CASP10 is a tandem-death-effector-domain initiator caspase recruited by FADD to Fas/CD95 and TRAIL death-inducing signaling complexes and to related cytosolic death platforms. Proximity-induced CASP10 activation generates an Asp-directed cysteine endopeptidase that can mature downstream caspases; prodomain-only isoforms can instead scaffold NF-kappaB signaling, and a CASP10-c-FLIP(L) protease complex has a survival role in myeloma cells by cleaving BCLAF1 to restrain autophagic cell death.
Curated functional classes representing distinct biological activities. These may be splice variants, cleavage products, or other forms with different functions.
CASP10_FULL_LENGTHCASP10_CCASP10_7| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004197 cysteine-type endopeptidase activity | IBA GO_REF:0000033 | ACCEPT | Summary: CASP10 is a catalytically active C14A family initiator caspase. Reason: The PAINT active-caspase transfer is appropriate for CASP10 because human CASP10 retains the caspase fold and catalytic His/Cys residues and hydrolyzes Asp-directed peptide substrates. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000047947 SUPPORTS TRANSFER The PAINT active-caspase node transfers to catalytically active human CASP10. Supporting Evidence: file:human/CASP10/CASP10-uniprot.txt Strict requirement for Asp at position P1 and has a preferred file:human/CASP10/CASP10-uniprot.txt FT ACT_SITE 358 file:human/CASP10/CASP10-uniprot.txt FT ACT_SITE 401 file:human/CASP10/CASP10-uniprot.txt DR PANTHER; PTHR48169:SF7; CASPASE 10; 1. |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:16916640 Engineered hybrid dimers: tracking the activation pathway of... | ACCEPT | Summary: CASP10 has Asp-directed cysteine endopeptidase activity. Reason: The cached abstract for this CASP7 activation paper hides the CASP10 assay details, but UniProt uses the study for CASP10 catalytic activity and the activity is independently established for this active initiator caspase. Supporting Evidence: file:human/CASP10/CASP10-uniprot.txt Strict requirement for Asp at position P1 and has a preferred |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:16920334 Protective role of Cop in Rip2/caspase-1/caspase-4-mediated ... | UNDECIDED | Summary: The COP/CARD-only protein abstract does not verify a CASP10-specific catalytic assay. Reason: The full text is unavailable locally, and the abstract is centered on CARD-only protein, RIP2, caspase-1, and caspase-4 rather than the CASP10 activity row. Supporting Evidence: PMID:16920334 Protective role of Cop in Rip2/caspase-1/caspase-4-mediated HeLa cell death. |
| GO:0004197 cysteine-type endopeptidase activity | IEA GO_REF:0000120 | ACCEPT | Summary: The InterPro caspase-domain mapping correctly recovers CASP10 cysteine endopeptidase activity. Reason: Unlike the pseudo-caspase c-FLIP, CASP10 has both p20/p10 peptidase domains and the conserved catalytic residues needed for C14A caspase activity. Supporting Evidence: file:human/CASP10/CASP10-uniprot.txt Strict requirement for Asp at position P1 and has a preferred file:human/CASP10/CASP10-uniprot.txt DR InterPro; IPR001309; Pept_C14_p20. file:human/CASP10/CASP10-uniprot.txt DR InterPro; IPR002138; Pept_C14_p10. |
| GO:0004197 cysteine-type endopeptidase activity | IMP PMID:11717445 Caspase-10 is an initiator caspase in death receptor signali... | ACCEPT | Summary: CASP10 is catalytically active during Fas and TRAIL death-receptor signaling. Reason: Wang et al. established CASP10 as an initiator caspase recruited and activated at Fas and TRAIL receptor complexes. Supporting Evidence: PMID:11717445 caspase-10 can function independently of caspase-8 in PMID:11717445 caspase-8 and -10 both interact with the death-effector domain of FADD. |
| GO:0004197 cysteine-type endopeptidase activity | IMP PMID:21980415 Identification of a conserved anti-apoptotic protein that mo... | ACCEPT | Summary: CASP10 activity is induced in a CAAP-suppressed mitochondrial amplification loop. Reason: CAAP depletion is not the canonical death-receptor context, but the paper measured increased CASP10 activity and a CASP10-dependent apoptotic amplification loop. Supporting Evidence: PMID:21980415 2.6-fold increase in caspase-10 activity for the substrate AEVD-pNA PMID:21980415 requires both caspase-3 and -10 |
| GO:0004197 cysteine-type endopeptidase activity | TAS PMID:10412980 Inherited human Caspase 10 mutations underlie defective lymp... | ACCEPT | Summary: ALPS CASP10 variants reduce death-receptor apoptosis through impaired caspase function. Reason: Inherited CASP10 missense variants decreased caspase activity and disrupted Fas ligand/TRAIL-induced apoptosis, supporting CASP10 as an active apoptotic caspase. Supporting Evidence: PMID:10412980 missense mutations in Caspase 10. These encode amino acid substitutions that decrease caspase activity |
| GO:0004197 cysteine-type endopeptidase activity | TAS PMID:8755496 In vitro activation of CPP32 and Mch3 by Mch4, a novel human... | ACCEPT | Summary: The original Mch4 cloning paper established CASP10 as an active cysteine endopeptidase. Reason: Recombinant Mch4/CASP10 generated an active protease that could cleave downstream effector procaspases in vitro. Supporting Evidence: PMID:8755496 Expression of Mch4 in Escherichia coli produced an active PMID:8755496 CPP32 and Mch3 are targets of mature Mch4 protease in apoptotic cells. |
| GO:0005515 protein binding | IPI PMID:12884866 Caspase-8 and caspase-10 activate NF-kappaB through RIP, NIK... | UNDECIDED | Summary: The NF-kappaB abstract verifies prodomain CASP10 signaling but not this exact P39429 partner row. Reason: The full text is unavailable locally and the abstract only names RIP and NIK as direct prodomain-CASP8/10 binders. Supporting Evidence: PMID:12884866 only NIK and RIP, but not RICK or IKKalpha/beta, could directly bind to PDCasp8/10. |
| GO:0005515 protein binding | IPI PMID:12884866 Caspase-8 and caspase-10 activate NF-kappaB through RIP, NIK... | REMOVE | Summary: CASP10 prodomain binding to RIPK1 is real but uninformative as a standalone protein-binding row. Reason: The mechanistic assertion from this paper is CASP10 prodomain-dependent NF-kappaB activation through RIP/NIK/IKKalpha, not a durable generic protein-binding molecular function for CASP10. Supporting Evidence: PMID:12884866 only NIK and RIP, but not RICK or IKKalpha/beta, could directly bind to PDCasp8/10. |
| GO:0005515 protein binding | IPI PMID:12884866 Caspase-8 and caspase-10 activate NF-kappaB through RIP, NIK... | UNDECIDED | Summary: The NF-kappaB abstract verifies prodomain CASP10 signaling but not this exact Q61160 partner row. Reason: The full text is unavailable locally and the abstract only names RIP and NIK as direct prodomain-CASP8/10 binders. Supporting Evidence: PMID:12884866 only NIK and RIP, but not RICK or IKKalpha/beta, could directly bind to PDCasp8/10. |
| GO:0005515 protein binding | IPI PMID:12887920 Induction of TNF receptor I-mediated apoptosis via two seque... | UNDECIDED | Summary: The TNFR1 complex-II abstract does not expose a CASP10-c-FLIP interaction assay. Reason: The cached abstract names FADD, CASP8, RIPK1 and FLIP(L) in TNFR1 complex II, but not CASP10, so the exact CASP10 partner row should be deferred to a full-text check. Supporting Evidence: PMID:12887920 RIP1 associate with FADD and caspase-8, forming a cytoplasmic complex |
| GO:0005515 protein binding | IPI PMID:12887920 Induction of TNF receptor I-mediated apoptosis via two seque... | UNDECIDED | Summary: The TNFR1 complex-II abstract does not expose a CASP10-CASP8 interaction assay. Reason: The cached abstract names FADD, CASP8, RIPK1 and FLIP(L) in TNFR1 complex II, but not CASP10, so the exact CASP10 partner row should be deferred to a full-text check. Supporting Evidence: PMID:12887920 RIP1 associate with FADD and caspase-8, forming a cytoplasmic complex |
| GO:0005515 protein binding | IPI PMID:17159907 Palmitoylation of CD95 facilitates formation of SDS-stable r... | MODIFY | Summary: CD95 hiDISCs recruit CASP10; the informative cellular-component assertion is CD95 DISC membership. Reason: The CD95 palmitoylation paper supports recruitment of CASP10 to high-molecular-weight CD95 DISCs, not an informative standalone CASP8-binding function. Proposed replacements: CD95 death-inducing signaling complex Supporting Evidence: PMID:17159907 DISC) with maximal recruitment of FADD, caspase-8/10 and c-FLIP occurring when |
| GO:0005515 protein binding | IPI PMID:17479112 Ectopic expression of the serine protease inhibitor PI9 modu... | REMOVE | Summary: SERPINB9/PI9 can interact with active CASP10, but the CASP10-side generic binding row is uninformative. Reason: The meaningful molecular function is the serpin activity of PI9 toward intermediate active caspase-8 and -10 forms; this row does not define a specific CASP10 activity. Supporting Evidence: PMID:17479112 PI9 inhibited apoptotic death by directly interacting with the intermediate active forms of caspase-8 and -10. |
| GO:0005515 protein binding | IPI PMID:19557502 RIOK3 interacts with caspase-10 and negatively regulates the... | REMOVE | Summary: RIOK3 binding modulates CASP10-dependent NF-kappaB signaling but is not a specific CASP10 molecular function. Reason: The interaction is direct, but the abstract does not justify a better CASP10 MF term and the generic protein-binding row adds no information about CASP10 activity. Supporting Evidence: PMID:19557502 RIOK3 interacted with caspase-10, and further, a GST pull-down assay and endogenous coimmunoprecipitation validated the interaction. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: The liver Y2H paper contributes only a large-scale generic PPI row. Reason: This high-throughput interactome screen does not provide mechanistic CASP10 evidence in the cached text, so the broad protein-binding row should not be retained. Supporting Evidence: PMID:21988832 we map the interactions of an unbiased selection of 5026 human liver expression proteins by yeast two-hybrid technology |
| GO:0005515 protein binding | IPI PMID:23541952 Control of autophagic cell death by caspase-10 in multiple m... | MODIFY | Summary: The CASP10-c-FLIP(L) myeloma complex is better represented by CASP10 negative regulation of autophagic cell death. Reason: In myeloma cells, IRF4 induces CASP10 and c-FLIP(L) to form a protease that cleaves BCLAF1 and restrains lethal autophagy; this is a direct noncanonical CASP10 function rather than generic binding. Proposed replacements: negative regulation of autophagic cell death Supporting Evidence: PMID:23541952 generating a protease that does not induce apoptosis but rather blocks an autophagy-dependent cell death pathway. Caspase-10 inhibits autophagy by cleaving the BCL2-interacting protein BCLAF1 |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: The proximity-ligation row is an uninformative generic PPI import. Reason: The cached abstract describes a pathway-scale PPI resource but does not establish a specific CASP10 activity to replace bare protein binding. Supporting Evidence: PMID:25241761 Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: The Rolland interactome row is an uninformative high-throughput XIAP protein-binding edge. Reason: A proteome-scale Y2H screen is not enough to keep a bare GO:0005515 assertion for CASP10 when no mechanistic CASP10 activity is exposed in the paper body. Supporting Evidence: PMID:25416956 A proteome-scale map of the human interactome network. |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: CASP10 acts in the cytoplasm, but cytoplasm is a broad location relative to DISC and ripoptosome contexts. Reason: The PAINT location transfer is defensible for an initiator caspase that acts in cytosolic and receptor-proximal complexes, but complex-specific membership is more informative. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000047947 SUPPORTS TRANSFER Cytoplasm is defensible for CASP10 but secondary to DISC and ripoptosome localization. Supporting Evidence: file:human/CASP10/CASP10-uniprot.txt Found in a Fas signaling CC complex consisting of FAS, FADD, CASP8 and CASP10. |
| GO:0005737 cytoplasm | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: The ARBA cytoplasm row is correct but broad. Reason: CASP10 is recruited from the cytosol to FADD-organized complexes; this generic location is less informative than CD95 DISC or ripoptosome membership. Supporting Evidence: file:human/CASP10/CASP10-uniprot.txt Found in a Fas signaling CC complex consisting of FAS, FADD, CASP8 and CASP10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-141310 | KEEP AS NON CORE | Summary: Reactome projects CASP10 to cytosol for the FasL/CD95 event. Reason: Cytosol is a plausible CASP10 location, but this row is a pathway-event projection rather than independent localization evidence. Supporting Evidence: Reactome:R-HSA-141310 FADD recruits caspase-10 precursor |
| GO:0005829 cytosol | TAS Reactome:R-HSA-141316 | KEEP AS NON CORE | Summary: Reactome projects CASP10 to cytosol for the TRAIL receptor event. Reason: Cytosol is a plausible CASP10 location, but this row is a pathway-event projection rather than independent localization evidence. Supporting Evidence: Reactome:R-HSA-141316 Caspase-10 precursor is recruited to the TRAIL:TRAIL receptor-2:FADD complex |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6798139 | KEEP AS NON CORE | Summary: Reactome projects CASP10 to cytosol for the TP53-induced CASP10 expression event. Reason: Cytosol is a plausible CASP10 location, but this row is a pathway-event projection rather than independent localization evidence. Supporting Evidence: Reactome:R-HSA-6798139 TP53 (p53) stimulates CASP10 expression |
| GO:0005829 cytosol | TAS Reactome:R-HSA-933523 | KEEP AS NON CORE | Summary: Reactome projects CASP10 to cytosol for the procaspase-8/10 dimerization event. Reason: Cytosol is a plausible CASP10 location, but this row is a pathway-event projection rather than independent localization evidence. Supporting Evidence: Reactome:R-HSA-933523 Procaspase-8/10 undergo dimerization |
| GO:0005829 cytosol | TAS Reactome:R-HSA-933526 | KEEP AS NON CORE | Summary: Reactome projects CASP10 to cytosol for the RIG-I/MDA5 FADD recruitment event. Reason: Cytosol is a plausible CASP10 location, but this row is a pathway-event projection rather than independent localization evidence. Supporting Evidence: Reactome:R-HSA-933526 Caspase-8 (CASP8) and caspase-10 (CASP10) are involved in RIG-I |
| GO:0005829 cytosol | TAS Reactome:R-HSA-933532 | KEEP AS NON CORE | Summary: Reactome projects CASP10 to cytosol for the caspase processing after dsRNA stimulation event. Reason: Cytosol is a plausible CASP10 location, but this row is a pathway-event projection rather than independent localization evidence. Supporting Evidence: Reactome:R-HSA-933532 Processing of caspases is required for activation of downstream signaling |
| GO:0005829 cytosol | TAS Reactome:R-HSA-933539 | KEEP AS NON CORE | Summary: Reactome projects CASP10 to cytosol for the IKK recruitment in the NF-kappaB branch event. Reason: Cytosol is a plausible CASP10 location, but this row is a pathway-event projection rather than independent localization evidence. Supporting Evidence: Reactome:R-HSA-933539 Recruitment of IKK complex |
| GO:0006508 proteolysis | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: CASP10 cleaves protein substrates, but proteolysis is broad relative to its initiator-caspase roles. Reason: The InterPro mapping correctly recognizes a protease, but cysteine-type endopeptidase activity and specific maturation events capture CASP10 more precisely. Supporting Evidence: file:human/CASP10/CASP10-uniprot.txt Strict requirement for Asp at position P1 and has a preferred |
| GO:0006915 apoptotic process | IBA GO_REF:0000033 | MODIFY | Summary: CASP10 is a death-receptor initiator; top-level apoptotic process should be narrowed. Reason: The active apoptotic caspase transfer is related, but CASP10 is best scoped to death-domain receptor signaling rather than undifferentiated apoptosis. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000047947 SUPPORTS SOURCE BUT NOT TARGET The node supports inherited active apoptotic-caspase biology, but CASP10 should be scoped to death-domain receptor signaling rather than top-level apoptotic process. Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors Supporting Evidence: PMID:11717445 caspase-10 can function independently of caspase-8 in PMID:11717445 caspase-8 and -10 both interact with the death-effector domain of FADD. |
| GO:0006915 apoptotic process | TAS PMID:10412980 Inherited human Caspase 10 mutations underlie defective lymp... | MODIFY | Summary: The ALPS apoptosis row should be narrowed to Fas/TRAIL death-receptor signaling. Reason: The disease paper ties CASP10 variants to defective Fas ligand and TRAIL responses, supporting the death-domain-receptor extrinsic pathway rather than a top-level apoptosis row. Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors Supporting Evidence: PMID:10412980 interfere with death receptor-induced apoptosis, particularly that stimulated by Fas ligand and TRAIL |
| GO:0008234 cysteine-type peptidase activity | IEA GO_REF:0000002 | MODIFY | Summary: Cysteine-type peptidase activity is correct but less specific than cysteine-type endopeptidase activity. Reason: The Peptidase C14A signature supports an Asp-directed endopeptidase, not merely a generic cysteine-type peptidase. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: InterPro:IPR015917 SUPPORTS SOURCE BUT NOT TARGET The Peptidase C14A signature supports the caspase fold but maps to a parent MF that is less specific than cysteine-type endopeptidase activity. Proposed replacements: cysteine-type endopeptidase activity Supporting Evidence: file:human/CASP10/CASP10-uniprot.txt Strict requirement for Asp at position P1 and has a preferred |
| GO:0031265 CD95 death-inducing signaling complex | IBA GO_REF:0000033 | ACCEPT | Summary: CASP10 is a bona fide CD95 DISC component. Reason: The PAINT CD95 DISC transfer is supported by human CASP10 recruitment to Fas/CD95 signaling complexes through FADD. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002573079 SUPPORTS TRANSFER CASP10 is a bona fide FADD-recruited CD95 DISC component. Supporting Evidence: PMID:11717445 caspase-10 can function independently of caspase-8 in PMID:11717445 caspase-8 and -10 both interact with the death-effector domain of FADD. |
| GO:0031265 CD95 death-inducing signaling complex | IDA PMID:11717445 Caspase-10 is an initiator caspase in death receptor signali... | ACCEPT | Summary: CASP10 is recruited and activated at the Fas/CD95 DISC. Reason: Fas crosslinking recruits CASP10 to the FADD-organized CD95 death-inducing signaling complex where its initiator-caspase activity is activated. Supporting Evidence: PMID:11717445 caspase-10 can function independently of caspase-8 in PMID:11717445 caspase-8 and -10 both interact with the death-effector domain of FADD. |
| GO:0031625 ubiquitin protein ligase binding | IPI PMID:15069192 Suppression of caspase-8- and -10-associated RING proteins r... | KEEP AS NON CORE | Summary: CARP/RFFL/RNF34 ubiquitin ligases bind and regulate DED caspases including CASP10. Reason: The E3-ligase interaction is real and regulatory, but peripheral to the death-effector-domain and caspase activities of CASP10. Supporting Evidence: PMID:15069192 Reciprocal coimmunoprecipitations as well as experiments with caspase-10 file:human/CASP10/CASP10-uniprot.txt and RNF34; negatively regulate CASP10 through proteasomal degradation. |
| GO:0035877 death effector domain binding | IPI PMID:11717445 Caspase-10 is an initiator caspase in death receptor signali... | ACCEPT | Summary: CASP10 tandem DEDs bind the FADD death effector domain during DISC assembly. Reason: DED-mediated binding to FADD is the specific adaptor interaction that recruits procaspase-10 to CD95/TRAIL death-inducing complexes. Supporting Evidence: PMID:11717445 caspase-10 can function independently of caspase-8 in PMID:11717445 caspase-8 and -10 both interact with the death-effector domain of FADD. |
| GO:0042981 regulation of apoptotic process | IEA GO_REF:0000120 | MODIFY | Summary: DED/domain evidence should be narrowed from generic apoptosis regulation to death-receptor extrinsic signaling. Reason: CASP10 DEDs mediate FADD recruitment in death-receptor complexes; the direct process is death-domain receptor signaling, not undifferentiated regulation of apoptotic process. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: InterPro:IPR001875 SUPPORTS SOURCE BUT NOT TARGET A death effector domain supports FADD/death-receptor complex recruitment, not undifferentiated regulation of apoptotic process. Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors Supporting Evidence: PMID:11717445 caspase-10 can function independently of caspase-8 in PMID:11717445 caspase-8 and -10 both interact with the death-effector domain of FADD. file:human/CASP10/CASP10-uniprot.txt DR Pfam; PF01335; DED; 2. |
| GO:0043123 positive regulation of canonical NF-kappaB signal transduction | IMP PMID:12884866 Caspase-8 and caspase-10 activate NF-kappaB through RIP, NIK... | KEEP AS NON CORE | Summary: Prodomain-only CASP10 isoforms can activate canonical NF-kappaB signaling. Reason: This is a direct but non-apoptotic prodomain branch; it should be retained as contextual rather than made a core death-execution function. Supporting Evidence: PMID:12884866 caspase-8 and -10 have roles in a non- or anti-apoptotic signaling pathway leading to NF-kappaB activation through RIP, NIK and IKKalpha. |
| GO:0043525 positive regulation of neuron apoptotic process | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: The neuron-specific apoptosis IBA is a tissue-context over-projection for human CASP10. Reason: The active-caspase ancestor supports apoptotic caspase biology, but local CASP10 evidence centers on death receptors, NF-kappaB and myeloma autophagy rather than neuron-specific apoptosis. Propagation Review Root cause: PROPAGATION BAD Failure modes: CONTEXT OR TISSUE MISMATCH ROLE CONFLATION Sources checked: PANTHER:PTN000047947 SUPPORTS SOURCE BUT NOT TARGET The active-caspase ancestor supports apoptotic caspase biology, but the neuron-specific positive-apoptosis term is not established for human CASP10. |
| GO:0051604 protein maturation | IDA PMID:16916640 Engineered hybrid dimers: tracking the activation pathway of... | ACCEPT | Summary: CASP10 matures downstream caspase substrates proteolytically. Reason: The GO-CAM and UniProt view of CASP10 as an upstream enzyme for effector-caspase maturation is consistent with its established Asp-directed endopeptidase activity. Supporting Evidence: file:human/CASP10/CASP10-uniprot.txt CASP7, CASP8 and CASP9. Hydrolyzes the small- molecule substrates file:human/CASP10/CASP10-uniprot.txt Strict requirement for Asp at position P1 and has a preferred |
| GO:0051604 protein maturation | IEA GO_REF:0000117 | ACCEPT | Summary: The ARBA protein-maturation row is sound for CASP10. Reason: CASP10 can proteolytically activate downstream effector caspases, so protein maturation is a valid process even though the substrate-specific GO-CAM carries the more precise interpretation. Supporting Evidence: file:human/CASP10/CASP10-uniprot.txt CASP7, CASP8 and CASP9. Hydrolyzes the small- molecule substrates file:human/CASP10/CASP10-uniprot.txt Strict requirement for Asp at position P1 and has a preferred |
| GO:0097342 ripoptosome | IDA PMID:21737330 cIAPs block Ripoptosome formation, a RIP1/caspase-8 containi... | ACCEPT | Summary: CASP10 is a component of the RIP1/FADD/CASP8/c-FLIP ripoptosome. Reason: The ripoptosome paper directly identified CASP10 in this cytosolic death platform, but does not establish enough CASP10-specific perturbation evidence to add a separate necroptosis process row. Supporting Evidence: PMID:21737330 It contains RIP1, FADD, caspase-8, caspase-10, and caspase inhibitor cFLIP isoforms. |
| GO:1900119 positive regulation of execution phase of apoptosis | IDA PMID:16916640 Engineered hybrid dimers: tracking the activation pathway of... | KEEP AS NON CORE | Summary: CASP10 can promote effector-caspase maturation upstream of apoptosis execution. Reason: This is plausible for CASP10-driven CASP7 maturation, but the core CASP10 process is receptor-proximal initiator function rather than the execution phase itself. Supporting Evidence: file:human/CASP10/CASP10-uniprot.txt CASP7, CASP8 and CASP9. Hydrolyzes the small- molecule substrates file:human/CASP10/CASP10-uniprot.txt Strict requirement for Asp at position P1 and has a preferred |
Loading supporting content…
Download this section (compressed HTML)Q: Should CASP10-c-FLIP(L) cleavage of BCLAF1 in myeloma be represented as a normal CASP10 activity, or only retained as a disease-cell-line context for negative regulation of autophagic cell death?
Q: Which CASP10 splice isoforms are abundant enough to warrant isoform-specific GO annotations for DED-only NF-kappaB scaffolding versus catalytically inactive dominant-negative death-receptor signaling?
Experiment: Use CASP8-null, CASP10-rescued human cells with catalytic-dead CASP10 controls and substrate N-terminomics after Fas or TRAIL stimulation to distinguish direct CASP10 substrates from CASP8-dependent cleavage events.
Hypothesis: CASP10 has CASP8-independent substrate preferences in FADD-containing death-receptor complexes.
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)