527 (/IPI)
Scaffold protein binding GO:0097110
Interacting selectively and non-covalently with a scaffold protein. Scaffold proteins are crucial regulators of many key signaling pathways. Although not strictly defined in function, they are known to interact and/or bind with multiple members of a signaling pathway, tethering them into complexes.
1 P29452 (/ISO)

There are 80 GO terms relating to "biological process"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Negative regulation of interleukin-1 beta secretion GO:0050713
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of interleukin-1 beta from a cell.
3 P57730 (/IDA) Q5EG05 (/IDA) Q5XLA6 (/IDA)
Positive regulation of interleukin-1 beta secretion GO:0050718
Any process that activates or increases the frequency, rate or extent of the regulated release of interleukin-1 beta from a cell.
3 P29452 (/IMP) P29466 (/IMP) P43527 (/IMP)
Negative regulation of protein binding GO:0032091
Any process that stops, prevents, or reduces the frequency, rate or extent of protein binding.
2 P57730 (/IDA) Q5EG05 (/IDA)
Positive regulation of I-kappaB kinase/NF-kappaB signaling GO:0043123
Any process that activates or increases the frequency, rate or extent of I-kappaB kinase/NF-kappaB signaling.
2 P29452 (/IDA) Q5EG05 (/IDA)
Positive regulation of cytokine secretion GO:0050715
Any process that activates or increases the frequency, rate or extent of the regulated release of cytokines from a cell.
2 P29452 (/IMP) P43527 (/IMP)
Cellular response to lipopolysaccharide GO:0071222
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.
2 Q5EG05 (/IDA) Q5XLA6 (/IDA)
Inhibition of cysteine-type endopeptidase activity GO:0097340
Any process that prevents the activation of an inactive cysteine-type endopeptidase.
2 P57730 (/IDA) Q5EG05 (/IDA)
Response to hypoxia GO:0001666
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 indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.
1 P43527 (/IDA)
Response to hypoxia GO:0001666
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 indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.
1 P29452 (/IMP)
Response to hypoxia GO:0001666
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 indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.
1 P29452 (/ISO)
Microglial cell activation GO:0001774
The change in morphology and behavior of a microglial cell resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor.
1 P43527 (/IMP)
Microglial cell activation GO:0001774
The change in morphology and behavior of a microglial cell resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor.
1 P29452 (/ISO)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
1 P29466 (/IDA)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
1 P29452 (/ISO)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
1 P29466 (/TAS)
Apoptotic process GO:0006915
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.
1 P43527 (/IEP)
Apoptotic process GO:0006915
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.
1 P29466 (/TAS)
Inflammatory response GO:0006954
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.
1 P57730 (/NAS)
Signal transduction GO:0007165
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.
1 P29466 (/TAS)
Midgut development GO:0007494
The process whose specific outcome is the progression of the midgut over time, from its formation to the mature structure. The midgut is the middle part of the alimentary canal from the stomach, or entrance of the bile duct, to, or including, the large intestine.
1 P43527 (/IEP)
Myoblast fusion GO:0007520
A process in which non-proliferating myoblasts fuse to existing fibers or to myotubes to form new fibers. A myoblast is a mononucleate cell type that, by fusion with other myoblasts, gives rise to the myotubes that eventually develop into skeletal muscle fibers.
1 P43527 (/IMP)
Myoblast fusion GO:0007520
A process in which non-proliferating myoblasts fuse to existing fibers or to myotubes to form new fibers. A myoblast is a mononucleate cell type that, by fusion with other myoblasts, gives rise to the myotubes that eventually develop into skeletal muscle fibers.
1 P29452 (/ISO)
Memory GO:0007613
The activities involved in the mental information processing system that receives (registers), modifies, stores, and retrieves informational stimuli. The main stages involved in the formation and retrieval of memory are encoding (processing of received information by acquisition), storage (building a permanent record of received information as a result of consolidation) and retrieval (calling back the stored information and use it in a suitable way to execute a given task).
1 P43527 (/IMP)
Memory GO:0007613
The activities involved in the mental information processing system that receives (registers), modifies, stores, and retrieves informational stimuli. The main stages involved in the formation and retrieval of memory are encoding (processing of received information by acquisition), storage (building a permanent record of received information as a result of consolidation) and retrieval (calling back the stored information and use it in a suitable way to execute a given task).
1 P29452 (/ISO)
Response to bacterium GO:0009617
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.
1 P29452 (/IMP)
Response to toxic substance GO:0009636
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 toxic stimulus.
1 P43527 (/IEP)
Regulation of autophagy GO:0010506
Any process that modulates the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.
1 P29452 (/IMP)
Negative regulation of tumor necrosis factor-mediated signaling pathway GO:0010804
Any process that decreases 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.
1 Q5EG05 (/IMP)
Response to organic cyclic compound GO:0014070
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 an organic cyclic compound stimulus.
1 P43527 (/IDA)
Response to organic cyclic compound GO:0014070
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 an organic cyclic compound stimulus.
1 P29452 (/ISO)
Protein processing GO:0016485
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
1 P29452 (/IDA)
Protein processing GO:0016485
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
1 P29452 (/IMP)
Protein autoprocessing GO:0016540
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.
1 P29466 (/IDA)
Protein autoprocessing GO:0016540
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.
1 P29452 (/ISO)
Cytokine-mediated signaling pathway GO:0019221
A series of molecular signals initiated by the binding of a cytokine to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
1 P29466 (/TAS)
Lung development GO:0030324
The process whose specific outcome is the progression of the lung over time, from its formation to the mature structure. In all air-breathing vertebrates the lungs are developed from the ventral wall of the oesophagus as a pouch which divides into two sacs. In amphibians and many reptiles the lungs retain very nearly this primitive sac-like character, but in the higher forms the connection with the esophagus becomes elongated into the windpipe and the inner walls of the sacs become more and more divided, until, in the mammals, the air spaces become minutely divided into tubes ending in small air cells, in the walls of which the blood circulates in a fine network of capillaries. In mammals the lungs are more or less divided into lobes, and each lung occupies a separate cavity in the thorax.
1 P43527 (/IEP)
Negative regulation of lipopolysaccharide-mediated signaling pathway GO:0031665
Any process that stops, prevents, or reduces the frequency, rate or extent of signaling in response to detection of lipopolysaccharide.
1 Q5EG05 (/IDA)
Response to lipopolysaccharide GO:0032496
Any process that results in a change in state or activity of an organism (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.
1 P29452 (/IDA)
Response to lipopolysaccharide GO:0032496
Any process that results in a change in state or activity of an organism (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.
1 P43527 (/IMP)
Response to lipopolysaccharide GO:0032496
Any process that results in a change in state or activity of an organism (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.
1 P29452 (/ISO)
Interleukin-1 beta production GO:0032611
The appearance of interleukin-1 beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
1 P29452 (/IGI)
Positive regulation of interleukin-1 beta production GO:0032731
Any process that activates or increases the frequency, rate, or extent of interleukin-1 beta production.
1 P29466 (/IMP)
Positive regulation of interleukin-1 beta production GO:0032731
Any process that activates or increases the frequency, rate, or extent of interleukin-1 beta production.
1 P29452 (/ISO)
Response to ATP GO:0033198
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 an ATP (adenosine 5'-triphosphate) stimulus.
1 P29452 (/IMP)
Response to drug GO:0042493
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 drug stimulus. A drug is a substance used in the diagnosis, treatment or prevention of a disease.
1 P43527 (/IDA)
Response to drug GO:0042493
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 drug stimulus. A drug is a substance used in the diagnosis, treatment or prevention of a disease.
1 P29452 (/ISO)
Regulation of apoptotic process GO:0042981
Any process that modulates the occurrence or rate of cell death by apoptotic process.
1 P29466 (/TAS)
Positive regulation of apoptotic process GO:0043065
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
1 P43527 (/IMP)
Positive regulation of apoptotic process GO:0043065
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
1 P29452 (/ISO)
Positive regulation of I-kappaB kinase/NF-kappaB signaling GO:0043123
Any process that activates or increases the frequency, rate or extent of I-kappaB kinase/NF-kappaB signaling.
1 P29466 (/IEP)
Positive regulation of I-kappaB kinase/NF-kappaB signaling GO:0043123
Any process that activates or increases the frequency, rate or extent of I-kappaB kinase/NF-kappaB signaling.
1 P29466 (/IMP)
Positive regulation of I-kappaB kinase/NF-kappaB signaling GO:0043123
Any process that activates or increases the frequency, rate or extent of I-kappaB kinase/NF-kappaB signaling.
1 P29452 (/ISO)
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic process GO:0043154
Any process that stops, prevents, or reduces the frequency, rate or extent of a cysteine-type endopeptidase activity involved in the apoptotic process.
1 Q5EG05 (/IDA)
Positive regulation of cysteine-type endopeptidase activity involved in apoptotic process GO:0043280
Any process that activates or increases the activity of a cysteine-type endopeptidase involved in the apoptotic process.
1 P29466 (/IMP)
Positive regulation of cysteine-type endopeptidase activity involved in apoptotic process GO:0043280
Any process that activates or increases the activity of a cysteine-type endopeptidase involved in the apoptotic process.
1 P29452 (/ISO)
Positive regulation of circadian sleep/wake cycle, non-REM sleep GO:0046010
Any process that activates or increases the duration or quality of non-rapid eye movement (NREM) sleep.
1 P43527 (/IMP)
Positive regulation of circadian sleep/wake cycle, non-REM sleep GO:0046010
Any process that activates or increases the duration or quality of non-rapid eye movement (NREM) sleep.
1 P29452 (/ISO)
Positive regulation of cytokine secretion GO:0050715
Any process that activates or increases the frequency, rate or extent of the regulated release of cytokines from a cell.
1 P29452 (/ISO)
Positive regulation of interleukin-1 alpha secretion GO:0050717
Any process that activates or increases the frequency, rate or extent of the regulated release of interleukin-1 alpha from a cell.
1 P29452 (/IMP)
Positive regulation of interleukin-1 beta secretion GO:0050718
Any process that activates or increases the frequency, rate or extent of the regulated release of interleukin-1 beta from a cell.
1 P29466 (/IDA)
Positive regulation of interleukin-1 beta secretion GO:0050718
Any process that activates or increases the frequency, rate or extent of the regulated release of interleukin-1 beta from a cell.
1 P29452 (/ISO)
Regulation of inflammatory response GO:0050727
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.
1 P29452 (/IMP)
Positive regulation of NF-kappaB transcription factor activity GO:0051092
Any process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB.
1 Q5EG05 (/IDA)
Mitochondrial depolarization GO:0051882
The process in which the potential difference across the mitochondrial membrane is reduced from its steady state level.
1 P29452 (/IMP)
Membrane hyperpolarization GO:0060081
The process in which membrane potential increases with respect to its steady-state potential, usually from negative potential to a more negative potential. For example, during the repolarization phase of an action potential the membrane potential often becomes more negative or hyperpolarized before returning to the steady-state resting potential.
1 P29452 (/IMP)
Pyroptosis GO:0070269
A caspase-1-dependent cell death subroutine that is associated with the generation of pyrogenic mediators such as IL-1beta and IL-18.
1 P29452 (/IMP)
Cellular response to lipopolysaccharide GO:0071222
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.
1 P29466 (/IMP)
Cellular response to lipopolysaccharide GO:0071222
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.
1 P29452 (/ISO)
Cellular response to mechanical stimulus GO:0071260
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.
1 P29466 (/IEP)
Cellular response to organic substance GO:0071310
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 organic substance stimulus.
1 P29466 (/IDA)
Cellular response to organic substance GO:0071310
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 organic substance stimulus.
1 P29452 (/ISO)
Cellular response to cytokine stimulus GO:0071345
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 cytokine stimulus.
1 P29466 (/TAS)
Cellular response to interferon-gamma GO:0071346
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.
1 P29466 (/IMP)
Cellular response to interferon-gamma GO:0071346
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.
1 P29452 (/ISO)
Cellular response to hypoxia GO:0071456
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 indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.
1 Q5EG05 (/IDA)
Cellular response to UV-C GO:0071494
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 UV-C radiation stimulus. UV-C radiation (UV-C light) spans the wavelengths 100 to 280 nm.
1 Q5EG05 (/IDA)
Programmed necrotic cell death GO:0097300
A necrotic cell death process that results from the activation of endogenous cellular processes, such as signaling involving death domain receptors or Toll-like receptors.
1 P29452 (/IDA)
Toxin transport GO:1901998
The directed movement of a toxin into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
1 P29452 (/IMP)
Positive regulation of tumor necrosis factor-mediated signaling pathway GO:1903265
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor-mediated signaling pathway.
1 P29466 (/IMP)
Positive regulation of tumor necrosis factor-mediated signaling pathway GO:1903265
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor-mediated signaling pathway.
1 P29452 (/ISO)

There are 26 GO terms relating to "cellular component"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
IPAF inflammasome complex GO:0072557
A protein 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.
6 P29466 (/ISS) P43527 (/ISS) Q9MZV6 (/ISS) Q9MZV7 (/ISS) Q9N2I1 (/ISS) Q9TV13 (/ISS)
NLRP1 inflammasome complex GO:0072558
A protein 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.
6 P29452 (/ISS) P43527 (/ISS) Q9MZV6 (/ISS) Q9MZV7 (/ISS) Q9N2I1 (/ISS) Q9TV13 (/ISS)
NLRP3 inflammasome complex GO:0072559
A protein 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.
6 P29452 (/ISS) P43527 (/ISS) Q9MZV6 (/ISS) Q9MZV7 (/ISS) Q9N2I1 (/ISS) Q9TV13 (/ISS)
AIM2 inflammasome complex GO:0097169
A protein 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.
6 P29452 (/ISS) P43527 (/ISS) Q9MZV6 (/ISS) Q9MZV7 (/ISS) Q9N2I1 (/ISS) Q9TV13 (/ISS)
Protein-containing complex GO:0032991
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.
5 P29466 (/IDA) P43527 (/IDA) P57730 (/IDA) Q5EG05 (/IDA) Q5XLA6 (/IDA)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
2 P29452 (/TAS) P29466 (/TAS)
Extracellular region GO:0005576
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.
1 P29452 (/IDA)
Nucleus GO:0005634
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.
1 P43527 (/IDA)
Nucleus GO:0005634
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.
1 P29452 (/ISO)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 P43527 (/IDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 P29452 (/ISO)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 P29452 (/TAS)
Protein-containing complex GO:0032991
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.
1 P29466 (/IMP)
Protein-containing complex GO:0032991
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.
1 P29452 (/ISO)
Neuron projection GO:0043005
A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
1 P43527 (/IDA)
Neuron projection GO:0043005
A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
1 P29452 (/ISO)
IPAF inflammasome complex GO:0072557
A protein 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.
1 P29452 (/IDA)
NLRP1 inflammasome complex GO:0072558
A protein 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.
1 P29466 (/IDA)
NLRP1 inflammasome complex GO:0072558
A protein 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.
1 P29452 (/ISO)
NLRP3 inflammasome complex GO:0072559
A protein 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.
1 P29466 (/IDA)
NLRP3 inflammasome complex GO:0072559
A protein 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.
1 P29452 (/ISO)
AIM2 inflammasome complex GO:0097169
A protein 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.
1 P29466 (/IDA)
AIM2 inflammasome complex GO:0097169
A protein 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.
1 P29452 (/ISO)
Protease inhibitor complex GO:0097179
A heterodimeric protein complex that contains a protease inhibitor and a protease; formation of the complex inhibits protease activity.
1 Q5EG05 (/IDA)
Protease inhibitor complex GO:0097179
A heterodimeric protein complex that contains a protease inhibitor and a protease; formation of the complex inhibits protease activity.
1 P29466 (/IMP)
Protease inhibitor complex GO:0097179
A heterodimeric protein complex that contains a protease inhibitor and a protease; formation of the complex inhibits protease activity.
1 P29452 (/ISO)
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