FADD

Summary: This row projects FADD onto a broad immune or host-defense readout.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a mouse organismal phenotype downstream of Fadd deficiency.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: The protease binding row reflects FADD recruitment of CASP8/CASP10 rather than an arbitrary protease or protein interaction.

Reason: Narrowing this to caspase binding preserves the supported initiator-caspase interaction and removes the uninformative generic binding term.

Proposed replacements: caspase binding

Summary: The protease binding row reflects FADD recruitment of CASP8/CASP10 rather than an arbitrary protease or protein interaction.

Reason: Narrowing this to caspase binding preserves the supported initiator-caspase interaction and removes the uninformative generic binding term.

Proposed replacements: caspase binding

Summary: The protease binding row reflects homotypic death-effector-domain contacts.

Reason: Death effector domain binding is more precise than a broad CASP8 or CFLAR protein-binding/protease-binding assertion.

Proposed replacements: death effector domain binding

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: FADD binds cytoplasmic death domains of activated FAS/TRAIL/TNFR-family receptors.

Reason: This receptor-binding activity is one side of the core FADD adaptor function that nucleates death-inducing signaling complexes.

Summary: FADD binds cytoplasmic death domains of activated FAS/TRAIL/TNFR-family receptors.

Reason: This receptor-binding activity is one side of the core FADD adaptor function that nucleates death-inducing signaling complexes.

Summary: FADD binds cytoplasmic death domains of activated FAS/TRAIL/TNFR-family receptors.

Reason: This receptor-binding activity is one side of the core FADD adaptor function that nucleates death-inducing signaling complexes.

Summary: This generic protein-binding import does not establish an informative FADD molecular function.

Reason: The row is either a high-throughput physical edge, a partner-specific screen hit, or a downstream contextual interaction that should not be promoted to a GO function for FADD.

Summary: The curated interaction is best understood as adaptor recruitment into a death, MAVS, or TNFR1 signaling platform.

Reason: Protein-macromolecule adaptor activity captures FADD bridging of DD-fold signaling proteins better than a bare protein-binding row.

Proposed replacements: protein-macromolecule adaptor activity

Summary: The locally cached evidence does not expose enough of the experiment to judge this annotation confidently.

Reason: Per GO review guidelines, this row is left unresolved because the accessible title/abstract is not sufficient to decide whether the curated FADD assertion is direct, contextual, or over-scoped.

Summary: This generic protein-binding import does not establish an informative FADD molecular function.

Reason: The row is either a high-throughput physical edge, a partner-specific screen hit, or a downstream contextual interaction that should not be promoted to a GO function for FADD.

Summary: The locally cached evidence does not expose enough of the experiment to judge this annotation confidently.

Reason: Per GO review guidelines, this row is left unresolved because the accessible title/abstract is not sufficient to decide whether the curated FADD assertion is direct, contextual, or over-scoped.

Summary: The locally cached evidence does not expose enough of the experiment to judge this annotation confidently.

Reason: Per GO review guidelines, this row is left unresolved because the accessible title/abstract is not sufficient to decide whether the curated FADD assertion is direct, contextual, or over-scoped.

Summary: The protein binding row reflects FADD recruitment of CASP8/CASP10 rather than an arbitrary protease or protein interaction.

Reason: Narrowing this to caspase binding preserves the supported initiator-caspase interaction and removes the uninformative generic binding term.

Proposed replacements: caspase binding

Summary: This generic protein-binding import does not establish an informative FADD molecular function.

Reason: The row is either a high-throughput physical edge, a partner-specific screen hit, or a downstream contextual interaction that should not be promoted to a GO function for FADD.

Summary: The curated interaction is best understood as adaptor recruitment into a death, MAVS, or TNFR1 signaling platform.

Reason: Protein-macromolecule adaptor activity captures FADD bridging of DD-fold signaling proteins better than a bare protein-binding row.

Proposed replacements: protein-macromolecule adaptor activity

Summary: The curated interaction involves a death-domain-containing TNF receptor family member.

Reason: Death receptor binding is the informative FADD molecular function for FAS, TRAIL receptor, or TNFR-superfamily cytoplasmic-tail binding.

Proposed replacements: death receptor binding

Summary: This generic protein-binding import does not establish an informative FADD molecular function.

Reason: The row is either a high-throughput physical edge, a partner-specific screen hit, or a downstream contextual interaction that should not be promoted to a GO function for FADD.

Summary: The locally cached evidence does not expose enough of the experiment to judge this annotation confidently.

Reason: Per GO review guidelines, this row is left unresolved because the accessible title/abstract is not sufficient to decide whether the curated FADD assertion is direct, contextual, or over-scoped.

Summary: The curated interaction involves a death-domain-containing TNF receptor family member.

Reason: Death receptor binding is the informative FADD molecular function for FAS, TRAIL receptor, or TNFR-superfamily cytoplasmic-tail binding.

Proposed replacements: death receptor binding

Summary: The protein binding row reflects FADD recruitment of CASP8/CASP10 rather than an arbitrary protease or protein interaction.

Reason: Narrowing this to caspase binding preserves the supported initiator-caspase interaction and removes the uninformative generic binding term.

Proposed replacements: caspase binding

Summary: This generic protein-binding import does not establish an informative FADD molecular function.

Reason: The row is either a high-throughput physical edge, a partner-specific screen hit, or a downstream contextual interaction that should not be promoted to a GO function for FADD.

Summary: The protein binding row reflects FADD recruitment of CASP8/CASP10 rather than an arbitrary protease or protein interaction.

Reason: Narrowing this to caspase binding preserves the supported initiator-caspase interaction and removes the uninformative generic binding term.

Proposed replacements: caspase binding

Summary: The curated interaction involves a death-domain-containing TNF receptor family member.

Reason: Death receptor binding is the informative FADD molecular function for FAS, TRAIL receptor, or TNFR-superfamily cytoplasmic-tail binding.

Proposed replacements: death receptor binding

Summary: The protein binding row reflects FADD recruitment of CASP8/CASP10 rather than an arbitrary protease or protein interaction.

Reason: Narrowing this to caspase binding preserves the supported initiator-caspase interaction and removes the uninformative generic binding term.

Proposed replacements: caspase binding

Summary: The curated interaction involves a death-domain-containing TNF receptor family member.

Reason: Death receptor binding is the informative FADD molecular function for FAS, TRAIL receptor, or TNFR-superfamily cytoplasmic-tail binding.

Proposed replacements: death receptor binding

Summary: This generic protein-binding import does not establish an informative FADD molecular function.

Reason: The row is either a high-throughput physical edge, a partner-specific screen hit, or a downstream contextual interaction that should not be promoted to a GO function for FADD.

Summary: The protein binding row reflects FADD recruitment of CASP8/CASP10 rather than an arbitrary protease or protein interaction.

Reason: Narrowing this to caspase binding preserves the supported initiator-caspase interaction and removes the uninformative generic binding term.

Proposed replacements: caspase binding

Summary: The curated interaction is best understood as adaptor recruitment into a death, MAVS, or TNFR1 signaling platform.

Reason: Protein-macromolecule adaptor activity captures FADD bridging of DD-fold signaling proteins better than a bare protein-binding row.

Proposed replacements: protein-macromolecule adaptor activity

Summary: The protein binding row reflects FADD recruitment of CASP8/CASP10 rather than an arbitrary protease or protein interaction.

Reason: Narrowing this to caspase binding preserves the supported initiator-caspase interaction and removes the uninformative generic binding term.

Proposed replacements: caspase binding

Summary: This generic protein-binding import does not establish an informative FADD molecular function.

Reason: The row is either a high-throughput physical edge, a partner-specific screen hit, or a downstream contextual interaction that should not be promoted to a GO function for FADD.

Summary: The curated interaction involves a death-domain-containing TNF receptor family member.

Reason: Death receptor binding is the informative FADD molecular function for FAS, TRAIL receptor, or TNFR-superfamily cytoplasmic-tail binding.

Proposed replacements: death receptor binding

Summary: The curated interaction involves a death-domain-containing TNF receptor family member.

Reason: Death receptor binding is the informative FADD molecular function for FAS, TRAIL receptor, or TNFR-superfamily cytoplasmic-tail binding.

Proposed replacements: death receptor binding

Summary: This generic protein-binding import does not establish an informative FADD molecular function.

Reason: The row is either a high-throughput physical edge, a partner-specific screen hit, or a downstream contextual interaction that should not be promoted to a GO function for FADD.

Summary: The curated interaction is best understood as adaptor recruitment into a death, MAVS, or TNFR1 signaling platform.

Reason: Protein-macromolecule adaptor activity captures FADD bridging of DD-fold signaling proteins better than a bare protein-binding row.

Proposed replacements: protein-macromolecule adaptor activity

Summary: The protein binding row reflects FADD recruitment of CASP8/CASP10 rather than an arbitrary protease or protein interaction.

Reason: Narrowing this to caspase binding preserves the supported initiator-caspase interaction and removes the uninformative generic binding term.

Proposed replacements: caspase binding

Summary: The curated interaction is best understood as adaptor recruitment into a death, MAVS, or TNFR1 signaling platform.

Reason: Protein-macromolecule adaptor activity captures FADD bridging of DD-fold signaling proteins better than a bare protein-binding row.

Proposed replacements: protein-macromolecule adaptor activity

Summary: The protein binding row reflects FADD recruitment of CASP8/CASP10 rather than an arbitrary protease or protein interaction.

Reason: Narrowing this to caspase binding preserves the supported initiator-caspase interaction and removes the uninformative generic binding term.

Proposed replacements: caspase binding

Summary: The curated interaction involves a death-domain-containing TNF receptor family member.

Reason: Death receptor binding is the informative FADD molecular function for FAS, TRAIL receptor, or TNFR-superfamily cytoplasmic-tail binding.

Proposed replacements: death receptor binding

Summary: This generic protein-binding import does not establish an informative FADD molecular function.

Reason: The row is either a high-throughput physical edge, a partner-specific screen hit, or a downstream contextual interaction that should not be promoted to a GO function for FADD.

Summary: The curated interaction involves a death-domain-containing TNF receptor family member.

Reason: Death receptor binding is the informative FADD molecular function for FAS, TRAIL receptor, or TNFR-superfamily cytoplasmic-tail binding.

Proposed replacements: death receptor binding

Summary: The protein binding row reflects FADD recruitment of CASP8/CASP10 rather than an arbitrary protease or protein interaction.

Reason: Narrowing this to caspase binding preserves the supported initiator-caspase interaction and removes the uninformative generic binding term.

Proposed replacements: caspase binding

Summary: This generic protein-binding import does not establish an informative FADD molecular function.

Reason: The row is either a high-throughput physical edge, a partner-specific screen hit, or a downstream contextual interaction that should not be promoted to a GO function for FADD.

Summary: The locally cached evidence does not expose enough of the experiment to judge this annotation confidently.

Reason: Per GO review guidelines, this row is left unresolved because the accessible title/abstract is not sufficient to decide whether the curated FADD assertion is direct, contextual, or over-scoped.

Summary: This generic protein-binding import does not establish an informative FADD molecular function.

Reason: The row is either a high-throughput physical edge, a partner-specific screen hit, or a downstream contextual interaction that should not be promoted to a GO function for FADD.

Summary: This generic protein-binding import does not establish an informative FADD molecular function.

Reason: The row is either a high-throughput physical edge, a partner-specific screen hit, or a downstream contextual interaction that should not be promoted to a GO function for FADD.

Summary: This generic protein-binding import does not establish an informative FADD molecular function.

Reason: The row is either a high-throughput physical edge, a partner-specific screen hit, or a downstream contextual interaction that should not be promoted to a GO function for FADD.

Summary: This generic protein-binding import does not establish an informative FADD molecular function.

Reason: The row is either a high-throughput physical edge, a partner-specific screen hit, or a downstream contextual interaction that should not be promoted to a GO function for FADD.

Summary: The locally cached evidence does not expose enough of the experiment to judge this annotation confidently.

Reason: Per GO review guidelines, this row is left unresolved because the accessible title/abstract is not sufficient to decide whether the curated FADD assertion is direct, contextual, or over-scoped.

Summary: The protein binding row reflects FADD recruitment of CASP8/CASP10 rather than an arbitrary protease or protein interaction.

Reason: Narrowing this to caspase binding preserves the supported initiator-caspase interaction and removes the uninformative generic binding term.

Proposed replacements: caspase binding

Summary: The curated interaction is best understood as adaptor recruitment into a death, MAVS, or TNFR1 signaling platform.

Reason: Protein-macromolecule adaptor activity captures FADD bridging of DD-fold signaling proteins better than a bare protein-binding row.

Proposed replacements: protein-macromolecule adaptor activity

Summary: The NleB1 interaction describes a bacterial effector modifying FADD rather than an activity of FADD.

Reason: FADD is the substrate of pathogen arginine GlcNAcylation, so this generic protein-binding row would assign the effector-side mechanism to the host target.

Summary: This FASL/FAS proximity or sensitization interaction does not establish a distinct FADD molecular function.

Reason: The relevant FADD role is already captured by death receptor binding, DISC assembly, and caspase binding; this row adds only a generic interaction edge.

Summary: The protein binding row reflects FADD recruitment of CASP8/CASP10 rather than an arbitrary protease or protein interaction.

Reason: Narrowing this to caspase binding preserves the supported initiator-caspase interaction and removes the uninformative generic binding term.

Proposed replacements: caspase binding

Summary: This FASL/FAS proximity or sensitization interaction does not establish a distinct FADD molecular function.

Reason: The relevant FADD role is already captured by death receptor binding, DISC assembly, and caspase binding; this row adds only a generic interaction edge.

Summary: This FASL/FAS proximity or sensitization interaction does not establish a distinct FADD molecular function.

Reason: The relevant FADD role is already captured by death receptor binding, DISC assembly, and caspase binding; this row adds only a generic interaction edge.

Summary: This FASL/FAS proximity or sensitization interaction does not establish a distinct FADD molecular function.

Reason: The relevant FADD role is already captured by death receptor binding, DISC assembly, and caspase binding; this row adds only a generic interaction edge.

Summary: This generic protein-binding import does not establish an informative FADD molecular function.

Reason: The row is either a high-throughput physical edge, a partner-specific screen hit, or a downstream contextual interaction that should not be promoted to a GO function for FADD.

Summary: The curated interaction involves a death-domain-containing TNF receptor family member.

Reason: Death receptor binding is the informative FADD molecular function for FAS, TRAIL receptor, or TNFR-superfamily cytoplasmic-tail binding.

Proposed replacements: death receptor binding

Summary: The curated interaction is best understood as adaptor recruitment into a death, MAVS, or TNFR1 signaling platform.

Reason: Protein-macromolecule adaptor activity captures FADD bridging of DD-fold signaling proteins better than a bare protein-binding row.

Proposed replacements: protein-macromolecule adaptor activity

Summary: The protein binding row reflects FADD recruitment of CASP8/CASP10 rather than an arbitrary protease or protein interaction.

Reason: Narrowing this to caspase binding preserves the supported initiator-caspase interaction and removes the uninformative generic binding term.

Proposed replacements: caspase binding

Summary: The curated interaction is best understood as adaptor recruitment into a death, MAVS, or TNFR1 signaling platform.

Reason: Protein-macromolecule adaptor activity captures FADD bridging of DD-fold signaling proteins better than a bare protein-binding row.

Proposed replacements: protein-macromolecule adaptor activity

Summary: This HuRI/BioPlex or other large-scale protein-binding row is not enough to define a FADD molecular function.

Reason: High-throughput generic protein-binding imports are uninformative for a well-defined signaling adaptor and should not be retained as GO functions.

Summary: This HuRI/BioPlex or other large-scale protein-binding row is not enough to define a FADD molecular function.

Reason: High-throughput generic protein-binding imports are uninformative for a well-defined signaling adaptor and should not be retained as GO functions.

Summary: This HuRI/BioPlex or other large-scale protein-binding row is not enough to define a FADD molecular function.

Reason: High-throughput generic protein-binding imports are uninformative for a well-defined signaling adaptor and should not be retained as GO functions.

Summary: This HuRI/BioPlex or other large-scale protein-binding row is not enough to define a FADD molecular function.

Reason: High-throughput generic protein-binding imports are uninformative for a well-defined signaling adaptor and should not be retained as GO functions.

Summary: This HuRI/BioPlex or other large-scale protein-binding row is not enough to define a FADD molecular function.

Reason: High-throughput generic protein-binding imports are uninformative for a well-defined signaling adaptor and should not be retained as GO functions.

Summary: This HuRI/BioPlex or other large-scale protein-binding row is not enough to define a FADD molecular function.

Reason: High-throughput generic protein-binding imports are uninformative for a well-defined signaling adaptor and should not be retained as GO functions.

Summary: This HuRI/BioPlex or other large-scale protein-binding row is not enough to define a FADD molecular function.

Reason: High-throughput generic protein-binding imports are uninformative for a well-defined signaling adaptor and should not be retained as GO functions.

Summary: This HuRI/BioPlex or other large-scale protein-binding row is not enough to define a FADD molecular function.

Reason: High-throughput generic protein-binding imports are uninformative for a well-defined signaling adaptor and should not be retained as GO functions.

Summary: This HuRI/BioPlex or other large-scale protein-binding row is not enough to define a FADD molecular function.

Reason: High-throughput generic protein-binding imports are uninformative for a well-defined signaling adaptor and should not be retained as GO functions.

Summary: This HuRI/BioPlex or other large-scale protein-binding row is not enough to define a FADD molecular function.

Reason: High-throughput generic protein-binding imports are uninformative for a well-defined signaling adaptor and should not be retained as GO functions.

Summary: This HuRI/BioPlex or other large-scale protein-binding row is not enough to define a FADD molecular function.

Reason: High-throughput generic protein-binding imports are uninformative for a well-defined signaling adaptor and should not be retained as GO functions.

Summary: This HuRI/BioPlex or other large-scale protein-binding row is not enough to define a FADD molecular function.

Reason: High-throughput generic protein-binding imports are uninformative for a well-defined signaling adaptor and should not be retained as GO functions.

Summary: This HuRI/BioPlex or other large-scale protein-binding row is not enough to define a FADD molecular function.

Reason: High-throughput generic protein-binding imports are uninformative for a well-defined signaling adaptor and should not be retained as GO functions.

Summary: This HuRI/BioPlex or other large-scale protein-binding row is not enough to define a FADD molecular function.

Reason: High-throughput generic protein-binding imports are uninformative for a well-defined signaling adaptor and should not be retained as GO functions.

Summary: This HuRI/BioPlex or other large-scale protein-binding row is not enough to define a FADD molecular function.

Reason: High-throughput generic protein-binding imports are uninformative for a well-defined signaling adaptor and should not be retained as GO functions.

Summary: This HuRI/BioPlex or other large-scale protein-binding row is not enough to define a FADD molecular function.

Reason: High-throughput generic protein-binding imports are uninformative for a well-defined signaling adaptor and should not be retained as GO functions.

Summary: The curated interaction involves a death-domain-containing TNF receptor family member.

Reason: Death receptor binding is the informative FADD molecular function for FAS, TRAIL receptor, or TNFR-superfamily cytoplasmic-tail binding.

Proposed replacements: death receptor binding

Summary: The curated interaction involves a death-domain-containing TNF receptor family member.

Reason: Death receptor binding is the informative FADD molecular function for FAS, TRAIL receptor, or TNFR-superfamily cytoplasmic-tail binding.

Proposed replacements: death receptor binding

Summary: The curated interaction involves a death-domain-containing TNF receptor family member.

Reason: Death receptor binding is the informative FADD molecular function for FAS, TRAIL receptor, or TNFR-superfamily cytoplasmic-tail binding.

Proposed replacements: death receptor binding

Summary: The protein binding row reflects FADD recruitment of CASP8/CASP10 rather than an arbitrary protease or protein interaction.

Reason: Narrowing this to caspase binding preserves the supported initiator-caspase interaction and removes the uninformative generic binding term.

Proposed replacements: caspase binding

Summary: The protein binding row reflects FADD recruitment of CASP8/CASP10 rather than an arbitrary protease or protein interaction.

Reason: Narrowing this to caspase binding preserves the supported initiator-caspase interaction and removes the uninformative generic binding term.

Proposed replacements: caspase binding

Summary: The protein binding row reflects homotypic death-effector-domain contacts.

Reason: Death effector domain binding is more precise than a broad CASP8 or CFLAR protein-binding/protease-binding assertion.

Proposed replacements: death effector domain binding

Summary: The locally cached evidence does not expose enough of the experiment to judge this annotation confidently.

Reason: Per GO review guidelines, this row is left unresolved because the accessible title/abstract is not sufficient to decide whether the curated FADD assertion is direct, contextual, or over-scoped.

Summary: FADD has reported nucleoplasmic localization, but this is separate from the canonical cytosolic DISC adaptor role.

Reason: Nuclear FADD biology is plausible and experimentally curated, yet the apoptosis review should keep it non-core until a direct nuclear molecular function is resolved.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is a soluble cytoplasmic/cytosolic adaptor recruited into membrane-proximal and cytosolic death-signaling complexes.

Reason: Cytosol/cytoplasm is the correct compartment for FADD before and during FAS, TRAIL, TNFR1, TLR, MAVS, and ripoptosome complex assembly.

Summary: FADD is recruited to the cytoplasmic face of activated death receptors rather than being a plasma-membrane integral protein.

Reason: The cytoplasmic side of plasma membrane term captures receptor-proximal DISC recruitment more precisely than plasma membrane.

Proposed replacements: cytoplasmic side of plasma membrane

Summary: The broad apoptosis or signaling term should be narrowed to death-domain-receptor extrinsic apoptotic signaling.

Reason: FADD directly bridges death-domain receptors to initiator caspases, so the supported biological-process term is the FAS/TRAIL/TNFR branch rather than generic apoptosis or signaling.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: This row projects FADD onto a broad immune or host-defense readout.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: The broad apoptosis or signaling term should be narrowed to death-domain-receptor extrinsic apoptotic signaling.

Reason: FADD directly bridges death-domain receptors to initiator caspases, so the supported biological-process term is the FAS/TRAIL/TNFR branch rather than generic apoptosis or signaling.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: FADD is a scaffold subunit of caspase-8/cFLIP DED assemblies.

Reason: The 2024 structural work directly places FADD in caspase-containing DED assemblies, so the caspase-complex cellular component is supported.

Summary: FADD directly mediates death-domain-receptor extrinsic apoptotic signaling by recruiting CASP8 or CASP10 to the DISC.

Reason: This is the canonical biological process executed by the FADD adaptor at FAS, TRAIL, and TNFR1 death platforms.

Summary: FADD directly mediates death-domain-receptor extrinsic apoptotic signaling by recruiting CASP8 or CASP10 to the DISC.

Reason: This is the canonical biological process executed by the FADD adaptor at FAS, TRAIL, and TNFR1 death platforms.

Summary: FADD directly mediates death-domain-receptor extrinsic apoptotic signaling by recruiting CASP8 or CASP10 to the DISC.

Reason: This is the canonical biological process executed by the FADD adaptor at FAS, TRAIL, and TNFR1 death platforms.

Summary: FADD acts on the cytoplasmic side of ligand-bound death receptors.

Reason: The adaptor binds the intracellular death domains of activated receptor trimers before DED-mediated procaspase recruitment.

Summary: FADD functions as a signaling adaptor between receptor or RIP-family death domains and CASP8/CASP10/CFLAR DED assemblies.

Reason: The term captures the core noncatalytic molecular work of FADD: bridging upstream death-domain platforms to downstream initiator caspases.

Summary: FADD functions as a signaling adaptor between receptor or RIP-family death domains and CASP8/CASP10/CFLAR DED assemblies.

Reason: The term captures the core noncatalytic molecular work of FADD: bridging upstream death-domain platforms to downstream initiator caspases.

Summary: FADD functions as a signaling adaptor between receptor or RIP-family death domains and CASP8/CASP10/CFLAR DED assemblies.

Reason: The term captures the core noncatalytic molecular work of FADD: bridging upstream death-domain platforms to downstream initiator caspases.

Summary: FADD is a core adaptor component of the death-inducing signaling complex.

Reason: FADD links receptor death domains to initiator caspase DEDs in productive CD95 and related death-inducing signaling complexes.

Summary: FADD is a death-inducing signaling complex component; this row is a generic DISC assertion from the PMLRARalpha/Fas paper.

Reason: Even though the local cache does not expose the PMLRARalpha experiment in full, FADD membership in the DISC is a direct, core property established across FAS death-receptor literature.

Summary: FADD is a core adaptor component of the death-inducing signaling complex.

Reason: FADD links receptor death domains to initiator caspase DEDs in productive CD95 and related death-inducing signaling complexes.

Summary: FADD is a core adaptor component of the death-inducing signaling complex.

Reason: FADD links receptor death domains to initiator caspase DEDs in productive CD95 and related death-inducing signaling complexes.

Summary: FADD is a core adaptor component of the CD95 death-inducing signaling complex.

Reason: FADD links receptor death domains to initiator caspase DEDs in productive CD95 and related death-inducing signaling complexes.

Summary: FADD is a core adaptor component of the CD95 death-inducing signaling complex.

Reason: FADD links receptor death domains to initiator caspase DEDs in productive CD95 and related death-inducing signaling complexes.

Summary: FADD is a core adaptor component of the CD95 death-inducing signaling complex.

Reason: FADD links receptor death domains to initiator caspase DEDs in productive CD95 and related death-inducing signaling complexes.

Summary: This row projects FADD onto a broad immune or host-defense readout.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a broad immune or host-defense readout.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: FADD can contribute to MAVS/RIG-I-like receptor antiviral and cytokine outputs.

Reason: These innate immune rows capture a real secondary branch of FADD signaling, but they are not the core death-receptor adaptor function.

Summary: FADD can contribute to MAVS/RIG-I-like receptor antiviral and cytokine outputs.

Reason: These innate immune rows capture a real secondary branch of FADD signaling, but they are not the core death-receptor adaptor function.

Summary: The curated interaction involves a death-domain-containing TNF receptor family member.

Reason: Death receptor binding is the informative FADD molecular function for FAS, TRAIL receptor, or TNFR-superfamily cytoplasmic-tail binding.

Proposed replacements: death receptor binding

Summary: The protein-containing complex is a death-inducing signaling complex.

Reason: FADD is not merely in an unspecified protein complex; its core complex context is the DISC.

Proposed replacements: death-inducing signaling complex

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: Receptor serine/threonine kinase binding (IEA), transferred from rat Fadd, where the annotated partners are the receptor-interacting kinases RIPK1 and RIPK3 rather than a receptor kinase.

Reason: The row is transferred from rat Fadd, where the term rests on a physical-interaction annotation from a study of FADD in RIPK1- and RIPK3-dependent programmed necrosis of cardiomyocytes (PMID:26038570). RIPK1 and RIPK3 are receptor-interacting serine/threonine kinases, cytosolic kinases recruited to death-receptor complexes, whereas this term is defined as binding to a receptor that itself possesses protein serine/threonine kinase activity, such as the TGF-beta receptor family. The source annotation therefore uses a term that does not describe the interaction it records, and nothing indicates that FADD binds a receptor serine/threonine kinase. The FADD-RIPK1 interaction itself is real but is not what this term states.

Summary: FADD functions as a signaling adaptor between receptor or RIP-family death domains and CASP8/CASP10/CFLAR DED assemblies.

Reason: The term captures the core noncatalytic molecular work of FADD: bridging upstream death-domain platforms to downstream initiator caspases.

Summary: FADD binds death-effector domains in CASP8, CASP10, and CFLAR-family partners.

Reason: DED binding is the specific molecular contact used by FADD to recruit initiator procaspases and cFLIP to death signaling platforms.

Summary: FADD binds death-effector domains in CASP8, CASP10, and CFLAR-family partners.

Reason: DED binding is the specific molecular contact used by FADD to recruit initiator procaspases and cFLIP to death signaling platforms.

Summary: FADD transduces TRAIL receptor signaling by linking ligand-bound TNFRSF10A/B to CASP8 at the DISC.

Reason: TRAIL-activated apoptotic signaling is a direct death-receptor context for FADD adaptor activity.

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a mouse organismal phenotype downstream of Fadd deficiency.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: FADD-FADD interaction recovered in a yeast two-hybrid interaction-profiling study of disease variants; consistent with the self-association shown in the early DISC studies.

Reason: FADD self-association is accepted in this review on the two early direct studies annotated to the same term, where oligomerization is treated as part of productive DISC assembly. This row reports the same FADD-FADD interaction from a yeast two-hybrid interaction-profiling study of disease variants; a systematic screen adds little mechanistic detail, but its result agrees with the directly demonstrated self-association and nothing contradicts it. Rows that share a term are judged alike, and duplication is not a ground for removing a true annotation, so the row is accepted with the others.

Summary: FADD-FADD interaction recovered with FADD as a bait in a Virotrap map of the TNF-induced signalling pathway; consistent with the self-association shown in the early DISC studies.

Reason: FADD self-association is accepted in this review on the two early direct studies annotated to the same term, where oligomerization is treated as part of productive DISC assembly. This row reports the same FADD-FADD interaction from a Virotrap interaction map of the TNF-induced signalling pathway in which FADD was one of the baits; a systematic screen adds little mechanistic detail, but its result agrees with the directly demonstrated self-association and nothing contradicts it. Rows that share a term are judged alike, and duplication is not a ground for removing a true annotation, so the row is accepted with the others.

Summary: FADD-FADD interaction recovered in a large-scale binary interaction study of genetic variants; consistent with the self-association shown in the early DISC studies.

Reason: FADD self-association is accepted in this review on the two early direct studies annotated to the same term, where oligomerization is treated as part of productive DISC assembly. This row reports the same FADD-FADD interaction from a large-scale binary interaction study of the effects of genetic variants; a systematic screen adds little mechanistic detail, but its result agrees with the directly demonstrated self-association and nothing contradicts it. Rows that share a term are judged alike, and duplication is not a ground for removing a true annotation, so the row is accepted with the others.

Summary: FADD-FADD interaction recovered in the systematic binary interaction map of the human proteome; consistent with the self-association shown in the early DISC studies.

Reason: FADD self-association is accepted in this review on the two early direct studies annotated to the same term, where oligomerization is treated as part of productive DISC assembly. This row reports the same FADD-FADD interaction from the systematic binary interaction map of the human proteome; a systematic screen adds little mechanistic detail, but its result agrees with the directly demonstrated self-association and nothing contradicts it. Rows that share a term are judged alike, and duplication is not a ground for removing a true annotation, so the row is accepted with the others.

Summary: FADD can self-associate through its death-effector-domain surface.

Reason: FADD oligomerization contributes to productive DISC architecture rather than being an isolated generic homomeric interaction.

Summary: FADD can self-associate through its death-effector-domain surface.

Reason: FADD oligomerization contributes to productive DISC architecture rather than being an isolated generic homomeric interaction.

Summary: The broad apoptosis or signaling term should be narrowed to death-domain-receptor extrinsic apoptotic signaling.

Reason: FADD directly bridges death-domain receptors to initiator caspases, so the supported biological-process term is the FAS/TRAIL/TNFR branch rather than generic apoptosis or signaling.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: The locally cached evidence does not expose enough of the experiment to judge this annotation confidently.

Reason: Per GO review guidelines, this row is left unresolved because the accessible title/abstract is not sufficient to decide whether the curated FADD assertion is direct, contextual, or over-scoped.

Summary: The broad apoptosis or signaling term should be narrowed to death-domain-receptor extrinsic apoptotic signaling.

Reason: FADD directly bridges death-domain receptors to initiator caspases, so the supported biological-process term is the FAS/TRAIL/TNFR branch rather than generic apoptosis or signaling.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: This row projects FADD onto a downstream cellular phenotype rather than a direct FADD step.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a downstream cellular phenotype rather than a direct FADD step.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: The curated interaction is best understood as adaptor recruitment into a death, MAVS, or TNFR1 signaling platform.

Reason: Protein-macromolecule adaptor activity captures FADD bridging of DD-fold signaling proteins better than a bare protein-binding row.

Proposed replacements: protein-macromolecule adaptor activity

Summary: FADD can contribute to MAVS/RIG-I-like receptor antiviral and cytokine outputs.

Reason: These innate immune rows capture a real secondary branch of FADD signaling, but they are not the core death-receptor adaptor function.

Summary: This row projects FADD onto a downstream cellular phenotype rather than a direct FADD step.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: FADD assembles a procaspase-activating DISC instead of generally increasing proteolysis.

Reason: Death-inducing signaling complex assembly captures the direct step performed by FADD upstream of CASP8 activation.

Proposed replacements: death-inducing signaling complex assembly

Summary: This row projects FADD onto a downstream cellular phenotype rather than a direct FADD step.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a mouse organismal phenotype downstream of Fadd deficiency.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a broad immune or host-defense readout.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: FADD can contribute to MAVS/RIG-I-like receptor antiviral and cytokine outputs.

Reason: These innate immune rows capture a real secondary branch of FADD signaling, but they are not the core death-receptor adaptor function.

Summary: This row projects FADD onto a broad immune or host-defense readout.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: FADD can contribute to MAVS/RIG-I-like receptor antiviral and cytokine outputs.

Reason: These innate immune rows capture a real secondary branch of FADD signaling, but they are not the core death-receptor adaptor function.

Summary: FADD participates in RIPK1/CASP8-containing ripoptosome or necroptotic signaling platforms.

Reason: The RIPK1/caspase-8/cFLIP branch is a supported cytosolic cell-death context, but it is secondary to FADD recruitment at FAS/TRAIL/TNFR death receptors.

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a downstream cellular phenotype rather than a direct FADD step.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: FADD is required to assemble the CASP8-activating death-inducing signaling complex.

Reason: FADD recruitment and DED polymerization are direct assembly steps that recruit procaspase-8 into receptor-proximal DISCs.

Summary: FADD is required to assemble the CASP8-activating death-inducing signaling complex.

Reason: FADD recruitment and DED polymerization are direct assembly steps that recruit procaspase-8 into receptor-proximal DISCs.

Summary: FADD binds initiator caspases CASP8 and CASP10 via death-effector-domain contacts.

Reason: Caspase binding is the downstream side of the FADD adaptor bridge in FAS, TRAIL, TNFR1, and related death complexes.

Summary: FADD binds initiator caspases CASP8 and CASP10 via death-effector-domain contacts.

Reason: Caspase binding is the downstream side of the FADD adaptor bridge in FAS, TRAIL, TNFR1, and related death complexes.

Summary: FADD binds initiator caspases CASP8 and CASP10 via death-effector-domain contacts.

Reason: Caspase binding is the downstream side of the FADD adaptor bridge in FAS, TRAIL, TNFR1, and related death complexes.

Summary: This FAS-dependent RIPK1 death-signaling row is specifically about a necroptotic branch.

Reason: The apoptotic-signaling parent should be replaced by necroptotic signaling for the RIP-dependent alternative death pathway.

Proposed replacements: necroptotic signaling pathway

Summary: The broad apoptosis or signaling term should be narrowed to death-domain-receptor extrinsic apoptotic signaling.

Reason: FADD directly bridges death-domain receptors to initiator caspases, so the supported biological-process term is the FAS/TRAIL/TNFR branch rather than generic apoptosis or signaling.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: The broad apoptosis or signaling term should be narrowed to death-domain-receptor extrinsic apoptotic signaling.

Reason: FADD directly bridges death-domain receptors to initiator caspases, so the supported biological-process term is the FAS/TRAIL/TNFR branch rather than generic apoptosis or signaling.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: The TRAIL evidence should use the TRAIL-activated descendant of extrinsic apoptotic signaling.

Reason: The FADD step is downstream of TNFRSF10A/B rather than a generic extrinsic apoptotic signaling event.

Proposed replacements: TRAIL-activated apoptotic signaling pathway

Summary: The broad apoptosis or signaling term should be narrowed to death-domain-receptor extrinsic apoptotic signaling.

Reason: FADD directly bridges death-domain receptors to initiator caspases, so the supported biological-process term is the FAS/TRAIL/TNFR branch rather than generic apoptosis or signaling.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: The broad apoptosis or signaling term should be narrowed to death-domain-receptor extrinsic apoptotic signaling.

Reason: FADD directly bridges death-domain receptors to initiator caspases, so the supported biological-process term is the FAS/TRAIL/TNFR branch rather than generic apoptosis or signaling.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: The broad apoptosis or signaling term should be narrowed to death-domain-receptor extrinsic apoptotic signaling.

Reason: FADD directly bridges death-domain receptors to initiator caspases, so the supported biological-process term is the FAS/TRAIL/TNFR branch rather than generic apoptosis or signaling.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: FADD participates in RIPK1/CASP8-containing ripoptosome or necroptotic signaling platforms.

Reason: The RIPK1/caspase-8/cFLIP branch is a supported cytosolic cell-death context, but it is secondary to FADD recruitment at FAS/TRAIL/TNFR death receptors.

Summary: FADD participates in RIPK1/CASP8-containing ripoptosome or necroptotic signaling platforms.

Reason: The RIPK1/caspase-8/cFLIP branch is a supported cytosolic cell-death context, but it is secondary to FADD recruitment at FAS/TRAIL/TNFR death receptors.

Summary: The broad apoptosis or signaling term should be narrowed to death-domain-receptor extrinsic apoptotic signaling.

Reason: FADD directly bridges death-domain receptors to initiator caspases, so the supported biological-process term is the FAS/TRAIL/TNFR branch rather than generic apoptosis or signaling.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: This row projects FADD onto a transferred mouse T-cell, lymphoid-organ, or immune phenotype.

Reason: FADD is an adaptor for death-receptor, RIPK1, and antiviral signaling complexes; this term is too broad or phenotype-level for the direct work of the human FADD protein.

Summary: The broad apoptosis or signaling term should be narrowed to death-domain-receptor extrinsic apoptotic signaling.

Reason: FADD directly bridges death-domain receptors to initiator caspases, so the supported biological-process term is the FAS/TRAIL/TNFR branch rather than generic apoptosis or signaling.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: The TWEAK/FN14 evidence supports extrinsic apoptotic signaling without establishing a specific death-domain receptor subclass.

Reason: Extrinsic apoptotic signaling is a better scope than positive regulation of the whole process for this contextual TNFRSF12A/TNF pathway.

Proposed replacements: extrinsic apoptotic signaling pathway