BCAP31 encodes BAP31, a multipass endoplasmic reticulum membrane protein involved in the handling of newly synthesized membrane proteins and in communication between the endoplasmic reticulum and mitochondria. It associates with selected clients and protein translocation machinery, directing misfolded CFTR toward degradation. Its cytoplasmic region also participates in a FIS1-associated platform that recruits procaspase-8. Caspase cleavage generates an ER-localized p20 fragment that promotes calcium-dependent apoptotic signaling. At ER-mitochondria contacts, BAP31 associates with TOMM40 and supports the mitochondrial localization of selected respiratory-chain proteins. Pathogenic BCAP31 variants cause an X-linked disorder with deafness, dystonia, and cerebral hypomyelination.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005789 endoplasmic reticulum membrane | IBA GO_REF:0000033 | ACCEPT | Summary: BCAP31 functions in the ER membrane. Reason: The membrane-integral ER location agrees with primary localization, client handling and ER-mitochondria contact experiments. Retain the phylogenetically inferred location. |
| GO:0006888 endoplasmic reticulum to Golgi vesicle-mediated transport | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: This historical trafficking IBA is superseded by the inspected PAINT family reassessment. Reason: The immutable GOA row is dated 20170228 and cites PANTHER:PTN000294723. The inspected interpro/panther/PTHR12701/PTHR12701-paint.tsv now contains four IBDs at that node and neither GO:0006888 nor GO:0070973. The curator reassessment recorded in GO issue 6385 is therefore reflected in the actual node, not merely a proposed change. Mark this historical propagation as over-annotated. Its original node and mouse donors remain in supporting_entities as provenance of the old assertion, not current support. Mouse Bap29/Bap31 perturbations and conditional human MHC-I export effects remain positive client-context evidence (PMID:15187134; PMID:17056546); retiring the ancestral process inference does not deny those experiments or equate a partial phenotype with absence of function. Propagation Review Root cause: SOURCE STALE OR MISSING Sources checked: PANTHER:PTN000294723 Β· PTN000294723 SOURCE STALE OR MISSING The 2017 GOA assertion cites this ancestral node for GO:0006888. The inspected PTHR12701 PAINT table contains four current IBDs at this node and no longer includes GO:0006888. This records the retired source assertion without inferring why the historical annotation was withdrawn; the current GO:0140388 IBD seeded by BCAP31 remains valid curator evidence. |
| GO:0070973 protein localization to endoplasmic reticulum exit site | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: This historical trafficking IBA is superseded by the inspected PAINT family reassessment. Reason: The immutable GOA row is dated 20170228 and cites PANTHER:PTN000294723. The inspected interpro/panther/PTHR12701/PTHR12701-paint.tsv now contains four IBDs at that node and neither GO:0006888 nor GO:0070973. The curator reassessment recorded in GO issue 6385 is therefore reflected in the actual node, not merely a proposed change. Mark this historical propagation as over-annotated. Its original node and mouse donors remain in supporting_entities as provenance of the old assertion, not current support. Mouse Bap29/Bap31 perturbations and conditional human MHC-I export effects remain positive client-context evidence (PMID:15187134; PMID:17056546); retiring the ancestral process inference does not deny those experiments or equate a partial phenotype with absence of function. Propagation Review Root cause: SOURCE STALE OR MISSING Sources checked: PANTHER:PTN000294723 Β· PTN000294723 SOURCE STALE OR MISSING The 2017 GOA assertion cites this ancestral node for GO:0070973. The inspected PTHR12701 PAINT table contains four current IBDs at this node and no longer includes GO:0070973. This records the retired source assertion without inferring why the historical annotation was withdrawn; the current GO:0140388 IBD seeded by BCAP31 remains valid curator evidence. |
| GO:0005783 endoplasmic reticulum | IEA GO_REF:0000002 | ACCEPT | Summary: BCAP31 is an ER membrane protein. Reason: Retain this broad ER localization: multiple human experiments independently support the ER pool. The computational mapping is consistent with the primary evidence. |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000120 | ACCEPT | Summary: BCAP31 is an ER membrane protein. Reason: Retain this broad ER localization: multiple human experiments independently support the ER pool. The computational mapping is consistent with the primary evidence. |
| GO:0006886 intracellular protein transport | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: BCAP31 participates in intracellular protein handling and transport. Reason: Client association and delivery to ER quality-control machinery support this broad process. The term does not specify whether a particular cargo is retained, exported or degraded, and does not imply that BCAP31 is an autonomous pore or motor. More precise ERAD and retrotransport annotations capture the best-established activity. |
| GO:0006915 apoptotic process | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: BCAP31 participates in context-dependent apoptotic signaling. Reason: Intact BCAP31 forms a FIS1-associated platform that recruits procaspase-8, and its membrane-retained p20 cleavage product can propagate ER calcium and mitochondrial apoptotic signals. These are activities beyond merely being consumed as a caspase substrate. Retain the broad process as a supported signaling context. |
| GO:0015031 protein transport | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: BCAP31 participates in intracellular protein handling and transport. Reason: Client association and delivery to ER quality-control machinery support this broad process. The term does not specify whether a particular cargo is retained, exported or degraded, and does not imply that BCAP31 is an autonomous pore or motor. More precise ERAD and retrotransport annotations capture the best-established activity. |
| GO:0016020 membrane | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: BCAP31 is membrane-associated. Reason: The broad location is correct for a multipass ER protein with additional context-dependent membrane pools. It does not require replacing every location with ER membrane. |
| GO:0016192 vesicle-mediated transport | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: BCAP31 can influence membrane-cargo trafficking. Reason: MHC-I association and export experiments support a context-dependent trafficking role. A role in retrotranslocation does not exclude all vesicle-related functions. Retain the broad keyword annotation without claiming that BCAP31 itself forms a vesicle coat or that all client effects reflect direct cargo-receptor activity. |
| GO:0033116 endoplasmic reticulum-Golgi intermediate compartment membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: BCAP31 has a reported ER-Golgi intermediate-compartment membrane pool. Reason: Retain the source localization as a secondary pool. ER residence and cycling do not by themselves negate a curated ERGIC location, but they also do not establish an obligate cargo-receptor mechanism. |
| GO:0005515 protein binding | IPI PMID:15024066 The yeast split-ubiquitin membrane protein two-hybrid screen... | KEEP AS NON CORE | Summary: BCAP31 associates with the membrane protein HACD2, historically called PTPLB. Reason: The study supports a selective client relationship and stabilization of PTPLB. It should not be recast as promotion of degradation of this client: the reported Bap31-deficient-cell phenotype is increased proteasomal disposal. Binding is retained without asserting a specific delivery activity not established for this partner. |
| GO:0005515 protein binding | IPI PMID:17500595 Huntingtin interacting proteins are genetic modifiers of neu... | KEEP AS NON CORE | Summary: BCAP31 has a source-attributed interaction with huntingtin. Reason: Retain the HTT interaction as supported context. Interaction-network evidence alone does not identify a client-transfer, adaptor or enzymatic function for this exact pair. |
| GO:0005515 protein binding | IPI PMID:18555783 BAP31 interacts with Sec61 translocons and promotes retrotra... | MODIFY | Summary: BCAP31 binds a newly synthesized CFTR client and supports its delivery to ERAD machinery. Reason: The CFTR F508del study supports N-terminal client association and delivery toward the Derlin-1 degradation pathway, motivating the broader carrier-activity refinement. The inspected PAINT node PTN000294723 carries GO:0140388, dated 20260603 and seeded by BCAP31 itself; this is a genuine target-grounded curator assignment. The specific ATP-coupled ratchet described by that term was not isolated in the material assessed here, so the broader refinement is retained with the mechanistic question recorded in core_functions. Machinery interactions remain distinct source rows. Proposed replacements: protein carrier activity Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21183955 Fis1 and Bap31 bridge the mitochondria-ER interface to estab... | MODIFY | Summary: BCAP31 associates with procaspase-8 in an apoptotic signaling platform. Reason: The FIS1-BCAP31 complex recruits procaspase-8; removal of the relevant BCAP31 cytoplasmic region prevents recruitment and activation. Bringing signaling components together is more informative than generic binding and fits signaling adaptor activity. This does not assign caspase catalysis to BCAP31, nor does it require calling its coiled-coil region a structurally canonical death-effector domain. Proposed replacements: signaling adaptor activity Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25854864 Interaction between human BAP31 and respiratory syncytial vi... | KEEP AS NON CORE | Summary: BCAP31 associates with the respiratory syncytial virus SH protein. Reason: Retain the viral interaction as infection-related context. It does not define a general BCAP31 molecular activity, and a specific cellular cargo function should not be transferred to a viral partner. |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | KEEP AS NON CORE | Summary: BCAP31 has a source-attributed association with BCAP29. Reason: The source partner is the related ER membrane protein BCAP29. Retain the supported association; these interaction maps do not alone establish a distinct enzymatic or client-delivery function for the pair. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: BCAP31 has a source-attributed association with TIMMDC1. Reason: Retain this interaction as mitochondrial-biogenesis context. A proteome interaction map does not by itself establish direct substrate transfer, import-pore activity or a stable BCAP31 respiratory-complex subunit. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | KEEP AS NON CORE | Summary: BCAP31 has a source-attributed interaction with APP. Reason: Retain the curated APP association from the neurodegeneration interaction map. The exact partner attribution is preserved, but no specific client-delivery or signaling-adaptor mechanism is established for this pair by the available source reading. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: BCAP31 has a source-attributed association with BCAP29. Reason: The source partner is the related ER membrane protein BCAP29. Retain the supported association; these interaction maps do not alone establish a distinct enzymatic or client-delivery function for the pair. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | KEEP AS NON CORE | Summary: BCAP31 has a source-attributed association with BCAP29. Reason: The source partner is the related ER membrane protein BCAP29. Retain the supported association; these interaction maps do not alone establish a distinct enzymatic or client-delivery function for the pair. |
| GO:0005515 protein binding | IPI PMID:36012204 Differential CFTR-Interactome Proximity Labeling Procedures ... | KEEP AS NON CORE | Summary: BCAP31 is associated with CFTR in the reported proximity-interaction context. Reason: Retain the curated association. The proximity study examines wild-type and mutant CFTR contexts; the precise source record is not automatically equivalent to the CFTRDeltaF508 client-delivery experiment in another paper. A carrier replacement is therefore not assigned solely by partner name. |
| GO:0005515 protein binding | IPI PMID:9334338 p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated prote... | KEEP AS NON CORE | Summary: BCAP31 associates with BCL2. Reason: The original study supports association with BCL2, including biochemical interaction assays. Retain this specific biological context without inferring that BCL2 is a transported client or that binding alone establishes the FIS1-procaspase adaptor mechanism. |
| GO:0000139 Golgi membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BCAP31 has experimentally supported Golgi-associated localization in the donor literature. Reason: Official comparative annotation records trace the donor Golgi annotation to the hepatic Golgi proteomics study, whose abstract includes analytical fractionation and immunogold validation of BAP31. Retain this secondary location without dismissing it as contamination or generalizing it to the predominant location in every human cell. |
| GO:0007283 spermatogenesis | IEA GO_REF:0000107 | UNDECIDED | Summary: The transferred spermatogenesis assignment is not yet resolved as a functional role. Reason: The official mouse donor record traces to expression-pattern evidence from a differential spermatogenesis expression survey. The complete abstract reports microarray and quantitative PCR across germ-cell stages, not a BCAP31-specific causal mechanism. The exact gene-level Results were not read, so neither a confident functional acceptance nor a claim that the experimental annotation is false is justified. |
| GO:0030136 clathrin-coated vesicle | IEA GO_REF:0000107 | REMOVE | Summary: The cited donor experiment contradicts BAP31 enrichment in clathrin-coated vesicles. Reason: The MGI cross-species Bcap31 comparison displays a rat IDA annotation citing PMID:9396746 and RGD:7483571; MGI is the display source, not the donor organism or annotation database. The unchanged source partners identify the rat UniProt/Ensembl protein. Its selected original fractionation Results and Figure 4 caption report strong cellubrevin enrichment but virtually no BAP31 in purified rat-liver clathrin-coated vesicles. This specific negative result contradicts the positive localization transfer. The decision is not based on lack of human data or on an assumption that ER proteins cannot visit clathrin compartments. |
| GO:0032580 Golgi cisterna membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BCAP31 has experimentally supported Golgi-associated localization in the donor literature. Reason: Official comparative annotation records trace the donor Golgi annotation to the hepatic Golgi proteomics study, whose abstract includes analytical fractionation and immunogold validation of BAP31. Retain this secondary location without dismissing it as contamination or generalizing it to the predominant location in every human cell. |
| GO:0042288 MHC class I protein binding | IEA GO_REF:0000107 | ACCEPT | Summary: BCAP31 binds MHC class I proteins. Reason: Mouse class-I association and human MHC-I co-immunoprecipitation independently support this specific binding function. Retain the molecular interaction while separating it from unresolved claims that BCAP31 is an obligatory export receptor for every class-I cargo. |
| GO:0044877 protein-containing complex binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BCAP31 associates with protein complexes. Reason: Mouse MHC-I peptide-loading-complex and tapasin association provides more substantive support than merely noting that BCAP31 belongs to large complexes. Retain the broad binding term as non-core context; it does not identify a separate catalytic activity. |
| GO:0005783 endoplasmic reticulum | IDA GO_REF:0000052 | ACCEPT | Summary: Human Protein Atlas evidence supports ER localization. Reason: Retain the source ER localization, which agrees with independent target-specific studies. A dedicated molecular function in every labeled subcompartment is not required to retain a localization annotation. |
| GO:0098553 lumenal side of endoplasmic reticulum membrane | TAS Reactome:R-HSA-8951499 | KEEP AS NON CORE | Summary: Reactome assigns BCAP31 to an ER-lumen-facing peptide-loading-complex context. Reason: Retain this curated side-of-membrane context without claiming that the whole multipass protein is soluble in the lumen or that its cytoplasmic C terminus contacts a luminal MHC domain. These pathway assignments are distinct from proving a particular binding interface or an obligatory export mechanism. |
| GO:0098553 lumenal side of endoplasmic reticulum membrane | TAS Reactome:R-HSA-983138 | KEEP AS NON CORE | Summary: Reactome assigns BCAP31 to an ER-lumen-facing peptide-loading-complex context. Reason: Retain this curated side-of-membrane context without claiming that the whole multipass protein is soluble in the lumen or that its cytoplasmic C terminus contacts a luminal MHC domain. These pathway assignments are distinct from proving a particular binding interface or an obligatory export mechanism. |
| GO:0098553 lumenal side of endoplasmic reticulum membrane | TAS Reactome:R-HSA-983142 | KEEP AS NON CORE | Summary: Reactome assigns BCAP31 to an ER-lumen-facing peptide-loading-complex context. Reason: Retain this curated side-of-membrane context without claiming that the whole multipass protein is soluble in the lumen or that its cytoplasmic C terminus contacts a luminal MHC domain. These pathway assignments are distinct from proving a particular binding interface or an obligatory export mechanism. |
| GO:0098553 lumenal side of endoplasmic reticulum membrane | TAS Reactome:R-HSA-983161 | KEEP AS NON CORE | Summary: Reactome assigns BCAP31 to an ER-lumen-facing peptide-loading-complex context. Reason: Retain this curated side-of-membrane context without claiming that the whole multipass protein is soluble in the lumen or that its cytoplasmic C terminus contacts a luminal MHC domain. These pathway assignments are distinct from proving a particular binding interface or an obligatory export mechanism. |
| GO:1904294 positive regulation of ERAD pathway | IGI PMID:18555783 BAP31 interacts with Sec61 translocons and promotes retrotra... | ACCEPT | Summary: BCAP31 promotes ER-associated degradation in the CFTR client pathway. Reason: Client engagement and functional cooperation with DERL1 support positive regulation of ERAD. This is active participation in substrate handling, not an inference based merely on being an ERAD substrate. |
| GO:2000060 positive regulation of ubiquitin-dependent protein catabolic process | IDA PMID:18555783 BAP31 interacts with Sec61 translocons and promotes retrotra... | ACCEPT | Summary: BCAP31 promotes ubiquitin-dependent catabolism in the studied client pathway. Reason: The CFTRDeltaF508 client-handling and degradation evidence supports this regulatory process. It does not assign ubiquitin-ligase or protease catalysis to BCAP31 and need not apply identically to clients such as HACD2 whose stability BCAP31 maintains. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-9837136 | ACCEPT | Summary: Reactome places BCAP31 in the ER membrane during RSV SH association. Reason: The viral reaction is consistent with the independently established ER membrane location; retain the localization separately from whether viral binding is a core molecular function. |
| GO:0005515 protein binding | IPI PMID:31206022 BAP31 regulates mitochondrial function via interaction with ... | KEEP AS NON CORE | Summary: BCAP31 associates with several mitochondrial-homeostasis and apoptosis-related proteins. Reason: Preserve the combined source partners NDUFS4, BCL2, VDAC1 and NDUFB11. They do not all have the same demonstrated functional consequence: selective mitochondrial localization effects concern NDUFS4/NDUFB11, whereas VDAC1 association lacks the matching localization effect. A single carrier or adaptor replacement would incorrectly assign one mechanism to the whole combined record. |
| GO:0034976 response to endoplasmic reticulum stress | IDA PMID:31206022 BAP31 regulates mitochondrial function via interaction with ... | ACCEPT | Summary: BCAP31 participates in an ER-stress response at ER-mitochondria contacts. Reason: The source links ER stress to altered BCAP31 contact-site association and mitochondrial protein localization. Retain the stress-response process without assigning a universal stress-sensor receptor or autonomous catalytic activity. |
| GO:0044233 mitochondria-associated endoplasmic reticulum membrane contact site | IDA PMID:31206022 BAP31 regulates mitochondrial function via interaction with ... | ACCEPT | Summary: BCAP31 localizes at ER-mitochondria membrane contacts. Reason: The TOMM40-associated BCAP31 pool and compartment analyses support this contact-site location. The location does not mean that BCAP31 is an integral mitochondrial inner-membrane protein. |
| GO:0070585 protein localization to mitochondrion | IGI PMID:31206022 BAP31 regulates mitochondrial function via interaction with ... | ACCEPT | Summary: BCAP31 supports mitochondrial localization of selected proteins in cooperation with TOMM40. Reason: The study links BCAP31/TOMM40 association to the mitochondrial distribution and stability of NDUFS4 and NDUFB11. Retain the process while distinguishing fractionation/turnover evidence from direct measurement of pore transit or an intrinsic BCAP31 import motor. |
| GO:0005783 endoplasmic reticulum | IDA PMID:24454821 Transmembrane and coiled-coil domain family 1 is a novel pro... | ACCEPT | Summary: The source experimentally supports ER localization of BCAP31. Reason: Retain the target-specific ER location. The different experimental contexts provide localization evidence without requiring every process discussed in each paper to be a core BCAP31 function. |
| GO:0097038 perinuclear endoplasmic reticulum | IDA PMID:25854864 Interaction between human BAP31 and respiratory syncytial vi... | ACCEPT | Summary: BCAP31 is present in the perinuclear ER in the viral interaction study. Reason: The reported perinuclear ER pool is consistent with its ER membrane biology. Retain the specific location without claiming that this experiment demonstrates constitutive cycling through an ER quality-control compartment. |
| GO:1904154 positive regulation of retrograde protein transport, ER to cytosol | IDA PMID:18555783 BAP31 interacts with Sec61 translocons and promotes retrotra... | ACCEPT | Summary: BCAP31 promotes ER-to-cytosol retrotransport of a misfolded client. Reason: The CFTRDeltaF508 study directly supports a role in delivery to and function of the Derlin-1 retrotranslocation pathway. BCAP31 is a client-handling participant; the annotation does not itself demonstrate a BCAP31 pore or ATP-dependent ratchet. |
| GO:0005783 endoplasmic reticulum | IDA PMID:18555783 BAP31 interacts with Sec61 translocons and promotes retrotra... | ACCEPT | Summary: The source experimentally supports ER localization of BCAP31. Reason: Retain the target-specific ER location. The different experimental contexts provide localization evidence without requiring every process discussed in each paper to be a core BCAP31 function. |
| GO:0005783 endoplasmic reticulum | IDA PMID:19401338 Role of syntaxin 18 in the organization of endoplasmic retic... | ACCEPT | Summary: The source experimentally supports ER localization of BCAP31. Reason: Retain the target-specific ER location. The different experimental contexts provide localization evidence without requiring every process discussed in each paper to be a core BCAP31 function. |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | KEEP AS NON CORE | Summary: Membrane proteomics supports a membrane-associated BCAP31 pool. Reason: Retain this broad high-throughput membrane localization. It is compatible with the ER membrane pool and should not be relabeled as plasma membrane merely because a membrane preparation was used. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-351894 | KEEP AS NON CORE | Summary: The Reactome cytosolic entity is the terminal BCAP31 cleavage fragment. Reason: The reaction explicitly places residues 238β246 in the cytosol, while residues 2β164 and 165β237 remain ER-associated. Retain the process-specific fragment location, correcting the inherited speculation that p20 is released into the cytosol. This is not a localization assertion for an independently translated splice isoform. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-351894 | ACCEPT | Summary: The caspase-cleavage reaction places BCAP31 at the ER membrane. Reason: Retain the full protein and membrane-associated cleavage-product ER context. Proteolytic fragments and alternatively spliced UniProt products are different entities. |
| GO:0005811 lipid droplet | IDA PMID:14741744 Identification of major proteins in the lipid droplet-enrich... | KEEP AS NON CORE | Summary: BCAP31 has a source-supported lipid-droplet-associated localization. Reason: Retain the curated localization from the hepatocyte lipid-droplet study as a secondary context. The ER is its major location, but that fact does not establish that the droplet signal is contamination or prove an ER-droplet-contact mechanism. |
| GO:2001244 positive regulation of intrinsic apoptotic signaling pathway | IMP PMID:21183955 Fis1 and Bap31 bridge the mitochondria-ER interface to estab... | KEEP AS NON CORE | Summary: BCAP31 positively regulates intrinsic apoptotic signaling in the FIS1 pathway. Reason: Intact BCAP31 helps recruit procaspase-8 to a FIS1-associated platform, and the resulting p20 product can transmit ER-calcium and mitochondrial signals. The selected original experiments include loss/deletion and downstream signaling tests, so a substrate-only exclusion is contradicted by the evidence. Retain the contextual process without asserting that BCAP31 is a constitutive proapoptotic factor in all cells. |
| GO:0005783 endoplasmic reticulum | IDA PMID:21183955 Fis1 and Bap31 bridge the mitochondria-ER interface to estab... | ACCEPT | Summary: The source experimentally supports ER localization of BCAP31. Reason: Retain the target-specific ER location. The different experimental contexts provide localization evidence without requiring every process discussed in each paper to be a core BCAP31 function. |
| GO:0005886 plasma membrane | IDA PMID:8706661 Molecular cloning and characterization of a transmembrane su... | KEEP AS NON CORE | Summary: The original 6C6 study supports cell-surface BCAP31 in its experimental context. Reason: Retain the experimental surface localization as non-core. Predominant ER residence and an ER-retrieval motif do not prove that an antibody-accessible surface pool is an artifact. Do not generalize the original topology interpretation to every BCAP31 population. |
| GO:0005515 protein binding | IPI PMID:18555783 BAP31 interacts with Sec61 translocons and promotes retrotra... | KEEP AS NON CORE | Summary: BCAP31 associates with SEC61B in membrane-protein quality control. Reason: Retain the SEC61B machinery interaction. Association with a translocon or ERAD component is not evidence that this partner is a transported client or that BCAP31 supplies the ATP-dependent motor activity of the larger pathway. |
| GO:0005515 protein binding | IPI PMID:18555783 BAP31 interacts with Sec61 translocons and promotes retrotra... | KEEP AS NON CORE | Summary: BCAP31 associates with TRAM1 in membrane-protein quality control. Reason: Retain the TRAM1 machinery interaction. Association with a translocon or ERAD component is not evidence that this partner is a transported client or that BCAP31 supplies the ATP-dependent motor activity of the larger pathway. |
| GO:0005515 protein binding | IPI PMID:18555783 BAP31 interacts with Sec61 translocons and promotes retrotra... | KEEP AS NON CORE | Summary: BCAP31 associates with DERL1 in membrane-protein quality control. Reason: Retain the DERL1 machinery interaction. Association with a translocon or ERAD component is not evidence that this partner is a transported client or that BCAP31 supplies the ATP-dependent motor activity of the larger pathway. |
| GO:0005515 protein binding | IPI PMID:21183955 Fis1 and Bap31 bridge the mitochondria-ER interface to estab... | MODIFY | Summary: BCAP31 associates with FIS1 in an apoptotic signaling platform. Reason: The FIS1-BCAP31 complex recruits procaspase-8; removal of the relevant BCAP31 cytoplasmic region prevents recruitment and activation. Bringing signaling components together is more informative than generic binding and fits signaling adaptor activity. This does not assign caspase catalysis to BCAP31, nor does it require calling its coiled-coil region a structurally canonical death-effector domain. Proposed replacements: signaling adaptor activity Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31206022 BAP31 regulates mitochondrial function via interaction with ... | KEEP AS NON CORE | Summary: BCAP31 associates with TOMM40 at ER-mitochondria contacts. Reason: Endogenous association and its functional connection to selected mitochondrial-protein localization support this interaction. TOMM40 is machinery rather than a demonstrated BCAP31-delivered client; co-IP and loss-of-function results do not establish a specific autonomous carrier activity for this pair. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | KEEP AS NON CORE | Summary: BCAP31 has a source-attributed interaction with HTT. Reason: Retain the curated HTT association from the neurodegeneration interaction map. The exact partner attribution is preserved, but no specific client-delivery or signaling-adaptor mechanism is established for this pair by the available source reading. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | KEEP AS NON CORE | Summary: BCAP31 has a source-attributed interaction with KLK6. Reason: Retain the curated KLK6 association from the neurodegeneration interaction map. The exact partner attribution is preserved, but no specific client-delivery or signaling-adaptor mechanism is established for this pair by the available source reading. |
| GO:0005515 protein binding | IPI PMID:9334338 p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated prote... | KEEP AS NON CORE | Summary: BCAP31 associates with procaspase-8 in the original apoptosis study. Reason: Retain the original CASP8 association. The later FIS1-platform study establishes a more specific signaling-adaptor mechanism for its own separately curated source records, but that mechanism is not claimed to have been demonstrated by the earlier binding/cleavage paper. |
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Download this section (compressed HTML)Q: How do BAP31-dependent client handling and MHC-I export differ across cell types and between BAP31 single loss and combined BAP29/BAP31 loss?
Q: Which molecular contacts mediate procaspase-8 recruitment by the BAP31 cytoplasmic region, given that its historical domain name does not establish a canonical death effector fold?
Q: Does BAP31 alter the import rate, delivery, retention, or degradation of specific mitochondrial precursors at ER-mitochondria contacts?
Experiment: Compare client binding and delivery by BAP31 variants in reconstituted systems and cellular rescue experiments, measuring folding, degradation, and surface arrival separately.
Experiment: Measure time-resolved import and turnover of NDUFS4 and NDUFB11 after acute BAP31 depletion, with controls for mitochondrial integrity and precursor availability.
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