BRCA2 is a predominantly nuclear genome-maintenance protein that promotes homologous recombination by binding RAD51 and single-stranded DNA and assembling productive RAD51 filaments on RPA-coated DNA. Its BRC repeats, DNA-binding regions and C-terminal RAD51-binding region coordinate this mediator activity with partners including PALB2 and DSS1. RAD51 performs the DNA strand-exchange reaction, which BRCA2 stimulates. BRCA2 also stabilizes RAD51 at reversed replication forks to protect nascent DNA from nucleolytic degradation, a role distinct from fork reversal itself. Its recombination functions extend to telomere maintenance and meiosis. Pathogenic variants cause BRCA2-related cancer predisposition, while biallelic variants can cause Fanconi anemia complementation group D1.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003697 single-stranded DNA binding | IBA GO_REF:0000033 | ACCEPT | Summary: BRCA2 binds single-stranded DNA as part of its recombination mediator mechanism. Reason: This PAINT inference through PANTHER:PTN000139030 agrees with direct human BRCA2 DNA-binding assays. The human target appearing in WITH/FROM is expected experimental grounding, not circularity. No claim about a specific evolutionary gain node is made without inspecting the underlying tree. |
| GO:0000724 double-strand break repair via homologous recombination | IBA GO_REF:0000033 | ACCEPT | Summary: BRCA2 promotes homologous repair of DNA double-strand breaks by assembling RAD51 on single-stranded DNA. Reason: The PANTHER:PTN000139030 inference is consistent with the directly assayed human mediator activity. The inference is retained without treating donor count or the human target in WITH/FROM as a defect. |
| GO:0000724 double-strand break repair via homologous recombination | IEA GO_REF:0000120 | ACCEPT | Summary: The combined electronic inference identifies BRCA2 homologous recombination repair function. Reason: The InterPro BRCA2/domain and mouse/Ensembl sources agree with direct full-length human BRCA2 experiments. This broad process assertion is valid alongside experimental and phylogenetic observations. |
| GO:0003677 DNA binding | IEA GO_REF:0000043 | ACCEPT | Summary: BRCA2 directly binds DNA, with preferential binding to single-stranded substrates in the purified-protein assays. Reason: The UniProt DNA-binding keyword mapping is supported by experimental human BRCA2 binding. Its breadth does not make the annotation incorrect; the source-specific ssDNA-binding annotation is retained separately. |
| GO:0006281 DNA repair | IEA GO_REF:0000120 | ACCEPT | Summary: BRCA2 is a DNA repair factor that activates RAD51-mediated homologous recombination. Reason: The broad DNA repair inference from BRCA2 family/keyword mappings accurately describes an established function. It does not imply that BRCA2 executes every DNA repair pathway. |
| GO:0005515 protein binding | IPI PMID:10373512 Interaction between the product of the breast cancer suscept... | KEEP AS NON CORE | Summary: Human DSS1 interaction is explicit in the abstract, including two-hybrid assays and endogenous co-immunoprecipitation. Reason: Full Results not read; preserve the two raw GOA observations. The matched GOA partner identifiers are UniProtKB:P60896. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10551859 Expression of BRC repeats in breast cancer cells disrupts th... | KEEP AS NON CORE | Summary: The abstract reports perturbation of the BRCA2-RAD51 complex by inducible wild-type versus mutant BRC4 in MCF7 cells. Reason: Abstract-only cache; fragment interference is not a naturally occurring isoform. The matched GOA partner identifiers are UniProtKB:Q06609. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:12442171 Insights into DNA recombination from the structure of a RAD5... | KEEP AS NON CORE | Summary: The abstract reports the structure of a BRCA2 BRC-repeat/RAD51 complex. Reason: Fragment structure supports binding, not autonomous BRCA2 strand-exchange activity; Results absent. The matched GOA partner identifiers are UniProtKB:Q06609. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15115758 Direct interaction of FANCD2 with BRCA2 in DNA damage respon... | KEEP AS NON CORE | Summary: The abstract explicitly reports BRCA2-FANCD2 two-hybrid interaction and co-immunoprecipitation in human and hamster cells. Reason: Do not confuse FANCD2 with the ubiquitin-ligase core complex; Results absent. The matched GOA partner identifiers are UniProtKB:Q9BXW9. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15800615 CDK-dependent phosphorylation of BRCA2 as a regulatory mecha... | KEEP AS NON CORE | Summary: The abstract reports direct RAD51 interaction with BRCA2 C-terminal material and inhibition by S3291 phosphorylation. Reason: Do not transfer the kinase activity to BRCA2; Results absent. The matched GOA partner identifiers are UniProtKB:Q06609. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16205630 DSS1 is required for the stability of BRCA2. | KEEP AS NON CORE | Summary: The abstract reports BRCA2-DSS1 association and reduced BRCA2 stability after DSS1 depletion. Reason: BRCA2 is the stabilized partner, not thereby a protease or ubiquitin ligase; Results absent. The matched GOA partner identifiers are UniProtKB:P60896. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17420451 Analysis of PALB2/FANCN-associated breast cancer families. | UNDECIDED | Summary: The available abstract and cached Discussion concern PALB2 families, variants, and functional consequences. Reason: The BRCA2-PALB2 target interaction assay is absent from the partial cache; obtain Results before adjudicating this source-specific row. The matched GOA partner identifiers are UniProtKB:Q86YC2. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17515903 Interaction with the BRCA2 C terminus protects RAD51-DNA fil... | KEEP AS NON CORE | Summary: The abstract explicitly reports human BRCA2 exon-27 peptide binding to oligomerized RAD51 and filament stabilization. Reason: Partner isoforms Q06609 and Q06609-1 must remain intact; an erratum is listed but not adjudicated here. The matched GOA partner identifiers are UniProtKB:Q06609, UniProtKB:Q06609-1. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17515904 Stabilization of RAD51 nucleoprotein filaments by the C-term... | KEEP AS NON CORE | Summary: The abstract reports direct binding of the BRCA2 C terminus to an interface in RAD51 filaments. Reason: Preserve the source partner isoform Q06609-1; this fragment is not a BRCA2 alternative product. The matched GOA partner identifiers are UniProtKB:Q06609-1. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17541404 Interactions between human BRCA2 protein and the meiosis-spe... | KEEP AS NON CORE | Summary: The abstract maps DMC1 binding to a distinct BRCA2 region and distinguishes it from RAD51-binding regions. Reason: DMC1 binding is explicit; avoid claiming the DMC1-binding region itself binds RAD51 or extrapolating to universal meiotic function. The matched GOA partner identifiers are UniProtKB:Q06609, UniProtKB:Q14565. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18212739 FANCG promotes formation of a newly identified protein compl... | KEEP AS NON CORE | Summary: The abstract reports FANCG-dependent BRCA2-FANCD2 co-precipitation in human and hamster cells. Reason: Preserve Q9BXW9 and Q9BXW9-2; the specific FANCD2 isoform observation requires the unavailable full Results. The matched GOA partner identifiers are UniProtKB:Q9BXW9, UniProtKB:Q9BXW9-2. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18264088 Resistance to therapy caused by intragenic deletion in BRCA2... | UNDECIDED | Summary: The abstract describes BRCA2 reversion alleles, restored RAD51 foci, and HR proficiency. Reason: RAD51 foci and HR rescue do not alone verify the BRCA2-RAD51 binding assay. Full source unavailable; do not infer misattribution. The matched GOA partner identifiers are UniProtKB:Q06609. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19303847 The BRC repeats of BRCA2 modulate the DNA-binding selectivit... | KEEP AS NON CORE | Summary: The abstract reports BRC-mediated regulation of RAD51 DNA binding and strand exchange. Reason: Useful priority evidence for mediator activity, but distinguish a purified BRC fragment from full-length BRCA2 and do not assign ATPase activity to BRCA2. The matched GOA partner identifiers are UniProtKB:Q06609. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19369211 PALB2 is an integral component of the BRCA complex required ... | KEEP AS NON CORE | Summary: The abstract identifies PALB2 as the bridge in a BRCA1-PALB2-BRCA2 complex. Reason: This supports complex association and does not imply a direct BRCA1-BRCA2 contact; complete source assays not reread here. The matched GOA partner identifiers are UniProtKB:Q86YC2. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19609323 Structural basis for recruitment of BRCA2 by PALB2. | KEEP AS NON CORE | Summary: The abstract reports a PALB2 domain structure with a BRCA2 peptide. Reason: Direct binding is supported; a later erratum is listed but not adjudicated here. The matched GOA partner identifiers are UniProtKB:Q86YC2. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19628690 The BRC repeats of human BRCA2 differentially regulate RAD51... | KEEP AS NON CORE | Summary: The abstract reports BRCA2 BRC1-8-mediated RAD51 loading and stimulated strand exchange. Reason: The nominal Full Text section only repeats the abstract; no Results are available in this cache. The matched GOA partner identifiers are UniProtKB:Q06609. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20421506 Mapping the physical and functional interactions between the... | KEEP AS NON CORE | Summary: The abstract maps direct p53-BRCA2 interactions using BRCA2 C-terminal and BRC regions. Reason: The cellular apoptosis/transcription effects are downstream context, not evidence for a new intrinsic enzyme activity. The matched GOA partner identifiers are UniProtKB:P04637. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20729832 Purified human BRCA2 stimulates RAD51-mediated recombination... | MODIFY | Summary: Purified full-length human BRCA2 binds RAD51 and stimulates RAD51-mediated DNA strand exchange by promoting productive RAD51-ssDNA filament assembly. Reason: The cited paper provides both interaction and functional biochemical evidence, supporting DNA strand exchange activator activity as a more informative molecular function. BRCA2 is the activator and RAD51 performs strand exchange. The same source also reports DMC1 binding, but this replacement does not assert DMC1 activation. The original generic term and both GOA partners remain unchanged in the source projection. Proposed replacements: DNA strand exchange activator activity Supporting Evidence: PMID:20729832 human RAD51 bound to BRCA2 |
| GO:0005515 protein binding | IPI PMID:20729859 Human BRCA2 protein promotes RAD51 filament formation on RPA... | KEEP AS NON CORE | Summary: The available body describes purified full-length BRCA2-RAD51 pull-downs and enhanced RAD51 loading on RPA-coated ssDNA. Reason: Strong core evidence; DSS1 stimulates the reaction, but BRCA2 itself is not the strand-exchange enzyme. The matched GOA partner identifiers are UniProtKB:Q06609. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21399666 A mitotic function for the high-mobility group protein HMG20... | KEEP AS NON CORE | Summary: The abstract distinguishes BRC5 binding to HMG20B from BRC4 binding to RAD51 and reports cellular interference with both interactions. Reason: Keep both GOA partners; do not collapse HMG20B cytokinesis context into RAD51 recombination activity. The matched GOA partner identifiers are UniProtKB:Q06609, UniProtKB:Q9P0W2. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21601571 Valine 1532 of human BRC repeat 4 plays an important role in... | KEEP AS NON CORE | Summary: The abstract explicitly reports mammalian two-hybrid and competitive-ELISA measurements of BRC4-RAD51 binding. Reason: This supports RAD51 interaction; it does not expose the BRCA2 self-interaction evidence underlying separate row 40. The matched GOA partner identifiers are UniProtKB:Q06609. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22116401 Synaptonemal complex protein SYCP3 impairs mitotic recombina... | KEEP AS NON CORE | Summary: The real Results report BRCA2-RAD51 interaction measurements in control, SYCP3-expressing, and SYCP3-depleted cells. Reason: GOA partner is RAD51, not SYCP3. The paper title is insufficient to identify which interaction the row asserts. The matched GOA partner identifiers are UniProtKB:Q06609. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22193777 ChAM, a novel motif that mediates PALB2 intrinsic chromatin ... | KEEP AS NON CORE | Summary: The available Introduction/Discussion identifies BRCA2 within the PALB2 complex and describes retained partner binding by the ChAM-deletion construct. Reason: The target assay panel is absent; retain only the stated complex/binding context and prioritize figure-level verification. The matched GOA partner identifiers are UniProtKB:Q86YC2. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22293751 APRIN is a cell cycle specific BRCA2-interacting protein req... | KEEP AS NON CORE | Summary: The abstract explicitly reports BRCA2 association with APRIN/PDS5B in a replication-stress and cell-cycle context. Reason: This supports the collapsed binding assertion. The SEM1, RAD51, and PALB2 source-specific observations are not individually verified from the abstract. The matched GOA partner identifiers are UniProtKB:P60896, UniProtKB:Q06609, UniProtKB:Q86YC2, UniProtKB:Q9NTI5. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24013206 A cancer-associated BRCA2 mutation reveals masked nuclear ex... | KEEP AS NON CORE | Summary: The abstract explicitly links BRCA2-DSS1 binding to masking of a BRCA2 nuclear-export signal. Reason: Do not equate being retained in the nucleus with transport-receptor activity; complete Results not reread here. The matched GOA partner identifiers are UniProtKB:P60896. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24141787 Breast cancer-associated missense mutants of the PALB2 WD40 ... | KEEP AS NON CORE | Summary: The abstract reports direct BRCA2 binding by the PALB2 WD40 domain and altered binding of PALB2 variants. Reason: RAD51C/PALB2 complex biology does not confer their molecular activities on BRCA2. The matched GOA partner identifiers are UniProtKB:Q86YC2. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24485656 Breast cancer proteins PALB2 and BRCA2 stimulate polymerase ... | KEEP AS NON CORE | Summary: The abstract and available Discussion/Conclusion explicitly report BRCA2-POLH association and stimulation of POLH synthesis on D-loop substrates. Reason: The exact PALB2 interaction panel is not in the partial cache. Polymerase stimulation is a separate evidence priority; BRCA2 is not assigned DNA polymerase activity. The matched GOA partner identifiers are UniProtKB:Q86YC2, UniProtKB:Q9Y253. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24981860 Human-chromatin-related protein interactions identify a deme... | UNDECIDED | Summary: Only the broad chromatin AP-MS screen abstract is available. Reason: The BRCA2-RAD51 data row is unavailable; absence from the abstract is not contrary evidence. The matched GOA partner identifiers are UniProtKB:Q06609. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25282148 Structure and mechanism of action of the BRCA2 breast cancer... | KEEP AS NON CORE | Summary: The abstract reports structural characterization of full-length BRCA2 alone and with RAD51, together with RAD51 filament nucleation. Reason: The actual Results describe purified full-length BRCA2-RAD51 complexes, structural reconstruction and increased RAD51 filament nucleation. Retain the binding property outside the activity-centered core. Figure and supplementary images were not inspected; this is not a claim that all cellular BRCA2 has one oligomeric state. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28319063 Compromised BRCA1-PALB2 interaction is associated with breas... | KEEP AS NON CORE | Summary: The available real Results explicitly state that the tested PALB2 variants retained BRCA2 interaction while selected variants lost BRCA1 binding. Reason: Do not treat the BRCA1-focused title as excluding a BRCA2 assay. The matched GOA partner identifiers are UniProtKB:Q86YC2. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:30410870 Two Missense Variants Detected in Breast Cancer Probands Pre... | KEEP AS NON CORE | Summary: The abstract describes a GFP-reassembly BRCA2-PALB2 assay and interaction-disrupting variants. Reason: Retain binding with assay context; this does not itself settle clinical pathogenicity. The matched GOA partner identifiers are UniProtKB:Q86YC2. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | UNDECIDED | Summary: The BioPlex abstract and partial Introduction/Discussion describe network-scale AP-MS. Reason: No BRCA2-specific interaction record is present in the cache; target PALB2 pair is unverified. The matched GOA partner identifiers are UniProtKB:Q86YC2. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:34591612 A protein interaction landscape of breast cancer. | UNDECIDED | Summary: The breast cancer interactome cache contains Abstract/Discussion but no BRCA2 target result. Reason: The BRCA2-PALB2 measurement is unavailable; BRCA1-spinophilin evidence from this paper does not establish this pair. The matched GOA partner identifiers are UniProtKB:Q86YC2. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:39009827 Proteome-scale characterisation of motif-based interactome r... | KEEP AS NON CORE | Summary: The actual Results and affinity table report binding of a wild-type BRCA2 peptide spanning residues 292-307 to MAP1LC3B, with stronger binding of the tested mutant peptide. Reason: Restrict to peptide/domain biophysics. This does not establish full-length cellular association, a physiological autophagy role, or an alternative BRCA2 product. The matched GOA partner identifiers are UniProtKB:Q9GZQ8. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9560268 The BRC repeats in BRCA2 are critical for RAD51 binding and ... | KEEP AS NON CORE | Summary: The abstract explicitly reports direct BRC-repeat/RAD51 binding and reciprocal cellular co-immunoprecipitation. Reason: Use primary evidence instead of the previous title-only quote. Do not label experimental fragments as isoforms. The matched GOA partner identifiers are UniProtKB:Q06609. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:21601571 Valine 1532 of human BRC repeat 4 plays an important role in... | UNDECIDED | Summary: The cited abstract assays human BRCA2 BRC4 interaction with RAD51; it does not expose the BRCA2 self-interaction experiment. Reason: GOA specifically supplies BRCA2 (UniProtKB:P51587) as the partner for this identical-protein-binding row. The cache is abstract-only, so the source-specific self-binding assay cannot be assessed. BRCA2 oligomerization is supported by another paper, but that does not verify this particular observation. |
| GO:0042802 identical protein binding | IPI PMID:25282148 Structure and mechanism of action of the BRCA2 breast cancer... | KEEP AS NON CORE | Summary: Purified full-length BRCA2 formed dimers in the structural and mass measurements reported by this study. Reason: The abstract and Results describe two-fold structural organization and mass measurements consistent with BRCA2 dimers. Retain self-association as a supported molecular property; do not generalize this in vitro structural state to all cellular BRCA2 or create a separate core activity. Supporting Evidence: |
| GO:0000722 telomere maintenance via recombination | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BRCA2 supports telomere maintenance through recruitment of RAD51 during telomere replication. Reason: The mouse/Ensembl transfer is corroborated by the cited human HeLa ChIP and BRCA2-depletion experiments and by mouse telomere phenotypes. This is a context-specific application of the recombination mediator function. |
| GO:0001556 oocyte maturation | IEA GO_REF:0000107 | UNDECIDED | Summary: The mouse donor evidence concerns meiotic progression and survival of oocytes, rather than a nonspecific ovarian phenotype. Reason: The recovered donor abstract describes abnormal meiotic progression with some oocytes nevertheless completing prophase, fertilizing and producing embryos in a human-BRCA2 BAC rescue model with low gonadal expression. This is relevant evidence for a germ-cell role, so a blanket downstream-phenotype dismissal is unwarranted. The stage-specific maturation experiment and its transfer to the human annotation have not been fully assessed; retain uncertainty rather than infer that BRCA2 controls every step of oocyte maturation. Supporting Evidence: GO_REF:0000107 |
| GO:0001833 inner cell mass cell proliferation | IEA GO_REF:0000107 | UNDECIDED | Summary: Mouse Brca2 loss impairs embryonic proliferation, but the specific inner-cell-mass assay remains unverified. Reason: The historical donor mapping identifies an embryonic deletion study whose abstract reports impaired proliferation, increased p21 and normal apoptosis. That distinguishes a proliferation defect from simple apoptotic loss, but the accessible abstract does not identify the inner-cell-mass experiment. Do not extrapolate whole-embryo proliferation to this precise cell population without inspecting that evidence. Supporting Evidence: GO_REF:0000107 |
| GO:0006302 double-strand break repair | IEA GO_REF:0000107 | ACCEPT | Summary: BRCA2 participates in double-strand break repair through homologous recombination. Reason: The ortholog transfer agrees with direct human biochemical and cell-extract evidence. This parent process is correct and does not attribute end joining or nucleolytic repair chemistry to BRCA2. |
| GO:0007283 spermatogenesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The BRCA2 recombination machinery has a conserved role in spermatogenesis. Reason: The mouse/Ensembl transfer is consistent with HSF2BP-BRCA2 interaction and mouse spermatogenesis findings in PMID:31242413. The human binding assay and the mouse developmental phenotype are distinguished; this is not presented as a directly assayed human fertility outcome. |
| GO:0007420 brain development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BRCA2-dependent genome maintenance supports survival and development of proliferating neural precursors. Reason: The historical mouse donor annotation is experimentally grounded in PMID:17476307. Its accessible abstract and Discussion describe nervous-system Brca2 deletion, accumulated DNA damage and p53-dependent neural loss, with substantial rescue after p53 loss. Retain the existing developmental association as a bounded, non-core role of genome maintenance during neurogenesis; this does not establish an independent neural-patterning activity. The cache contains Abstract, Introduction and Discussion, not the complete Results or Methods. |
| GO:0008283 cell population proliferation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BRCA2 supports cell population expansion through genome maintenance and a reported cytokinesis-associated interaction. Reason: The historical mouse annotations concern embryonic and neural proliferation. Independent human-cell evidence in PMID:21399666 links the BRC5-HMG20b interaction to efficient completion of cytokinesis: BRC5 perturbation delayed division and increased binucleation without the RAD51-focus defect produced by BRC4. Retain this broad cellular outcome as non-core, while distinguishing the tested peptide perturbations from a universal mitogenic activity of BRCA2. |
| GO:0008585 female gonad development | IEA GO_REF:0000107 | UNDECIDED | Summary: The donor study reports germ-cell loss, but the particular female-gonad developmental claim remains unresolved. Reason: The recovered mouse donor abstract describes a truncating Brca2 allele and absent germ cells. Those observations are relevant to gonadal maintenance, but the accessible abstract does not isolate the ovarian assay or distinguish gonadal morphogenesis from secondary germ-cell depletion. Retain the source assertion pending inspection of that experiment; do not reject it from a paper title or infer an ovarian developmental mechanism from infertility alone. Supporting Evidence: GO_REF:0000107 |
| GO:0008630 intrinsic apoptotic signaling pathway in response to DNA damage | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Apoptotic signaling follows unrepaired damage after Brca2 loss; this does not demonstrate that BRCA2 executes that signaling pathway. Reason: The mapped mouse evidence in PMID:17476307 links Brca2 deficiency to accumulated damage and p53-dependent neural apoptosis. This supports BRCA2 as a genome-maintenance factor whose failure activates the death response, rather than identifying it as a component transmitting the apoptotic signal to execution. Mark the unqualified electronic process assignment as over-annotated. This does not deny the separate human BRCA2-p53 interaction or its reported inhibitory effects on p53 activity in PMID:20421506. |
| GO:0010165 response to X-ray | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BRCA2-mediated repair contributes to cellular responses to X-ray-induced DNA lesions. Reason: This ortholog-derived response annotation is compatible with the established repair function and is retained outside the activity-centered core. The particular donor irradiation assay was not reread; the annotation does not imply radiation sensing by BRCA2. |
| GO:0010225 response to UV-C | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BRCA2 participates in the response to UV-associated DNA damage. Reason: The ortholog-derived response annotation is consistent with reported relocalization of BRCA2 to replication sites after UV irradiation. Retain the broad response context without equating it with nucleotide-excision repair catalysis. |
| GO:0010332 response to gamma radiation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BRCA2-mediated homologous repair contributes to responses to gamma-radiation-induced DNA damage. Reason: The cached human MCF-7 study reports that inducible wild-type BRC4 disrupted the BRCA2-RAD51 complex and caused gamma-irradiation hypersensitivity, impaired radiation-induced RAD51 foci and a G2/M-checkpoint defect; the mutant BRC4 control did not disrupt the complex. This independently supports the broad response context. The original mouse donor irradiation assay was not inspected, and no independent radiation-sensor function is inferred. |
| GO:0030097 hemopoiesis | IEA GO_REF:0000107 | UNDECIDED | Summary: The donor evidence demonstrates hematopoietic dysfunction, but the breadth of a hemopoiesis role remains unresolved. Reason: The historical mouse donor study reports fewer colony-forming cells, chromosomal instability, impaired marrow repopulation and a stem-cell proliferation defect in a hypomorphic Brca2 model. This is more specific than an inference from Fanconi-anemia diagnosis alone. The available abstract does not distinguish a role in lineage development from maintenance of proliferating progenitors, so retain uncertainty for this broad developmental process until the relevant assays can be assessed. Supporting Evidence: GO_REF:0000107 |
| GO:0030330 DNA damage response, signal transduction by p53 class mediator | IEA GO_REF:0000107 | UNDECIDED | Summary: BRCA2 influences p53 responses, but its assignment to the p53 DNA-damage signaling cascade remains unresolved. Reason: Historical MGI evidence used an older p53-to-p21 term now replaced by this broader term, but the original donor publication was not accessible. Independent human evidence in PMID:20421506 shows BRCA2-p53 binding and suppression of p53-mediated transcription and apoptosis under the tested expression conditions; that is not equivalent to establishing BRCA2 as a signal-transducing component. Preserve the annotation as unresolved rather than deny this direct regulatory interaction or assume that all p53 effects are secondary. |
| GO:0031297 replication fork processing | IEA GO_REF:0000107 | ACCEPT | Summary: BRCA2 protects reversed replication forks by stabilizing RAD51 nucleofilaments and limiting nascent-DNA degradation. Reason: The ortholog inference is corroborated by human-cell fork experiments in PMID:29038466. BRCA2-dependent protection is distinguished from fork reversal itself, which the study found can occur without BRCA2. The process is a major biological role even though no separate catalytic molecular function is asserted. Supporting Evidence: GO_REF:0000107 PMID:29038466 These data show that BRCA2 generally protects reversed forks from nucleolytic degradation also in conditions of mild replication interference |
| GO:0032465 regulation of cytokinesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BRCA2 participates in cytokinesis regulation through a context distinct from RAD51-dependent repair. Reason: The ortholog transfer is consistent with the BRCA2-HMG20B interaction and cytokinesis perturbations reported in PMID:21399666. The BRC5/HMG20B context is separated from BRC4/RAD51 repair activity; centrosome localization alone is not used to establish cytokinesis. |
| GO:0042771 intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: p53-mediated apoptosis is a response to Brca2 deficiency, rather than a demonstrated intrinsic BRCA2 function. Reason: The mapped neural evidence in PMID:17476307 describes p53-dependent elimination of cells accumulating damage after Brca2 loss. This direction of effect supports protection from the initiating lesions, not participation by BRCA2 in the p53-to-apoptotic-execution cascade itself. The unqualified electronic pathway assignment is therefore over-annotated. The separate BRCA2-p53 binding and inhibitory activity reported in human assays (PMID:20421506) remains acknowledged and does not convert BRCA2 into a pro-apoptotic signaling factor. |
| GO:0043009 chordate embryonic development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BRCA2 supports embryonic development through genome maintenance in proliferating embryonic cells. Reason: The historical donor mapping points to the mouse null-embryo study summarized in PMID:9171368. Its abstract reports early growth retardation and disorganization, with less severe phenotypes in a p53-null background. Retain this existing developmental association as non-core and bounded to genome-maintenance-dependent embryonic viability; it is not evidence for a distinct body-patterning activity. Only the cached abstract was available for this paper. |
| GO:0045931 positive regulation of mitotic cell cycle | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BRCA2 contributes to successful mitotic progression, including a separable cytokinesis-associated function. Reason: The mouse donor abstract links cell-cycle arrest to repair failure and largely intact checkpoint/apoptotic mechanisms, so that evidence alone should not be read as direct activation of cell-cycle regulators. Independent human-cell experiments in PMID:21399666 support a BRC5-HMG20b-dependent contribution to cytokinesis completion that is separable from the BRC4-RAD51 repair interaction. Retain the broad positive-regulation annotation as non-core with these assay boundaries, rather than classifying every division phenotype as secondary to DNA damage. |
| GO:0051276 chromosome organization | IEA GO_REF:0000107 | ACCEPT | Summary: BRCA2 preserves chromosome organization through its direct role in homologous-recombination repair. Reason: This broad annotation is compatible with BRCA2-mediated assembly of RAD51 on single-stranded DNA and restoration of chromosome integrity. Purified human full-length BRCA2 directly promotes RAD51-dependent DNA strand exchange in PMID:20729832; the historical mouse donor studies independently report chromosomal breaks or instability. Accept the broad genome-maintenance process without implying a structural chromosome-coating role or attributing RAD51 strand-exchange catalysis to BRCA2. |
| GO:0071425 hematopoietic stem cell proliferation | IEA GO_REF:0000107 | UNDECIDED | Summary: The donor evidence directly measures a hematopoietic stem-cell defect, but its proliferative interpretation needs the original assay context. Reason: The recovered donor abstract reports both competitive-repopulation failure and a proliferation defect of hypomorphic Brca2 hematopoietic stem cells in their physiological environment. It therefore cannot be dismissed as a generic downstream tissue phenotype. The full assay and its separation of self-renewal, survival and cell division were not inspected; retain a source-specific unresolved judgment rather than claim those distinctions were established. Supporting Evidence: GO_REF:0000107 |
| GO:0072089 stem cell proliferation | IEA GO_REF:0000107 | UNDECIDED | Summary: BRCA2 is important for stem-cell viability and expansion, but the specific transferred donor assays remain incompletely assessed. Reason: Historical mouse mappings identify two truncating-allele studies. Their accessible summaries establish repair-associated proliferative defects, while independent human-BRCA2 complementation in mouse embryonic stem cells (PMID:21719596) chiefly tests survival and repair competence. Survival rescue alone does not identify the rate or mechanism of stem-cell proliferation. The relevant donor stem-cell experiments remain uninspected, so retain uncertainty without denying the established genome-maintenance requirement. |
| GO:0090398 cellular senescence | IEA GO_REF:0000107 | UNDECIDED | Summary: A mouse Brca2 C-terminal deletion accelerates senescence, but this does not by itself assign the wild-type protein a senescence-execution role. Reason: The recovered donor abstract reports premature senescence with preserved irradiation checkpoints and initially comparable cell-cycle progression, attributing the phenotype to defective recombinational repair. That gives the annotation a specific source basis while raising a direction-of-effect issue: preventing damage-induced senescence differs from executing the senescence program. Without the full relevant experiment and donor annotation context, retain uncertainty rather than manufacture a more specific regulatory replacement. Supporting Evidence: GO_REF:0000107 |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:28398198 Functional and mutational landscapes of BRCA1 for homology-d... | ACCEPT | Summary: The study supports the BRCA1-PALB2-BRCA2 repair axis in homology-directed repair. Reason: Although its title emphasizes BRCA1, real Results test BRCA2 depletion in SSA assays and PALB2 mutants defective in BRCA2 binding in HR reporter assays. The annotation is consistent with the established BRCA2 HR function. The observed HR defect of a PALB2 binding mutant is distinguished from a purified BRCA2 reaction; the GOA IDA evidence code remains unchanged. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26833090 Non-catalytic Roles for XPG with BRCA1 and BRCA2 in Homologo... | KEEP AS NON CORE | Summary: The abstract and Discussion explicitly identify a BRCA2/XPG/PALB2/RAD51/DSS1 complex and direct XPG-BRCA2 interaction. Reason: Preserve the complete partner group; complex co-association does not demonstrate every pair as a direct binary contact. The matched GOA partner identifiers are UniProtKB:P28715, UniProtKB:P60896, UniProtKB:Q06609, UniProtKB:Q86YC2. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31242413 HSF2BP Interacts with a Conserved Domain of BRCA2 and Is Req... | KEEP AS NON CORE | Summary: The abstract identifies an HSF2BP-BRCA2 complex and maps the interaction to a specified human BRCA2 region. Reason: The spermatogenesis phenotype is from mouse; do not relabel all human consequences as directly assayed. The matched GOA partner identifiers are UniProtKB:O75031. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IDA PMID:9774970 Stable interaction between the products of the BRCA1 and BRC... | KEEP AS NON CORE | Summary: The abstract reports a biochemical complex containing BRCA1 and BRCA2. Reason: This IDA GOA row has no WITH/FROM value; do not manufacture a partner field. Complex association is not a direct binary-contact claim. The matched GOA partner identifiers are no WITH/FROM partner supplied. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0000724 double-strand break repair via homologous recombination | IMP PMID:21719596 A comprehensive functional characterization of BRCA2 variant... | ACCEPT | Summary: Human BRCA2 variants alter homologous recombination repair in the mouse ES-cell functional assay. Reason: The abstract explicitly reports human BRCA2 variant tests, including HR proficiency of the delta105 internal-deletion product, and the cached Discussion explains the human-gene/mouse-cell system. Retain the gene-level HR function; a disease-associated transcript is not converted into an invented UniProt isoform. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21719596 A comprehensive functional characterization of BRCA2 variant... | UNDECIDED | Summary: The abstract and partial body describe BRCA2 variants and a functional internal-deletion transcript. Reason: No DSS1 interaction measurement is visible in this cache; obtain the corresponding Results before adjudicating the specific partner assertion. The matched GOA partner identifiers are UniProtKB:P60896. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25585578 FBH1 influences DNA replication fork stability and homologou... | UNDECIDED | Summary: The abstract reports RAD51 ubiquitylation by SCF-FBH1 and related cellular phenotypes. Reason: The BRCA2-RAD51 interaction experiment is unavailable; do not infer a wrong-gene error or a BRCA2 E3 activity from the paper focus. The matched GOA partner identifiers are UniProtKB:Q06609. Supporting Evidence: |
| GO:0010484 histone H3 acetyltransferase activity | IDA PMID:9619837 The BRCA2 is a histone acetyltransferase. | UNDECIDED | Summary: An early study reports acetylation of histone H3 by BRCA2 amino-terminal material, while a later study finds no intrinsic BRCA2 HAT activity. Reason: The positive abstract explicitly includes histone H3 among the acetylated substrates, whereas PMID:9824164 reports no intrinsic amino-terminal BRCA2 HAT activity and identifies associated P/CAF activity. The available abstracts do not resolve whether the H3 assay reflects BRCA2 catalysis or a copurifying acetyltransferase, because purification and control experiments are unavailable. Keep this positive experimental assertion UNDECIDED; the opposing NOT assertion is retained separately. No exhaustive replication-history claim is made. Supporting Evidence: PMID:9619837 Our results demonstrate that BRCA2 proteins acetylate primarily H3 and H4 of free histones. PMID:9824164 we find no evidence in support of an intrinsic HAT activity in BRCA2 amino-terminus. |
| GO:0010485 histone H4 acetyltransferase activity | IDA PMID:9619837 The BRCA2 is a histone acetyltransferase. | UNDECIDED | Summary: An early study reports acetylation of histone H4 by BRCA2 amino-terminal material, while a later study finds no intrinsic BRCA2 HAT activity. Reason: The positive abstract explicitly includes histone H4 among the acetylated substrates, whereas PMID:9824164 reports no intrinsic amino-terminal BRCA2 HAT activity and identifies associated P/CAF activity. The available abstracts do not resolve whether the H4 assay reflects BRCA2 catalysis or a copurifying acetyltransferase, because purification and control experiments are unavailable. Keep this positive experimental assertion UNDECIDED; the opposing NOT assertion is retained separately. No exhaustive replication-history claim is made. Supporting Evidence: PMID:9619837 Our results demonstrate that BRCA2 proteins acetylate primarily H3 and H4 of free histones. PMID:9824164 we find no evidence in support of an intrinsic HAT activity in BRCA2 amino-terminus. |
| GO:0005515 protein binding | IPI PMID:19423707 PALB2 regulates recombinational repair through chromatin ass... | KEEP AS NON CORE | Summary: The abstract explicitly describes the PALB2-BRCA2-RAD51 repair assembly and PALB2-dependent localization of BRCA2. Reason: Preserve the complex-association context; oligomerization described in this abstract primarily concerns PALB2, not BRCA2. The matched GOA partner identifiers are UniProtKB:Q86YC2. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:20729832 Purified human BRCA2 stimulates RAD51-mediated recombination... | ACCEPT | Summary: Purified human BRCA2 promotes RAD51-mediated homologous recombination. Reason: The actual Results show direct RAD51 binding, preferential DNA substrate binding, and stimulation of RAD51 strand exchange. BRCA2 acts as mediator/activator; the strand-exchange reaction is executed by RAD51. Supporting Evidence: |
| GO:0003697 single-stranded DNA binding | IDA PMID:20729832 Purified human BRCA2 stimulates RAD51-mediated recombination... | ACCEPT | Summary: Purified full-length human BRCA2 directly binds single-stranded DNA. Reason: The Results include direct DNA-binding measurements. This experimentally established molecular property remains valid alongside the more informative DNA strand exchange activator core. Supporting Evidence: |
| GO:0002020 protease binding | IPI PMID:15314155 BRCA2 is ubiquitinated in vivo and interacts with USP11, a d... | KEEP AS NON CORE | Summary: BRCA2 forms specific complexes with the deubiquitinating enzyme USP11. Reason: The abstract and cached Discussion support USP11 association but leave direct versus indirect contact unresolved. The physiological survival role was reported to be independent of BRCA2 deubiquitination; the study does not establish that endogenous USP11 controls BRCA2 stability. Retain protease binding without transferring USP11 enzymatic activity to BRCA2. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:12242698 Highlight: BRCA1 and BRCA2 proteins in breast cancer. | UNDECIDED | Summary: The available review abstract discusses BRCA1/BRCA2 functions broadly. Reason: It does not verify the two GOA partner-specific experiments (P38398 and Q9GKK8). Trace the primary citation without changing machine identifiers. The matched GOA partner identifiers are UniProtKB:P38398, UniProtKB:Q9GKK8. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15967112 WDRPUH, a novel WD-repeat-containing protein, is highly expr... | KEEP AS NON CORE | Summary: The abstract explicitly reports WDRPUH association with BRCA2. Reason: Do not remove solely because the study emphasizes WDRPUH or hepatocellular carcinoma; source-specific assay detail remains a follow-up priority. The matched GOA partner identifiers are UniProtKB:Q8N1V2. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:11597317 BRCA2 and homologous recombination. | UNDECIDED | Summary: The accessible source is a review that discusses RAD51-BRCA2 interaction and names original studies. Reason: The biological interaction is well-supported elsewhere, but this IPI citation requires a primary-evidence provenance trace. No claim of misattribution is made. The matched GOA partner identifiers are UniProtKB:Q06609. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15930293 BRCA2 suppresses cell proliferation via stabilizing MAGE-D1. | KEEP AS NON CORE | Summary: The abstract explicitly reports BRCA2 binding and stabilization of MAGE-D1. Reason: Stabilization and proliferation effects do not imply that BRCA2 has E3 ligase or deubiquitinase activity. The matched GOA partner identifiers are UniProtKB:Q9Y5V3. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16099937 Analysis of albumin-associated peptides and proteins from ov... | KEEP AS NON CORE | Summary: The structured abstract explicitly reports specific BRCA2 fragments bound to serum albumin, including immunological confirmation in the study workflow. Reason: Describe fragment/carrier-protein context; do not claim a normal full-length nuclear BRCA2-albumin function or populate isoforms from serum fragments. The matched GOA partner identifiers are UniProtKB:P02768. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16275750 Centrobin: a novel daughter centriole-associated protein tha... | KEEP AS NON CORE | Summary: The real Results state that centrobin was identified using a BRCA2 C-terminal bait in a yeast two-hybrid screen. Reason: Physiological significance of the interaction is not resolved there. The centrobin-focused abstract does not invalidate the BRCA2 assay. The matched GOA partner identifiers are UniProtKB:Q8N137. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9774970 Stable interaction between the products of the BRCA1 and BRC... | KEEP AS NON CORE | Summary: The abstract explicitly reports biochemical co-complex association of BRCA1 and BRCA2. Reason: Retain P38398 WITH/FROM and distinguish this IPI row from the separate IDA row 68; neither proves a direct binary contact. The matched GOA partner identifiers are UniProtKB:P38398. The accessible evidence supports the collapsed generic interaction assertion, which is retained as non-core; this does not validate every partner as a direct binary contact. Supporting Evidence: |
| GO:0043015 gamma-tubulin binding | IPI PMID:17286961 Interference with BRCA2, which localizes to the centrosome d... | UNDECIDED | Summary: The cited abstract supports BRCA2 centrosome localization and centrosome-cycle perturbations, but does not expose the gamma-tubulin interaction assay. Reason: Only the abstract is available. Colocalization and abnormal centrosome duplication do not independently establish gamma-tubulin binding. Preserve this source-specific IPI annotation as unresolved without asserting a misattribution. Supporting Evidence: |
| GO:0004402 histone acetyltransferase activity | IDA NOT PMID:9824164 BRCA2 associates with acetyltransferase activity when bound ... | ACCEPT | Summary: The negated annotation records that the tested BRCA2 amino terminus lacked intrinsic histone acetyltransferase activity. Reason: The cached abstract explicitly reports no evidence of intrinsic HAT activity and assigns associated acetyltransferase activity to bound P/CAF. Retain negated:true and ACCEPT this negative assertion in the experimental scope reported. The conflicting positive H3/H4 claims remain UNDECIDED because complete assays are unavailable. Supporting Evidence: PMID:9824164 we find no evidence in support of an intrinsic HAT activity in BRCA2 amino-terminus. |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: BRCA2 acts predominantly in the nucleus during recombination repair. Reason: The PAINT inference agrees with direct BRCA2 nuclear localization and repair studies. A complete family-tree reanalysis was not performed and no phylogenetic defect is asserted. |
| GO:0006355 regulation of DNA-templated transcription | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: BRCA2 has reported transcriptional regulatory activity involving its amino-terminal region and P/CAF association. Reason: The PANTHER:PTN000139030 inference includes target experimental support and is consistent with the accessible PMID:9824164 abstract. It does not require intrinsic HAT activity. The original PMID:9126734 cache lacks scientific text, so its exact activation assay is not independently verified here. |
| GO:0006338 chromatin remodeling | IEA GO_REF:0000108 | UNDECIDED | Summary: This logical inference derives chromatin remodeling from the positive histone H3 acetyltransferase annotation. Reason: GOA WITH/FROM identifies GO:0010484 as the proximate source. That positive HAT assertion is unresolved in light of the conflicting study and unavailable full assays, so the dependent remodeling inference is also unresolved. P/CAF association alone does not demonstrate intrinsic BRCA2 acetyltransferase activity. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: The electronic annotation places BRCA2 in the nucleus. Reason: This localization agrees with direct human BRCA2 immunodetection and nuclear repair function. |
| GO:0005813 centrosome | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: BRCA2 has a centrosomal pool during S and early M phases. Reason: The UniProt subcellular-location mapping agrees with the direct BRCA2 CLS/localization study. Retain this compartment outside the primary nuclear repair core. |
| GO:0006310 DNA recombination | IEA GO_REF:0000120 | ACCEPT | Summary: BRCA2 supports DNA recombination by activating RAD51-mediated strand exchange. Reason: The broad electronic inference is directly consistent with purified human BRCA2 mediator activity. |
| GO:0006974 DNA damage response | IEA GO_REF:0000120 | ACCEPT | Summary: BRCA2 performs homologous repair within the DNA damage response. Reason: The annotation captures repair participation; it does not claim that BRCA2 is an upstream damage sensor or checkpoint kinase. |
| GO:0000152 nuclear ubiquitin ligase complex | IDA PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | KEEP AS NON CORE | Summary: BRCA2 was recovered as a component of the BRCC complex, which contains ubiquitin ligase activity. Reason: The abstract explicitly includes BRCA2 in isolated BRCC. The reconstituted four-subunit E3 complex instead contains BRCA1, BARD1, BRCC45 and BRCC36, excluding BRCA2. Retain complex membership as non-core and do not infer intrinsic BRCA2 ubiquitin ligase activity; complete fractionation and localization assays are unavailable. Supporting Evidence: |
| GO:0005634 nucleus | IDA PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | ACCEPT | Summary: BRCA2 nuclear localization is consistent with its recovery in the DNA repair complex studied here. Reason: The abstract establishes BRCC membership but does not display the nuclear-localization assay. The cellular compartment is independently well established by direct BRCA2 studies, so the curator assignment is retained without overstating source-specific access. |
| GO:0071479 cellular response to ionizing radiation | IMP PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | UNDECIDED | Summary: The BRCC study reports radiation sensitivity after BRCC36 and BRCC45 depletion. Reason: The abstract does not expose a BRCA2-specific perturbation underlying this IMP row, and full text is unavailable. Established BRCA2 repair biology does not identify the particular experimental comparison; retain the annotation as unresolved rather than assigning the other subunits phenotypes to BRCA2. Supporting Evidence: |
| GO:2000001 regulation of DNA damage checkpoint | NAS PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | UNDECIDED | Summary: BRCC complex perturbation affects the DNA damage checkpoint in the cited study. Reason: The accessible abstract specifically describes BRCC36/BRCC45 depletion and does not resolve the BRCA2 contribution underlying this NAS assertion. Complex membership alone does not establish a distinct checkpoint-regulatory mechanism for BRCA2. Supporting Evidence: |
| GO:0005694 chromosome | IEA GO_REF:0000107 | ACCEPT | Summary: BRCA2 associates with chromosomes during DNA repair and at telomeres. Reason: The ortholog transfer is consistent with human telomeric ChIP and BRCA2 chromatin-associated repair machinery. This is an anatomical association, not an inference that BRCA2 restructures all chromosomes. |
| GO:0005737 cytoplasm | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BRCA2 can occupy a cytoplasmic pool in addition to its predominant nuclear localization. Reason: The broad ortholog-derived compartment assertion is consistent with BRCA2 trafficking and centrosome localization. Mutant cytoplasmic retention is not treated as evidence that normal recombination repair occurs in the cytoplasm. |
| GO:0007141 male meiosis I | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BRCA2 participates in meiotic recombination during male meiosis I. Reason: The ortholog transfer agrees with synaptonemal-complex localization, meiotic HSF2BP interactions and the established recombination mediator mechanism. The mouse spermatogenesis phenotype is not recast as a directly tested human phenotype. |
| GO:0070200 establishment of protein localization to telomere | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BRCA2 promotes recruitment of RAD51 to telomeres. Reason: The transferred annotation is independently supported by human HeLa ChIP after BRCA2 depletion. This is a telomere-specific deployment of the mediator mechanism. |
| GO:0005634 nucleus | NAS PMID:19369211 PALB2 is an integral component of the BRCA complex required ... | ACCEPT | Summary: BRCA2 participates in a nuclear BRCA1-PALB2-BRCA2 repair assembly. Reason: The accessible abstract and Discussion describe the complex and DNA-damage localization context. Nuclear localization is consistent with direct BRCA2 studies, while the complete experimental panels of this paper are not cached. |
| GO:1990391 DNA repair complex | IPI PMID:19369211 PALB2 is an integral component of the BRCA complex required ... | ACCEPT | Summary: PALB2 links BRCA1 and BRCA2 in a complex supporting homologous recombination repair. Reason: The abstract and Discussion explicitly support BRCA1-PALB2-BRCA2 complex formation. GO:1990391 is a broad DNA repair complex term; it does not require direct BRCA1-BRCA2 contact or confer BRCA1-BARD1 ligase activity on BRCA2. No narrower complex identifier is invented. Supporting Evidence: |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | ACCEPT | Summary: BRCA2 localizes to the nucleoplasm. Reason: The immunofluorescence-derived GOA assertion is consistent with direct nuclear BRCA2 repair studies. The underlying atlas images were not reopened, and the annotation is retained on the established localization rather than claimed as a newly inspected image result. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: The immunofluorescence-derived source reports a cytosolic BRCA2 pool. Reason: Retain the curator-provided secondary compartment without making it a site of recombination activity. The atlas images and antibody-specific controls were not available for reinspection; BRCA2 import/export and cytoplasmic pools are independently documented. Supporting Evidence: GO_REF:0000052 Reactome:R-HSA-9709273 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9763200 | KEEP AS NON CORE | Summary: The Reactome event describes SEM1-binding-defective BRCA2 mutants and their cytosolic retention. Reason: Retain cytosol as a context-specific localization. The cached event summary was inspected; mutant-retention observations are not generalized to a normal full-length cytosolic repair function. The source is an event summary, not a newly reviewed primary localization experiment. Supporting Evidence: Reactome:R-HSA-9763200 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9709571 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: BRCA2 mutants with BRC defects or a defect in the C-terminal RAD51 binding site do not bind RAD51. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005634 nucleus | IDA PMID:26833090 Non-catalytic Roles for XPG with BRCA1 and BRCA2 in Homologo... | ACCEPT | Summary: BRCA2 participates in nuclear repair assemblies with XPG, PALB2 and RAD51. Reason: The abstract and Discussion report BRCA2 chromatin association and the higher-order repair complex. These support the nuclear context, although the cached body lacks the full localization Results and images. Supporting Evidence: |
| GO:0032991 protein-containing complex | IDA PMID:26833090 Non-catalytic Roles for XPG with BRCA1 and BRCA2 in Homologo... | ACCEPT | Summary: BRCA2 is part of a protein complex with XPG, PALB2, RAD51 and DSS1. Reason: The abstract and Discussion explicitly identify the higher-order complex. The broad complex term is correct; it does not imply all constituent pairs interact directly or that BRCA2 possesses XPG nuclease activity. Supporting Evidence: |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9709601 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: Defective recruitment of BRCA2 and RAD51 due to loss of BRCA2 function in PALB2 binding. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9709268 | KEEP AS NON CORE | Summary: The Reactome event describes nuclear-localization-defective BRCA2 mutants retained in the cytosol. Reason: Retain cytosol as a context-specific localization. The cached event summary was inspected; mutant-retention observations are not generalized to a normal full-length cytosolic repair function. The source is an event summary, not a newly reviewed primary localization experiment. Supporting Evidence: Reactome:R-HSA-9709268 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9709273 | KEEP AS NON CORE | Summary: The Reactome event describes cytosolic BRCA2 before nuclear import and regulation of its retention by SEM1. Reason: Retain cytosol as a context-specific localization. The cached event summary was inspected; mutant-retention observations are not generalized to a normal full-length cytosolic repair function. The source is an event summary, not a newly reviewed primary localization experiment. Supporting Evidence: Reactome:R-HSA-9709273 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9763137 | KEEP AS NON CORE | Summary: The Reactome event describes SEM1 binding, BRCA2 oligomerization and cytosolic mislocalization when this interaction is defective. Reason: Retain cytosol as a context-specific localization. The cached event summary was inspected; mutant-retention observations are not generalized to a normal full-length cytosolic repair function. The source is an event summary, not a newly reviewed primary localization experiment. Supporting Evidence: Reactome:R-HSA-9763137 |
| GO:0032991 protein-containing complex | IDA PMID:9774970 Stable interaction between the products of the BRCA1 and BRC... | ACCEPT | Summary: BRCA1 and BRCA2 coexist in a biochemical complex. Reason: The abstract explicitly reports the complex and subnuclear colocalization. A complex-membership annotation does not require direct binary contact; PALB2-mediated bridging is supported in a later study. |
| GO:0000800 lateral element | IDA PMID:9774970 Stable interaction between the products of the BRCA1 and BRC... | KEEP AS NON CORE | Summary: BRCA2 localizes on axial elements of developing synaptonemal complexes. Reason: This meiotic localization is explicitly reported in the abstract. Retain the existing lateral-element annotation as the curator mapping of that observation, without claiming the images or exact meiotic stage were reexamined. Supporting Evidence: |
| GO:0000781 chromosome, telomeric region | IDA PMID:21076401 BRCA2 acts as a RAD51 loader to facilitate telomere replicat... | KEEP AS NON CORE | Summary: BRCA2 associates with telomeric DNA during S and G2 phases. Reason: The actual Results describe BRCA2 ChIP from synchronized human HeLa cells and a cell-cycle-dependent telomeric signal. This directly supports the telomeric compartment; the full mouse and human tumor analyses are separate contexts. Supporting Evidence: |
| GO:0070200 establishment of protein localization to telomere | IDA PMID:21076401 BRCA2 acts as a RAD51 loader to facilitate telomere replicat... | KEEP AS NON CORE | Summary: BRCA2 enables RAD51 association with telomeric DNA. Reason: The real Results report loss of RAD51 telomeric ChIP signal after BRCA2 depletion in human HeLa cells. This supports establishment of protein localization to telomeres as a specialized use of BRCA2 mediator activity. Supporting Evidence: |
| GO:1990426 mitotic recombination-dependent replication fork processing | IMP PMID:21076401 BRCA2 acts as a RAD51 loader to facilitate telomere replicat... | ACCEPT | Summary: BRCA2-dependent homologous recombination supports replication-fork processing at telomeres. Reason: The Results include BRCA2-depleted human HeLa telomere fragility and impaired telomeric replication, with complementary mouse experiments. The Discussion proposes recombination-mediated handling/restart of stalled or broken forks. This is distinguished from the reversed-fork protection mechanism tested in PMID:29038466; the source does not show BRCA2 itself reverses forks. Supporting Evidence: PMID:29038466 These data show that BRCA2 generally protects reversed forks from nucleolytic degradation also in conditions of mild replication interference |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685242 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: CHEK1 phosphorylates BRCA2. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685341 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: BCDX2 complex stabilizes RAD51 filament. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685838 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: CX3 complex binds D-loop structures. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686410 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: BLM mediates dissolution of double Holliday junction. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686440 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: MUS81:EME1,EME2 cleaves D-loop. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686469 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: Resolution of D-loops cleaved by MUS81:EME1 or MUS81:EME2. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686483 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: Resolution of Holliday junctions cleaved by GEN1 or SLX1A:SLX4:MUS81:EME1,(MUS81:EME2). Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693539 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: Ligation of DNA and formation of Holliday structures following repair synthesis. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693561 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: RAD51 binds BRCA2 at resected DNA DSBs. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693584 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: Cleavage of Holliday junctions by GEN1 or SLX1A:SLX4:MUS81:EME1,(MUS81:EME2). Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693589 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: D-loop dissociation and strand annealing. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693593 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: D-loop extension by DNA polymerases. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693620 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: D-loop formation mediated by PALB2, BRCA2 and RAD51. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9701199 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: Defective D-loop formation mediated by PALB2, BRCA2 and RAD51 due to loss-of-function of BRCA1 in PALB2 binding. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9704330 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: Defective D-loop formation mediated by PALB2, BRCA2 and RAD51 due to loss-of-function of PALB2 in BRCA1 binding. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9704408 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: Defective D-loop formation mediated by PALB2, BRCA2 and RAD51 due to loss-of-function of PALB2 in binding to BRCA2/RAD51/RAD51C. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9853389 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: FIGNL1 binds RAD51. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0005813 centrosome | IDA PMID:21276791 Homologous recombination proteins are associated with centro... | KEEP AS NON CORE | Summary: The cited study associates homologous recombination proteins with centrosomes. Reason: The abstract explicitly names XRCC2 and RAD51 but does not enumerate the BRCA2 assay; no wrong-gene conclusion follows. BRCA2 centrosome localization is independently demonstrated in PMID:17286961 and annotated by the source curator, so it is retained as a secondary compartment with the source-specific access limit explicit. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9709273 | ACCEPT | Summary: BRCA2 is annotated to the nucleoplasm in the Reactome event: BRCA2 translocates to the nucleus. Reason: The cached event summary places the observation within nuclear homologous repair or BRCA2 import. Retain the established compartment while distinguishing BRCA2 participation from the catalytic steps performed by the other named proteins. Disease-variant events do not demonstrate an added wild-type activity; the cache does not expose every underlying physical-entity membership. |
| GO:0051298 centrosome duplication | IMP PMID:17286961 Interference with BRCA2, which localizes to the centrosome d... | KEEP AS NON CORE | Summary: Interference with BRCA2 centrosomal localization perturbs centrosome duplication and positioning. Reason: The abstract reports a BRCA2 centrosomal-localization peptide that displaces endogenous BRCA2 and produces abnormal centrosome duplication. This is evidence for a context-specific centrosome-cycle role, not merely an assumed consequence of HR deficiency. Supporting Evidence: |
| GO:0045893 positive regulation of DNA-templated transcription | IDA PMID:9126734 Transcriptional activation functions in BRCA2. | UNDECIDED | Summary: The cited early report concerns transcriptional activation by BRCA2, but its scientific text is not present in the cache. Reason: The local record contains citation metadata and a title only, despite an Abstract heading. PMID:9824164 discusses prior transcriptional potential and P/CAF recruitment, but that does not replace access to the original activation assay. Retain this specific experimental assertion as unresolved. |
| GO:0033593 BRCA2-MAGE-D1 complex | IDA PMID:15930293 BRCA2 suppresses cell proliferation via stabilizing MAGE-D1. | KEEP AS NON CORE | Summary: BRCA2 forms a complex with MAGE-D1. Reason: The abstract and Discussion report BRCA2 binding and stabilization of MAGE-D1. Keep the named complex outside the recombination-centered core; its reported stability effects do not establish BRCA2 ubiquitin ligase or deubiquitinase activity. Supporting Evidence: |
| GO:0033600 negative regulation of mammary gland epithelial cell proliferation | IDA PMID:15930293 BRCA2 suppresses cell proliferation via stabilizing MAGE-D1. | KEEP AS NON CORE | Summary: BRCA2 suppresses mammary epithelial cell proliferation in a MAGE-D1-dependent experimental context. Reason: The abstract and Discussion describe synergistic growth suppression, loss of the effect when MAGE-D1 is depleted, and the mammary epithelial cell context. This specific regulatory experiment is retained; it does not justify treating every developmental or proliferation phenotype as a direct BRCA2 function. Supporting Evidence: |
| GO:0005634 nucleus | IDA PMID:17286961 Interference with BRCA2, which localizes to the centrosome d... | ACCEPT | Summary: BRCA2 is predominantly nuclear, with a separately described centrosomal pool. Reason: The abstract explicitly states the predominant nuclear localization. The S/early-M restriction refers to centrosomal localization and is not recast as the only period of nuclear localization. Supporting Evidence: |
| GO:0005634 nucleus | IDA PMID:9560268 The BRC repeats in BRCA2 are critical for RAD51 binding and ... | ACCEPT | Summary: Antibodies to BRCA2 identified the gene product as a nuclear protein. Reason: The abstract explicitly reports the approximately 390-kDa nuclear BRCA2 protein as well as RAD51 interactions. Nuclear localization is core to the recombination mechanism. Supporting Evidence: |
| GO:0005634 nucleus | IDA PMID:9774970 Stable interaction between the products of the BRCA1 and BRC... | ACCEPT | Summary: BRCA2 colocalizes with BRCA1 in subnuclear foci in somatic cells. Reason: This localization is explicitly reported in the abstract; the separate synaptonemal-complex observation is not used to claim all BRCA2 is constitutively nuclear. Supporting Evidence: |
| GO:0005813 centrosome | IDA PMID:17286961 Interference with BRCA2, which localizes to the centrosome d... | KEEP AS NON CORE | Summary: BRCA2 localizes to centrosomes during S and early M phases. Reason: The abstract identifies a BRCA2 centrosomal localization signal and describes localization of the corresponding GFP fusion plus interference with endogenous BRCA2 localization. Retain the experimentally stated secondary compartment. Supporting Evidence: |
| GO:0006289 nucleotide-excision repair | IMP PMID:16845393 The role of BRCA2 in replication-coupled DNA interstrand cro... | UNDECIDED | Summary: The paper separates BRCA2-dependent repair of replication-associated double-strand breaks from nucleotide-excision removal of the remaining cross-link lesion. Reason: The abstract establishes BRCA2-dependent ICL repair and separately states a requirement for nucleotide-excision repair, but does not expose a BRCA2-specific role in the excision step. Full assays are unavailable, so the existing IMP NER annotation remains unresolved rather than being removed or mechanically replaced. Supporting Evidence: |
| GO:0006302 double-strand break repair | IMP PMID:16845393 The role of BRCA2 in replication-coupled DNA interstrand cro... | ACCEPT | Summary: BRCA2 is required to complete repair of replication-associated double-strand breaks arising at interstrand cross-links. Reason: The abstract reports deficient repair in human CAPAN-1 extracts and restoration after BRCA2 expression. It explicitly links BRCA2 to repair of replication-mediated breaks, supporting this process annotation without assigning the separate excision reaction to BRCA2. Supporting Evidence: |
| GO:0030141 secretory granule | IDA PMID:8589722 BRCA1 is secreted and exhibits properties of a granin. | UNDECIDED | Summary: The abstract mentions a granin-like motif in BRCA2 but does not describe a BRCA2 secretory-granule localization assay. Reason: The experimental localization statements in the available abstract concern BRCA1 and granins. The unseen full paper may contain additional BRCA2 experiments; the title or abstract emphasis does not establish a wrong-gene annotation. Preserve this source-specific localization as unresolved pending the full target assay. Supporting Evidence: |
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Download this section (compressed HTML)Q: Which GO molecular-function term best represents BRCA2-dependent stabilization of protective RAD51 filaments at reversed replication forks, given the separation from homologous-recombination repair observed with BRCA2 S3291A in PMID:29038466?
Q: Can the complete purification and substrate-control experiments in PMID:9619837 and PMID:9824164 resolve the conflicting claims of intrinsic amino-terminal BRCA2 H3/H4 acetyltransferase activity versus associated P/CAF activity?
Q: For the remaining unresolved mouse-to-human Ensembl process transfers, can the complete oocyte, inner-cell-mass, gonadal, hematopoietic, stem-cell and senescence assays distinguish the specific process contribution from survival or damage responses, and can the historical MGI mappings be reconciled with the exact 2025 donor annotation provenance?
Experiment: After reassessing the two original reports, compare independently purified BRCA2 amino-terminal constructs and full-length BRCA2 with matched purification controls, defined H3/H4 substrates and P/CAF depletion or reconstitution. Verify protein composition and acetylated products so that association and intrinsic catalysis can be distinguished.
Hypothesis: The HAT activity associated with BRCA2 preparations depends on a copurifying acetyltransferase rather than intrinsic BRCA2 catalysis.
Type: Purified-protein reconstitution with contamination controls
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