BCL10 is a noncatalytic immune signaling adaptor with an N-terminal caspase recruitment domain. Activated CARD-containing proteins, including CARD9, CARD11 and CARD14, nucleate BCL10 assemblies that recruit and organize MALT1 and downstream signaling machinery. These cytoplasmic and membrane-associated CARD-BCL10-MALT1 complexes promote canonical NF-kappaB activation through regulated ubiquitin and kinase signaling. BCL10 self-association also provides a platform for MALT1 activation. The adaptor supports antigen-receptor responses in lymphocytes and selected innate responses, with dependence varying by receptor and cell type. Biallelic loss of BCL10 causes combined immunodeficiency, whereas dysregulated expression or activating signaling assemblies can contribute to lymphoma. Nuclear localization, transcriptional coactivation and effects on apoptosis occur in particular experimental or pathological contexts.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001772 immunological synapse | IEA GO_REF:0000107 | ACCEPT | Summary: BCL10 is recruited to receptor-associated immune signaling assemblies. Reason: The mouse ortholog inference agrees with the human T-cell evidence for stimulus-dependent recruitment of BCL10 with CARD11 and downstream IKK. This location describes a signaling site, not a constitutive transmembrane receptor. |
| GO:0001819 positive regulation of cytokine production | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BCL10-dependent signaling promotes cytokine production. Reason: Cytokine induction is a downstream output of BCL10 signaling-adaptor activity. The exact cytokine response depends on receptor and cell type, so the broad output is retained separately from the principal molecular function. |
| GO:0001843 neural tube closure | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neural tube closure is a developmental consequence supported in mouse Bcl10 deficiency. Reason: PMID:11163238 reports exencephaly in a fraction of Bcl10-null embryos. Preserve the ortholog-based developmental annotation without elevating this phenotype to the core biochemical role or claiming a demonstrated human neural-tube mechanism. |
| GO:0001843 neural tube closure | ISS PMID:11163238 Bcl10 is a positive regulator of antigen receptor-induced ac... | KEEP AS NON CORE | Summary: Neural tube closure is a developmental consequence supported in mouse Bcl10 deficiency. Reason: PMID:11163238 reports exencephaly in a fraction of Bcl10-null embryos. Preserve the ortholog-based developmental annotation without elevating this phenotype to the core biochemical role or claiming a demonstrated human neural-tube mechanism. |
| GO:0002020 protease binding | IPI PMID:18223652 T cell antigen receptor stimulation induces MALT1 paracaspas... | KEEP AS NON CORE | Summary: BCL10 associates with the MALT1 protease in immune signaling complexes. Reason: The source identifies MALT1 as the protease partner. The observed association is consistent with the central adaptor mechanism; MALT1 performs proteolysis, while BCL10 organizes its activation. Protease binding is retained as a specific interaction, not as BCL10 protease activity. |
| GO:0002096 polkadots | IEA GO_REF:0000107 | ACCEPT | Summary: BCL10 participates in antigen-receptor-induced cytoplasmic signaling clusters. Reason: The ortholog-derived polkadot localization is consistent with BCL10 higher-order signaling assemblies. These structures are associated with CBM signal propagation and should not be confused with unrelated protein aggregates. |
| GO:0002224 toll-like receptor signaling pathway | IDA PMID:16831874 The IRAK-1-BCL10-MALT1-TRAF6-TAK1 cascade mediates signaling... | KEEP AS NON CORE | Summary: A BCL10-containing pathway can transmit TLR4 signals. Reason: The cited study describes IRAK1 recruitment of BCL10 and a Pellino2/TRAF6/TAK1 signaling cascade after LPS stimulation. This is a supported receptor context, but human BCL10 deficiency has cell-type-dependent innate effects; normal responses in tested patient myeloid cells preclude universal TLR dependence. |
| GO:0002250 adaptive immune response | IBA GO_REF:0000033 | ACCEPT | Summary: BCL10 is a central adaptor for adaptive immune receptor signaling. Reason: Human loss-of-function evidence and antigen-receptor studies establish a role in lymphocyte activation. The IBA retains its ancestral source and the TAS remains a traceable pathway statement; no identity of evidence strength across these records is implied. |
| GO:0002250 adaptive immune response | IMP PMID:25365219 Inherited BCL10 deficiency impairs hematopoietic and nonhema... | ACCEPT | Summary: BCL10 is a central adaptor for adaptive immune receptor signaling. Reason: Human loss-of-function evidence and antigen-receptor studies establish a role in lymphocyte activation. The IBA retains its ancestral source and the TAS remains a traceable pathway statement; no identity of evidence strength across these records is implied. |
| GO:0002250 adaptive immune response | TAS PMID:16831874 The IRAK-1-BCL10-MALT1-TRAF6-TAK1 cascade mediates signaling... | ACCEPT | Summary: BCL10 is a central adaptor for adaptive immune receptor signaling. Reason: Human loss-of-function evidence and antigen-receptor studies establish a role in lymphocyte activation. The IBA retains its ancestral source and the TAS remains a traceable pathway statement; no identity of evidence strength across these records is implied. |
| GO:0002906 negative regulation of mature B cell apoptotic process | IDA PMID:15878976 Bcl10 can promote survival of antigen-stimulated B lymphocyt... | KEEP AS NON CORE | Summary: BCL10 can support survival of activated B lymphocytes. Reason: The cited study reports NF-kappaB-dependent protection of WEHI-231 cells and enhanced survival of primary B cells after withdrawal of activating stimuli. This context-dependent survival output does not define a constitutive anti-apoptotic molecular activity. |
| GO:0003713 transcription coactivator activity | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: BCL10 has experimentally reported transcriptional coactivation capacity. Reason: The PAINT coactivator assertion has target experimental grounding in PMID15207693. Retain this context-limited activity without treating the target in WITH/FROM as circular or claiming that the ancestral node was independently reconstructed. |
| GO:0003713 transcription coactivator activity | IDA PMID:15207693 Characterization of Bcl10 as a potential transcriptional act... | KEEP AS NON CORE | Summary: BCL10 has experimentally reported transcriptional coactivation capacity. Reason: The mammalian Gal4-tethering assay and TFIIB association support a contextual transcriptional activation activity. They do not establish constitutive native recruitment to promoters or sequence-specific DNA recognition. Defer to the experimental curation within these limits. |
| GO:0005515 protein binding | IPI PMID:10187771 Equine herpesvirus-2 E10 gene product, but not its cellular ... | MODIFY | Summary: The viral E10 interaction identifies CARD domain binding by BCL10. Reason: The complete abstract reports direct CARD-dependent interaction between viral v-CARMEN/E10 and cellular c-CARMEN/BCL10. This identifies a reciprocal CARD interface and supports refining the generic binding term. The viral protein's autonomous NF-kappaB and JNK activation is distinct from the cellular protein in these experiments and is not assigned to BCL10. Proposed replacements: CARD domain binding Supporting Evidence: PMID:10187771 v-CARMEN and c-CARMEN interact directly in a CARD-dependent manner |
| GO:0005515 protein binding | IPI PMID:1040062 [Nurses replies to expectations of the nursing profession]. | KEEP AS NON CORE | Summary: Retain the corrected-source TRADD association as non-core. Reason: The original PMID1040062 is an unrelated nursing citation; its existing formal replacement PMID10400625 reports c-E10/BCL10 co-precipitation with TRADD (Q15628). Preserve the original source identifier and replacement record. This supports the source-specific protein association without resolving purified binary affinity or a more informative BCL10 molecular function. Retain GO:0005515 as KEEP_AS_NON_CORE under the explicit CLINGEN_MENDELIAN project instruction. Lack of a supported narrower term is not evidence against the measured association. Supporting Evidence: PMID:10400625 In transfection experiments c-E10 oligomerizes, binds to the cytoplasmic portion of TRAIL receptor 1 (DR4) and coprecipitates with TRADD. |
| GO:0005515 protein binding | IPI PMID:11053425 CARD9 is a novel caspase recruitment domain-containing prote... | MODIFY | Summary: BCL10 recognizes the CARD domain of CARD9. Reason: The complete abstract identifies CARD9 by a mammalian two-hybrid assay against the BCL10 CARD and reports endogenous association. That abstract localizes the contact on BCL10; selected CARD9 CARD-templating experiments in PMID:31296852 independently establish the reciprocal CARD interface, supporting binding to the partner CARD9 CARD domain. Refine the generic parent while preserving the original IPI assertion and partner. No complete-paper assay reconstruction is claimed. Proposed replacements: CARD domain binding Supporting Evidence: PMID:11053425 interacts selectively with the CARD activation domain of BCL10. |
| GO:0005515 protein binding | IPI PMID:11259443 Card10 is a novel caspase recruitment domain/membrane-associ... | MODIFY | Summary: BCL10 binds the CARD-containing signaling scaffold CARD10. Reason: The complete abstract explicitly connects CARD10 binding and signaling to its N-terminal CARD domain. Refine the existing physical-interaction assertion to CARD domain binding. This records the identified interaction surface, not the entire signaling-adaptor mechanism or catalytic activity. Proposed replacements: CARD domain binding Supporting Evidence: PMID:11259443 CARD10 binds to BCL10 and signals the activation of NF-kappaB through its N-terminal effector CARD domain. |
| GO:0005515 protein binding | IPI PMID:11278692 CARD11 and CARD14 are novel caspase recruitment domain (CARD... | MODIFY | Summary: BCL10 forms a CARD-mediated interaction with CARD14. Reason: The abstract states that the CARD domains of CARD11 and CARD14 associate with the BCL10 CARD. The original partner Q9BXL6 is CARD14, as independently checked in the normal UniProt record. Refine to CARD domain binding while preserving that accession and the original IPI evidence. Proposed replacements: CARD domain binding Supporting Evidence: PMID:11278692 CARD11 and CARD14 associate specifically with the CARD domain of BCL10 |
| GO:0005515 protein binding | IPI PMID:11278692 CARD11 and CARD14 are novel caspase recruitment domain (CARD... | MODIFY | Summary: BCL10 forms a CARD-mediated interaction with CARD11. Reason: The abstract states that the CARD domains of CARD11 and CARD14 associate with the BCL10 CARD. The original partner Q9BXL7 is CARD11, as independently checked in the normal UniProt record. Refine to CARD domain binding while preserving that accession and the original IPI evidence. Proposed replacements: CARD domain binding Supporting Evidence: PMID:11278692 CARD11 and CARD14 associate specifically with the CARD domain of BCL10 |
| GO:0005515 protein binding | IPI PMID:11466612 Interchangeable binding of Bcl10 to TRAF2 and cIAPs regulate... | MODIFY | Summary: Refine the curated TRAF2 interaction to ubiquitin protein ligase binding. Reason: The original source describes phosphorylation-dependent exchange of BCL10 between TRAF2 and cIAP partners during apoptosis experiments; this does not establish a universal immune-signaling complex. The IPI partner Q12933 is TRAF2. Its E3 ligase classification is supported by cofactor-dependent biochemical activity in PMID:20577214 and a separate substrate context in PMID:28489822. GO:0031625 identifies this binding partner class; catalytic activity need not be measured in the BCL10 interaction assay. Earlier negative biochemical results in PMID:19810754 concern tested conditions and do not invalidate the partner-class refinement. This assigns neither ubiquitin-ligase activity nor activation of TRAF2 to BCL10. The existing cIAP2 binding row represents a separate partner and provenance. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005515 protein binding | IPI PMID:11472070 CLAN, a novel human CED-4-like gene. | MODIFY | Summary: BCL10 binds the CARD domain of CLAN/NLRC4. Reason: The complete abstract explicitly identifies the human CLAN CARD as binding BCL10. This establishes recognition of the partner domain and supports CARD domain binding. The paper leaves physiological consequences unresolved; the interaction alone does not establish an apoptotic role for BCL10. Proposed replacements: CARD domain binding Supporting Evidence: PMID:11472070 The CARD of the CLAN proteins binds a number of other CARD-containing proteins including caspase-1, BCL10 |
| GO:0005515 protein binding | IPI PMID:12154360 CARMA1 is a critical lipid raft-associated regulator of TCR-... | MODIFY | Summary: Refine the CARD11 interaction to CARD domain binding. Reason: The complete abstract directly assigns CARMA1/CARD11 binding to its CARD and reports stimulus-dependent association with BCL10 and BCL10 movement into lipid rafts in T cells. Independent human CARD11 CARD-construct templating of BCL10 filaments in PMID:31296852 establishes the reciprocal CARD contact used for this refinement. The engineered constructs do not imply equivalent binding in every full-length CARD11 conformation. Proposed replacements: CARD domain binding Supporting Evidence: PMID:12154360 CARMA1 interacts with Bcl10 via its caspase-recruitment domain (CARD). |
| GO:0005515 protein binding | IPI PMID:14695475 Bcl10 activates the NF-kappaB pathway through ubiquitination... | MODIFY | Summary: Refine the curated interaction to ubiquitin conjugating enzyme binding. Reason: The curator-attributed IPI partner P61088 is UBE2N/UBC13. The complete source abstract explicitly identifies UBC13 as a ubiquitin-conjugating enzyme required for BCL10-dependent NEMO ubiquitination. Retain the original physical-association evidence with a term identifying the enzyme class; this is not a deduction of binding solely from pathway necessity. The exact pairwise assay is not exposed by the abstract and was not independently rederived. Neither E2 catalysis nor paracaspase activity is assigned to BCL10. Proposed replacements: ubiquitin conjugating enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:14695475 Bcl10 activates the NF-kappaB pathway through ubiquitination... | MODIFY | Summary: The source-attributed MALT1 association can be represented as protease binding. Reason: Retain the curated IPI interaction with Q9UDY8/MALT1 and refine its partner class to protease binding. The original abstract establishes a paracaspase-dependent signaling context but does not expose the pairwise interaction assay. Independent recombinant CBM assembly in PMID:24074955 places MALT1 around the BCL10 filament and measures MALT1 activation. This corroboration does not transfer MALT1 proteolysis or ubiquitin-enzyme activity to BCL10; the term already exists in this review. Proposed replacements: protease binding Supporting Evidence: PMID:24074955 only Bcl10 and MALT1 contribute to the diameters of the complexes. |
| GO:0005515 protein binding | IPI PMID:16280327 A pathway for tumor necrosis factor-alpha-induced Bcl10 nucl... | KEEP AS NON CORE | Summary: Retain the context-specific BCL10-BCL3 association as non-core. Reason: The PMID16280327 abstract reports Akt1-dependent phosphorylation of BCL10 followed by BCL3 (P20749) association during TNFalpha-induced nuclear translocation in human MCF7 cells. This directly supports the annotated association in that experimental context. No more informative BCL10 molecular function is established by this association. Retain GO:0005515 as KEEP_AS_NON_CORE under the explicit CLINGEN_MENDELIAN project instruction. This does not generalize the nuclear mechanism to every cell type or transfer BCL3 activity to BCL10. Supporting Evidence: PMID:16280327 Bcl10 subsequently complexes with Bcl3 |
| GO:0005515 protein binding | IPI PMID:16280327 A pathway for tumor necrosis factor-alpha-induced Bcl10 nucl... | MODIFY | Summary: Refine the AKT1 interaction to protein kinase B binding. Reason: P31749 is AKT1, and the same paper already supplies the specific protein kinase B binding assertion in this source set. Its complete abstract reports AKT1 phosphorylation of BCL10 during TNFalpha-induced nuclear translocation in human MCF7 cells. Retain this contextual substrate-kinase interaction with a more specific binding term; it does not establish that BCL10 activates AKT1 or has kinase activity. Proposed replacements: protein kinase B binding Supporting Evidence: PMID:16280327 Akt1, activated by TNFalpha, phosphorylates Bcl10 at Ser218 and Ser231 |
| GO:0005515 protein binding | IPI PMID:16809782 Ca2+/calmodulin-dependent protein kinase II is a modulator o... | MODIFY | Summary: Refine the CARD11 interaction to CARD domain binding. Reason: The source examines CaMKII-dependent CARD11 phosphorylation and CBM recruitment. Selected Methods specify human CARMA1 and mouse Bcl10 cDNAs; this heterologous experiment is not described as a purified human BCL10 assay. Independent human CARD11 CARD-construct templating of BCL10 filaments in PMID:31296852 establishes the reciprocal CARD contact used for this refinement. The engineered constructs do not imply equivalent binding in every full-length CARD11 conformation. Proposed replacements: CARD domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16831874 The IRAK-1-BCL10-MALT1-TRAF6-TAK1 cascade mediates signaling... | MODIFY | Summary: Refine the curated interaction to protein kinase binding. Reason: The source partner P51617-1 is IRAK1. The complete abstract describes IRAK1 recruitment of BCL10 to the TLR4 complex and their subsequent dissociation. Refine the curated association to protein kinase binding while retaining the source partner isoform. In this pathway IRAK1 acts as an upstream adaptor; the binding term does not claim that its kinase activity is required for recruitment, that BCL10 is a kinase, or that the interaction occurs in every cell type. The isoform-specific construct was not independently inspected. Proposed replacements: protein kinase binding Supporting Evidence: PMID:16831874 recruits BCL10 to the TLR4 signaling complex |
| GO:0005515 protein binding | IPI PMID:17052756 Bcl10 is phosphorylated on Ser138 by Ca2+/calmodulin-depende... | MODIFY | Summary: Refine the curated interaction to protein kinase binding. Reason: The curated IPI partner Q9UQM7 is CAMK2A. The complete abstract reports CaMKII phosphorylation of BCL10 Ser138 and perturbations of this phosphorylation, establishing a kinase-substrate context for the curated association. Refine its partner class to protein kinase binding. BCL10 remains the regulated substrate, not the kinase; inhibition and siRNA effects alone are not treated as new physical-binding assays. The source-specific binding assay and CAMK2A construct were not independently rederived from the abstract. Proposed replacements: protein kinase binding Supporting Evidence: PMID:17052756 CaMKII phosphorylates Bcl10 on Ser138. |
| GO:0005515 protein binding | IPI PMID:17363905 Phosphorylation and ubiquitination of the IkappaB kinase com... | KEEP AS NON CORE | Summary: Retain the CARMA1-dependent BCL10-NEMO coassociation as non-core. Reason: Selected PMID17363905 Results immunoprecipitate endogenous NEMO (Q9Y6K9) from CARMA1-deficient and CARMA1-reconstituted JPM50.6 cells after PMA/ionomycin stimulation. BCL10 and CARMA1 associate with NEMO in the reconstituted cells. This resolves the source-specific complex association; it does not establish a purified binary BCL10-NEMO interface. Retain GO:0005515 as KEEP_AS_NON_CORE under the explicit CLINGEN_MENDELIAN project instruction. Do not infer BCL10 ubiquitin recognition, kinase activity or ubiquitin-ligase activity from this coassociation. Supporting Evidence: PMID:17363905 CARMA1 facilitates the interaction between NEMO and BCL10. |
| GO:0005515 protein binding | IPI PMID:17948050 Malt1 ubiquitination triggers NF-kappaB signaling upon T-cel... | MODIFY | Summary: Refine the CARD11 interaction to CARD domain binding. Reason: Selected Discussion places BCL10-MALT1 recruitment to CARD11 upstream of TRAF6-dependent MALT1 ubiquitination and IKK recruitment. This assembly context preserves the curated CARD11 association; the ligase activity belongs to TRAF6. Independent human CARD11 CARD-construct templating of BCL10 filaments in PMID:31296852 establishes the reciprocal CARD contact used for this refinement. The engineered constructs do not imply equivalent binding in every full-length CARD11 conformation. Proposed replacements: CARD domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17948050 Malt1 ubiquitination triggers NF-kappaB signaling upon T-cel... | MODIFY | Summary: Refine the MALT1 association to protease binding. Reason: Selected Discussion reports that MALT1 C-terminal lysine mutants retain BCL10 association and integrate into CBM despite impaired ubiquitin signaling. TRAF6 supplies the ubiquitin-ligase activity. Independent human recombinant CBM reconstitution in PMID:24074955 places MALT1 around the BCL10 filament and measures MALT1 activity. This corroborates recognition of the protease partner, separately from the original association assay. Protease binding does not assign MALT1 catalysis to BCL10. Proposed replacements: protease binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18287044 NEMO recognition of ubiquitinated Bcl10 is required for T ce... | KEEP AS NON CORE | Summary: Retain ubiquitin-dependent BCL10-NEMO association as non-core. Reason: Selected PMID18287044 Results show GST-NEMO pull-down and endogenous coimmunoprecipitation of ubiquitinated BCL10 in stimulated Jurkat cells. Unmodified BCL10 and ubiquitin-binding-defective NEMO(L329P) do not support the observed association. These assays examine BCL10 itself in its modified context, resolving the source-specific protein association. NEMO reads the attached ubiquitin chains; BCL10 is the modified recruitment platform, not the ubiquitin-binding reader. Retain GO:0005515 as KEEP_AS_NON_CORE under the explicit CLINGEN_MENDELIAN project instruction. This does not assert an unmodified-polypeptide interface, purified binary affinity or a narrower BCL10 molecular function. Supporting Evidence: PMID:18287044 NEMO interacts only with ubiquitin-modified Bcl10 |
| GO:0005515 protein binding | IPI PMID:19118383 Casein kinase 1alpha governs antigen-receptor-induced NF-kap... | MODIFY | Summary: Refine the CARD11 interaction to CARD domain binding. Reason: Selected Results show stimulus-dependent CBM association with CK1alpha in Jurkat and BJAB cells and impaired BCL10/MALT1 recruitment after CK1alpha perturbation. Co-immunoprecipitation identifies the assembled platform, rather than resolving each pairwise interface. Independent human CARD11 CARD-construct templating of BCL10 filaments in PMID:31296852 establishes the reciprocal CARD contact used for this refinement. The engineered constructs do not imply equivalent binding in every full-length CARD11 conformation. Proposed replacements: CARD domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19118383 Casein kinase 1alpha governs antigen-receptor-induced NF-kap... | MODIFY | Summary: Refine the MALT1 association to protease binding. Reason: Selected Results identify stimulus-dependent CBM association with CK1alpha and BCL10/MALT1 recruitment. These co-immunoprecipitation experiments support complex assembly; they are not a complete binary-interface map. Independent human recombinant CBM reconstitution in PMID:24074955 places MALT1 around the BCL10 filament and measures MALT1 activity. This corroborates recognition of the protease partner, separately from the original association assay. Protease binding does not assign MALT1 catalysis to BCL10. Proposed replacements: protease binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19444310 COP9 signalosome controls the Carma1-Bcl10-Malt1 complex upo... | MODIFY | Summary: Refine the CARD11 interaction to CARD domain binding. Reason: The complete available abstract examines COP9 regulation of CBM assembly and BCL10 stability. The curator-supplied CARD11 association is retained, but that abstract does not independently resolve the binding interface. Independent human CARD11 CARD-construct templating of BCL10 filaments in PMID:31296852 establishes the reciprocal CARD contact used for this refinement. The engineered constructs do not imply equivalent binding in every full-length CARD11 conformation. Proposed replacements: CARD domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19444310 COP9 signalosome controls the Carma1-Bcl10-Malt1 complex upo... | MODIFY | Summary: Refine the MALT1 association to protease binding. Reason: The complete available abstract concerns COP9 control of CBM assembly and BCL10 stability. Retain the curator-supplied MALT1 partner while acknowledging that its original pairwise assay is not exposed by the abstract. Independent human recombinant CBM reconstitution in PMID:24074955 places MALT1 around the BCL10 filament and measures MALT1 activity. This corroborates recognition of the protease partner, separately from the original association assay. Protease binding does not assign MALT1 catalysis to BCL10. Proposed replacements: protease binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19815501 Mechanisms of NKT cell anergy induction involve Cbl-b-promot... | MODIFY | Summary: Refine the CARD11 interaction to CARD domain binding. Reason: The complete available abstract reports that CARMA1 monoubiquitination disrupts its BCL10 association during NKT-cell anergy. This regulatory effect does not make BCL10 a ubiquitin enzyme; the full source-specific assay was not inspected. Independent human CARD11 CARD-construct templating of BCL10 filaments in PMID:31296852 establishes the reciprocal CARD contact used for this refinement. The engineered constructs do not imply equivalent binding in every full-length CARD11 conformation. Proposed replacements: CARD domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21157432 Dephosphorylation of Carma1 by PP2A negatively regulates T-c... | MODIFY | Summary: Refine the CARD11 interaction to CARD domain binding. Reason: The complete available abstract describes PP2A control of CARD11 phosphorylation and CBM formation in Jurkat and murine Th1 cells. Preserve the original CARD11 partner assertion without assigning PP2A phosphatase activity to BCL10 or reconstructing a pairwise assay from the abstract. Independent human CARD11 CARD-construct templating of BCL10 filaments in PMID:31296852 establishes the reciprocal CARD contact used for this refinement. The engineered constructs do not imply equivalent binding in every full-length CARD11 conformation. Proposed replacements: CARD domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21157432 Dephosphorylation of Carma1 by PP2A negatively regulates T-c... | MODIFY | Summary: Refine the MALT1 association to protease binding. Reason: The complete available abstract concerns PP2A regulation of CARD11 phosphorylation and CBM assembly. The curated MALT1 association is retained without claiming that the abstract independently resolves the BCL10-MALT1 interface. Independent human recombinant CBM reconstitution in PMID:24074955 places MALT1 around the BCL10 filament and measures MALT1 activity. This corroborates recognition of the protease partner, separately from the original association assay. Protease binding does not assign MALT1 catalysis to BCL10. Proposed replacements: protease binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22267217 Dectin-1 is an extracellular pathogen sensor for the inducti... | MODIFY | Summary: Refine the CARD9 interaction to CARD domain binding. Reason: The complete abstract describes a CARD9-BCL10-MALT1 scaffold in dectin-1-induced IL1B transcription and caspase-8/ASC-dependent processing. The retained CARD9 association does not assign cytokine proteolysis or apoptosis to BCL10. Separate selected Results and Methods in PMID:31296852 directly show human CARD9 CARD-containing filament templates contacting recombinant human BCL10, with additional engineered yeast nucleation experiments. This establishes the reciprocal CARD interface independently of the original pair-level assay; it does not imply that every CARD9 conformational state binds equivalently. Proposed replacements: CARD domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22267217 Dectin-1 is an extracellular pathogen sensor for the inducti... | MODIFY | Summary: Refine the MALT1 association to protease binding. Reason: The complete abstract places BCL10 and MALT1 in the dectin-1/CARD9 scaffold that directs IL1B transcription and recruits caspase-8/ASC for processing. It does not make BCL10 the protease performing cytokine processing. Independent human recombinant CBM reconstitution in PMID:24074955 places MALT1 around the BCL10 filament and measures MALT1 activity. This corroborates recognition of the protease partner, separately from the original association assay. Protease binding does not assign MALT1 catalysis to BCL10. Proposed replacements: protease binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22528498 Protein kinase C-Ξ΄ negatively regulates T cell receptor-indu... | MODIFY | Summary: Refine the CARD11 interaction to CARD domain binding. Reason: Selected cached Discussion distinguishes PKCdelta inhibition of MALT1-TRAF6 recruitment from its lack of apparent effect on CARD11 association with BCL10 or MALT1. The inhibitory pathway effect therefore does not contradict the retained CARD11-BCL10 interaction. Independent human CARD11 CARD-construct templating of BCL10 filaments in PMID:31296852 establishes the reciprocal CARD contact used for this refinement. The engineered constructs do not imply equivalent binding in every full-length CARD11 conformation. Proposed replacements: CARD domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22528498 Protein kinase C-Ξ΄ negatively regulates T cell receptor-indu... | MODIFY | Summary: Refine the MALT1 association to protease binding. Reason: Selected Discussion reports preserved CARD11-BCL10/MALT1 assembly during PKCdelta-mediated inhibition of MALT1-TRAF6 recruitment. Retain the curated BCL10-MALT1 association in that regulatory context. Independent human recombinant CBM reconstitution in PMID:24074955 places MALT1 around the BCL10 filament and measures MALT1 activity. This corroborates recognition of the protease partner, separately from the original association assay. Protease binding does not assign MALT1 catalysis to BCL10. Proposed replacements: protease binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24412244 Charting the molecular links between driver and susceptibili... | MODIFY | Summary: Refine the curated interaction to protein kinase B binding. Reason: The original source is a colorectal-cancer interaction-network study and the curated partner P31749 is AKT1. PMID:16280327 independently supports BCL10-AKT1 association in the TNFalpha-induced phosphorylation and nuclear-translocation pathway, and the source set already includes an IPI protein kinase B binding assertion from that paper. Refine this screen-derived row consistently to the same partner class. The exact colorectal-screen pair and construct remain uninspected; the MCF7 mechanism is corroboration of the interaction, not a claim that the screen measured that mechanism or that BCL10 activates AKT1. Proposed replacements: protein kinase B binding |
| GO:0005515 protein binding | IPI PMID:25011391 Combining immunofluorescence with in situ proximity ligation... | MODIFY | Summary: Refine the curated interaction to protein kinase C binding. Reason: The complete abstract explicitly examines PKCzeta-BCL10 complexes in untreated and etoposide-treated C4-I cells, using immunofluorescence and proximity ligation at the nuclear envelope with prior biochemical corroboration. Q05513 is PKCzeta, so protein kinase C binding is more specific than the suggested parent protein kinase binding. Retain the curated IPI relationship without claiming purified binary affinity, a mapped interface, or protein-kinase activity of BCL10. Proposed replacements: protein kinase C binding Supporting Evidence: PMID:25011391 interactions between protein kinase-CΞΆ (PKCΞΆ) and Bcl10 |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | MODIFY | Summary: Refine the curated TRAF2 interaction to ubiquitin protein ligase binding. Reason: The source is a proteome-scale human binary interaction map. Its exact supplementary pair and construct were not independently rechecked. The IPI partner Q12933 is TRAF2. Its E3 ligase classification is supported by cofactor-dependent biochemical activity in PMID:20577214 and a separate substrate context in PMID:28489822. GO:0031625 identifies this binding partner class; catalytic activity need not be measured in the BCL10 interaction assay. Earlier negative biochemical results in PMID:19810754 concern tested conditions and do not invalidate the partner-class refinement. This assigns neither ubiquitin-ligase activity nor activation of TRAF2 to BCL10. The existing cIAP2 binding row represents a separate partner and provenance. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | MODIFY | Summary: Refine the CARD9 interaction to CARD domain binding. Reason: The source is a proteome-scale human binary interaction map. Retain the curator-supplied CARD9 pair; its exact supplementary construct and validation were not independently inspected. Separate selected Results and Methods in PMID:31296852 directly show human CARD9 CARD-containing filament templates contacting recombinant human BCL10, with additional engineered yeast nucleation experiments. This establishes the reciprocal CARD interface independently of the original pair-level assay; it does not imply that every CARD9 conformational state binds equivalently. Proposed replacements: CARD domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25910212 Widespread macromolecular interaction perturbations in human... | MODIFY | Summary: Refine the curated TRAF2 interaction to ubiquitin protein ligase binding. Reason: The source examines interactions perturbed by Mendelian-disease variants. The curated association is preserved without transferring a variant-specific phenotype or claiming inspection of the exact supplementary construct. The IPI partner Q12933 is TRAF2. Its E3 ligase classification is supported by cofactor-dependent biochemical activity in PMID:20577214 and a separate substrate context in PMID:28489822. GO:0031625 identifies this binding partner class; catalytic activity need not be measured in the BCL10 interaction assay. Earlier negative biochemical results in PMID:19810754 concern tested conditions and do not invalidate the partner-class refinement. This assigns neither ubiquitin-ligase activity nor activation of TRAF2 to BCL10. The existing cIAP2 binding row represents a separate partner and provenance. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005515 protein binding | IPI PMID:26488816 Ubiquitin Ligase TRIM62 Regulates CARD9-Mediated Anti-fungal... | MODIFY | Summary: Refine the CARD9 interaction to CARD domain binding. Reason: The complete abstract examines CARD9 regulation by TRIM62, including CARD9 ubiquitination and a truncation variant. The exact source-specific BCL10 interaction assay was not independently reconstructed, and TRIM62 ligase activity is not assigned to BCL10. Separate selected Results and Methods in PMID:31296852 directly show human CARD9 CARD-containing filament templates contacting recombinant human BCL10, with additional engineered yeast nucleation experiments. This establishes the reciprocal CARD interface independently of the original pair-level assay; it does not imply that every CARD9 conformational state binds equivalently. Proposed replacements: CARD domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27070702 Targeting Non-proteolytic Protein Ubiquitination for the Tre... | MODIFY | Summary: Refine the MALT1 association to protease binding. Reason: The complete abstract places BCL10 in the CBM ubiquitin scaffold of ABC diffuse large B-cell lymphoma. cIAP1/2 and LUBAC supply ubiquitin-enzyme activities; the source-specific BCL10-MALT1 pair assay was not independently reconstructed. Independent human recombinant CBM reconstitution in PMID:24074955 places MALT1 around the BCL10 filament and measures MALT1 activity. This corroborates recognition of the protease partner, separately from the original association assay. Protease binding does not assign MALT1 catalysis to BCL10. Proposed replacements: protease binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27070702 Targeting Non-proteolytic Protein Ubiquitination for the Tre... | KEEP AS NON CORE | Summary: Retain ubiquitin-dependent BCL10-NEMO coassociation in ABC DLBCL as non-core. Reason: Selected PMID27070702 Figure 4 Results report constitutive association of ubiquitinated BCL10 with NEMO in ABC DLBCL cells, disruption by SMAC-mimetic treatment, and coimmunoprecipitation with WT NEMO but not its ubiquitin-binding-defective L329P mutant in HBL1 cells. These target-specific experiments resolve the modified-protein/complex association. NEMO recognizes ubiquitin attached to BCL10; no ubiquitin-binding or catalytic activity is transferred to BCL10. Retain GO:0005515 as KEEP_AS_NON_CORE under the explicit CLINGEN_MENDELIAN project instruction. This does not claim purified affinity or a direct unmodified-polypeptide interface. Supporting Evidence: PMID:27070702 Polyubiquitinated BCL10 was co-immunoprecipitated with WT NEMO |
| GO:0005515 protein binding | IPI PMID:27071417 Psoriasis mutations disrupt CARD14 autoinhibition promoting ... | MODIFY | Summary: Refine the CARD14 partner-isoform 1 interaction to CARD domain binding. Reason: The original complete abstract reports constitutive BCL10/MALT1 association with CARD14 E138A and G117S mutants, unlike wild-type CARD14 in that experiment. PMID:11278692 explicitly identifies reciprocal binding of the CARD14 and BCL10 CARD domains. The canonical CARD14 partner isoform 1 contains the N-terminal CARD. This combines the curated isoform-specific partner assertion with independent domain evidence; the original isoform-specific construct assay was not independently inspected. The partner accession remains a supporting entity, not a BCL10 isoform annotation. Proposed replacements: CARD domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27071417 Psoriasis mutations disrupt CARD14 autoinhibition promoting ... | MODIFY | Summary: Refine the CARD14 partner-isoform 2 interaction to CARD domain binding. Reason: The original complete abstract reports constitutive BCL10/MALT1 association with CARD14 E138A and G117S mutants, unlike wild-type CARD14 in that experiment. PMID:11278692 explicitly identifies reciprocal binding of the CARD14 and BCL10 CARD domains. The official UniProt isoform 2 lacks residues 741-1004 and retains the CARD at residues 15-107; it is not the cardless isoform 3. This combines the curated isoform-specific partner assertion with independent domain evidence; the original isoform-specific construct assay was not independently inspected. The partner accession remains a supporting entity, not a BCL10 isoform annotation. Proposed replacements: CARD domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27071417 Psoriasis mutations disrupt CARD14 autoinhibition promoting ... | MODIFY | Summary: Refine the MALT1 association to protease binding. Reason: The complete original abstract reports constitutive BCL10/MALT1 association with activating CARD14 mutants and BCL10/MALT1-dependent signaling in keratinocytes. The mutant context is retained rather than generalized to constitutive wild-type CARD14 assembly. Independent human recombinant CBM reconstitution in PMID:24074955 places MALT1 around the BCL10 filament and measures MALT1 activity. This corroborates recognition of the protease partner, separately from the original association assay. Protease binding does not assign MALT1 catalysis to BCL10. Proposed replacements: protease binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27107012 Pooled-matrix protein interaction screens using Barcode Fusi... | KEEP AS NON CORE | Summary: Retain the source-verified BCL10-COG6 screen association as non-core. Reason: The PMID27107012 source uses barcode-fusion yeast two-hybrid interaction mapping. IntAct records EBI-11773232 (IM-25015-675; MI:2215 barcode fusion genetics two hybrid) and EBI-11781927 (IM-25015-1582; MI:1356 validated two hybrid) explicitly link human BCL10 O95999 to COG6 Q9Y2V7 and this PMID, with Table EV2 and figure provenance. This verifies the exact curated pair/source/method linkage, not independent replication of GOA or a new audit of all screen controls and figure images. Retain GO:0005515 as KEEP_AS_NON_CORE under the explicit CLINGEN_MENDELIAN project instruction. The screen does not establish an endogenous Golgi role or a more informative BCL10 molecular function. |
| GO:0005515 protein binding | IPI PMID:31296852 Structures of autoinhibited and polymerized forms of CARD9 r... | MODIFY | Summary: CARD11 contacts template BCL10 assembly through CARD-mediated binding. Reason: Human CARD11 constructs form helical templates that accelerate BCL10 polymerization; antibody-decorated filaments demonstrate continuous CARD11-BCL10 assemblies. These selected Results and Methods support CARD domain binding for the original CARD11 partner. They do not establish all full-length endogenous conformations or make BCL10 a kinase. Proposed replacements: CARD domain binding Supporting Evidence: PMID:31296852 demonstrating direct templating as the mechanism of enhanced Bcl10 polymerization. |
| GO:0005515 protein binding | IPI PMID:31296852 Structures of autoinhibited and polymerized forms of CARD9 r... | MODIFY | Summary: CARD9 templates BCL10 assembly through CARD-mediated binding. Reason: Selected Results and Methods show CARD9 CARD-coiled-coil mutant filaments directly templating recombinant human BCL10 assembly, with additional engineered yeast nucleation experiments. Refine the existing CARD9 interaction to CARD domain binding. The construct and assay context does not imply that every CARD9 conformational state binds equivalently. Proposed replacements: CARD domain binding Supporting Evidence: PMID:31296852 demonstrating direct templating by the CARD92β152 filaments |
| GO:0005515 protein binding | IPI PMID:31774199 Paracaspase MALT1 regulates glioma cell survival by controll... | MODIFY | Summary: Refine the MALT1 association to protease binding. Reason: The complete abstract examines MALT1 activity in patient-derived glioma stem-like cells. Preserve the curated BCL10-MALT1 interaction, but its exact supplementary interaction evidence was not independently recovered. Independent human recombinant CBM reconstitution in PMID:24074955 places MALT1 around the BCL10 filament and measures MALT1 activity. This corroborates recognition of the protease partner, separately from the original association assay. Protease binding does not assign MALT1 catalysis to BCL10. Proposed replacements: protease binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: Refine the curated TRAF2 interaction to ubiquitin protein ligase binding. Reason: The source is the HuRI binary interaction map. Its exact supplementary pair and an endogenous complex were not independently verified. The IPI partner Q12933 is TRAF2. Its E3 ligase classification is supported by cofactor-dependent biochemical activity in PMID:20577214 and a separate substrate context in PMID:28489822. GO:0031625 identifies this binding partner class; catalytic activity need not be measured in the BCL10 interaction assay. Earlier negative biochemical results in PMID:19810754 concern tested conditions and do not invalidate the partner-class refinement. This assigns neither ubiquitin-ligase activity nor activation of TRAF2 to BCL10. The existing cIAP2 binding row represents a separate partner and provenance. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Retain the source-verified HuRI BCL10-COG6 association as non-core. Reason: The PMID32296183 HuRI records explicitly link human BCL10 O95999 and COG6 Q9Y2V7: IntAct EBI-23098775 (IM-25472-43058; MI:0397 two hybrid array), EBI-24457201 (IM-25472-128838; MI:1356 validated two hybrid), and EBI-24966990 (IM-25472-18194; MI:1112 two hybrid prey pooling), each with Supplementary Table 9 provenance. This verifies the exact curated pair/source/method linkage, not independent replication of GOA or an endogenous complex. Retain GO:0005515 as KEEP_AS_NON_CORE under the explicit CLINGEN_MENDELIAN project instruction. The screen does not establish a Golgi function or a more informative BCL10 molecular function. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: Refine the curated TRAF2 interaction to ubiquitin protein ligase binding. Reason: The source is BioPlex affinity-purification interaction mapping. Coassociation may reflect a complex and does not establish purified direct affinity or a new signaling mechanism. The IPI partner Q12933 is TRAF2. Its E3 ligase classification is supported by cofactor-dependent biochemical activity in PMID:20577214 and a separate substrate context in PMID:28489822. GO:0031625 identifies this binding partner class; catalytic activity need not be measured in the BCL10 interaction assay. Earlier negative biochemical results in PMID:19810754 concern tested conditions and do not invalidate the partner-class refinement. This assigns neither ubiquitin-ligase activity nor activation of TRAF2 to BCL10. The existing cIAP2 binding row represents a separate partner and provenance. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: Refine the MALT1 association to protease binding. Reason: The complete abstract describes BioPlex affinity-purification interaction mapping in 293T and HCT116 cells. The curated MALT1 coassociation is retained, while its exact supplementary pair was not inspected and the screen is not treated as a direct binary-affinity measurement. Independent human recombinant CBM reconstitution in PMID:24074955 places MALT1 around the BCL10 filament and measures MALT1 activity. This corroborates recognition of the protease partner, separately from the original association assay. Protease binding does not assign MALT1 catalysis to BCL10. Proposed replacements: protease binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | MODIFY | Summary: Refine the MALT1 association to protease binding. Reason: The complete abstract describes integrated interaction and imaging mapping in U2OS cells. Preserve the curated MALT1 pair in this context; its exact supplementary evidence and construct details were not independently inspected. Independent human recombinant CBM reconstitution in PMID:24074955 places MALT1 around the BCL10 filament and measures MALT1 activity. This corroborates recognition of the protease partner, separately from the original association assay. Protease binding does not assign MALT1 catalysis to BCL10. Proposed replacements: protease binding Supporting Evidence: |
| GO:0005634 nucleus | IDA PMID:16280327 A pathway for tumor necrosis factor-alpha-induced Bcl10 nucl... | KEEP AS NON CORE | Summary: BCL10 can enter the nucleus in a stimulus-dependent cancer-cell context. Reason: The source describes TNFalpha-induced Akt1 phosphorylation and BCL3-associated nuclear translocation in MCF7 cells. Nuclear localization is supported but is not the predominant location of the immune signaling adaptor. |
| GO:0005737 cytoplasm | IDA PMID:11021819 BCL10 expression in normal and neoplastic lymphoid tissue. N... | ACCEPT | Summary: BCL10 is a cytoplasmic signaling adaptor. Reason: Immunohistochemistry shows predominantly cytoplasmic BCL10 in normal lymphoid populations; some MALT lymphomas additionally show nuclear localization. |
| GO:0005737 cytoplasm | IDA PMID:11053425 CARD9 is a novel caspase recruitment domain-containing prote... | ACCEPT | Summary: BCL10 is a cytoplasmic signaling adaptor. Reason: The CARD9 interaction study places BCL10 in the cellular signaling compartment; independent human lymphoid immunohistochemistry supports cytoplasmic residence. |
| GO:0005737 cytoplasm | IDA PMID:11238466 Equine herpesvirus protein E10 induces membrane recruitment ... | ACCEPT | Summary: BCL10 is a cytoplasmic signaling adaptor. Reason: The viral E10 study describes redistribution of cellular BCL10 from the cytoplasm to membrane-associated signaling sites; the initial cytoplasmic localization is retained. |
| GO:0005737 cytoplasm | IDA PMID:11278692 CARD11 and CARD14 are novel caspase recruitment domain (CARD... | ACCEPT | Summary: BCL10 is a cytoplasmic signaling adaptor. Reason: CARD11/CARD14 signaling studies are consistent with cytoplasmic BCL10 before receptor-associated assembly. |
| GO:0005737 cytoplasm | IDA PMID:15082780 Degradation of Bcl10 induced by T-cell activation negatively... | ACCEPT | Summary: BCL10 is a cytoplasmic signaling adaptor. Reason: The T-cell activation study follows cytoplasmic BCL10 before stimulus-dependent degradation. |
| GO:0005737 cytoplasm | IEA GO_REF:0000107 | ACCEPT | Summary: BCL10 is a cytoplasmic signaling adaptor. Reason: The ortholog transfer agrees with the direct human cellular localization evidence. |
| GO:0005764 lysosome | IDA PMID:15082780 Degradation of Bcl10 induced by T-cell activation negatively... | KEEP AS NON CORE | Summary: BCL10 transiently localizes to lysosomal vesicles during signaling termination. Reason: The source reports lysosomal BCL10 localization as the protein is downregulated after TCR/CD28 stimulation. This is supported turnover localization, not evidence that BCL10 is a lysosomal enzyme or a constitutive lysosome-resident scaffold. |
| GO:0005829 cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: The BCL10 signaling-adaptor function is active in the cytosol. Reason: The IBA agrees with direct cellular evidence and reconstituted signaling. The is_active_in qualifier is retained; the actual ancestral placement was not reanalyzed. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: The cytosolic localization is consistent with the established cellular distribution. Reason: Retain the source HPA-derived imaging assertion. GO_REF:0000052 identifies the curation method; it is not a publication reporting an independent BCL10 experiment. Primary cellular studies corroborate the broad location. |
| GO:0005829 cytosol | IDA PMID:12154360 CARMA1 is a critical lipid raft-associated regulator of TCR-... | ACCEPT | Summary: BCL10 occupies the cytosolic compartment of receptor-signaling pathways. Reason: The direct source studies and ortholog inference agree with cytosolic BCL10 and stimulus-dependent recruitment into signaling complexes. Compartment assignment does not make BCL10 a catalyst of every downstream reaction. |
| GO:0005829 cytosol | IDA PMID:16831874 The IRAK-1-BCL10-MALT1-TRAF6-TAK1 cascade mediates signaling... | ACCEPT | Summary: BCL10 occupies the cytosolic compartment of receptor-signaling pathways. Reason: The direct source studies and ortholog inference agree with cytosolic BCL10 and stimulus-dependent recruitment into signaling complexes. Compartment assignment does not make BCL10 a catalyst of every downstream reaction. |
| GO:0005829 cytosol | IEA GO_REF:0000107 | ACCEPT | Summary: BCL10 occupies the cytosolic compartment of receptor-signaling pathways. Reason: The direct source studies and ortholog inference agree with cytosolic BCL10 and stimulus-dependent recruitment into signaling complexes. Compartment assignment does not make BCL10 a catalyst of every downstream reaction. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1168644 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'CARMA1 recruits MALT1 and BCL10 forming CBM Complex'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202453 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'Auto-ubiquitination of TRAF6'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202459 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'Phosphorylation of Bcl10'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202466 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'Interaction of Bcl10 to CARMA1'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202472 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'Translocation of TRAF6 to CBM complex'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202478 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'Interaction and oligomerization of MALT1 to Bcl10'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202489 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'Oligomerization of Bcl10'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202500 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'Activation of IKK complex'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202510 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'Activation of TAK1-TAB2 complex'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202534 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'Ubiquitination of NEMO by TRAF6'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730861 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'Recruitment of TAK1 kinase complex to oligo-K63-pUb-TRAF6'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730864 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'Recruitment of TRAF6 to CBM complex by binding to MALT1'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730876 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'Phosphorylation of IKK-beta by TAK1'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730899 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'Oligomerization of BCL10 and MALT1'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730900 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'Activation of TAK1 complex bound to pUb-TRAF6'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730903 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'Oligomerization of TRAF6'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730904 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'Auto-ubiquitination of TRAF6'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5607732 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'K63polyUb-TAK1 autophosphorylates'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5607733 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'BCL10 binds CARD9'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5607736 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'MALT1 oligomerizes'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5607737 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'BCL10 oligomerizes'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5607742 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'K63polyUb-p-3T,1S-TAK1 phosphorylates IKK-beta'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5607744 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'MALT1 binds BCL10'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5607747 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'TRAF6 binds MALT1 oligomers'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5607751 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'TRAF6 oligomerizes'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5607756 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'TRAF6 oligomer autoubiquitinates'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5607757 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'K63polyUb-TRAF6 ubiquitinates TAK1'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5607759 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'TRIKA2 binds K63polyUb-TRAF6 oligomer'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8939323 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'RNF181 binds BCL10 and Ubiquitin:E2'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8939335 | ACCEPT | Summary: The curated pathway places the BCL10-containing signaling system in the cytosol. Reason: Retain the cytosolic location associated with the Reactome event 'RNF181 polyubiquinates BCL10'. This is a compartment assertion; participation of BCL10-containing complexes does not assign the event's kinase, ubiquitin-ligase or protease chemistry to BCL10. |
| GO:0005881 cytoplasmic microtubule | IDA PMID:23264731 MTR120/KIAA1383, a novel microtubule-associated protein, pro... | UNDECIDED | Summary: The microtubule localization needs the target-specific experimental context. Reason: The paper includes a human ORFeome localization screen in transfected HeLa cells, so its MTR120-focused title does not discredit the BCL10 annotation. The BCL10-specific Figure 1 image/list entry has not been inspected. Retain uncertainty; do not transfer MTR120 microtubule binding or stabilization to BCL10. The retained normal cache contains Introduction and Discussion after the abstract, with full_text_available set to true; it does not contain the target-specific Figure 1 image/list or the complete Methods/Results. This availability flag is not a claim of complete experimental coverage. |
| GO:0006915 apoptotic process | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Apoptotic effects have been reported in BCL10 overexpression systems. Reason: The family-derived assertion is compatible with early cell experiments and context-dependent apoptosis regulation. It does not define BCL10 as an apoptotic enzyme or establish a universal requirement for death signaling. Bcl10-deficient cells retain responses to several apoptotic stimuli. |
| GO:0012501 programmed cell death | IDA PMID:10400625 c-E10 is a caspase-recruiting domain-containing protein that... | UNDECIDED | Summary: The broad programmed-cell-death assertion requires the original experimental context. Reason: PMID:10400625 directly supports death-receptor-associated binding and NF-kappaB activation in its abstract. Whether the source paper directly assays BCL10-dependent programmed death was not resolved from the abstract alone; other overexpression reports do not replace that source-specific check. |
| GO:0019209 kinase activator activity | IBA GO_REF:0000033 | ACCEPT | Summary: BCL10 contributes to activation of kinases through an oligomeric signaling complex. Reason: The IBA retains the qualified complex-level activity. The complete abstract of PMID:15125833 reports purified BCL10/MALT1 oligomer-dependent IKK activation through TRAF6, TAK1 and ubiquitination enzymes. The target in WITH/FROM is valid descendant evidence, not circularity. No new PAINT node-placement audit is claimed. Preserve contributes_to; this is not an assertion that isolated BCL10 binds and activates a kinase on its own. |
| GO:0019209 kinase activator activity | IDA PMID:15125833 The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activ... | ACCEPT | Summary: BCL10 contributes to activation of kinases through an oligomeric signaling complex. Reason: The complete abstract reports reconstitution from BCL10 to IKK with MALT1, TRAF6, TAK1 and ubiquitination enzymes, with activity restricted to BCL10/MALT1 oligomers. Accept the curator-supplied contributes_to assertion for the noncatalytic component of this activating assembly. The full paper was unavailable in the normal cache; direct autonomous BCL10 kinase activation is not inferred. Supporting Evidence: PMID:15125833 oligomeric forms of BCL10 and MALT1 can activate IKK in vitro. |
| GO:0030674 protein-macromolecule adaptor activity | IDA PMID:15125833 The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activ... | MODIFY | Summary: BCL10 specifically acts as a signaling adaptor. Reason: The PMID:15125833 abstract reports that reconstituted BCL10-MALT1 oligomers initiate signaling through TRAF6 and TAK1 to IKK. Human-protein reconstitution in PMID:24074955 (Results, Figures 1 and 3A-B) resolves BCL10's role: CARMA1 nucleates BCL10 filaments that organize MALT1 and increase MALT1 protease activity, whereas monomeric BCL10 E53R does not produce the same activation. BCL10 supplies a noncatalytic signaling assembly, making GO:0035591 more informative than the general adaptor parent. The historical c-E10/BCL10 adaptor interpretation in the PMID:10400625 abstract corroborates this role. Proposed replacements: signaling adaptor activity |
| GO:0031398 positive regulation of protein ubiquitination | IDA PMID:14695475 Bcl10 activates the NF-kappaB pathway through ubiquitination... | ACCEPT | Summary: BCL10 promotes ubiquitin-dependent assembly of the NF-kappaB signaling machinery. Reason: The cited study links BCL10 to MALT1/UBC13-dependent NEMO ubiquitination. BCL10 performs the organizing step that enables signaling; ubiquitin transfer is performed by the conjugation machinery. This does not assign ligase activity to BCL10. |
| GO:0031625 ubiquitin protein ligase binding | IPI PMID:16395405 cIAP2 is a ubiquitin protein ligase for BCL10 and is dysregu... | KEEP AS NON CORE | Summary: BCL10 binds a ubiquitin ligase that regulates its abundance. Reason: The cited cIAP2 study demonstrates recognition and degradation of BCL10. Retain this substrate-regulator interaction separately from the central adaptor function; being ubiquitinated does not establish that BCL10 catalyzes ubiquitination. |
| GO:0031663 lipopolysaccharide-mediated signaling pathway | IDA PMID:16831874 The IRAK-1-BCL10-MALT1-TRAF6-TAK1 cascade mediates signaling... | KEEP AS NON CORE | Summary: BCL10 participates in an LPS-responsive signaling context. Reason: The cited IRAK1/Pellino2/TRAF6/TAK1 study supports BCL10-dependent signaling after LPS stimulation. Human loss-of-function results show that dependence differs between myeloid cells and fibroblasts, so this is not a universal innate response requirement. |
| GO:0032094 response to food | IDA PMID:17095757 Carrageenan induces interleukin-8 production through distinc... | KEEP AS NON CORE | Summary: Carrageenan exposure engages BCL10-dependent inflammatory signaling in cultured intestinal cells. Reason: The source directly examines carrageenan exposure of human intestinal epithelial preparations and cell lines, with BCL10 knockdown reducing IL8 induction. Retain the exposure context without implying a general role in digestion, feeding or every dietary response. |
| GO:0032449 CBM complex | IBA GO_REF:0000033 | ACCEPT | Summary: BCL10 is an integral component of CARD-BCL10-MALT1 signaling complexes. Reason: Reconstitution, structural assembly and human-cell immunoprecipitation support CBM membership. CARD9, CARD11 and CARD14 contexts are distinct receptor inputs to related assemblies; the original experimental, phylogenetic and statement evidence records are preserved. |
| GO:0032449 CBM complex | IDA PMID:24074955 Structural architecture of the CARMA1/Bcl10/MALT1 signalosom... | ACCEPT | Summary: BCL10 is an integral component of CARD-BCL10-MALT1 signaling complexes. Reason: The selected full-text experiments reconstitute human CARMA1/CARD11, BCL10 and MALT1 into a filamentous complex; anti-BCL10 immunoprecipitation from HBL-1 cells also retrieves all three components. These results support CBM membership directly. Supporting Evidence: |
| GO:0032449 CBM complex | IDA PMID:28628108 Germline hypomorphic CARD11 mutations in severe atopic disea... | ACCEPT | Summary: BCL10 is an integral component of CARD-BCL10-MALT1 signaling complexes. Reason: Retain the curator-supplied CBM membership: it is independently established by the recombinant assembly and human-cell immunoprecipitation in PMID:24074955. The complete available PMID:28628108 abstract describes CARD11 variants and signaling defects but does not describe a BCL10-specific complex assay; that paper-specific experiment has not been independently inspected. This limit does not contradict the established membership. |
| GO:0032449 CBM complex | IEA GO_REF:0000107 | ACCEPT | Summary: BCL10 is an integral component of CARD-BCL10-MALT1 signaling complexes. Reason: Reconstitution, structural assembly and human-cell immunoprecipitation support CBM membership. CARD9, CARD11 and CARD14 contexts are distinct receptor inputs to related assemblies; the original experimental, phylogenetic and statement evidence records are preserved. |
| GO:0032449 CBM complex | IPI PMID:19118383 Casein kinase 1alpha governs antigen-receptor-induced NF-kap... | ACCEPT | Summary: BCL10 is an integral component of CARD-BCL10-MALT1 signaling complexes. Reason: The full-text Results identify stimulus-dependent association of CARMA1/CARD11, BCL10 and MALT1 with CK1alpha in Jurkat and BJAB cells and recruitment of CK1alpha/IKKbeta in MALT1 and BCL10 precipitations. They directly support CBM assembly despite the paper focusing on CK1alpha. Co-immunoprecipitation is not treated as a complete pairwise interface map. Supporting Evidence: PMID:19118383 CARMA1, BCL10, and MALT1 associated with CK1Ξ± |
| GO:0032449 CBM complex | IPI PMID:22267217 Dectin-1 is an extracellular pathogen sensor for the inducti... | ACCEPT | Summary: BCL10 is an integral component of CARD-BCL10-MALT1 signaling complexes. Reason: The complete abstract explicitly describes a CARD9-BCL10-MALT1 scaffold during dectin-1 signaling. This supports the conserved CBM organization in that innate immune context. MALT1/caspase-8 functions in cytokine processing are not attributed to BCL10 as protease activity. Supporting Evidence: PMID:22267217 CARD9-Bcl-10-MALT1 scaffold directed IL1B transcription |
| GO:0032449 CBM complex | IPI PMID:27071417 Psoriasis mutations disrupt CARD14 autoinhibition promoting ... | ACCEPT | Summary: BCL10 is an integral component of CARD-BCL10-MALT1 signaling complexes. Reason: The complete available abstract reports constitutive interaction of psoriasis-associated CARD14 mutants with BCL10 and MALT1, accompanied by BCL10/MALT1-dependent NF-kappaB activation in keratinocytes. This supports a CARD14-context CBM assembly; the abstract does not establish that every CARD14 state is constitutively complexed. Full figures and constructs were not inspected. Supporting Evidence: PMID:27071417 CARD14(E138A) and CARD14(G117S) psoriasis mutants interacted constitutively with BCL10 and MALT1 |
| GO:0032449 CBM complex | NAS PMID:15125833 The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activ... | ACCEPT | Summary: BCL10 is an integral component of CARD-BCL10-MALT1 signaling complexes. Reason: Reconstitution, structural assembly and human-cell immunoprecipitation support CBM membership. CARD9, CARD11 and CARD14 contexts are distinct receptor inputs to related assemblies; the original experimental, phylogenetic and statement evidence records are preserved. |
| GO:0032496 response to lipopolysaccharide | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BCL10 can participate in cellular responses to LPS. Reason: Retain the ortholog-derived response annotation with the experimental TLR4 context. Human innate dependence varies by cell type; the response should not be presented as an invariant property of every myeloid lineage. |
| GO:0032755 positive regulation of interleukin-6 production | NAS PMID:16647297 Adaptors discriminate mast-cell cytokine production from eic... | KEEP AS NON CORE | Summary: BCL10-containing signaling complexes promote mast-cell IL6 production. Reason: The cited review describes the BCL10-MALT1 complex in cytokine induction downstream of Fc-epsilon receptor signaling. The original acts_upstream_of qualifier is retained; this downstream effector output is not a second molecular function. |
| GO:0032757 positive regulation of interleukin-8 production | IMP PMID:17095757 Carrageenan induces interleukin-8 production through distinc... | KEEP AS NON CORE | Summary: BCL10 supports IL8 induction in a defined epithelial inflammatory response. Reason: BCL10 siRNA reduces carrageenan-induced IL8 in NCM460 cells in the cited study. This context-specific cytokine output is retained without treating it as an independent biochemical activity. |
| GO:0032761 positive regulation of lymphotoxin A production | NAS PMID:16647297 Adaptors discriminate mast-cell cytokine production from eic... | UNDECIDED | Summary: The lymphotoxin-A-specific attribution needs clarification. Reason: The accessible review abstract discusses mast-cell IL6 and TNF production. GO:0032761 specifically concerns lymphotoxin A (TNF-beta), which cannot be inferred from unspecified TNF or IL6. The full review and underlying lymphotoxin experiment were not inspected; no replacement or biological refutation is established. |
| GO:0032765 positive regulation of mast cell cytokine production | NAS PMID:16647297 Adaptors discriminate mast-cell cytokine production from eic... | KEEP AS NON CORE | Summary: BCL10 contributes upstream of mast-cell cytokine production. Reason: The cited review distinguishes BCL10/MALT1-dependent cytokine production from degranulation and eicosanoid secretion. Preserve the original acts_upstream_of qualifier and this context-specific output. |
| GO:0032991 protein-containing complex | IDA PMID:14695475 Bcl10 activates the NF-kappaB pathway through ubiquitination... | KEEP AS NON CORE | Summary: BCL10 forms protein-containing complexes in multiple signaling contexts. Reason: The generic complex-membership assertion is retained. BCL10 occurs in CBM assemblies and also in stimulus-specific nuclear or regulatory complexes; replacing every broad source complex with a single composition would overstate the exact experimental assignment. The specific CBM records describe its principal assembly. |
| GO:0032991 protein-containing complex | IDA PMID:16280327 A pathway for tumor necrosis factor-alpha-induced Bcl10 nucl... | KEEP AS NON CORE | Summary: BCL10 forms protein-containing complexes in multiple signaling contexts. Reason: The generic complex-membership assertion is retained. BCL10 occurs in CBM assemblies and also in stimulus-specific nuclear or regulatory complexes; replacing every broad source complex with a single composition would overstate the exact experimental assignment. The specific CBM records describe its principal assembly. |
| GO:0032991 protein-containing complex | IDA PMID:22267217 Dectin-1 is an extracellular pathogen sensor for the inducti... | KEEP AS NON CORE | Summary: BCL10 forms protein-containing complexes in multiple signaling contexts. Reason: The generic complex-membership assertion is retained. BCL10 occurs in CBM assemblies and also in stimulus-specific nuclear or regulatory complexes; replacing every broad source complex with a single composition would overstate the exact experimental assignment. The specific CBM records describe its principal assembly. |
| GO:0032991 protein-containing complex | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: BCL10 forms protein-containing complexes in multiple signaling contexts. Reason: The generic complex-membership assertion is retained. BCL10 occurs in CBM assemblies and also in stimulus-specific nuclear or regulatory complexes; replacing every broad source complex with a single composition would overstate the exact experimental assignment. The specific CBM records describe its principal assembly. |
| GO:0035591 signaling adaptor activity | IEA GO_REF:0000107 | ACCEPT | Summary: Signaling adaptor activity is the principal molecular function of BCL10. Reason: Human-protein experiments in PMID:24074955 (Results, Figures 1 and 3A-B) show CARMA1 initiating BCL10 polymerization and the resulting assembly promoting MALT1 protease activity. Cellular CARMA1-BCL10 complexes and endogenous CBM assemblies (Figures 3C-D) corroborate the assembly mechanism. Together with the oligomer-dependent downstream signaling described in the PMID:15125833 abstract and the earlier adaptor interpretation in PMID:10400625, these results support BCL10's own noncatalytic signaling-adaptor function. This human evidence corroborates the ortholog-derived IEA without recasting that source assertion as a separate direct assay. |
| GO:0038061 non-canonical NF-kappaB signal transduction | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BCL10 has a reported context-specific noncanonical NF-kappaB signaling role. Reason: PMID19897484 reports that BCL10 silencing reduces carrageenan-induced nuclear p52/RelB responses in mouse embryonic fibroblasts and human NCM460 colonic epithelial cells, together with reduced NIK phosphorylation. The normal cached Methods, Results and Discussion support a stimulus-dependent upstream noncanonical signaling role, not intrinsic BCL10 kinase activity or a universal requirement in every cell. The original electronic donor chain was not reconstructed. Supporting Evidence: |
| GO:0042802 identical protein binding | IEA GO_REF:0000107 | ACCEPT | Summary: BCL10 self-association supports formation of its signaling filament. Reason: Direct structural and mutant-complementation experiments establish functional BCL10-BCL10 interfaces. Preserve each source self-interaction record, including high-throughput evidence, without claiming each independently resolves filament geometry or physiological assembly. |
| GO:0042802 identical protein binding | IPI PMID:10187771 Equine herpesvirus-2 E10 gene product, but not its cellular ... | ACCEPT | Summary: BCL10 self-association supports formation of its signaling filament. Reason: Direct structural and mutant-complementation experiments establish functional BCL10-BCL10 interfaces. Preserve each source self-interaction record, including high-throughput evidence, without claiming each independently resolves filament geometry or physiological assembly. |
| GO:0042802 identical protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | ACCEPT | Summary: BCL10 self-association supports formation of its signaling filament. Reason: Direct structural and mutant-complementation experiments establish functional BCL10-BCL10 interfaces. Preserve each source self-interaction record, including high-throughput evidence, without claiming each independently resolves filament geometry or physiological assembly. |
| GO:0042802 identical protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | ACCEPT | Summary: BCL10 self-association supports formation of its signaling filament. Reason: Direct structural and mutant-complementation experiments establish functional BCL10-BCL10 interfaces. Preserve each source self-interaction record, including high-throughput evidence, without claiming each independently resolves filament geometry or physiological assembly. |
| GO:0042802 identical protein binding | ISS PMID:16831874 The IRAK-1-BCL10-MALT1-TRAF6-TAK1 cascade mediates signaling... | ACCEPT | Summary: BCL10 self-association supports formation of its signaling filament. Reason: Direct structural and mutant-complementation experiments establish functional BCL10-BCL10 interfaces. Preserve each source self-interaction record, including high-throughput evidence, without claiming each independently resolves filament geometry or physiological assembly. |
| GO:0042981 regulation of apoptotic process | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: The CARD-family assignment is compatible with context-dependent apoptosis regulation. Reason: BCL10 can affect cell survival in some overexpression and activation settings, while Bcl10-null cells retain susceptibility to multiple apoptotic stimuli. The broad domain-derived process is retained as non-core rather than treated as the defining function. |
| GO:0043065 positive regulation of apoptotic process | IDA PMID:11821383 CARD-8 protein, a new CARD family member that regulates casp... | KEEP AS NON CORE | Summary: BCL10 has contextual pro-apoptotic activity in transfection experiments. Reason: Original Figure 7C and adjacent Results explicitly assay BCL10 as a comparator in transiently transfected MCF7 cells, measuring cell death at 36 hours. The CARD8-focused title is not a citation error. Retain the contextual pro-death annotation; CARD8-specific inhibitor and death-receptor experiments are not BCL10 results. |
| GO:0043065 positive regulation of apoptotic process | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Pro-apoptotic effects are context dependent. Reason: The ortholog-based assertion is compatible with early phosphorylation/overexpression studies, but it does not establish universal BCL10-dependent apoptosis in human cells. |
| GO:0043122 regulation of canonical NF-kappaB signal transduction | NAS PMID:19118383 Casein kinase 1alpha governs antigen-receptor-induced NF-kap... | MODIFY | Summary: BCL10 positively regulates the canonical NF-kappaB pathway. Reason: The full-text Results in the original paper include BCL10 silencing and reduced CBM recruitment/NF-kappaB output. CK1alpha has both positive scaffolding and negative phosphorylation effects; its negative feedback on CARD11 does not make the assembled BCL10 adaptor an inhibitor. The source regulation term can therefore be refined to positive regulation of canonical NF-kappaB signaling. Proposed replacements: positive regulation of canonical NF-kappaB signal transduction Supporting Evidence: PMID:19118383 BCL10/MALT1 recruitment to CK1Ξ±/CARMA1 and NF-ΞΊB activation were diminished |
| GO:0043122 regulation of canonical NF-kappaB signal transduction | NAS PMID:27071417 Psoriasis mutations disrupt CARD14 autoinhibition promoting ... | MODIFY | Summary: BCL10 positively regulates the canonical NF-kappaB pathway. Reason: The original abstract reports CARD14 mutant interaction with BCL10/MALT1 and BCL10/MALT1-dependent NF-kappaB activation in keratinocytes. Together with the established BCL10 signaling platform, this supports the positive direction of regulation. The replacement describes BCL10 participation in assembling the activating complex, not CARD14 disease causation or MALT1 protease activity. Proposed replacements: positive regulation of canonical NF-kappaB signal transduction Supporting Evidence: PMID:27071417 triggered BCL10- and MALT1-dependent activation of NF-ΞΊB in keratinocytes. |
| GO:0043122 regulation of canonical NF-kappaB signal transduction | NAS PMID:30467369 CARD-BCL-10-MALT1 signalling in protective and pathological ... | MODIFY | Summary: BCL10 positively regulates the canonical NF-kappaB pathway. Reason: The original review abstract discusses CBM platforms and canonical NF-kappaB regulation. The positive direction is independently supported by the primary BCL10 knockdown/reconstitution and ubiquitin-dependent NEMO experiments in PMID:18287044. BCL10 supplies the signaling scaffold; its role is more than merely being necessary or being ubiquitinated. Refine the existing regulation assertion without adding a new process claim. Proposed replacements: positive regulation of canonical NF-kappaB signal transduction Supporting Evidence: PMID:18287044 When wild-type Bcl10 expression was restored, however, Bcl10KD cells responded robustly |
| GO:0043123 positive regulation of canonical NF-kappaB signal transduction | IDA PMID:10400625 c-E10 is a caspase-recruiting domain-containing protein that... | ACCEPT | Summary: BCL10-dependent signaling assembly promotes canonical NF-kappaB activation. Reason: The original complete abstract reports that induced c-E10/BCL10 expression activates NF-kappaB. It does not alone resolve all modern canonical/noncanonical distinctions; selected BCL10/CBM and NEMO/IKK experiments in PMID:24074955 and PMID:18287044 independently support the canonical activating role retained here. Supporting Evidence: PMID:10400625 results in NF-kappaB activation |
| GO:0043123 positive regulation of canonical NF-kappaB signal transduction | IDA PMID:14695475 Bcl10 activates the NF-kappaB pathway through ubiquitination... | ACCEPT | Summary: BCL10-dependent signaling assembly promotes canonical NF-kappaB activation. Reason: The original complete abstract explicitly assigns BCL10 an adaptor role promoting NF-kappaB through paracaspase- and UBC13-dependent NEMO ubiquitination. Accept positive regulation, while attributing ubiquitin transfer to the enzymatic machinery rather than to BCL10. Supporting Evidence: PMID:14695475 adaptor protein Bcl10 promotes activation of NF-kappaB transcription factors |
| GO:0043123 positive regulation of canonical NF-kappaB signal transduction | IDA PMID:18287044 NEMO recognition of ubiquitinated Bcl10 is required for T ce... | ACCEPT | Summary: BCL10-dependent signaling assembly promotes canonical NF-kappaB activation. Reason: Selected full-text Results show BCL10 knockdown and rescue of T-cell NF-kappaB signaling, together with loss of NEMO binding and impaired IKK/NF-kappaB responses after disrupting BCL10 ubiquitination sites. The scaffold and recruitment experiments support active participation in signal propagation, not a kinase or ubiquitin-ligase activity for BCL10. Supporting Evidence: PMID:18287044 disruption of Bcl10 ubiquitination markedly inhibits IKK activation. |
| GO:0043123 positive regulation of canonical NF-kappaB signal transduction | IDA PMID:24074955 Structural architecture of the CARMA1/Bcl10/MALT1 signalosom... | ACCEPT | Summary: BCL10-dependent signaling assembly promotes canonical NF-kappaB activation. Reason: The selected full-text cellular assay tests BCL10 filament-interface mutants in 293T cells. Mutants with defective assembly reduce NF-kappaB reporter activity, whereas wild type and control mutants remain active. These experiments link BCL10 polymerization to positive signal propagation. Supporting Evidence: |
| GO:0043123 positive regulation of canonical NF-kappaB signal transduction | IDA PMID:27777308 Molecular Determinants of Scaffold-induced Linear Ubiquitiny... | ACCEPT | Summary: BCL10-dependent signaling assembly promotes canonical NF-kappaB activation. Reason: The complete original abstract places BCL10 in a CARD11-associated complex inducing IKK/NF-kappaB and identifies ubiquitinated BCL10 as an intermediate that recruits NEMO. BCL10 provides an assembly and recruitment platform; HOIP is the ubiquitin enzyme. The available abstract supports this distinction without a claim to have read the full paper or figures. Supporting Evidence: PMID:27777308 multicomponent complex that induces IΞΊB kinase (IKK) activity and NF-ΞΊB activation. |
| GO:0043123 positive regulation of canonical NF-kappaB signal transduction | IEA GO_REF:0000107 | ACCEPT | Summary: BCL10-dependent signaling assembly promotes canonical NF-kappaB activation. Reason: The ortholog-derived positive-regulation term is corroborated by the human BCL10 assembly/NEMO/IKK studies. The complete PMID:27777308 abstract explicitly links the BCL10-containing complex to IKK and NF-kappaB activation. This is independent human corroboration, not a reconstruction of the electronic propagation pipeline. Supporting Evidence: PMID:27777308 multicomponent complex that induces IΞΊB kinase (IKK) activity and NF-ΞΊB activation. |
| GO:0043123 positive regulation of canonical NF-kappaB signal transduction | IEP PMID:12761501 Large-scale identification and characterization of human gen... | ACCEPT | Summary: BCL10-dependent signaling assembly promotes canonical NF-kappaB activation. Reason: The complete original abstract establishes an overexpression luciferase-reporter screen in HEK293 cells but does not identify BCL10 individually. Preserve the curator-supplied reporter assertion because direct BCL10 assembly and perturbation experiments independently establish the function. The short original-source anchor identifies assay scope only; the BCL10-specific screen entry and supplements were not independently inspected. Supporting Evidence: PMID:12761501 examined whether it activated the transcription of a luciferase reporter gene |
| GO:0043422 protein kinase B binding | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: BCL10 binds Akt1 in a regulated phosphorylation and localization pathway. Reason: PMID:16280327 reports Akt1 phosphorylation of BCL10 during TNFalpha-induced nuclear translocation in MCF7 cells. Retain the direct interaction and inherited assertion as a contextual substrate-kinase relationship; no Akt kinase activity is assigned to BCL10. |
| GO:0043422 protein kinase B binding | IPI PMID:16280327 A pathway for tumor necrosis factor-alpha-induced Bcl10 nucl... | KEEP AS NON CORE | Summary: BCL10 binds Akt1 in a regulated phosphorylation and localization pathway. Reason: PMID:16280327 reports Akt1 phosphorylation of BCL10 during TNFalpha-induced nuclear translocation in MCF7 cells. Retain the direct interaction and inherited assertion as a contextual substrate-kinase relationship; no Akt kinase activity is assigned to BCL10. Supporting Evidence: PMID:16280327 Akt1, activated by TNFalpha, phosphorylates Bcl10 at Ser218 and Ser231 |
| GO:0044877 protein-containing complex binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BCL10 interacts with multiprotein signaling assemblies. Reason: The generic ortholog-derived complex-binding assertion is compatible with BCL10 biology but does not identify a separate molecular role. The signaling-adaptor term and specific CBM membership are the mechanistic summary. |
| GO:0045087 innate immune response | IEP PMID:16831874 The IRAK-1-BCL10-MALT1-TRAF6-TAK1 cascade mediates signaling... | ACCEPT | Summary: BCL10 contributes to innate immune signaling in defined receptor and cell contexts. Reason: The source TLR4 study and CARD9-associated signaling support the broad innate role, while human BCL10 deficiency demonstrates different requirements in fibroblasts and tested myeloid cells. The core is an adaptor used by several receptor systems, not an assertion that every innate response requires BCL10. |
| GO:0045121 membrane raft | EXP PMID:17287217 Caveolin-1 triggers T-cell activation via CD26 in associatio... | ACCEPT | Summary: BCL10 is recruited to membrane-raft-associated signaling complexes. Reason: The CD26/caveolin study reports recruitment of BCL10 with CARD11 and IKK to lipid rafts. This is a peripheral assembly location, not a transmembrane topology. |
| GO:0045121 membrane raft | IEA GO_REF:0000120 | ACCEPT | Summary: BCL10 is recruited to membrane-raft-associated signaling complexes. Reason: The CD26/caveolin study reports recruitment of BCL10 with CARD11 and IKK to lipid rafts. This is a peripheral assembly location, not a transmembrane topology. |
| GO:0045893 positive regulation of DNA-templated transcription | IDA PMID:15207693 Characterization of Bcl10 as a potential transcriptional act... | KEEP AS NON CORE | Summary: BCL10 can stimulate transcription in an experimental nuclear context. Reason: Retain the reported transactivation phenotype in its engineered mammalian assay context; do not equate reporter activity with a universal endogenous transcriptional program. |
| GO:0048471 perinuclear region of cytoplasm | IDA PMID:16127295 Accumulation of BCL10 at the perinuclear region is required ... | KEEP AS NON CORE | Summary: Overexpressed BCL10 can accumulate in perinuclear filaments. Reason: The primary study describes high-expression filaments near the endoplasmic reticulum in HeLa or COS-1 cells, with diffuse cytoplasmic distribution at lower expression. This supported localization is retained with its experimental dependence. |
| GO:0048471 perinuclear region of cytoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Overexpressed BCL10 can accumulate in perinuclear filaments. Reason: The primary study describes high-expression filaments near the endoplasmic reticulum in HeLa or COS-1 cells, with diffuse cytoplasmic distribution at lower expression. This supported localization is retained with its experimental dependence. |
| GO:0050700 CARD domain binding | IEA GO_REF:0000107 | ACCEPT | Summary: CARD-mediated contacts organize BCL10 signaling assemblies. Reason: Selected human CARD9/CARD11 and BCL10 recombinant assembly experiments establish domain-mediated templating; the complete early CARD-binding abstracts provide independent corroboration. The CARD domain-binding inference is therefore supported beyond a sequence motif. Engineered constructs and yeast nucleation assays are not represented as an exhaustive endogenous human interaction map. Supporting Evidence: PMID:31296852 CARDβCARD interaction critical for subsequent signal propagation |
| GO:0050852 T cell receptor signaling pathway | IDA PMID:15125833 The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activ... | ACCEPT | Summary: BCL10 links T-cell receptor signaling to downstream effector activation. Reason: The cited reconstitution and T-cell experiments support direct participation as a signal-organizing adaptor. Kinases and ubiquitin enzymes perform the downstream chemistry. |
| GO:0050862 positive regulation of T cell receptor signaling pathway | IDA PMID:18287044 NEMO recognition of ubiquitinated Bcl10 is required for T ce... | ACCEPT | Summary: BCL10-dependent assembly promotes propagation of T-cell receptor signals. Reason: The cited studies connect BCL10 ubiquitination, NEMO recruitment and downstream NF-kappaB activation. The positive regulatory role concerns this signaling branch and does not imply BCL10 initiates antigen recognition or all TCR outputs. |
| GO:0050862 positive regulation of T cell receptor signaling pathway | IDA PMID:27777308 Molecular Determinants of Scaffold-induced Linear Ubiquitiny... | ACCEPT | Summary: BCL10-dependent assembly promotes propagation of T-cell receptor signals. Reason: The cited studies connect BCL10 ubiquitination, NEMO recruitment and downstream NF-kappaB activation. The positive regulatory role concerns this signaling branch and does not imply BCL10 initiates antigen recognition or all TCR outputs. |
| GO:0051059 NF-kappaB binding | IBA GO_REF:0000033 | UNDECIDED | Summary: Direct NF-kappaB protein binding requires verification beyond promoter binding. Reason: The PAINT node has not been reconstructed. The target paper examined here demonstrates NF-kappaB binding to BCL10 regulatory DNA, which does not itself establish BCL10 binding to NF-kappaB protein. Preserve the assertion pending the protein-association evidence; the target in WITH/FROM is not circular. |
| GO:0051059 NF-kappaB binding | IDA PMID:16280327 A pathway for tumor necrosis factor-alpha-induced Bcl10 nucl... | UNDECIDED | Summary: Direct NF-kappaB protein binding requires verification beyond promoter binding. Reason: The complete abstract and selected original Figure 3 caption/Results concern p65 association with BCL10 regulatory DNA by ChIP and EMSA. Those assays do not resolve the protein-binding assertion. The complete paper and any separate interaction evidence were not inspected, so do not REMOVE or declare curator misattribution. |
| GO:0051260 protein homooligomerization | IDA PMID:24074955 Structural architecture of the CARMA1/Bcl10/MALT1 signalosom... | ACCEPT | Summary: BCL10 polymerizes through functional self-interfaces. Reason: Reconstituted filaments, interface disruption and complementary charge-reversal rescue in the cited structural study establish BCL10 participation in its own assembly. This is a step BCL10 physically performs, not merely a downstream loss-of-function phenotype. |
| GO:0061760 antifungal innate immune response | IEA GO_REF:0000107 | ACCEPT | Summary: BCL10 participates in CARD9-associated antifungal immune signaling. Reason: The ortholog-derived assertions agree with CARD9/BCL10/MALT1 signaling and the dectin1-associated complex in human dendritic cells. The inherited BCL10-deficiency study cautions that tested human myeloid responses can remain intact, so the statement is receptor- and cell-context dependent. |
| GO:0061760 antifungal innate immune response | ISS GO_REF:0000024 | ACCEPT | Summary: BCL10 participates in CARD9-associated antifungal immune signaling. Reason: The ortholog-derived assertions agree with CARD9/BCL10/MALT1 signaling and the dectin1-associated complex in human dendritic cells. The inherited BCL10-deficiency study cautions that tested human myeloid responses can remain intact, so the statement is receptor- and cell-context dependent. |
| GO:0071222 cellular response to lipopolysaccharide | IEP PMID:16831874 The IRAK-1-BCL10-MALT1-TRAF6-TAK1 cascade mediates signaling... | KEEP AS NON CORE | Summary: BCL10 participates in a cellular LPS-response context. Reason: The source IEP is preserved alongside the direct IRAK1/Pellino2/TRAF6/TAK1 signaling evidence from the same study. Expression response alone does not establish a universal requirement across human cell types. |
| GO:0071260 cellular response to mechanical stimulus | IEP PMID:19593445 Expression of the Bcl-2 protein BAD promotes prostate cancer... | UNDECIDED | Summary: The mechanical-stimulus annotation has an unresolved citation mismatch. Reason: The cited normal paper examines BAD-driven prostate cancer proliferation and xenograft growth. Selected Methods, Results and Discussion, plus the root full-narrative review, do not substantiate BCL10 mechanical-stimulus expression. Mark the reference MISCITED for this assertion while leaving the biological process unresolved; no intended replacement has been established. |
| GO:0097190 apoptotic signaling pathway | IMP PMID:22267217 Dectin-1 is an extracellular pathogen sensor for the inducti... | UNDECIDED | Summary: The apoptosis assertion needs separation from non-apoptotic caspase8 signaling. Reason: The available evidence establishes a BCL10-containing dectin-1/caspase-8 inflammasome pathway for IL1B expression and processing. Apoptotic signaling requires a death-triggering signal, and caspase-8 activity alone does not establish it. Relevant death experiments and the full paper were not inspected; do not remove the experimental assertion from abstract-only reasoning. |
| GO:0140296 general transcription initiation factor binding | IPI PMID:15207693 Characterization of Bcl10 as a potential transcriptional act... | KEEP AS NON CORE | Summary: BCL10 associates with the general transcription factor TFIIB. Reason: The source reports interaction with TFIIB, consistent with the annotated general initiation-factor binding. This is a non-core interaction, not evidence that BCL10 itself selects a transcription start site. |
| GO:2001238 positive regulation of extrinsic apoptotic signaling pathway | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: BCL10 can promote extrinsic-death signaling in experimental contexts. Reason: The primary phosphorylation/partner-switching study supports apoptosis effects of overexpressed BCL10 and altered cIAP/TRAF2 association. Preserve the direct and ancestral assertions with that context, without claiming that BCL10 is indispensable for all death-receptor responses. |
| GO:2001238 positive regulation of extrinsic apoptotic signaling pathway | IDA PMID:11466612 Interchangeable binding of Bcl10 to TRAF2 and cIAPs regulate... | KEEP AS NON CORE | Summary: BCL10 can promote extrinsic-death signaling in experimental contexts. Reason: The primary phosphorylation/partner-switching study supports apoptosis effects of overexpressed BCL10 and altered cIAP/TRAF2 association. Preserve the direct and ancestral assertions with that context, without claiming that BCL10 is indispensable for all death-receptor responses. |
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Download this section (compressed HTML)Q: Which BCL10-containing molecular assembly underlies the reported nuclear transcriptional activity, and how does it differ from cytoplasmic CBM signaling?
Q: Can the source experiments or curators resolve the NF-kappaB protein-binding, microtubule-location, mechanical-stimulus and inflammasome-versus-apoptosis annotations identified here?
Q: Which human cell types require BCL10 for the noncanonical NIK/p100/p52 pathway, independently of its effects on canonical NF-kappaB and p100 abundance?
Experiment: Compare wild-type and assembly-interface BCL10 mutants at matched near-endogenous abundance in lymphocytes and fibroblasts, measuring CBM assembly, MALT1 activity, NEMO recruitment and separate canonical versus noncanonical NF-kappaB readouts.
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