XIAP is a cytosolic and nuclear inhibitor-of-apoptosis protein with three BIR domains and a C-terminal RING E3 ubiquitin-ligase domain. Its BIR2/linker and BIR3 elements directly inhibit active apoptotic caspases, while its RING domain ubiquitinates pathway-specific substrates in apoptosis, NOD1/NOD2 innate immune signaling, Wnt/TLE transcriptional control, copper homeostasis, and interferon regulation. Direct apoptotic protease inhibition targets caspase-3 and caspase-7 through the BIR2-associated linker and caspase-9 through BIR3; these mechanisms do not imply inhibition of every caspase or all IAP-family proteins.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004842 ubiquitin-protein transferase activity | IDA PMID:19473982 X-linked inhibitor of apoptosis protein (XIAP) regulates PTE... | MODIFY | Summary: XIAP RING-domain ubiquitin transfer is better captured by ubiquitin protein ligase activity. Reason: The seeded term or process is a broad proxy for XIAP's catalytic RING E3 activity. Replace it with GO:0061630, the specific ubiquitin protein ligase molecular function supported by direct XIAP substrate-ubiquitination studies. Proposed replacements: ubiquitin protein ligase activity |
| GO:0004842 ubiquitin-protein transferase activity | IDA PMID:20154138 Regulation of the copper chaperone CCS by XIAP-mediated ubiq... | MODIFY | Summary: XIAP RING-domain ubiquitin transfer is better captured by ubiquitin protein ligase activity. Reason: The seeded term or process is a broad proxy for XIAP's catalytic RING E3 activity. Replace it with GO:0061630, the specific ubiquitin protein ligase molecular function supported by direct XIAP substrate-ubiquitination studies. Proposed replacements: ubiquitin protein ligase activity |
| GO:0004842 ubiquitin-protein transferase activity | IDA PMID:21931591 cIAP1/2 are direct E3 ligases conjugating diverse types of u... | MODIFY | Summary: XIAP RING-domain ubiquitin transfer is better captured by ubiquitin protein ligase activity. Reason: The seeded term or process is a broad proxy for XIAP's catalytic RING E3 activity. Replace it with GO:0061630, the specific ubiquitin protein ligase molecular function supported by direct XIAP substrate-ubiquitination studies. Proposed replacements: ubiquitin protein ligase activity |
| GO:0004842 ubiquitin-protein transferase activity | IDA PMID:22304967 XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt ... | MODIFY | Summary: XIAP RING-domain ubiquitin transfer is better captured by ubiquitin protein ligase activity. Reason: The seeded term or process is a broad proxy for XIAP's catalytic RING E3 activity. Replace it with GO:0061630, the specific ubiquitin protein ligase molecular function supported by direct XIAP substrate-ubiquitination studies. Proposed replacements: ubiquitin protein ligase activity |
| GO:0004842 ubiquitin-protein transferase activity | IDA PMID:22607974 The ubiquitin ligase XIAP recruits LUBAC for NOD2 signaling ... | MODIFY | Summary: XIAP RING-domain ubiquitin transfer is better captured by ubiquitin protein ligase activity. Reason: The seeded term or process is a broad proxy for XIAP's catalytic RING E3 activity. Replace it with GO:0061630, the specific ubiquitin protein ligase molecular function supported by direct XIAP substrate-ubiquitination studies. Proposed replacements: ubiquitin protein ligase activity |
| GO:0004842 ubiquitin-protein transferase activity | IDA PMID:29452636 Disruption of XIAP-RIP2 Association Blocks NOD2-Mediated Inf... | MODIFY | Summary: XIAP RING-domain ubiquitin transfer is better captured by ubiquitin protein ligase activity. Reason: The seeded term or process is a broad proxy for XIAP's catalytic RING E3 activity. Replace it with GO:0061630, the specific ubiquitin protein ligase molecular function supported by direct XIAP substrate-ubiquitination studies. Proposed replacements: ubiquitin protein ligase activity |
| GO:0004842 ubiquitin-protein transferase activity | IMP PMID:29020630 Degradation of Bcl-2 by XIAP and ARTS Promotes Apoptosis. | MODIFY | Summary: XIAP RING-domain ubiquitin transfer is better captured by ubiquitin protein ligase activity. Reason: The seeded term or process is a broad proxy for XIAP's catalytic RING E3 activity. Replace it with GO:0061630, the specific ubiquitin protein ligase molecular function supported by direct XIAP substrate-ubiquitination studies. Proposed replacements: ubiquitin protein ligase activity |
| GO:0004869 cysteine-type endopeptidase inhibitor activity | IDA PMID:11257230 Structural basis of caspase-7 inhibition by XIAP. | ACCEPT | Summary: XIAP directly inhibits cysteine-type endopeptidases (caspases). The genus term is correct as it stands; the apoptotic context is carried by the module and core functions, not by a precomposed term. Reason: The genus GO:0004869 is the right term. An earlier pass proposed MODIFY to the precomposed GO:0043027; per projects/INVOLVED_IN_PRECOMPOSITION.md that adds only the apoptotic context, which is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and the core functions. Superseded reasoning (it argued for the precomposed term), retained only for its evidence: XIAP BIR2/linker directly blocks caspase-3 and caspase-7 substrate grooves, and BIR3 restrains processed caspase-9. Replace the broad row with GO:0043027 to capture the direct caspase-inhibitor activity in apoptosis. Supporting Evidence: PMID:11257230 Here we present the crystal structure of caspase-7 in complex with a potent inhibitory fragment from XIAP |
| GO:0004869 cysteine-type endopeptidase inhibitor activity | IDA PMID:11257231 Structural basis of caspase inhibition by XIAP: differential... | ACCEPT | Summary: XIAP directly inhibits cysteine-type endopeptidases (caspases). The genus term is correct as it stands; the apoptotic context is carried by the module and core functions, not by a precomposed term. Reason: The genus GO:0004869 is the right term. An earlier pass proposed MODIFY to the precomposed GO:0043027; per projects/INVOLVED_IN_PRECOMPOSITION.md that adds only the apoptotic context, which is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and the core functions. Superseded reasoning (it argued for the precomposed term), retained only for its evidence: XIAP BIR2/linker directly blocks caspase-3 and caspase-7 substrate grooves, and BIR3 restrains processed caspase-9. Replace the broad row with GO:0043027 to capture the direct caspase-inhibitor activity in apoptosis. |
| GO:0004869 cysteine-type endopeptidase inhibitor activity | IDA PMID:16916640 Engineered hybrid dimers: tracking the activation pathway of... | ACCEPT | Summary: XIAP directly inhibits cysteine-type endopeptidases (caspases). The genus term is correct as it stands; the apoptotic context is carried by the module and core functions, not by a precomposed term. Reason: The genus GO:0004869 is the right term. An earlier pass proposed MODIFY to the precomposed GO:0043027; per projects/INVOLVED_IN_PRECOMPOSITION.md that adds only the apoptotic context, which is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and the core functions. Superseded reasoning (it argued for the precomposed term), retained only for its evidence: XIAP BIR2/linker directly blocks caspase-3 and caspase-7 substrate grooves, and BIR3 restrains processed caspase-9. Replace the broad row with GO:0043027 to capture the direct caspase-inhibitor activity in apoptosis. |
| GO:0004869 cysteine-type endopeptidase inhibitor activity | IDA PMID:9230442 X-linked IAP is a direct inhibitor of cell-death proteases. | ACCEPT | Summary: XIAP directly inhibits cysteine-type endopeptidases (caspases). The genus term is correct as it stands; the apoptotic context is carried by the module and core functions, not by a precomposed term. Reason: The genus GO:0004869 is the right term. An earlier pass proposed MODIFY to the precomposed GO:0043027; per projects/INVOLVED_IN_PRECOMPOSITION.md that adds only the apoptotic context, which is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and the core functions. Superseded reasoning (it argued for the precomposed term), retained only for its evidence: XIAP BIR2/linker directly blocks caspase-3 and caspase-7 substrate grooves, and BIR3 restrains processed caspase-9. Replace the broad row with GO:0043027 to capture the direct caspase-inhibitor activity in apoptosis. Supporting Evidence: PMID:9230442 Here we show that human X-chromosome-linked IAP directly inhibits at least two members of the caspase family of cell-death proteases, caspase-3 and caspase-7. |
| GO:0004869 cysteine-type endopeptidase inhibitor activity | IEA GO_REF:0000117 | ACCEPT | Summary: XIAP directly inhibits cysteine-type endopeptidases (caspases). The genus term is correct as it stands; the apoptotic context is carried by the module and core functions, not by a precomposed term. Reason: The genus GO:0004869 is the right term. An earlier pass proposed MODIFY to the precomposed GO:0043027; per projects/INVOLVED_IN_PRECOMPOSITION.md that adds only the apoptotic context, which is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and the core functions. Superseded reasoning (it argued for the precomposed term), retained only for its evidence: XIAP BIR2/linker directly blocks caspase-3 and caspase-7 substrate grooves, and BIR3 restrains processed caspase-9. Replace the broad row with GO:0043027 to capture the direct caspase-inhibitor activity in apoptosis. |
| GO:0005515 protein binding | IPI PMID:11140638 Structural basis of IAP recognition by Smac/DIABLO. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:11257230 Structural basis of caspase-7 inhibition by XIAP. | MODIFY | Summary: XIAP directly inhibits cysteine-type endopeptidases (caspases); the row is modified to cysteine-type endopeptidase inhibitor activity, with the apoptotic context carried by the module and core functions. Reason: The replacement is the genus rather than the precomposed GO:0043027 (projects/INVOLVED_IN_PRECOMPOSITION.md); the apoptotic context is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and the core functions. Earlier reasoning, retained for its evidence (its term id updated to the genus): XIAP BIR2/linker directly blocks caspase-3 and caspase-7 substrate grooves, and BIR3 restrains processed caspase-9. Replace the broad row with GO:0004869 to capture the direct caspase-inhibitor activity in apoptosis. Proposed replacements: cysteine-type endopeptidase inhibitor activity |
| GO:0005515 protein binding | IPI PMID:11257231 Structural basis of caspase inhibition by XIAP: differential... | MODIFY | Summary: XIAP directly inhibits cysteine-type endopeptidases (caspases); the row is modified to cysteine-type endopeptidase inhibitor activity, with the apoptotic context carried by the module and core functions. Reason: The replacement is the genus rather than the precomposed GO:0043027 (projects/INVOLVED_IN_PRECOMPOSITION.md); the apoptotic context is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and the core functions. Earlier reasoning, retained for its evidence (its term id updated to the genus): XIAP BIR2/linker directly blocks caspase-3 and caspase-7 substrate grooves, and BIR3 restrains processed caspase-9. Replace the broad row with GO:0004869 to capture the direct caspase-inhibitor activity in apoptosis. Proposed replacements: cysteine-type endopeptidase inhibitor activity |
| GO:0005515 protein binding | IPI PMID:11257232 Structural basis for the inhibition of caspase-3 by XIAP. | MODIFY | Summary: XIAP directly inhibits cysteine-type endopeptidases (caspases); the row is modified to cysteine-type endopeptidase inhibitor activity, with the apoptotic context carried by the module and core functions. Reason: The replacement is the genus rather than the precomposed GO:0043027 (projects/INVOLVED_IN_PRECOMPOSITION.md); the apoptotic context is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and the core functions. Earlier reasoning, retained for its evidence (its term id updated to the genus): XIAP BIR2/linker directly blocks caspase-3 and caspase-7 substrate grooves, and BIR3 restrains processed caspase-9. Replace the broad row with GO:0004869 to capture the direct caspase-inhibitor activity in apoptosis. Proposed replacements: cysteine-type endopeptidase inhibitor activity |
| GO:0005515 protein binding | IPI PMID:11583623 A serine protease, HtrA2, is released from the mitochondria ... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:11602612 The serine protease Omi/HtrA2 regulates apoptosis by binding... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:11604410 HtrA2 promotes cell death through its serine protease activi... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:11604410 HtrA2 promotes cell death through its serine protease activi... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:11604410 HtrA2 promotes cell death through its serine protease activi... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:11801603 SMAC negatively regulates the anti-apoptotic activity of mel... | UNDECIDED | Summary: The cached abstract does not verify this exact XIAP interaction row. Reason: This experimental IPI row may be supported by a table or control in the full text, but the locally cached abstract foregrounds a different IAP, antagonist, or interaction context. Leave it undecided rather than overruling a curator assertion from incomplete evidence. |
| GO:0005515 protein binding | IPI PMID:11801603 SMAC negatively regulates the anti-apoptotic activity of mel... | MODIFY | Summary: Independent biochemical evidence identifies XIAP as a direct caspase-9 inhibitor. Reason: The original interaction-screen or antagonist-study record remains intact; its exact experimental context is not substituted by the independent source. PMID:12620238 directly establishes XIAP BIR3 inhibition of caspase-9, supporting this functional refinement of the known interaction at gene level. The replacement is the genus rather than the precomposed GO:0043027 (projects/INVOLVED_IN_PRECOMPOSITION.md); the apoptotic context is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and the core functions. Proposed replacements: cysteine-type endopeptidase inhibitor activity Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:11801603 SMAC negatively regulates the anti-apoptotic activity of mel... | UNDECIDED | Summary: The cached abstract does not verify this exact XIAP interaction row. Reason: This experimental IPI row may be supported by a table or control in the full text, but the locally cached abstract foregrounds a different IAP, antagonist, or interaction context. Leave it undecided rather than overruling a curator assertion from incomplete evidence. |
| GO:0005515 protein binding | IPI PMID:11865055 IAP suppression of apoptosis involves distinct mechanisms: t... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:12620238 Mechanism of XIAP-mediated inhibition of caspase-9. | MODIFY | Summary: XIAP directly inhibits cysteine-type endopeptidases (caspases); the row is modified to cysteine-type endopeptidase inhibitor activity, with the apoptotic context carried by the module and core functions. Reason: The replacement is the genus rather than the precomposed GO:0043027 (projects/INVOLVED_IN_PRECOMPOSITION.md); the apoptotic context is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and the core functions. Earlier reasoning, retained for its evidence (its term id updated to the genus): XIAP BIR2/linker directly blocks caspase-3 and caspase-7 substrate grooves, and BIR3 restrains processed caspase-9. Replace the broad row with GO:0004869 to capture the direct caspase-inhibitor activity in apoptosis. Proposed replacements: cysteine-type endopeptidase inhibitor activity |
| GO:0005515 protein binding | IPI PMID:14685266 A novel role for XIAP in copper homeostasis through regulati... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:16282325 Distinct BIR domains of cIAP1 mediate binding to and ubiquit... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:17318174 Notch inhibits apoptosis by direct interference with XIAP ub... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:17318174 Notch inhibits apoptosis by direct interference with XIAP ub... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:17318174 Notch inhibits apoptosis by direct interference with XIAP ub... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:18022362 IAP antagonists induce autoubiquitination of c-IAPs, NF-kapp... | MODIFY | Summary: Independent biochemical evidence identifies XIAP as a direct caspase-9 inhibitor. Reason: The original interaction-screen or antagonist-study record remains intact; its exact experimental context is not substituted by the independent source. PMID:12620238 directly establishes XIAP BIR3 inhibition of caspase-9, supporting this functional refinement of the known interaction at gene level. The replacement is the genus rather than the precomposed GO:0043027 (projects/INVOLVED_IN_PRECOMPOSITION.md); the apoptotic context is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and the core functions. Proposed replacements: cysteine-type endopeptidase inhibitor activity Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19012568 Binding properties of the C-terminal domain of VIAF. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:19273858 S-nitrosylation of XIAP compromises neuronal survival in Par... | MODIFY | Summary: XIAP directly inhibits cysteine-type endopeptidases (caspases); the row is modified to cysteine-type endopeptidase inhibitor activity, with the apoptotic context carried by the module and core functions. Reason: The replacement is the genus rather than the precomposed GO:0043027 (projects/INVOLVED_IN_PRECOMPOSITION.md); the apoptotic context is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and the core functions. Earlier reasoning, retained for its evidence (its term id updated to the genus): XIAP BIR2/linker directly blocks caspase-3 and caspase-7 substrate grooves, and BIR3 restrains processed caspase-9. Replace the broad row with GO:0004869 to capture the direct caspase-inhibitor activity in apoptosis. Proposed replacements: cysteine-type endopeptidase inhibitor activity |
| GO:0005515 protein binding | IPI PMID:19473982 X-linked inhibitor of apoptosis protein (XIAP) regulates PTE... | MODIFY | Summary: PTEN substrate binding is better represented by XIAP ubiquitin protein ligase activity. Reason: PTEN is a direct XIAP ubiquitination substrate. The original generic protein-binding row should be replaced with GO:0061630, which captures the catalytic RING E3 activity assayed in the same study. Proposed replacements: ubiquitin protein ligase activity Supporting Evidence: PMID:19473982 Finally, we found that XIAP can directly ubiquitinate PTEN in vitro. |
| GO:0005515 protein binding | IPI PMID:19549727 Analysis of the human E2 ubiquitin conjugating enzyme protei... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:19549727 Analysis of the human E2 ubiquitin conjugating enzyme protei... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:19549727 Analysis of the human E2 ubiquitin conjugating enzyme protei... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:19549727 Analysis of the human E2 ubiquitin conjugating enzyme protei... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:19549727 Analysis of the human E2 ubiquitin conjugating enzyme protei... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:19667203 XIAP mediates NOD signaling via interaction with RIP2. | REMOVE | Summary: XIAP-RIPK2 binding is mechanistic but should not be kept as generic protein binding. Reason: XIAP uses BIR2 to bind RIPK2 and its RING domain ubiquitinates RIPK2 in the NOD1/NOD2 signalosome. GOA already carries specific NOD1, NOD2, K63-ubiquitination, and ubiquitin-ligase rows for that biology. Supporting Evidence: PMID:29452636 we identify NOD2 signaling and XIAP-dependent ubiquitination sites on RIP2 and show that mutating these lysine residues adversely affects NOD2 pathway signaling. |
| GO:0005515 protein binding | IPI PMID:19667203 XIAP mediates NOD signaling via interaction with RIP2. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:20154138 Regulation of the copper chaperone CCS by XIAP-mediated ubiq... | MODIFY | Summary: CCS substrate binding is better represented by XIAP ubiquitin protein ligase activity. Reason: CCS is a direct XIAP ubiquitination substrate. The original generic protein-binding row should be replaced with GO:0061630, which captures the catalytic RING E3 activity assayed in the same study. Proposed replacements: ubiquitin protein ligase activity Supporting Evidence: PMID:20154138 We also find that CCS is a target of the E3 ubiquitin ligase activity of XIAP |
| GO:0005515 protein binding | IPI PMID:20171186 Molecular interaction between HAX-1 and XIAP inhibits apopto... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:21185211 ARTS and Siah collaborate in a pathway for XIAP degradation. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:21185211 ARTS and Siah collaborate in a pathway for XIAP degradation. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:21185211 ARTS and Siah collaborate in a pathway for XIAP degradation. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:21536684 Survivin monomer plays an essential role in apoptosis regula... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:21695558 ARTS binds to a distinct domain in XIAP-BIR3 and promotes ap... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:21695558 ARTS binds to a distinct domain in XIAP-BIR3 and promotes ap... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:21849505 The USP19 deubiquitinase regulates the stability of c-IAP1 a... | REMOVE | Summary: The primary full text confirms XIAP association with USP19. Reason: PMID:21849505 explicitly reports XIAP-USP19 association in Figure 1B and states its consequence is unclear. Remove only the uninformative bare protein-binding annotation under current policy; the measured interaction is retained and no new catalytic function is inferred. Supporting Evidence: PMID:21849505 In addition, XIAP associated with USP19 |
| GO:0005515 protein binding | IPI PMID:21931591 cIAP1/2 are direct E3 ligases conjugating diverse types of u... | REMOVE | Summary: XIAP-RIPK2 binding is mechanistic but should not be kept as generic protein binding. Reason: XIAP uses BIR2 to bind RIPK2 and its RING domain ubiquitinates RIPK2 in the NOD1/NOD2 signalosome. GOA already carries specific NOD1, NOD2, K63-ubiquitination, and ubiquitin-ligase rows for that biology. Supporting Evidence: PMID:29452636 we identify NOD2 signaling and XIAP-dependent ubiquitination sites on RIP2 and show that mutating these lysine residues adversely affects NOD2 pathway signaling. |
| GO:0005515 protein binding | IPI PMID:21931591 cIAP1/2 are direct E3 ligases conjugating diverse types of u... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:22117219 IAPs regulate the plasticity of cell migration by directly t... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:22304967 XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt ... | REMOVE | Summary: TLE3/TCF7L2 interactions are better captured by XIAP-dependent Wnt signaling. Reason: XIAP acts in a nuclear TCF/Lef complex where it monoubiquitylates Groucho/TLE to promote canonical Wnt signaling. The specific Wnt and E3 rows capture this function better than generic protein binding. Supporting Evidence: PMID:22304967 Upon Wnt pathway activation, XIAP is recruited to TCF/Lef where it monoubiquitylates Groucho (Gro)/TLE. |
| GO:0005515 protein binding | IPI PMID:22304967 XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt ... | REMOVE | Summary: TLE3/TCF7L2 interactions are better captured by XIAP-dependent Wnt signaling. Reason: XIAP acts in a nuclear TCF/Lef complex where it monoubiquitylates Groucho/TLE to promote canonical Wnt signaling. The specific Wnt and E3 rows capture this function better than generic protein binding. Supporting Evidence: PMID:22304967 Upon Wnt pathway activation, XIAP is recruited to TCF/Lef where it monoubiquitylates Groucho (Gro)/TLE. |
| GO:0005515 protein binding | IPI PMID:22465666 Identification of a novel protein kinase CΞ΄-Smac complex tha... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:22508683 Molecular and biochemical characterization of a unique mutat... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:23251006 Impairment of glioma stem cell survival and growth by a nove... | REMOVE | Summary: XIAP-SMAC binding is supported by biochemical interaction experiments. Reason: The reciprocal DIABLO evidence guide verifies the purified XIAP fragment in PMID:23251006, and PMID:14512414 independently establishes the interaction. Remove only the uninformative bare protein-binding term; SMAC binds XIAP BIR domains, which does not mean XIAP itself has BIR-domain-binding activity. |
| GO:0005515 protein binding | IPI PMID:23818254 Disease-causing mutations in the XIAP BIR2 domain impair NOD... | REMOVE | Summary: XIAP-RIPK2 binding is mechanistic but should not be kept as generic protein binding. Reason: XIAP uses BIR2 to bind RIPK2 and its RING domain ubiquitinates RIPK2 in the NOD1/NOD2 signalosome. GOA already carries specific NOD1, NOD2, K63-ubiquitination, and ubiquitin-ligase rows for that biology. Supporting Evidence: PMID:29452636 we identify NOD2 signaling and XIAP-dependent ubiquitination sites on RIP2 and show that mutating these lysine residues adversely affects NOD2 pathway signaling. |
| GO:0005515 protein binding | IPI PMID:23818254 Disease-causing mutations in the XIAP BIR2 domain impair NOD... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:23818254 Disease-causing mutations in the XIAP BIR2 domain impair NOD... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:24698088 Dual regulatory switch confers tighter control on HtrA2 prot... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | MODIFY | Summary: XIAP directly inhibits cysteine-type endopeptidases (caspases); the row is modified to cysteine-type endopeptidase inhibitor activity, with the apoptotic context carried by the module and core functions. Reason: The replacement is the genus rather than the precomposed GO:0043027 (projects/INVOLVED_IN_PRECOMPOSITION.md); the apoptotic context is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and the core functions. Earlier reasoning, retained for its evidence (its term id updated to the genus): XIAP BIR2/linker directly blocks caspase-3 and caspase-7 substrate grooves, and BIR3 restrains processed caspase-9. Replace the broad row with GO:0004869 to capture the direct caspase-inhibitor activity in apoptosis. Proposed replacements: cysteine-type endopeptidase inhibitor activity |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | MODIFY | Summary: XIAP directly inhibits cysteine-type endopeptidases (caspases); the row is modified to cysteine-type endopeptidase inhibitor activity, with the apoptotic context carried by the module and core functions. Reason: The replacement is the genus rather than the precomposed GO:0043027 (projects/INVOLVED_IN_PRECOMPOSITION.md); the apoptotic context is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and the core functions. Earlier reasoning, retained for its evidence (its term id updated to the genus): XIAP BIR2/linker directly blocks caspase-3 and caspase-7 substrate grooves, and BIR3 restrains processed caspase-9. Replace the broad row with GO:0004869 to capture the direct caspase-inhibitor activity in apoptosis. Proposed replacements: cysteine-type endopeptidase inhibitor activity |
| GO:0005515 protein binding | IPI PMID:25260751 The MEKK1 PHD ubiquitinates TAB1 to activate MAPKs in respon... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:25502805 A massively parallel pipeline to clone DNA variants and exam... | MODIFY | Summary: Independent biochemical evidence identifies XIAP as a direct caspase-9 inhibitor. Reason: The original interaction-screen or antagonist-study record remains intact; its exact experimental context is not substituted by the independent source. PMID:12620238 directly establishes XIAP BIR3 inhibition of caspase-9, supporting this functional refinement of the known interaction at gene level. The replacement is the genus rather than the precomposed GO:0043027 (projects/INVOLVED_IN_PRECOMPOSITION.md); the apoptotic context is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and the core functions. Proposed replacements: cysteine-type endopeptidase inhibitor activity Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25910212 Widespread macromolecular interaction perturbations in human... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:27107012 Pooled-matrix protein interaction screens using Barcode Fusi... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:27107012 Pooled-matrix protein interaction screens using Barcode Fusi... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:27107012 Pooled-matrix protein interaction screens using Barcode Fusi... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:27107012 Pooled-matrix protein interaction screens using Barcode Fusi... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:28642151 The role of the LB structural loop and its interactions with... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:28642151 The role of the LB structural loop and its interactions with... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:29020630 Degradation of Bcl-2 by XIAP and ARTS Promotes Apoptosis. | REMOVE | Summary: The ARTS-BCL2 ternary-complex row is redundant with XIAP E3-ligase evidence. Reason: ARTS scaffolds XIAP and BCL2 so XIAP can ubiquitylate BCL2 during apoptosis. The same paper supports XIAP RING E3-ligase activity; keeping the ternary interaction as GO:0005515 would duplicate that mechanism at lower specificity. Supporting Evidence: PMID:29020630 XIAP serves as an E3 ligase for Bcl-2 and that ARTS is essential for this process. |
| GO:0005515 protein binding | IPI PMID:29892012 An interactome perturbation framework prioritizes damaging m... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:29997244 LuTHy: a double-readout bioluminescence-based two-hybrid tec... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31036715 Discerning the mechanism of action of HtrA4: a serine protea... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31260151 The HtrA3 protease promotes drug-induced death of lung cance... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31260151 The HtrA3 protease promotes drug-induced death of lung cance... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31260151 The HtrA3 protease promotes drug-induced death of lung cance... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31467278 Maximizing binary interactome mapping with a minimal number ... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31467278 Maximizing binary interactome mapping with a minimal number ... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31470122 Cellular substrates and pro-apoptotic function of the human ... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31470122 Cellular substrates and pro-apoptotic function of the human ... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31470122 Cellular substrates and pro-apoptotic function of the human ... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:31617661 Global Interactome Mapping of Mitochondrial Intermembrane Sp... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: XIAP-RIPK2 binding is mechanistic but should not be kept as generic protein binding. Reason: XIAP uses BIR2 to bind RIPK2 and its RING domain ubiquitinates RIPK2 in the NOD1/NOD2 signalosome. GOA already carries specific NOD1, NOD2, K63-ubiquitination, and ubiquitin-ligase rows for that biology. Supporting Evidence: PMID:29452636 we identify NOD2 signaling and XIAP-dependent ubiquitination sites on RIP2 and show that mutating these lysine residues adversely affects NOD2 pathway signaling. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005515 protein binding | IPI PMID:38191507 Understanding the molecular mechanism of pathogenic variants... | REMOVE | Summary: XIAP-RIPK2 binding is mechanistic but should not be kept as generic protein binding. Reason: XIAP uses BIR2 to bind RIPK2 and its RING domain ubiquitinates RIPK2 in the NOD1/NOD2 signalosome. GOA already carries specific NOD1, NOD2, K63-ubiquitination, and ubiquitin-ligase rows for that biology. Supporting Evidence: PMID:29452636 we identify NOD2 signaling and XIAP-dependent ubiquitination sites on RIP2 and show that mutating these lysine residues adversely affects NOD2 pathway signaling. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Generic XIAP protein-binding annotation. Reason: The row records a physical interaction but GO:0005515 does not capture XIAP's caspase-inhibitor or RING E3-ligase molecular function. Removal does not dispute the interaction; it removes an uninformative XIAP-side MF row. |
| GO:0005634 nucleus | EXP PMID:15665297 cIAP1 Localizes to the nuclear compartment and modulates the... | MODIFY | Summary: Supported nuclear subcompartments refine the broad nuclear assignment. Reason: The gene has independently supported nucleoplasmic Wnt-regulatory localization and a curated HPA nucleolar observation. Refine the broad nucleus assertion to both supported compartments; this does not require a separate nucleolar biochemical activity or assign the same compartment to every experimental condition. Proposed replacements: nucleoplasm nucleolus |
| GO:0005634 nucleus | IBA GO_REF:0000033 | MODIFY | Summary: Supported nuclear subcompartments refine the broad nuclear assignment. Reason: The gene has independently supported nucleoplasmic Wnt-regulatory localization and a curated HPA nucleolar observation. Refine the broad nucleus assertion to both supported compartments; this does not require a separate nucleolar biochemical activity or assign the same compartment to every experimental condition. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000005166 SUPPORTS TRANSFER The original broader claim is retained as biologically supported. Target/ortholog evidence refines its scope; this does not reject the ancestral placement or treat target experimental grounding as circular. Proposed replacements: nucleoplasm nucleolus |
| GO:0005634 nucleus | IDA PMID:22304967 XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt ... | MODIFY | Summary: Supported nuclear subcompartments refine the broad nuclear assignment. Reason: The gene has independently supported nucleoplasmic Wnt-regulatory localization and a curated HPA nucleolar observation. Refine the broad nucleus assertion to both supported compartments; this does not require a separate nucleolar biochemical activity or assign the same compartment to every experimental condition. Proposed replacements: nucleoplasm nucleolus |
| GO:0005634 nucleus | IEA GO_REF:0000044 | MODIFY | Summary: Supported nuclear subcompartments refine the broad nuclear assignment. Reason: The gene has independently supported nucleoplasmic Wnt-regulatory localization and a curated HPA nucleolar observation. Refine the broad nucleus assertion to both supported compartments; this does not require a separate nucleolar biochemical activity or assign the same compartment to every experimental condition. Proposed replacements: nucleoplasm nucleolus |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-3322429 | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-3322431 | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-3322434 | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005730 nucleolus | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Nucleolar localization is retained as a contextual observation. Reason: The HPA localization assertion concerns presence, not a requirement to demonstrate a separate nucleolar biochemical function. There is no contradictory localization evidence; retain the curated imaging observation without making nucleolar activity a core. |
| GO:0005737 cytoplasm | EXP PMID:21628460 TRIM32 protein sensitizes cells to tumor necrosis factor (TN... | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. Supporting Evidence: |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005737 cytoplasm | IC PMID:36394357 XAF1 prevents hyperproduction of type I interferon upon vira... | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005737 cytoplasm | IDA PMID:15665297 cIAP1 Localizes to the nuclear compartment and modulates the... | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005737 cytoplasm | IDA PMID:22304967 XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt ... | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. Supporting Evidence: |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005737 cytoplasm | TAS PMID:8654366 A conserved family of cellular genes related to the baculovi... | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005829 cytosol | TAS PMID:8654366 A conserved family of cellular genes related to the baculovi... | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-114354 | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-114392 | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6807134 | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9627078 | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9627104 | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9627107 | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9627350 | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9627369 | ACCEPT | Summary: XIAP has curated cytoplasmic or nuclear localization, but this location row is broader than its molecular roles. Reason: XIAP functions in cytoplasmic/cytosolic caspase and signaling assemblies and in nucleoplasmic TLE/TCF regulation. Retain this supported compartment at the resolution of the original experiment or ortholog inference; soluble versus assembled pools and nuclear translocation do not establish a single exclusive location. PMID:22304967 supports the nuclear signaling pool and PMID:11257230 the caspase-inhibitor mechanism. |
| GO:0006974 DNA damage response | IEP PMID:18049476 Che-1 activates XIAP expression in response to DNA damage. | KEEP AS NON CORE | Summary: XIAP contributes to a survival response after DNA damage. Reason: PMID:18049476 places XIAP downstream of Che-1/NF-kappaB and reports XIAP expression is necessary for the antiapoptotic activity. A response-to-damage term does not require DNA repair catalysis. Retain the stress-dependent survival response without assigning XIAP a repair enzyme or damage-sensor role. Supporting Evidence: |
| GO:0010804 negative regulation of tumor necrosis factor-mediated signaling pathway | IDA PMID:11865055 IAP suppression of apoptosis involves distinct mechanisms: t... | KEEP AS NON CORE | Summary: XIAP attenuates the apoptotic branch of TNF signaling. Reason: The GO definition covers a decrease in rate or extent of TNF-mediated signaling; it does not require inhibition of every downstream branch. XIAP protects against TNF-induced apoptosis through caspase inhibition and TAK1/JNK-dependent survival signaling. This context can coexist with positive NF-kappaB/JNK regulation. Supporting Evidence: |
| GO:0010804 negative regulation of tumor necrosis factor-mediated signaling pathway | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: XIAP attenuates the apoptotic branch of TNF signaling. Reason: The GO definition covers a decrease in rate or extent of TNF-mediated signaling; it does not require inhibition of every downstream branch. XIAP protects against TNF-induced apoptosis through caspase inhibition and TAK1/JNK-dependent survival signaling. This context can coexist with positive NF-kappaB/JNK regulation. Supporting Evidence: |
| GO:0019899 enzyme binding | IEA GO_REF:0000117 | MODIFY | Summary: Specific apoptotic caspase inhibition refines the enzyme-binding assertion. Reason: XIAP directly binds and inhibits caspases-3/7 and caspase-9. The broad enzyme-binding claim is true; refine it to its experimentally established inhibitory activity rather than removing a true broad term. The replacement is the genus rather than the precomposed GO:0043027 (projects/INVOLVED_IN_PRECOMPOSITION.md); the apoptotic context is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and the core functions. Proposed replacements: cysteine-type endopeptidase inhibitor activity |
| GO:0030510 regulation of BMP signaling pathway | TAS PMID:18414036 IAPs: more than just inhibitors of apoptosis proteins. | UNDECIDED | Summary: The review-only BMP signaling row is not locally resolvable. Reason: The cached paper is a review abstract, and the original BMP/TAB1 evidence is not present locally. Leave this TAS row undecided rather than accepting or rejecting it from incomplete evidence. |
| GO:0031398 positive regulation of protein ubiquitination | IBA GO_REF:0000033 | MODIFY | Summary: XIAP promotes LUBAC-dependent linear ubiquitination. Reason: XIAP both catalyzes substrate ubiquitination and recruits another ligase, LUBAC, to NOD2/RIPK2 complexes. Refine positive regulation of protein ubiquitination to the already represented linear-polyubiquitination control process. This retains the regulatory process rather than replacing a BP with E3 molecular activity; XIAP is not itself assigned linear-chain synthesis. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000799425 SUPPORTS TRANSFER The original broader claim is retained as biologically supported. Target/ortholog evidence refines its scope; this does not reject the ancestral placement or treat target experimental grounding as circular. Proposed replacements: positive regulation of protein linear polyubiquitination Supporting Evidence: |
| GO:0031398 positive regulation of protein ubiquitination | IDA PMID:21931591 cIAP1/2 are direct E3 ligases conjugating diverse types of u... | MODIFY | Summary: XIAP promotes LUBAC-dependent linear ubiquitination. Reason: XIAP both catalyzes substrate ubiquitination and recruits another ligase, LUBAC, to NOD2/RIPK2 complexes. Refine positive regulation of protein ubiquitination to the already represented linear-polyubiquitination control process. This retains the regulatory process rather than replacing a BP with E3 molecular activity; XIAP is not itself assigned linear-chain synthesis. Proposed replacements: positive regulation of protein linear polyubiquitination Supporting Evidence: |
| GO:0032481 positive regulation of type I interferon production | IDA PMID:36394357 XAF1 prevents hyperproduction of type I interferon upon vira... | KEEP AS NON CORE | Summary: XIAP has a non-apoptotic interferon-regulatory role through the XAF1/IRF7 axis. Reason: The XAF1 study and GO-CAM place XIAP E3-ligase activity upstream of IRF7 and type-I-interferon production; this is direct but outside apoptosis. Supporting Evidence: PMID:36394357 XAF1 is associated specifically with IRF7 and inhibits the activity of XIAP. |
| GO:0032496 response to lipopolysaccharide | IEA GO_REF:0000107 | UNDECIDED | Summary: The LPS-specific source experiment remains unresolved. Reason: The mouse donor has an experimental annotation to PMID:35263589. Its accessible abstract emphasizes Reg3gamma/EXTL3/BCL10 and does not expose the XIAP experiment; a targeted source search did not recover that result. NOD pathway specialization is not evidence that an LPS response is false. Defer the particular response assignment pending the primary experiment. Supporting Evidence: |
| GO:0032991 protein-containing complex | IEA GO_REF:0000117 | MODIFY | Summary: The supported caspase-inhibitor assembly refines the broad complex location. Reason: XIAP is a physical component of experimentally characterized caspase-inhibitor complexes. The broad protein-containing-complex claim is correct and is refined to the existing specific complex, not removed as redundant. Proposed replacements: protease inhibitor complex Supporting Evidence: |
| GO:0033554 cellular response to stress | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: XIAP participates in stress-dependent survival responses. Reason: The cellular response-to-stress term includes a change in cellular activity following stress. XIAP-mediated survival after DNA damage supports this broad response; breadth alone is not evidence of over-annotation. No stress-sensor activity is inferred. Supporting Evidence: |
| GO:0042742 defense response to bacterium | IDA PMID:29452636 Disruption of XIAP-RIP2 Association Blocks NOD2-Mediated Inf... | ACCEPT | Summary: XIAP contributes enzymatically to antibacterial innate signaling. Reason: XIAP-mediated RIPK2 ubiquitination supports NOD1/NOD2 recognition pathways and downstream inflammatory signaling. This is performed defense-response work, not merely correlation with infection. Retain the defense process alongside its more mechanistic pathway annotations. |
| GO:0042802 identical protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | ACCEPT | Summary: XIAP self-association is supported by structural and biochemical evidence. Reason: Identical-protein binding captures supported XIAP homomeric association, including functionally important RING assembly. The special removal policy for bare GO:0005515 does not apply to this specific binding term. Retain the original experiment and its construct context. |
| GO:0042802 identical protein binding | IPI PMID:19273858 S-nitrosylation of XIAP compromises neuronal survival in Par... | ACCEPT | Summary: XIAP self-association is supported by structural and biochemical evidence. Reason: Identical-protein binding captures supported XIAP homomeric association, including functionally important RING assembly. The special removal policy for bare GO:0005515 does not apply to this specific binding term. Retain the original experiment and its construct context. |
| GO:0042802 identical protein binding | IPI PMID:27107012 Pooled-matrix protein interaction screens using Barcode Fusi... | ACCEPT | Summary: XIAP self-association is supported by structural and biochemical evidence. Reason: Identical-protein binding captures supported XIAP homomeric association, including functionally important RING assembly. The special removal policy for bare GO:0005515 does not apply to this specific binding term. Retain the original experiment and its construct context. |
| GO:0042802 identical protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | ACCEPT | Summary: XIAP self-association is supported by structural and biochemical evidence. Reason: Identical-protein binding captures supported XIAP homomeric association, including functionally important RING assembly. The special removal policy for bare GO:0005515 does not apply to this specific binding term. Retain the original experiment and its construct context. |
| GO:0042981 regulation of apoptotic process | IDA PMID:11865055 IAP suppression of apoptosis involves distinct mechanisms: t... | MODIFY | Summary: XIAP anti-apoptotic activity should be represented by negative regulation of apoptotic process. Reason: The PMID:11865055 study assayed XIAP as protecting cells from TNF- or ICE-induced apoptosis through TAK1/JNK and caspase inhibition, so the parent regulation term should be narrowed to the negative-regulation child. Proposed replacements: negative regulation of apoptotic process |
| GO:0043027 cysteine-type endopeptidase inhibitor activity involved in apoptotic process | IBA GO_REF:0000033 | MODIFY | Summary: PAINT inference of the core XIAP caspase inhibitor activity; the row is modified to the genus cysteine-type endopeptidase inhibitor activity, with the apoptotic context carried by the module and core functions. Reason: The precomposed GO:0043027 is replaced by its genus GO:0004869 (projects/INVOLVED_IN_PRECOMPOSITION.md); the activity is unchanged and the apoptotic context is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and the core functions (see decomposed_into). The PAINT propagation itself is sound. Evidence: BIR-mediated inhibition of caspase-3, caspase-7, and caspase-9 is a conserved, experimentally grounded XIAP function. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000953271 SUPPORTS TRANSFER The IAP node supports the caspase inhibitor activity, which is core for XIAP; the MODIFY only decomposes the precomposed term to its genus and does not dispute the transfer. Proposed replacements: cysteine-type endopeptidase inhibitor activity Context of precomposed term: module apoptotic_execution_phase / xiap_caspase_inhibitor in core functions Decomposed from the precomposed GO:0043027 (projects/INVOLVED_IN_PRECOMPOSITION.md) to its genus GO:0004869; the claim is unchanged and the apoptotic context is carried by the module apoptotic_execution_phase#xiap_caspase_inhibitor and this review's core functions. |
| GO:0043066 negative regulation of apoptotic process | IBA GO_REF:0000033 | ACCEPT | Summary: XIAP directly inhibits apoptotic caspases and thereby negatively regulates apoptosis. Reason: This is the right broad biological-process assertion for the caspase-inhibitor activity of XIAP. |
| GO:0043066 negative regulation of apoptotic process | IDA PMID:11257230 Structural basis of caspase-7 inhibition by XIAP. | ACCEPT | Summary: XIAP directly inhibits apoptotic caspases and thereby negatively regulates apoptosis. Reason: This is the right broad biological-process assertion for the caspase-inhibitor activity of XIAP. Supporting Evidence: PMID:11257230 Here we present the crystal structure of caspase-7 in complex with a potent inhibitory fragment from XIAP |
| GO:0043066 negative regulation of apoptotic process | IDA PMID:11583623 A serine protease, HtrA2, is released from the mitochondria ... | ACCEPT | Summary: XIAP directly inhibits apoptotic caspases and thereby negatively regulates apoptosis. Reason: This is the right broad biological-process assertion for the caspase-inhibitor activity of XIAP. Supporting Evidence: PMID:11604410 DIABLO/Smac, prevent XIAP inhibition of active caspase 3 in vitro and is able to counteract XIAP protection of mammalian NT2 cells against UV-induced cell death. |
| GO:0043066 negative regulation of apoptotic process | IEA GO_REF:0000117 | ACCEPT | Summary: XIAP directly inhibits apoptotic caspases and thereby negatively regulates apoptosis. Reason: This is the right broad biological-process assertion for the caspase-inhibitor activity of XIAP. |
| GO:0043066 negative regulation of apoptotic process | IMP PMID:18049476 Che-1 activates XIAP expression in response to DNA damage. | ACCEPT | Summary: XIAP directly inhibits apoptotic caspases and thereby negatively regulates apoptosis. Reason: This is the right broad biological-process assertion for the caspase-inhibitor activity of XIAP. |
| GO:0043066 negative regulation of apoptotic process | IMP PMID:22173242 RIP1 is required for IAP inhibitor-mediated sensitization of... | ACCEPT | Summary: XIAP directly inhibits apoptotic caspases and thereby negatively regulates apoptosis. Reason: This is the right broad biological-process assertion for the caspase-inhibitor activity of XIAP. |
| GO:0043066 negative regulation of apoptotic process | NAS PMID:11257230 Structural basis of caspase-7 inhibition by XIAP. | ACCEPT | Summary: XIAP directly inhibits apoptotic caspases and thereby negatively regulates apoptosis. Reason: This is the right broad biological-process assertion for the caspase-inhibitor activity of XIAP. Supporting Evidence: PMID:11257230 Here we present the crystal structure of caspase-7 in complex with a potent inhibitory fragment from XIAP |
| GO:0043123 positive regulation of canonical NF-kappaB signal transduction | IDA PMID:19667203 XIAP mediates NOD signaling via interaction with RIP2. | ACCEPT | Summary: XIAP positively regulates canonical NF-kappaB signaling downstream of NOD receptors. Reason: RIPK2 ubiquitination and LUBAC recruitment promote the signaling complex that activates NF-kappaB. The positive-control process is biologically supported; replacing it with ubiquitination or pathway membership alone would lose its regulatory meaning. |
| GO:0043123 positive regulation of canonical NF-kappaB signal transduction | IDA PMID:22607974 The ubiquitin ligase XIAP recruits LUBAC for NOD2 signaling ... | ACCEPT | Summary: XIAP positively regulates canonical NF-kappaB signaling downstream of NOD receptors. Reason: RIPK2 ubiquitination and LUBAC recruitment promote the signaling complex that activates NF-kappaB. The positive-control process is biologically supported; replacing it with ubiquitination or pathway membership alone would lose its regulatory meaning. |
| GO:0045088 regulation of innate immune response | TAS PMID:21447281 Inhibitor of apoptosis (IAP) proteins in regulation of infla... | ACCEPT | Summary: XIAP regulates innate immune signal propagation. Reason: Direct NOD1/NOD2-RIPK2 ubiquitination and LUBAC recruitment support the broad innate-immune regulatory claim. Immune regulation is a major XIAP function independent of its caspase inhibition, not an over-annotation because this audit also considers apoptosis. |
| GO:0046330 positive regulation of JNK cascade | IDA PMID:11865055 IAP suppression of apoptosis involves distinct mechanisms: t... | KEEP AS NON CORE | Summary: XIAP can activate TAK1/JNK signaling as a non-core survival branch. Reason: PMID:11865055 supports XIAP/TAB1/TAK1-dependent JNK activation in an overexpression survival system; this is peripheral to the direct caspase-inhibitor activity. |
| GO:0046330 positive regulation of JNK cascade | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: XIAP can activate TAK1/JNK signaling as a non-core survival branch. Reason: PMID:11865055 supports XIAP/TAB1/TAK1-dependent JNK activation in an overexpression survival system; this is peripheral to the direct caspase-inhibitor activity. |
| GO:0050727 regulation of inflammatory response | TAS PMID:21447281 Inhibitor of apoptosis (IAP) proteins in regulation of infla... | KEEP AS NON CORE | Summary: XIAP modulates inflammatory output through innate signaling. Reason: NOD/RIPK2 signaling and the inflammatory phenotype of XIAP deficiency support regulation of inflammation. This process is retained with its cellular and disease context; it does not mean XIAP is itself a cytokine or that all inflammatory branches have the same sign. |
| GO:0051726 regulation of cell cycle | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: XIAP can control cell-cycle progression through its RING-dependent signaling activity. Reason: PMID:23720779 reports reduced cyclin D1 expression and cell-cycle transition in XIAP-deficient human cancer cells, with a requirement for XIAP E3 function in PP2A/c-Jun regulation. This target evidence supports a contextual cell-cycle role and gives no basis to reject the PAINT ancestral placement merely because other IAPs also regulate the cell cycle. Supporting Evidence: |
| GO:0055070 copper ion homeostasis | TAS PMID:17382285 XIAP: cell death regulation meets copper homeostasis. | KEEP AS NON CORE | Summary: XIAP ubiquitinates COMMD1 and CCS in copper-homeostasis biology. Reason: The copper branch is real but non-apoptotic and secondary to XIAP's caspase-inhibitor and RING E3 activities. Supporting Evidence: PMID:20154138 We also find that CCS is a target of the E3 ubiquitin ligase activity of XIAP |
| GO:0060785 regulation of apoptosis involved in tissue homeostasis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Tissue-homeostasis apoptosis regulation is supported by mouse ortholog experiments. Reason: Native Xiap loss modifies the ARTS/Sept4-dependent intestinal crypt survival phenotype in PMID:30389919. Retain the human ortholog inference with its mouse tissue context explicit, rather than treating lack of a direct human tissue experiment as contradiction. Supporting Evidence: |
| GO:0061630 ubiquitin protein ligase activity | EXP PMID:19473982 X-linked inhibitor of apoptosis protein (XIAP) regulates PTE... | ACCEPT | Summary: XIAP has intrinsic RING-domain ubiquitin protein ligase activity. Reason: XIAP is a bona fide RING E3 ubiquitin ligase that ubiquitinates multiple substrates, including PTEN, CCS, RIPK2, Groucho/TLE proteins, IRF7-pathway components, and BCL2 in different contexts. Supporting Evidence: PMID:20154138 We also find that CCS is a target of the E3 ubiquitin ligase activity of XIAP |
| GO:0061630 ubiquitin protein ligase activity | EXP PMID:20154138 Regulation of the copper chaperone CCS by XIAP-mediated ubiq... | ACCEPT | Summary: XIAP has intrinsic RING-domain ubiquitin protein ligase activity. Reason: XIAP is a bona fide RING E3 ubiquitin ligase that ubiquitinates multiple substrates, including PTEN, CCS, RIPK2, Groucho/TLE proteins, IRF7-pathway components, and BCL2 in different contexts. Supporting Evidence: |
| GO:0061630 ubiquitin protein ligase activity | EXP PMID:21931591 cIAP1/2 are direct E3 ligases conjugating diverse types of u... | ACCEPT | Summary: XIAP has intrinsic RING-domain ubiquitin protein ligase activity. Reason: XIAP is a bona fide RING E3 ubiquitin ligase that ubiquitinates multiple substrates, including PTEN, CCS, RIPK2, Groucho/TLE proteins, IRF7-pathway components, and BCL2 in different contexts. Supporting Evidence: |
| GO:0061630 ubiquitin protein ligase activity | EXP PMID:22304967 XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt ... | ACCEPT | Summary: XIAP has intrinsic RING-domain ubiquitin protein ligase activity. Reason: XIAP is a bona fide RING E3 ubiquitin ligase that ubiquitinates multiple substrates, including PTEN, CCS, RIPK2, Groucho/TLE proteins, IRF7-pathway components, and BCL2 in different contexts. Supporting Evidence: PMID:22304967 Upon Wnt pathway activation, XIAP is recruited to TCF/Lef where it monoubiquitylates Groucho (Gro)/TLE. |
| GO:0061630 ubiquitin protein ligase activity | EXP PMID:22607974 The ubiquitin ligase XIAP recruits LUBAC for NOD2 signaling ... | ACCEPT | Summary: XIAP has intrinsic RING-domain ubiquitin protein ligase activity. Reason: XIAP is a bona fide RING E3 ubiquitin ligase that ubiquitinates multiple substrates, including PTEN, CCS, RIPK2, Groucho/TLE proteins, IRF7-pathway components, and BCL2 in different contexts. Supporting Evidence: PMID:22607974 We find that XIAP ubiquitylates RIPK2 and recruits the linear ubiquitin chain assembly complex (LUBAC) to NOD2. |
| GO:0061630 ubiquitin protein ligase activity | EXP PMID:30026309 Small molecule inhibitors reveal an indispensable scaffoldin... | ACCEPT | Summary: XIAP has intrinsic RING-domain ubiquitin protein ligase activity. Reason: XIAP is a bona fide RING E3 ubiquitin ligase that ubiquitinates multiple substrates, including PTEN, CCS, RIPK2, Groucho/TLE proteins, IRF7-pathway components, and BCL2 in different contexts. Supporting Evidence: |
| GO:0061630 ubiquitin protein ligase activity | IBA GO_REF:0000033 | ACCEPT | Summary: XIAP has intrinsic RING-domain ubiquitin protein ligase activity. Reason: XIAP is a bona fide RING E3 ubiquitin ligase that ubiquitinates multiple substrates, including PTEN, CCS, RIPK2, Groucho/TLE proteins, IRF7-pathway components, and BCL2 in different contexts. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:29452636 Disruption of XIAP-RIP2 Association Blocks NOD2-Mediated Inf... | ACCEPT | Summary: XIAP has intrinsic RING-domain ubiquitin protein ligase activity. Reason: XIAP is a bona fide RING E3 ubiquitin ligase that ubiquitinates multiple substrates, including PTEN, CCS, RIPK2, Groucho/TLE proteins, IRF7-pathway components, and BCL2 in different contexts. Supporting Evidence: PMID:29452636 we identify NOD2 signaling and XIAP-dependent ubiquitination sites on RIP2 and show that mutating these lysine residues adversely affects NOD2 pathway signaling. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:36394357 XAF1 prevents hyperproduction of type I interferon upon vira... | ACCEPT | Summary: XIAP has intrinsic RING-domain ubiquitin protein ligase activity. Reason: XIAP is a bona fide RING E3 ubiquitin ligase that ubiquitinates multiple substrates, including PTEN, CCS, RIPK2, Groucho/TLE proteins, IRF7-pathway components, and BCL2 in different contexts. Supporting Evidence: PMID:36394357 XAF1 is associated specifically with IRF7 and inhibits the activity of XIAP. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:36749823 USP47 deubiquitylates Groucho/TLE to promote Wnt-Ξ²-catenin s... | ACCEPT | Summary: XIAP has intrinsic RING-domain ubiquitin protein ligase activity. Reason: XIAP is a bona fide RING E3 ubiquitin ligase that ubiquitinates multiple substrates, including PTEN, CCS, RIPK2, Groucho/TLE proteins, IRF7-pathway components, and BCL2 in different contexts. Supporting Evidence: |
| GO:0061630 ubiquitin protein ligase activity | IEA GO_REF:0000120 | ACCEPT | Summary: XIAP has intrinsic RING-domain ubiquitin protein ligase activity. Reason: XIAP is a bona fide RING E3 ubiquitin ligase that ubiquitinates multiple substrates, including PTEN, CCS, RIPK2, Groucho/TLE proteins, IRF7-pathway components, and BCL2 in different contexts. |
| GO:0061630 ubiquitin protein ligase activity | TAS Reactome:R-HSA-6807134 | ACCEPT | Summary: XIAP has intrinsic RING-domain ubiquitin protein ligase activity. Reason: XIAP is a bona fide RING E3 ubiquitin ligase that ubiquitinates multiple substrates, including PTEN, CCS, RIPK2, Groucho/TLE proteins, IRF7-pathway components, and BCL2 in different contexts. |
| GO:0070424 regulation of nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway | TAS PMID:20888210 To fight or die - inhibitor of apoptosis proteins at the cro... | ACCEPT | Summary: The NLR signaling row summarizes direct XIAP-RIPK2 biology. Reason: XIAP E3-dependent RIPK2 ubiquitination and NOD1/NOD2 signaling are independently established major molecular roles of this gene (PMIDs:22607974,29452636). Retain this immune-pathway claim on its own biological merits, alongside caspase inhibition; the scope of an apoptosis module does not make immune function non-core. |
| GO:0070427 nucleotide-binding oligomerization domain containing 1 signaling pathway | IDA PMID:29452636 Disruption of XIAP-RIP2 Association Blocks NOD2-Mediated Inf... | ACCEPT | Summary: XIAP acts directly in NOD1 signaling through RIPK2 ubiquitination. Reason: XIAP E3-dependent RIPK2 ubiquitination and NOD1/NOD2 signaling are independently established major molecular roles of this gene (PMIDs:22607974,29452636). Retain this immune-pathway claim on its own biological merits, alongside caspase inhibition; the scope of an apoptosis module does not make immune function non-core. Supporting Evidence: PMID:29452636 we identify NOD2 signaling and XIAP-dependent ubiquitination sites on RIP2 and show that mutating these lysine residues adversely affects NOD2 pathway signaling. |
| GO:0070431 nucleotide-binding oligomerization domain containing 2 signaling pathway | IDA PMID:19667203 XIAP mediates NOD signaling via interaction with RIP2. | ACCEPT | Summary: XIAP acts directly in NOD2 signaling through RIPK2 ubiquitination. Reason: XIAP E3-dependent RIPK2 ubiquitination and NOD1/NOD2 signaling are independently established major molecular roles of this gene (PMIDs:22607974,29452636). Retain this immune-pathway claim on its own biological merits, alongside caspase inhibition; the scope of an apoptosis module does not make immune function non-core. Supporting Evidence: PMID:22607974 We find that XIAP ubiquitylates RIPK2 and recruits the linear ubiquitin chain assembly complex (LUBAC) to NOD2. PMID:29452636 we identify NOD2 signaling and XIAP-dependent ubiquitination sites on RIP2 and show that mutating these lysine residues adversely affects NOD2 pathway signaling. PMID:30026309 RIPK2 inhibitors function instead by antagonizing XIAP-binding and XIAP-mediated ubiquitination of RIPK2. |
| GO:0070431 nucleotide-binding oligomerization domain containing 2 signaling pathway | IDA PMID:22607974 The ubiquitin ligase XIAP recruits LUBAC for NOD2 signaling ... | ACCEPT | Summary: XIAP acts directly in NOD2 signaling through RIPK2 ubiquitination. Reason: XIAP E3-dependent RIPK2 ubiquitination and NOD1/NOD2 signaling are independently established major molecular roles of this gene (PMIDs:22607974,29452636). Retain this immune-pathway claim on its own biological merits, alongside caspase inhibition; the scope of an apoptosis module does not make immune function non-core. Supporting Evidence: PMID:22607974 We find that XIAP ubiquitylates RIPK2 and recruits the linear ubiquitin chain assembly complex (LUBAC) to NOD2. PMID:29452636 we identify NOD2 signaling and XIAP-dependent ubiquitination sites on RIP2 and show that mutating these lysine residues adversely affects NOD2 pathway signaling. PMID:30026309 RIPK2 inhibitors function instead by antagonizing XIAP-binding and XIAP-mediated ubiquitination of RIPK2. |
| GO:0070431 nucleotide-binding oligomerization domain containing 2 signaling pathway | IDA PMID:29452636 Disruption of XIAP-RIP2 Association Blocks NOD2-Mediated Inf... | ACCEPT | Summary: XIAP acts directly in NOD2 signaling through RIPK2 ubiquitination. Reason: XIAP E3-dependent RIPK2 ubiquitination and NOD1/NOD2 signaling are independently established major molecular roles of this gene (PMIDs:22607974,29452636). Retain this immune-pathway claim on its own biological merits, alongside caspase inhibition; the scope of an apoptosis module does not make immune function non-core. Supporting Evidence: PMID:22607974 We find that XIAP ubiquitylates RIPK2 and recruits the linear ubiquitin chain assembly complex (LUBAC) to NOD2. PMID:29452636 we identify NOD2 signaling and XIAP-dependent ubiquitination sites on RIP2 and show that mutating these lysine residues adversely affects NOD2 pathway signaling. PMID:30026309 RIPK2 inhibitors function instead by antagonizing XIAP-binding and XIAP-mediated ubiquitination of RIPK2. |
| GO:0070534 protein K63-linked ubiquitination | IDA PMID:29452636 Disruption of XIAP-RIP2 Association Blocks NOD2-Mediated Inf... | ACCEPT | Summary: XIAP mediates K63-linked ubiquitination of RIPK2 in NOD signaling. Reason: XIAP E3-dependent RIPK2 ubiquitination and NOD1/NOD2 signaling are independently established major molecular roles of this gene (PMIDs:22607974,29452636). Retain this immune-pathway claim on its own biological merits, alongside caspase inhibition; the scope of an apoptosis module does not make immune function non-core. Supporting Evidence: PMID:29452636 we identify NOD2 signaling and XIAP-dependent ubiquitination sites on RIP2 and show that mutating these lysine residues adversely affects NOD2 pathway signaling. |
| GO:0090263 positive regulation of canonical Wnt signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt signaling. Reason: XIAP directly monoubiquitinates Groucho/TLE corepressors and promotes their exchange for beta-catenin at TCF/Lef. This mechanistically supported Wnt role is retained alongside the other E3 outputs, independently of the apoptosis-module scope (PMID:22304967). Supporting Evidence: PMID:22304967 Upon Wnt pathway activation, XIAP is recruited to TCF/Lef where it monoubiquitylates Groucho (Gro)/TLE. |
| GO:0090263 positive regulation of canonical Wnt signaling pathway | IMP PMID:22304967 XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt ... | ACCEPT | Summary: XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt signaling. Reason: XIAP directly monoubiquitinates Groucho/TLE corepressors and promotes their exchange for beta-catenin at TCF/Lef. This mechanistically supported Wnt role is retained alongside the other E3 outputs, independently of the apoptosis-module scope (PMID:22304967). Supporting Evidence: PMID:22304967 Upon Wnt pathway activation, XIAP is recruited to TCF/Lef where it monoubiquitylates Groucho (Gro)/TLE. |
| GO:0097179 protease inhibitor complex | IPI PMID:11257230 Structural basis of caspase-7 inhibition by XIAP. | ACCEPT | Summary: XIAP forms a protease-inhibitor complex with caspase-7. Reason: The caspase-7 structural study directly supports XIAP in a caspase-inhibitory complex, the physical state underlying its apoptotic caspase inhibitor activity. Supporting Evidence: PMID:11257230 Here we present the crystal structure of caspase-7 in complex with a potent inhibitory fragment from XIAP |
| GO:0120283 protein serine/threonine kinase binding | IPI PMID:11865055 IAP suppression of apoptosis involves distinct mechanisms: t... | KEEP AS NON CORE | Summary: XIAP binds MAP3K7/TAK1 in a non-core JNK/NF-kappaB signaling branch. Reason: Protein serine/threonine kinase binding is more specific than generic protein binding and reflects the TAK1/JNK arm of XIAP signaling. |
| GO:1902530 positive regulation of protein linear polyubiquitination | IDA PMID:21931591 cIAP1/2 are direct E3 ligases conjugating diverse types of u... | ACCEPT | Summary: XIAP recruits LUBAC to promote linear ubiquitination. Reason: The source series supports a distinction between XIAP E3 activity and positive control of HOIP/LUBAC-mediated linear-chain formation. PMID:21931591 reports stronger cIAP1 effects and weaker XIAP effects in its particular assays, which does not negate the XIAP-LUBAC recruitment mechanism established in PMID:22607974. Both rows judge the same supported process; neither attributes direct linear-chain catalysis to XIAP. |
| GO:1902530 positive regulation of protein linear polyubiquitination | IDA PMID:22607974 The ubiquitin ligase XIAP recruits LUBAC for NOD2 signaling ... | ACCEPT | Summary: XIAP recruits LUBAC to promote linear ubiquitination. Reason: The source series supports a distinction between XIAP E3 activity and positive control of HOIP/LUBAC-mediated linear-chain formation. PMID:21931591 reports stronger cIAP1 effects and weaker XIAP effects in its particular assays, which does not negate the XIAP-LUBAC recruitment mechanism established in PMID:22607974. Both rows judge the same supported process; neither attributes direct linear-chain catalysis to XIAP. |
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Download this section (compressed HTML)Q: Which XIAP substrate-specific ubiquitination events are physiological enough for GO-CAM modeling beyond RIPK2, TLE/Groucho, PTEN, CCS, IRF7-pathway components, and BCL2?
Q: Should SMAC/DIABLO, HTRA2/3/4, and ARTS antagonism of XIAP be represented only on the antagonist gene products, or does GO need a complex term that cleanly captures XIAP neutralization without adding generic XIAP protein-binding rows?
Experiment: Use endogenous XIAP rescue alleles that selectively disrupt BIR2-RIPK2, BIR3-SMAC/ARTS, and RING/E2 interfaces, then quantify RIPK2 K63 ubiquitination, TLE monoubiquitylation, caspase-3/7/9 activity, and substrate turnover in NOD2-stimulated, Wnt-stimulated, and apoptotic human cells.
Hypothesis: XIAP substrate choice is determined by separable BIR and RING surfaces rather than by a single generic E3-ligase state.
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