CASP7 is a short-prodomain executioner caspase that is synthesized as a cytosolic zymogen and activated by initiator caspases, granzyme B, CASP1, or calpain cleavage into an Asp-directed cysteine endopeptidase. In apoptosis, mature CASP7 cleaves PARP1, p23, YY1, claspin, and other nuclear and cytosolic substrates, using a positively charged N-terminal exosite that can bind RNA to accelerate PARP1 and RNA-binding-protein proteolysis. CASP7 is inhibited by IAP proteins such as XIAP/BIRC4 and BIRC6 and by PAK2 phosphorylation, and it also has non-apoptotic roles in inflammasome/NF-kB signaling and SMPD1 activation for membrane-pore repair.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003723 RNA binding | IDA PMID:31586028 Caspase-7 uses RNA to enhance proteolysis of poly(ADP-ribose... | ACCEPT | Summary: CASP7 binds nucleic acids through its N-terminal exosite, and RNA promotes efficient PARP1 and RNA-binding-protein cleavage. Reason: RNA binding is a direct noncatalytic activity of the CASP7 N-terminal exosite that enhances substrate selection. Supporting Evidence: PMID:31586028 caspase-7, but not caspase-3 or a caspase-7 with a mutated exosite, binds nucleic acids |
| GO:0004190 aspartic-type endopeptidase activity | IEA GO_REF:0000107 | MODIFY | Summary: CASP7 cleaves internal peptide bonds using a catalytic cysteine. Reason: CASP7 cleaves internal peptide bonds using a catalytic cysteine. Asp at the substrate cleavage site specifies recognition, not an aspartic catalytic mechanism. The supported specific activity is cysteine-type endopeptidase activity. Proposed replacements: cysteine-type endopeptidase activity Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Belongs to the peptidase C14A family. PMID:35705808 Caspase-7 cleaves ASM |
| GO:0004197 cysteine-type endopeptidase activity | IBA GO_REF:0000033 | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:11257230 Structural basis of caspase-7 inhibition by XIAP. | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:16123041 Cleavage of claspin by caspase-7 during apoptosis inhibits t... | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:16352606 Caspase-7 is directly activated by the approximately 700-kDa... | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:16374543 Nuclear caspase-3 and caspase-7 activation, and poly(ADP-rib... | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:16916640 Engineered hybrid dimers: tracking the activation pathway of... | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:17646170 Proteolytic cleavage of ataxin-7 by caspase-7 modulates cell... | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:18723680 Executioner caspase-3 and caspase-7 are functionally distinc... | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:19581639 Dissecting an allosteric switch in caspase-7 using chemical ... | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:19617626 Calpain-1 cleaves and activates caspase-7. | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:20566630 Identification of functional regions defining different acti... | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:21157428 Caspase-8 and caspase-7 sequentially mediate proteolytic act... | ACCEPT | Summary: CASP7 directly cleaves and activates pro-acid sphingomyelinase in TNF receptosomes. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: PMID:21157428 caspase-7 mediates A-SMase activation by direct interaction resulting in proteolytic cleavage of the 72-kDa pro-A-SMase |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:22184066 Phosphorylation of the transcription factor YY1 by CK2Ξ± prev... | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:22451931 Caspase-7 uses an exosite to promote poly(ADP ribose) polyme... | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:22464733 Inflammasome-activated caspase 7 cleaves PARP1 to enhance th... | ACCEPT | Summary: Inflammasome-activated CASP7 cleaves nuclear PARP1 after LPS stimulation. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: PMID:22464733 after LPS stimulation, caspase 7 is activated by caspase 1, translocates to the nucleus, and cleaves PARP1 |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:23650375 Structural snapshots reveal distinct mechanisms of procaspas... | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:23897474 Structural asymmetry of procaspase-7 bound to a specific inh... | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:24904167 Caspase-mediated cleavage of phospholipid flippase for apopt... | ACCEPT | Summary: CASP7 has independently established cysteine-type endopeptidase activity. Reason: CASP7 has independently established cysteine-type endopeptidase activity. The catalytic cysteine and Asp-directed substrate cleavage distinguish caspases from aspartic proteases. A source that does not isolate this activity by itself does not negate the same-target biochemical claim; the original citation remains preserved for provenance. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Belongs to the peptidase C14A family. PMID:35705808 Caspase-7 cleaves ASM |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:27032039 Reprogramming Caspase-7 Specificity by Regio-Specific Mutati... | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:27889207 Dual Site Phosphorylation of Caspase-7 by PAK2 Blocks Apopto... | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:28863261 Characterization of Hsp90 Co-Chaperone p23 Cleavage by Caspa... | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:31586028 Caspase-7 uses RNA to enhance proteolysis of poly(ADP-ribose... | ACCEPT | Summary: CASP7 cleaves PARP1 and RNA-binding proteins through an RNA-assisted exosite mechanism. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: PMID:31586028 caspase-7, but not caspase-3 or a caspase-7 with a mutated exosite, binds nucleic acids |
| GO:0004197 cysteine-type endopeptidase activity | IDA PMID:37327784 Gasdermin D licenses MHCII induction to maintain food tolera... | ACCEPT | Summary: CASP7 has independently established cysteine-type endopeptidase activity. Reason: CASP7 has independently established cysteine-type endopeptidase activity. The catalytic cysteine and Asp-directed substrate cleavage distinguish caspases from aspartic proteases. A source that does not isolate this activity by itself does not negate the same-target biochemical claim; the original citation remains preserved for provenance. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Belongs to the peptidase C14A family. PMID:35705808 Caspase-7 cleaves ASM |
| GO:0004197 cysteine-type endopeptidase activity | IEA GO_REF:0000120 | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0004197 cysteine-type endopeptidase activity | IMP PMID:22253444 Apoptotic DNA degradation into oligonucleosomal fragments, b... | ACCEPT | Summary: CASP7 has independently established cysteine-type endopeptidase activity. Reason: CASP7 has independently established cysteine-type endopeptidase activity. The catalytic cysteine and Asp-directed substrate cleavage distinguish caspases from aspartic proteases. A source that does not isolate this activity by itself does not negate the same-target biochemical claim; the original citation remains preserved for provenance. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Belongs to the peptidase C14A family. PMID:35705808 Caspase-7 cleaves ASM |
| GO:0004197 cysteine-type endopeptidase activity | ISS GO_REF:0000024 | ACCEPT | Summary: This row correctly annotates CASP7 as an Asp-directed cysteine endopeptidase. Reason: CASP7 is a cysteine endopeptidase with strict P1 Asp specificity; this activity is the basis of its apoptosis, inflammatory PARP1, and SMPD1 substrate-cleavage roles. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt preferred cleavage sequence of Asp-Glu-Val-Asp |
| GO:0005515 protein binding | IPI PMID:11084335 ML-IAP, a novel inhibitor of apoptosis that is preferentiall... | UNDECIDED | Summary: This generic protein-binding row cites an abstract about ML-IAP/BIRC7 while GOA lists BIRC2 as the interactor. Reason: ML-IAP/BIRC7 and BIRC2 are both IAP-family caspase regulators, but the cached record does not verify the specific BIRC2-CASP7 edge and full text is not locally available. Supporting Evidence: PMID:11084335 ML-IAP, a novel human IAP, inhibits apoptosis induced by death |
| GO:0005515 protein binding | IPI PMID:11257230 Structural basis of caspase-7 inhibition by XIAP. | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: XIAP binds and blocks the CASP7 active site. That inhibitory interaction is real, but CASP7 itself is the inhibited cysteine endopeptidase. Supporting Evidence: PMID:11257230 Structural basis of caspase-7 inhibition by XIAP. |
| GO:0005515 protein binding | IPI PMID:11257231 Structural basis of caspase inhibition by XIAP: differential... | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: The XIAP BIR2-linker interaction explains endogenous inhibition of CASP7, not a distinct generic binding activity for CASP7. Supporting Evidence: PMID:11257231 Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain. |
| GO:0005515 protein binding | IPI PMID:12888622 Caspase cleavage of tau: linking amyloid and neurofibrillary... | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: MAPT is a CASP7 substrate in an in vitro tau-cleavage study; substrate recognition is captured by cysteine endopeptidase/proteolysis rows rather than uninformative protein binding. Supporting Evidence: PMID:12888622 tau is proteolyzed by multiple caspases at a highly |
| GO:0005515 protein binding | IPI PMID:21157428 Caspase-8 and caspase-7 sequentially mediate proteolytic act... | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: SMPD1 is a CASP7 substrate in receptosomes; the same paper supports direct proteolytic activation of pro-A-SMase and is better captured as CASP7 protease/protein maturation. Supporting Evidence: PMID:21157428 Caspase-8 and caspase-7 sequentially mediate proteolytic activation of acid |
| GO:0005515 protein binding | IPI PMID:21555521 Phosphorylation of caspase-7 by p21-activated protein kinase... | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: PAK2 phosphorylates and inhibits CASP7, making CASP7 the regulated kinase substrate rather than a gene product whose function is generic protein binding. Supporting Evidence: PMID:21555521 phosphorylate caspase-7 at the Ser-30, Thr-173, and |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: This is a proteome-scale interactome edge without evidence for a CASP7-specific molecular function. Supporting Evidence: PMID:25416956 A proteome-scale map of the human interactome network. |
| GO:0005515 protein binding | IPI PMID:31467278 Maximizing binary interactome mapping with a minimal number ... | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: This is a high-throughput binary interactome edge without evidence for a CASP7-specific molecular function. Supporting Evidence: PMID:31467278 Maximizing binary interactome mapping with a minimal number of assays. |
| GO:0005515 protein binding | IPI PMID:31470122 Cellular substrates and pro-apoptotic function of the human ... | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: HTRA4 was reported to bind and degrade CASP7; CASP7 is the HTRA4 target, not the effector in that interaction. Supporting Evidence: PMID:31470122 Cellular substrates and pro-apoptotic function of the human HtrA4 protease. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: This is a reference-map binary-interactome edge without evidence for a CASP7-specific molecular function. Supporting Evidence: PMID:32296183 A reference map of the human binary protein interactome. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: This is a reference-map binary-interactome edge without evidence for a CASP7-specific molecular function. Supporting Evidence: PMID:32296183 A reference map of the human binary protein interactome. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: This is a reference-map binary-interactome edge without evidence for a CASP7-specific molecular function. Supporting Evidence: PMID:32296183 A reference map of the human binary protein interactome. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: This BioPlex/neurodegenerative-disease interactome edge is only generic high-throughput binding and does not define a CASP7 activity. Supporting Evidence: PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: This BioPlex/neurodegenerative-disease interactome edge is only generic high-throughput binding and does not define a CASP7 activity. Supporting Evidence: PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: This BioPlex/neurodegenerative-disease interactome edge is only generic high-throughput binding and does not define a CASP7 activity. Supporting Evidence: PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: This BioPlex/neurodegenerative-disease interactome edge is only generic high-throughput binding and does not define a CASP7 activity. Supporting Evidence: PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains. |
| GO:0005515 protein binding | IPI PMID:32911434 A functionally defined high-density NRF2 interactome reveals... | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: The NRF2 interactome edge is outside CASP7 apoptosis biology and does not establish a specific CASP7 molecular function. Supporting Evidence: PMID:32911434 A functionally defined high-density NRF2 interactome reveals new conditional regulators of ARE transactivation. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: This BioPlex proteome-scale AP-MS edge lacks evidence for a CASP7-specific molecular function. Supporting Evidence: PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein-binding row for a CASP7 interaction. Reason: This BioPlex proteome-scale AP-MS edge lacks evidence for a CASP7-specific molecular function. Supporting Evidence: PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. |
| GO:0005576 extracellular region | IEA GO_REF:0000120 | ACCEPT | Summary: CASP7 has a documented extracellular/receptosomal role in proteolytic pro-A-SMase activation. Reason: The SMPD1 branch requires CASP7-dependent maturation of secretory pro-A-SMase in TNF-R1 receptosomes and related extracellular repair contexts, so extracellular region is a real CASP7 site of action rather than only a pathway projection. Supporting Evidence: PMID:21157428 caspase-7 mediates A-SMase activation by direct interaction resulting in proteolytic cleavage of the 72-kDa pro-A-SMase |
| GO:0005576 extracellular region | TAS PMID:21157428 Caspase-8 and caspase-7 sequentially mediate proteolytic act... | ACCEPT | Summary: CASP7 has a documented extracellular/receptosomal role in proteolytic pro-A-SMase activation. Reason: The SMPD1 branch requires CASP7-dependent maturation of secretory pro-A-SMase in TNF-R1 receptosomes and related extracellular repair contexts, so extracellular region is a real CASP7 site of action rather than only a pathway projection. Supporting Evidence: PMID:21157428 caspase-7 mediates A-SMase activation by direct interaction resulting in proteolytic cleavage of the 72-kDa pro-A-SMase |
| GO:0005634 nucleus | IDA PMID:16374543 Nuclear caspase-3 and caspase-7 activation, and poly(ADP-rib... | ACCEPT | Summary: CASP7 has a supported nuclear pool and cleaves nuclear substrates. Reason: CASP7 has a supported nuclear pool and cleaves nuclear substrates. Retain nucleus because the available localization evidence is not uniformly resolved to a single nuclear subcompartment. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Nucleus |
| GO:0005634 nucleus | IDA PMID:17167422 Hsp70 regulates erythropoiesis by preventing caspase-3-media... | ACCEPT | Summary: CASP7 has a supported nuclear pool and cleaves nuclear substrates. Reason: CASP7 has a supported nuclear pool and cleaves nuclear substrates. Retain nucleus because the available localization evidence is not uniformly resolved to a single nuclear subcompartment. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Nucleus |
| GO:0005634 nucleus | IDA PMID:19617626 Calpain-1 cleaves and activates caspase-7. | ACCEPT | Summary: CASP7 has a supported nuclear pool and cleaves nuclear substrates. Reason: CASP7 has a supported nuclear pool and cleaves nuclear substrates. Retain nucleus because the available localization evidence is not uniformly resolved to a single nuclear subcompartment. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Nucleus |
| GO:0005634 nucleus | IDA PMID:21555521 Phosphorylation of caspase-7 by p21-activated protein kinase... | ACCEPT | Summary: CASP7 has a supported nuclear pool and cleaves nuclear substrates. Reason: CASP7 has a supported nuclear pool and cleaves nuclear substrates. Retain nucleus because the available localization evidence is not uniformly resolved to a single nuclear subcompartment. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Nucleus |
| GO:0005634 nucleus | IDA PMID:22464733 Inflammasome-activated caspase 7 cleaves PARP1 to enhance th... | ACCEPT | Summary: CASP7 has a supported nuclear pool and cleaves nuclear substrates. Reason: CASP7 has a supported nuclear pool and cleaves nuclear substrates. Retain nucleus because the available localization evidence is not uniformly resolved to a single nuclear subcompartment. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Nucleus |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: CASP7 has a supported nuclear pool and cleaves nuclear substrates. Reason: CASP7 has a supported nuclear pool and cleaves nuclear substrates. Retain nucleus because the available localization evidence is not uniformly resolved to a single nuclear subcompartment. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Nucleus |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-351936 | ACCEPT | Summary: CASP7 acts on nuclear substrates in the nucleoplasm during apoptosis. Reason: CASP7 acts on nuclear substrates in the nucleoplasm during apoptosis. This is a site of its core proteolytic function, not merely an incidental location. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Nucleus |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9029680 | ACCEPT | Summary: CASP7 acts on nuclear substrates in the nucleoplasm during apoptosis. Reason: CASP7 acts on nuclear substrates in the nucleoplasm during apoptosis. This is a site of its core proteolytic function, not merely an incidental location. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Nucleus |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | MODIFY | Summary: CASP7 acts in a soluble cytosolic pool during proteolytic signaling. Reason: CASP7 acts in a soluble cytosolic pool during proteolytic signaling. Refine the broad cytoplasm annotation to the supported cytosol compartment; nuclear or extracellular pools are represented separately. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000047947 SUPPORTS TRANSFER The conserved original claim is defensible; the target evidence supports the stated refinement. This assessment does not relocate the PAINT ancestral assertion. Proposed replacements: cytosol Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Cytoplasm |
| GO:0005737 cytoplasm | IDA PMID:21555521 Phosphorylation of caspase-7 by p21-activated protein kinase... | MODIFY | Summary: CASP7 acts in a soluble cytosolic pool during proteolytic signaling. Reason: CASP7 acts in a soluble cytosolic pool during proteolytic signaling. Refine the broad cytoplasm annotation to the supported cytosol compartment; nuclear or extracellular pools are represented separately. Proposed replacements: cytosol Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Cytoplasm |
| GO:0005737 cytoplasm | TAS PMID:8576161 ICE-LAP3, a novel mammalian homologue of the Caenorhabditis ... | MODIFY | Summary: CASP7 acts in a soluble cytosolic pool during proteolytic signaling. Reason: CASP7 acts in a soluble cytosolic pool during proteolytic signaling. Refine the broad cytoplasm annotation to the supported cytosol compartment; nuclear or extracellular pools are represented separately. Proposed replacements: cytosol Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Cytoplasm |
| GO:0005829 cytosol | IDA PMID:16352606 Caspase-7 is directly activated by the approximately 700-kDa... | ACCEPT | Summary: CASP7 is a cytosolic executioner caspase before activation and redistribution to some substrates. Reason: Cytoplasm/cytosol is a correct major location for procaspase-7 and active CASP7. Supporting Evidence: PMID:8576161 Pro-ICE-LAP3 is a 35-kDa protein localized to the cytoplasm |
| GO:0005829 cytosol | IDA PMID:17167422 Hsp70 regulates erythropoiesis by preventing caspase-3-media... | ACCEPT | Summary: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. Reason: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. A Reactome reaction may describe production or activation of the protein rather than localization measurement; that source limitation does not contradict the location itself. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Cytoplasm |
| GO:0005829 cytosol | IEA GO_REF:0000044 | ACCEPT | Summary: CASP7 is a cytosolic executioner caspase before activation and redistribution to some substrates. Reason: Cytoplasm/cytosol is a correct major location for procaspase-7 and active CASP7. Supporting Evidence: PMID:8576161 Pro-ICE-LAP3 is a 35-kDa protein localized to the cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-114261 | ACCEPT | Summary: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. Reason: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. A Reactome reaction may describe production or activation of the protein rather than localization measurement; that source limitation does not contradict the location itself. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-114354 | ACCEPT | Summary: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. Reason: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. A Reactome reaction may describe production or activation of the protein rather than localization measurement; that source limitation does not contradict the location itself. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-114392 | ACCEPT | Summary: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. Reason: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. A Reactome reaction may describe production or activation of the protein rather than localization measurement; that source limitation does not contradict the location itself. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-201628 | ACCEPT | Summary: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. Reason: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. A Reactome reaction may describe production or activation of the protein rather than localization measurement; that source limitation does not contradict the location itself. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-201634 | ACCEPT | Summary: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. Reason: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. A Reactome reaction may describe production or activation of the protein rather than localization measurement; that source limitation does not contradict the location itself. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-201639 | ACCEPT | Summary: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. Reason: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. A Reactome reaction may describe production or activation of the protein rather than localization measurement; that source limitation does not contradict the location itself. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-351901 | ACCEPT | Summary: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. Reason: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. A Reactome reaction may describe production or activation of the protein rather than localization measurement; that source limitation does not contradict the location itself. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9029680 | ACCEPT | Summary: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. Reason: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. A Reactome reaction may describe production or activation of the protein rather than localization measurement; that source limitation does not contradict the location itself. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9627107 | ACCEPT | Summary: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. Reason: A cytosolic pool of CASP7 is independently supported by its curated localization and apoptotic substrate processing. A Reactome reaction may describe production or activation of the protein rather than localization measurement; that source limitation does not contradict the location itself. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Cytoplasm |
| GO:0006508 proteolysis | IDA PMID:12888622 Caspase cleavage of tau: linking amyloid and neurofibrillary... | ACCEPT | Summary: CASP7 directly catalyzes proteolysis of diverse substrates. Reason: CASP7 directly catalyzes proteolysis of diverse substrates. This process is core and spans destructive and regulatory cleavage, so no single narrower protein-processing process replaces its full scope. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Belongs to the peptidase C14A family. PMID:35705808 Caspase-7 cleaves ASM |
| GO:0006508 proteolysis | IEA GO_REF:0000120 | ACCEPT | Summary: CASP7 directly catalyzes proteolysis of diverse substrates. Reason: CASP7 directly catalyzes proteolysis of diverse substrates. This process is core and spans destructive and regulatory cleavage, so no single narrower protein-processing process replaces its full scope. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Belongs to the peptidase C14A family. PMID:35705808 Caspase-7 cleaves ASM |
| GO:0006915 apoptotic process | IBA GO_REF:0000033 | MODIFY | Summary: CASP7 directly performs proteolytic steps of apoptotic execution. Reason: CASP7 directly performs proteolytic steps of apoptotic execution. Refine the broad process to execution phase of apoptosis, without asserting that this single caspase is obligatory in every tissue or genetic background. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000047947 SUPPORTS TRANSFER The conserved original claim is defensible; the target evidence supports the stated refinement. This assessment does not relocate the PAINT ancestral assertion. Proposed replacements: execution phase of apoptosis Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Belongs to the peptidase C14A family. PMID:35705808 Caspase-7 cleaves ASM |
| GO:0006915 apoptotic process | IDA PMID:17464193 Identification of novel regulators of apoptosis using a high... | MODIFY | Summary: CASP7 directly performs proteolytic steps of apoptotic execution. Reason: CASP7 directly performs proteolytic steps of apoptotic execution. Refine the broad process to execution phase of apoptosis, without asserting that this single caspase is obligatory in every tissue or genetic background. Proposed replacements: execution phase of apoptosis Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Belongs to the peptidase C14A family. PMID:35705808 Caspase-7 cleaves ASM |
| GO:0006915 apoptotic process | TAS PMID:8567622 Identification and characterization of CPP32/Mch2 homolog 1,... | MODIFY | Summary: CASP7 directly performs proteolytic steps of apoptotic execution. Reason: CASP7 directly performs proteolytic steps of apoptotic execution. Refine the broad process to execution phase of apoptosis, without asserting that this single caspase is obligatory in every tissue or genetic background. Proposed replacements: execution phase of apoptosis Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Belongs to the peptidase C14A family. PMID:35705808 Caspase-7 cleaves ASM |
| GO:0008233 peptidase activity | IDA PMID:19740745 A truncated form of p23 down-regulates telomerase activity v... | MODIFY | Summary: CASP7 cleaves internal peptide bonds using a catalytic cysteine. Reason: CASP7 cleaves internal peptide bonds using a catalytic cysteine. Asp at the substrate cleavage site specifies recognition, not an aspartic catalytic mechanism. The supported specific activity is cysteine-type endopeptidase activity. Proposed replacements: cysteine-type endopeptidase activity Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Belongs to the peptidase C14A family. PMID:35705808 Caspase-7 cleaves ASM |
| GO:0008234 cysteine-type peptidase activity | IEA GO_REF:0000120 | MODIFY | Summary: CASP7 cleaves internal peptide bonds using a catalytic cysteine. Reason: CASP7 cleaves internal peptide bonds using a catalytic cysteine. Asp at the substrate cleavage site specifies recognition, not an aspartic catalytic mechanism. The supported specific activity is cysteine-type endopeptidase activity. Proposed replacements: cysteine-type endopeptidase activity Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Belongs to the peptidase C14A family. PMID:35705808 Caspase-7 cleaves ASM |
| GO:0008234 cysteine-type peptidase activity | TAS PMID:8567622 Identification and characterization of CPP32/Mch2 homolog 1,... | MODIFY | Summary: CASP7 cleaves internal peptide bonds using a catalytic cysteine. Reason: CASP7 cleaves internal peptide bonds using a catalytic cysteine. Asp at the substrate cleavage site specifies recognition, not an aspartic catalytic mechanism. The supported specific activity is cysteine-type endopeptidase activity. Proposed replacements: cysteine-type endopeptidase activity Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt Belongs to the peptidase C14A family. PMID:35705808 Caspase-7 cleaves ASM |
| GO:0009617 response to bacterium | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Caspase-7 contributes to bacterial-response programs, including SMPD1 processing and membrane repair. Reason: Caspase-7 contributes to bacterial-response programs, including SMPD1 processing and membrane repair. Native infection evidence is strongest in mice (PMID:35705808); retain the human inference as contextual, without treating the enzyme as a pathogen sensor. Supporting Evidence: |
| GO:0030163 protein catabolic process | IDA PMID:16374543 Nuclear caspase-3 and caspase-7 activation, and poly(ADP-rib... | ACCEPT | Summary: CASP7 directly cleaves proteins and contributes to their dismantling during apoptosis. Reason: CASP7 directly cleaves proteins and contributes to their dismantling during apoptosis. Retain this core catabolic participation without assuming every regulatory cleavage causes complete protein degradation. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt proteolytically cleaving target proteins |
| GO:0030163 protein catabolic process | IDA PMID:22184066 Phosphorylation of the transcription factor YY1 by CK2Ξ± prev... | ACCEPT | Summary: CASP7 directly cleaves proteins and contributes to their dismantling during apoptosis. Reason: CASP7 directly cleaves proteins and contributes to their dismantling during apoptosis. Retain this core catabolic participation without assuming every regulatory cleavage causes complete protein degradation. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt proteolytically cleaving target proteins |
| GO:0030163 protein catabolic process | IDA PMID:22464733 Inflammasome-activated caspase 7 cleaves PARP1 to enhance th... | ACCEPT | Summary: CASP7 directly cleaves proteins and contributes to their dismantling during apoptosis. Reason: CASP7 directly cleaves proteins and contributes to their dismantling during apoptosis. Retain this core catabolic participation without assuming every regulatory cleavage causes complete protein degradation. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt proteolytically cleaving target proteins |
| GO:0030163 protein catabolic process | IEA GO_REF:0000107 | ACCEPT | Summary: CASP7 directly cleaves proteins and contributes to their dismantling during apoptosis. Reason: CASP7 directly cleaves proteins and contributes to their dismantling during apoptosis. Retain this core catabolic participation without assuming every regulatory cleavage causes complete protein degradation. Supporting Evidence: file:human/CASP7/CASP7-uniprot.txt proteolytically cleaving target proteins |
| GO:0043525 positive regulation of neuron apoptotic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: This row captures a tissue- or cell-type-specific apoptotic context for CASP7 orthologs. Reason: The row is consistent with CASP7 executioner-caspase biology but is not a distinct central CASP7 molecular role. Supporting Evidence: PMID:16916640 Caspase-7 is an obligate dimer of catalytic domains, with generation of activity requiring limited proteolysis |
| GO:0051146 striated muscle cell differentiation | IEA GO_REF:0000107 | UNDECIDED | Summary: A conserved executioner role does not rule out this specific developmental or stimulus context. Reason: A conserved executioner role does not rule out this specific developmental or stimulus context. The available evidence does not resolve the exact target-specific claim, so the previous unsupported removal is replaced by an explicit evidence gap. Supporting Evidence: PMID:16916640 Caspase-7 is an obligate dimer of catalytic domains, with generation of activity requiring limited proteolysis |
| GO:0051604 protein maturation | IDA PMID:21157428 Caspase-8 and caspase-7 sequentially mediate proteolytic act... | ACCEPT | Summary: CASP7 matures pro-A-SMase/SMPD1 by proteolytic cleavage. Reason: Protein maturation is the correct process for CASP7 cleavage of pro-A-SMase to an active SMPD1 enzyme. Supporting Evidence: PMID:21157428 caspase-7 mediates A-SMase activation by direct interaction resulting in proteolytic cleavage of the 72-kDa pro-A-SMase |
| GO:0051604 protein maturation | IEA GO_REF:0000120 | ACCEPT | Summary: CASP7 matures pro-A-SMase/SMPD1 by proteolytic cleavage. Reason: Protein maturation is the correct process for CASP7 cleavage of pro-A-SMase to an active SMPD1 enzyme. Supporting Evidence: PMID:21157428 caspase-7 mediates A-SMase activation by direct interaction resulting in proteolytic cleavage of the 72-kDa pro-A-SMase |
| GO:0070227 lymphocyte apoptotic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: This row captures a tissue- or cell-type-specific apoptotic context for CASP7 orthologs. Reason: The row is consistent with CASP7 executioner-caspase biology but is not a distinct central CASP7 molecular role. Supporting Evidence: PMID:16916640 Caspase-7 is an obligate dimer of catalytic domains, with generation of activity requiring limited proteolysis |
| GO:0070227 lymphocyte apoptotic process | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: This row captures a tissue- or cell-type-specific apoptotic context for CASP7 orthologs. Reason: The row is consistent with CASP7 executioner-caspase biology but is not a distinct central CASP7 molecular role. Supporting Evidence: PMID:16916640 Caspase-7 is an obligate dimer of catalytic domains, with generation of activity requiring limited proteolysis |
| GO:0071222 cellular response to lipopolysaccharide | IDA PMID:22464733 Inflammasome-activated caspase 7 cleaves PARP1 to enhance th... | KEEP AS NON CORE | Summary: CASP7 is activated by CASP1 after LPS stimulation and cleaves PARP1 in the nucleus. Reason: The LPS/NF-kB branch is a direct but context-specific non-apoptotic CASP7 role. Supporting Evidence: PMID:22464733 after LPS stimulation, caspase 7 is activated by caspase 1, translocates to the nucleus, and cleaves PARP1 |
| GO:0071887 leukocyte apoptotic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: This row captures a tissue- or cell-type-specific apoptotic context for CASP7 orthologs. Reason: The row is consistent with CASP7 executioner-caspase biology but is not a distinct central CASP7 molecular role. Supporting Evidence: PMID:16916640 Caspase-7 is an obligate dimer of catalytic domains, with generation of activity requiring limited proteolysis |
| GO:0072734 cellular response to staurosporine | IMP PMID:22253444 Apoptotic DNA degradation into oligonucleosomal fragments, b... | UNDECIDED | Summary: A conserved executioner role does not rule out this specific developmental or stimulus context. Reason: A conserved executioner role does not rule out this specific developmental or stimulus context. The available evidence does not resolve the exact target-specific claim, so the previous unsupported removal is replaced by an explicit evidence gap. Supporting Evidence: PMID:22253444 After staurosporine treatment, the preferential processing of ICAD in the cytosolic fraction |
| GO:0097190 apoptotic signaling pathway | IEA GO_REF:0000107 | MODIFY | Summary: CASP7 is a downstream executioner caspase, not an upstream apoptotic signaling component. Reason: The generic apoptotic signaling assertion should be tightened to execution phase of apoptosis. Proposed replacements: execution phase of apoptosis Supporting Evidence: PMID:16916640 Caspase-7 is an obligate dimer of catalytic domains, with generation of activity requiring limited proteolysis |
| GO:0097194 execution phase of apoptosis | IBA GO_REF:0000033 | ACCEPT | Summary: CASP7 executes apoptosis after activation by initiator caspases and cleaves apoptotic substrates. Reason: Execution phase of apoptosis is the precise core biological process for CASP7. Supporting Evidence: PMID:16916640 Caspase-7 is an obligate dimer of catalytic domains, with generation of activity requiring limited proteolysis |
| GO:0097194 execution phase of apoptosis | IDA PMID:16374543 Nuclear caspase-3 and caspase-7 activation, and poly(ADP-rib... | ACCEPT | Summary: CASP7 executes apoptosis after activation by initiator caspases and cleaves apoptotic substrates. Reason: Execution phase of apoptosis is the precise core biological process for CASP7. Supporting Evidence: PMID:16916640 Caspase-7 is an obligate dimer of catalytic domains, with generation of activity requiring limited proteolysis |
| GO:0097194 execution phase of apoptosis | IDA PMID:16916640 Engineered hybrid dimers: tracking the activation pathway of... | ACCEPT | Summary: CASP7 executes apoptosis after activation by initiator caspases and cleaves apoptotic substrates. Reason: Execution phase of apoptosis is the precise core biological process for CASP7. Supporting Evidence: PMID:16916640 Caspase-7 is an obligate dimer of catalytic domains, with generation of activity requiring limited proteolysis |
| GO:0097194 execution phase of apoptosis | IDA PMID:22184066 Phosphorylation of the transcription factor YY1 by CK2Ξ± prev... | ACCEPT | Summary: CASP7 executes apoptosis after activation by initiator caspases and cleaves apoptotic substrates. Reason: Execution phase of apoptosis is the precise core biological process for CASP7. Supporting Evidence: PMID:16916640 Caspase-7 is an obligate dimer of catalytic domains, with generation of activity requiring limited proteolysis |
| GO:0097194 execution phase of apoptosis | IDA PMID:31586028 Caspase-7 uses RNA to enhance proteolysis of poly(ADP-ribose... | ACCEPT | Summary: CASP7 executes apoptosis after activation by initiator caspases and cleaves apoptotic substrates. Reason: Execution phase of apoptosis is the precise core biological process for CASP7. Supporting Evidence: PMID:16916640 Caspase-7 is an obligate dimer of catalytic domains, with generation of activity requiring limited proteolysis |
| GO:0097194 execution phase of apoptosis | IEA GO_REF:0000117 | ACCEPT | Summary: CASP7 executes apoptosis after activation by initiator caspases and cleaves apoptotic substrates. Reason: Execution phase of apoptosis is the precise core biological process for CASP7. Supporting Evidence: PMID:16916640 Caspase-7 is an obligate dimer of catalytic domains, with generation of activity requiring limited proteolysis |
Loading supporting contentβ¦
Download this section (compressed HTML)Q: Should human CASP7 carry a direct extracellular-region annotation for the gasdermin/perforin pore-repair SMPD1 pathway, or should current human assertions remain similarity-based until the pathway is demonstrated in human primary cells?
Q: Should CASP7 RNA binding be modeled as a substrate-recognition cofactor for PARP1 and RNA-binding protein cleavage in GO-CAM annotations rather than as a standalone flat MF row?
Suggested experts: Denault JB
Experiment: Use isogenic CASP7 knockout cells rescued with wild-type CASP7 or K38-K41 exosite mutants and perform apoptotic N-terminomics plus RNAse/add-back cleavage assays for PARP1, p23, and RNA-binding protein substrates.
Hypothesis: CASP7 N-terminal RNA binding determines a discrete nuclear substrate repertoire during apoptotic execution.
Type: structure-function degradomics
Experiment: Trigger inflammasome or granzyme/perforin pore formation in human epithelial or hepatocyte models, perturb CASP7 cleavage and secretion, and assay extracellular pro-SMPD1 processing, ceramide production, and membrane resealing.
Hypothesis: Human CASP7 is secreted through GSDMD or perforin pores and activates extracellular SMPD1 for ceramide-dependent membrane repair.
Type: cellular pathway rescue assay
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