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 21: caspase-8 isoform X1

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 32 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
Cysteine-type endopeptidase activity involved in apoptotic process GO:0097153
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.
24 A0A2I3HAC6 (/ISS) B2CMK5 (/ISS) F7BWD5 (/ISS) F7IAY8 (/ISS) G1LHK8 (/ISS) G1PSK3 (/ISS) G3TKG8 (/ISS) G7N8N1 (/ISS) G7N8N1 (/ISS) H2P8A2 (/ISS)
(14 more)
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.
5 O89110 (/IDA) O89110 (/IDA) Q14790 (/IDA) Q14790 (/IDA) Q9JHX4 (/IDA)
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).
5 O89110 (/IPI) O89110 (/IPI) Q14790 (/IPI) Q14790 (/IPI) Q9JHX4 (/IPI)
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.
4 O89110 (/IDA) O89110 (/IDA) Q14790 (/IDA) Q14790 (/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.
4 O89110 (/IMP) O89110 (/IMP) Q14790 (/IMP) Q14790 (/IMP)
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
2 O89110 (/IDA) O89110 (/IDA)
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
2 O89110 (/IMP) O89110 (/IMP)
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 O89110 (/IGI) O89110 (/IGI)
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 O89110 (/ISO) O89110 (/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.
2 Q14790 (/TAS) Q14790 (/TAS)
Death receptor binding GO:0005123
Interacting selectively and non-covalently with any member of the death receptor (DR) family. The DR family falls within the tumor necrosis factor receptor superfamily and is characterized by a cytoplasmic region of ~80 residues termed the death domain (DD).
2 O89110 (/ISO) O89110 (/ISO)
Tumor necrosis factor receptor binding GO:0005164
Interacting selectively and non-covalently with the tumor necrosis factor receptor.
2 O89110 (/ISO) O89110 (/ISO)
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.
2 O89110 (/ISO) O89110 (/ISO)
Cysteine-type peptidase activity GO:0008234
Catalysis of the hydrolysis of 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 Q14790 (/TAS) Q14790 (/TAS)
Ubiquitin protein ligase binding GO:0031625
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
2 Q14790 (/IPI) Q14790 (/IPI)
Ubiquitin protein ligase binding GO:0031625
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
2 O89110 (/ISO) O89110 (/ISO)
Death effector domain binding GO:0035877
Interacting selectively and non-covalently with a DED domain (death effector domain) of a protein, a homotypic protein interaction module composed of a bundle of six alpha-helices that is related in structure to the death domain (DD).
2 Q14790 (/IPI) Q14790 (/IPI)
Death effector domain binding GO:0035877
Interacting selectively and non-covalently with a DED domain (death effector domain) of a protein, a homotypic protein interaction module composed of a bundle of six alpha-helices that is related in structure to the death domain (DD).
2 O89110 (/ISO) O89110 (/ISO)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
2 Q14790 (/IPI) Q14790 (/IPI)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
2 O89110 (/ISO) O89110 (/ISO)
Protein-containing complex binding GO:0044877
Interacting selectively and non-covalently with a macromolecular complex.
2 O89110 (/ISO) O89110 (/ISO)
Protein heterodimerization activity GO:0046982
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
2 O89110 (/IPI) O89110 (/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.
2 Q14790 (/IPI) Q14790 (/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.
2 O89110 (/ISO) O89110 (/ISO)
Cysteine-type endopeptidase activity involved in apoptotic process GO:0097153
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.
2 O89110 (/IDA) O89110 (/IDA)
Cysteine-type endopeptidase activity involved in apoptotic process GO:0097153
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.
2 Q14790 (/IMP) Q14790 (/IMP)
Cysteine-type endopeptidase activity involved in apoptotic process GO:0097153
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.
2 O89110 (/ISO) O89110 (/ISO)
Cysteine-type endopeptidase activity involved in apoptotic signaling pathway GO:0097199
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 signaling pathway.
2 Q14790 (/IMP) Q14790 (/IMP)
Cysteine-type endopeptidase activity involved in apoptotic signaling pathway GO:0097199
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 signaling pathway.
2 O89110 (/ISO) O89110 (/ISO)
Death receptor binding GO:0005123
Interacting selectively and non-covalently with any member of the death receptor (DR) family. The DR family falls within the tumor necrosis factor receptor superfamily and is characterized by a cytoplasmic region of ~80 residues termed the death domain (DD).
1 Q9JHX4 (/IPI)
Tumor necrosis factor receptor binding GO:0005164
Interacting selectively and non-covalently with the tumor necrosis factor receptor.
1 Q9JHX4 (/IPI)
Protein-containing complex binding GO:0044877
Interacting selectively and non-covalently with a macromolecular complex.
1 Q9JHX4 (/IPI)

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
Execution phase of apoptosis GO:0097194
A stage of the apoptotic process that starts with the controlled breakdown of the cell through the action of effector caspases or other effector molecules (e.g. cathepsins, calpains etc.). Key steps of the execution phase are 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.
26 A0A2I3HAC6 (/ISS) B2CMK5 (/ISS) F7BWD5 (/ISS) F7IAY8 (/ISS) G1LHK8 (/ISS) G1PSK3 (/ISS) G3TKG8 (/ISS) G7N8N1 (/ISS) G7N8N1 (/ISS) H2P8A2 (/ISS)
(16 more)
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.
23 A0A2I3HAC6 (/ISS) B2CMK5 (/ISS) F7BWD5 (/ISS) F7IAY8 (/ISS) G1LHK8 (/ISS) G1PSK3 (/ISS) G3TKG8 (/ISS) G7N8N1 (/ISS) G7N8N1 (/ISS) H2P8A2 (/ISS)
(13 more)
Macrophage differentiation GO:0030225
The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage.
4 O89110 (/TAS) O89110 (/TAS) Q14790 (/TAS) Q14790 (/TAS)
Extrinsic apoptotic signaling pathway GO:0097191
A series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with either a ligand binding to a cell surface receptor, or a ligand being withdrawn from a cell surface receptor (e.g. in the case of signaling by dependence receptors), and ends when the execution phase of apoptosis is triggered.
4 O89110 (/IDA) O89110 (/IDA) Q14790 (/IDA) Q14790 (/IDA)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
3 Q14790 (/IDA) Q14790 (/IDA) Q9JHX4 (/IDA)
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.
3 Q14790 (/IMP) Q14790 (/IMP) Q9JHX4 (/IMP)
Angiogenesis GO:0001525
Blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels.
2 O89110 (/IMP) O89110 (/IMP)
Neural tube formation GO:0001841
The formation of a tube from the flat layer of ectodermal cells known as the neural plate. This will give rise to the central nervous system.
2 O89110 (/IMP) O89110 (/IMP)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
2 O89110 (/ISO) O89110 (/ISO)
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.
2 O89110 (/IDA) O89110 (/IDA)
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.
2 Q14790 (/IGI) Q14790 (/IGI)
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.
2 O89110 (/ISO) O89110 (/ISO)
Activation of cysteine-type endopeptidase activity involved in apoptotic process GO:0006919
Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process.
2 O89110 (/IDA) O89110 (/IDA)
Activation of cysteine-type endopeptidase activity involved in apoptotic process GO:0006919
Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process.
2 Q14790 (/TAS) Q14790 (/TAS)
Cell surface receptor signaling pathway GO:0007166
A series of molecular signals initiated by activation of a receptor on the surface of a cell. The pathway begins with binding of an extracellular ligand to a cell surface receptor, or for receptors that signal in the absence of a ligand, by ligand-withdrawal or the activity of a constitutively active receptor. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
2 Q14790 (/TAS) Q14790 (/TAS)
Heart development GO:0007507
The process whose specific outcome is the progression of the heart over time, from its formation to the mature structure. The heart is a hollow, muscular organ, which, by contracting rhythmically, keeps up the circulation of the blood.
2 O89110 (/IMP) O89110 (/IMP)
Extrinsic apoptotic signaling pathway via death domain receptors GO:0008625
A series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with a ligand binding to a death domain receptor on the cell surface, and ends when the execution phase of apoptosis is triggered.
2 O89110 (/IMP) O89110 (/IMP)
Regulation of tumor necrosis factor-mediated signaling pathway GO:0010803
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.
2 Q14790 (/TAS) Q14790 (/TAS)
Natural killer cell activation GO:0030101
The change in morphology and behavior of a natural killer cell in response to a cytokine, chemokine, cellular ligand, or soluble factor.
2 Q14790 (/TAS) Q14790 (/TAS)
Macrophage differentiation GO:0030225
The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage.
2 O89110 (/IMP) O89110 (/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.
2 Q14790 (/IMP) Q14790 (/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.
2 O89110 (/ISO) O89110 (/ISO)
Toll-like receptor 3 signaling pathway GO:0034138
Any series of molecular signals generated as a consequence of binding to toll-like receptor 3.
2 Q14790 (/TAS) Q14790 (/TAS)
Response to tumor necrosis factor GO:0034612
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 tumor necrosis factor stimulus.
2 Q14790 (/IMP) Q14790 (/IMP)
Response to tumor necrosis factor GO:0034612
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 tumor necrosis factor stimulus.
2 O89110 (/ISO) O89110 (/ISO)
TRIF-dependent toll-like receptor signaling pathway GO:0035666
Any series of molecular signals generated as a consequence of binding to a toll-like receptor where the TRIF adaptor mediates transduction of the signal. Toll-like receptors directly bind pattern motifs from a variety of microbial sources to initiate innate immune response.
2 Q14790 (/TAS) Q14790 (/TAS)
TRAIL-activated apoptotic signaling pathway GO:0036462
An extrinsic apoptotic signaling pathway initiated by the binding of the ligand TRAIL (tumor necrosis factor-related apoptosis-inducing ligand) to a death receptor on the cell surface.
2 Q14790 (/IDA) Q14790 (/IDA)
TRAIL-activated apoptotic signaling pathway GO:0036462
An extrinsic apoptotic signaling pathway initiated by the binding of the ligand TRAIL (tumor necrosis factor-related apoptosis-inducing ligand) to a death receptor on the cell surface.
2 O89110 (/ISO) O89110 (/ISO)
Suppression by virus of host cysteine-type endopeptidase activity involved in apoptotic process GO:0039650
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host caspase activity. Caspases are cysteine-type endopeptidases which contribute to the apoptotic process.
2 Q14790 (/TAS) Q14790 (/TAS)
T cell activation GO:0042110
The change in morphology and behavior of a mature or immature T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
2 Q14790 (/TAS) Q14790 (/TAS)
B cell activation GO:0042113
The change in morphology and behavior of a mature or immature B cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
2 Q14790 (/TAS) Q14790 (/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.
2 O89110 (/IDA) O89110 (/IDA)
Positive regulation of apoptotic process GO:0043065
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
2 O89110 (/IMP) O89110 (/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.
2 Q14790 (/IEP) Q14790 (/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.
2 Q14790 (/IMP) Q14790 (/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.
2 O89110 (/ISO) O89110 (/ISO)
Negative regulation of I-kappaB kinase/NF-kappaB signaling GO:0043124
Any process that stops, prevents, or reduces the frequency, rate or extent of -kappaB kinase/NF-kappaB signaling.
2 Q14790 (/IMP) Q14790 (/IMP)
Negative regulation of I-kappaB kinase/NF-kappaB signaling GO:0043124
Any process that stops, prevents, or reduces the frequency, rate or extent of -kappaB kinase/NF-kappaB signaling.
2 O89110 (/ISO) O89110 (/ISO)
Response to ethanol GO:0045471
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 ethanol stimulus.
2 O89110 (/ISO) O89110 (/ISO)
Positive regulation of macrophage differentiation GO:0045651
Any process that activates or increases the frequency, rate or extent of macrophage differentiation.
2 Q14790 (/IMP) Q14790 (/IMP)
Positive regulation of macrophage differentiation GO:0045651
Any process that activates or increases the frequency, rate or extent of macrophage differentiation.
2 O89110 (/ISO) O89110 (/ISO)
Positive regulation of proteolysis GO:0045862
Any process that activates or increases the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein.
2 Q14790 (/IDA) Q14790 (/IDA)
Positive regulation of proteolysis GO:0045862
Any process that activates or increases the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein.
2 O89110 (/ISO) O89110 (/ISO)
Cardiac muscle tissue development GO:0048738
The process whose specific outcome is the progression of cardiac muscle over time, from its formation to the mature structure.
2 O89110 (/TAS) O89110 (/TAS)
Proteolysis involved in cellular protein catabolic process GO:0051603
The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
2 Q14790 (/IMP) Q14790 (/IMP)
Proteolysis involved in cellular protein catabolic process GO:0051603
The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
2 O89110 (/ISO) O89110 (/ISO)
Regulation of necroptotic process GO:0060544
Any process that modulates the rate, frequency or extent of a necroptotic process, 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.
2 Q14790 (/TAS) Q14790 (/TAS)
Negative regulation of necroptotic process GO:0060546
Any process that decreases the rate, frequency or extent of a necroptotic process, 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.
2 O89110 (/IGI) O89110 (/IGI)
Syncytiotrophoblast cell differentiation involved in labyrinthine layer development GO:0060715
The process in which a chorionic trophoblast cell acquires specialized features of a syncytiotrophoblast of the labyrinthine layer of the placenta.
2 Q14790 (/TAS) Q14790 (/TAS)
Regulation of thymocyte apoptotic process GO:0070243
Any process that modulates the occurrence or rate of thymocyte death by apoptotic process.
2 O89110 (/IGI) O89110 (/IGI)
Nucleotide-binding oligomerization domain containing signaling pathway GO:0070423
Any series of molecular signals generated as a consequence of binding to a nucleotide-binding oligomerization domain containing (NOD) protein.
2 Q14790 (/TAS) Q14790 (/TAS)
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.
2 Q14790 (/IEP) Q14790 (/IEP)
Death-inducing signaling complex assembly GO:0071550
A process of protein complex assembly in which the arrangement and bonding together of the set of components that form the protein complex is mediated by a death domain (DD) interaction, as part of the extrinsic apoptotic signaling pathway.
2 Q14790 (/TAS) Q14790 (/TAS)
Apoptotic signaling pathway GO:0097190
A series of molecular signals which triggers the apoptotic death of a cell. The pathway starts with reception of a signal, and ends when the execution phase of apoptosis is triggered.
2 O89110 (/IDA) O89110 (/IDA)
Apoptotic signaling pathway GO:0097190
A series of molecular signals which triggers the apoptotic death of a cell. The pathway starts with reception of a signal, and ends when the execution phase of apoptosis is triggered.
2 Q14790 (/IMP) Q14790 (/IMP)
Apoptotic signaling pathway GO:0097190
A series of molecular signals which triggers the apoptotic death of a cell. The pathway starts with reception of a signal, and ends when the execution phase of apoptosis is triggered.
2 O89110 (/ISO) O89110 (/ISO)
Apoptotic signaling pathway GO:0097190
A series of molecular signals which triggers the apoptotic death of a cell. The pathway starts with reception of a signal, and ends when the execution phase of apoptosis is triggered.
2 Q14790 (/TAS) Q14790 (/TAS)
Extrinsic apoptotic signaling pathway GO:0097191
A series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with either a ligand binding to a cell surface receptor, or a ligand being withdrawn from a cell surface receptor (e.g. in the case of signaling by dependence receptors), and ends when the execution phase of apoptosis is triggered.
2 O89110 (/IGI) O89110 (/IGI)
Extrinsic apoptotic signaling pathway GO:0097191
A series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with either a ligand binding to a cell surface receptor, or a ligand being withdrawn from a cell surface receptor (e.g. in the case of signaling by dependence receptors), and ends when the execution phase of apoptosis is triggered.
2 O89110 (/ISO) O89110 (/ISO)
Execution phase of apoptosis GO:0097194
A stage of the apoptotic process that starts with the controlled breakdown of the cell through the action of effector caspases or other effector molecules (e.g. cathepsins, calpains etc.). Key steps of the execution phase are 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.
2 Q14790 (/IMP) Q14790 (/IMP)
Execution phase of apoptosis GO:0097194
A stage of the apoptotic process that starts with the controlled breakdown of the cell through the action of effector caspases or other effector molecules (e.g. cathepsins, calpains etc.). Key steps of the execution phase are 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.
2 O89110 (/ISO) O89110 (/ISO)
Execution phase of apoptosis GO:0097194
A stage of the apoptotic process that starts with the controlled breakdown of the cell through the action of effector caspases or other effector molecules (e.g. cathepsins, calpains etc.). Key steps of the execution phase are 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.
2 Q14790 (/TAS) Q14790 (/TAS)
Activation of cysteine-type endopeptidase activity GO:0097202
Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase.
2 Q14790 (/IDA) Q14790 (/IDA)
Activation of cysteine-type endopeptidase activity GO:0097202
Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase.
2 O89110 (/ISO) O89110 (/ISO)
Hepatocyte apoptotic process GO:0097284
Any apoptotic process in a hepatocyte, the main structural component of the liver.
2 O89110 (/IMP) O89110 (/IMP)
Activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway GO:0097296
Any process that initiates the activity of an inactive cysteine-type endopeptidase involved in the apoptotic signaling pathway.
2 Q14790 (/TAS) Q14790 (/TAS)
Positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway GO:1900740
Any process that activates or increases the frequency, rate or extent of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway.
2 Q14790 (/TAS) Q14790 (/TAS)
Positive regulation of neuron death GO:1901216
Any process that activates or increases the frequency, rate or extent of neuron death.
2 O89110 (/ISO) O89110 (/ISO)
Regulation of extrinsic apoptotic signaling pathway via death domain receptors GO:1902041
Any process that modulates the frequency, rate or extent of extrinsic apoptotic signaling pathway via death domain receptors.
2 Q14790 (/TAS) Q14790 (/TAS)
Negative regulation of extrinsic apoptotic signaling pathway via death domain receptors GO:1902042
Any process that stops, prevents or reduces the frequency, rate or extent of extrinsic apoptotic signaling pathway via death domain receptors.
2 Q14790 (/TAS) Q14790 (/TAS)
Regulation of apoptotic signaling pathway GO:2001233
Any process that modulates the frequency, rate or extent of apoptotic signaling pathway.
2 O89110 (/IGI) O89110 (/IGI)
Positive regulation of extrinsic apoptotic signaling pathway GO:2001238
Any process that activates or increases the frequency, rate or extent of extrinsic apoptotic signaling pathway.
2 O89110 (/IGI) O89110 (/IGI)
Response to cold GO:0009409
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 cold stimulus, a temperature stimulus below the optimal temperature for that organism.
1 Q9JHX4 (/IEP)
Response to cobalt ion GO:0032025
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 cobalt ion stimulus.
1 Q9JHX4 (/IEP)
Response to estradiol GO:0032355
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 stimulus by estradiol, a C18 steroid hormone hydroxylated at C3 and C17 that acts as a potent estrogen.
1 Q9JHX4 (/IEP)
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 Q9JHX4 (/IEP)
Response to ethanol GO:0045471
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 ethanol stimulus.
1 Q9JHX4 (/IDA)
Response to antibiotic GO:0046677
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 antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms.
1 Q9JHX4 (/IEP)
Cellular response to organic cyclic compound GO:0071407
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 cyclic compound stimulus.
1 Q9JHX4 (/IEP)
Positive regulation of neuron death GO:1901216
Any process that activates or increases the frequency, rate or extent of neuron death.
1 Q9JHX4 (/IMP)

There are 30 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
Ripoptosome GO:0097342
A protein complex whose core components are the receptor-interacting serine/threonine-protein kinases RIPK1 and RIPK3 (also called RIP1 and RIP3). Formation of the ripoptosome can induce an extrinsic apoptotic signaling pathway or a necroptotic signaling pathway. The composition of this protein complex may depend on several factors including nature of the signal, cell type and more.
26 A0A2I3HAC6 (/ISS) B2CMK5 (/ISS) F7BWD5 (/ISS) F7IAY8 (/ISS) G1LHK8 (/ISS) G1PSK3 (/ISS) G3TKG8 (/ISS) G7N8N1 (/ISS) G7N8N1 (/ISS) H2P8A2 (/ISS)
(16 more)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
4 A0A024R3Z8 (/IDA) Q14790 (/IDA) Q14790 (/IDA) Q9JHX4 (/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.
3 O89110 (/IDA) O89110 (/IDA) Q9JHX4 (/IDA)
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
3 A0A024R3Z8 (/IDA) Q14790 (/IDA) Q14790 (/IDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
3 O89110 (/IDA) O89110 (/IDA) Q9JHX4 (/IDA)
Death-inducing signaling complex GO:0031264
A protein complex formed by the association of signaling proteins with a death receptor upon ligand binding. The complex includes procaspases and death domain-containing proteins in addition to the ligand-bound receptor, and may control the activation of caspases 8 and 10.
3 Q14790 (/IDA) Q14790 (/IDA) Q9JHX4 (/IDA)
CD95 death-inducing signaling complex GO:0031265
A protein complex formed upon binding of Fas/CD95/APO-1 to its ligand. The complex includes FADD/Mort1, procaspase-8/10 and c-FLIP in addition to the ligand-bound receptor.
3 Q14790 (/IDA) Q14790 (/IDA) Q9JHX4 (/IDA)
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.
3 Q14790 (/IDA) Q14790 (/IDA) Q9JHX4 (/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.
2 O89110 (/ISO) O89110 (/ISO)
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
2 O89110 (/ISO) O89110 (/ISO)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
2 O89110 (/ISO) O89110 (/ISO)
Mitochondrion GO:0005739
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.
2 O89110 (/HDA) O89110 (/HDA)
Mitochondrion GO:0005739
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.
2 Q14790 (/TAS) Q14790 (/TAS)
Mitochondrial outer membrane GO:0005741
The outer, i.e. cytoplasm-facing, lipid bilayer of the mitochondrial envelope.
2 Q14790 (/TAS) Q14790 (/TAS)
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 O89110 (/ISO) O89110 (/ISO)
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 Q14790 (/TAS) Q14790 (/TAS)
Cytoskeleton GO:0005856
Any of the various filamentous elements that form the internal framework of cells, and typically remain after treatment of the cells with mild detergent to remove membrane constituents and soluble components of the cytoplasm. The term embraces intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
2 Q14790 (/TAS) Q14790 (/TAS)
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
2 O89110 (/IDA) O89110 (/IDA)
Noc1p-Noc2p complex GO:0030690
A heterodimer associated with 90S and 66S preribosomes. Predominantly, but not exclusively, nucleolar; involved in ribosomal large subunit biogenesis.
2 O89110 (/IMP) O89110 (/IMP)
Death-inducing signaling complex GO:0031264
A protein complex formed by the association of signaling proteins with a death receptor upon ligand binding. The complex includes procaspases and death domain-containing proteins in addition to the ligand-bound receptor, and may control the activation of caspases 8 and 10.
2 O89110 (/ISO) O89110 (/ISO)
CD95 death-inducing signaling complex GO:0031265
A protein complex formed upon binding of Fas/CD95/APO-1 to its ligand. The complex includes FADD/Mort1, procaspase-8/10 and c-FLIP in addition to the ligand-bound receptor.
2 O89110 (/ISO) O89110 (/ISO)
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.
2 O89110 (/ISO) O89110 (/ISO)
Neuron projection GO:0043005
A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
2 O89110 (/ISO) O89110 (/ISO)
Cell body GO:0044297
The portion of a cell bearing surface projections such as axons, dendrites, cilia, or flagella that includes the nucleus, but excludes all cell projections.
2 O89110 (/ISO) O89110 (/ISO)
Membrane raft GO:0045121
Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
2 O89110 (/ISO) O89110 (/ISO)
Ripoptosome GO:0097342
A protein complex whose core components are the receptor-interacting serine/threonine-protein kinases RIPK1 and RIPK3 (also called RIP1 and RIP3). Formation of the ripoptosome can induce an extrinsic apoptotic signaling pathway or a necroptotic signaling pathway. The composition of this protein complex may depend on several factors including nature of the signal, cell type and more.
2 Q14790 (/IDA) Q14790 (/IDA)
Ripoptosome GO:0097342
A protein complex whose core components are the receptor-interacting serine/threonine-protein kinases RIPK1 and RIPK3 (also called RIP1 and RIP3). Formation of the ripoptosome can induce an extrinsic apoptotic signaling pathway or a necroptotic signaling pathway. The composition of this protein complex may depend on several factors including nature of the signal, cell type and more.
2 O89110 (/ISO) O89110 (/ISO)
Neuron projection GO:0043005
A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
1 Q9JHX4 (/IDA)
Cell body GO:0044297
The portion of a cell bearing surface projections such as axons, dendrites, cilia, or flagella that includes the nucleus, but excludes all cell projections.
1 Q9JHX4 (/IDA)
Membrane raft GO:0045121
Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
1 Q9JHX4 (/IDA)