BARD1 is the BRCA1-associated RING-domain protein that combines nuclear chromatin recognition with regulation of DNA repair. Its N-terminal RING forms a heterodimer with BRCA1, while its ankyrin repeats and tandem BRCT domains recognize nucleosomes bearing unmethylated H4K20 and damage-induced H2A ubiquitin marks. This recognition recruits and positions the BRCA1–BARD1 complex on post-replicative chromatin. BARD1 contributes to the complex's ubiquitin ligase activity toward C-terminal H2A lysines; BRCA1 supplies the demonstrated E2-binding interface. Through separate DNA-binding and RAD51 contacts, the heterodimer promotes homologous DNA pairing and stimulates DNA-end resection machinery during homologous recombination. BARD1 also participates in context-dependent regulation of RNA processing, protein stability and cell survival.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000151 ubiquitin ligase complex | NAS PMID:14976165 BRCA1 : BARD1 induces the formation of conjugated ubiquitin ... | MODIFY | Summary: BARD1 is a subunit of the BRCA1–BARD1 ubiquitin ligase complex. Reason: The cellular ubiquitination study concerns the BRCA1–BARD1 heterodimer. Its established identity supports the specific complex term instead of the generic ligase-complex parent. Source assertion: PMID:14976165. Proposed replacements: BRCA1-BARD1 complex |
| GO:0000152 nuclear ubiquitin ligase complex | IDA PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | ACCEPT | Summary: BARD1 participates in a nuclear ubiquitin ligase assembly. Reason: The source reports a larger BRCC assembly and reconstitution with BRCA1, BARD1, BRCC45 and BRCC36. Retain this experimentally assigned nuclear complex context; restricting that assertion to the isolated heterodimer would discard the broader assembly actually investigated. The abstract does not establish every BARD1-specific localization experiment. Source assertion: PMID:14636569. |
| GO:0001894 tissue homeostasis | TAS PMID:15782130 BARD1 induces apoptosis by catalysing phosphorylation of p53... | KEEP AS NON CORE | Summary: Tissue homeostasis is a downstream context of BARD1-dependent cell survival and apoptosis. Reason: The source links BARD1, p53 stabilization and apoptosis in particular cellular settings. This broad tissue-level consequence is retained as non-core rather than made a direct molecular function. Source assertion: PMID:15782130. |
| GO:0003723 RNA binding | IDA PMID:12419249 BRCA1 supports XIST RNA concentration on the inactive X chro... | KEEP AS NON CORE | Summary: BARD1 has an experimentally assigned RNA association outside its principal chromatin-repair role. Reason: The original XIST study assayed BARD1 despite its BRCA1-focused title: the selected original Results report XIST in anti-BARD1 precipitates, while leaving direct versus indirect association unresolved. Preserve the curated positive RNA-binding assertion as non-core, without treating that experiment as a purified binary-binding assay or asserting the disputed XIST-localization model. The canonical cache is abstract-only; selected original Results were read separately by root. Source assertion: PMID:12419249. |
| GO:0004842 ubiquitin-protein transferase activity | IDA PMID:12890688 The BRCA1/BARD1 heterodimer assembles polyubiquitin chains t... | MODIFY | Summary: BARD1 contributes to the E3 ubiquitin ligase activity of BRCA1–BARD1. Reason: The relevant chemistry is E3-mediated substrate ubiquitination, which is more specific than generic ubiquitin transferase activity. BARD1 stabilizes and positions the heterodimer; the observed E2 interface is on BRCA1. This is a contribution to complex activity, not an autonomous E1/E2 or isolated-BARD1 enzyme claim. Existing source fields, including contributes_to where present, are retained. Source assertion: PMID:12890688. Proposed replacements: ubiquitin protein ligase activity |
| GO:0004842 ubiquitin-protein transferase activity | IDA PMID:20351172 The UBXN1 protein associates with autoubiquitinated forms of... | MODIFY | Summary: BARD1 contributes to the E3 ubiquitin ligase activity of BRCA1–BARD1. Reason: The relevant chemistry is E3-mediated substrate ubiquitination, which is more specific than generic ubiquitin transferase activity. BARD1 stabilizes and positions the heterodimer; the observed E2 interface is on BRCA1. This is a contribution to complex activity, not an autonomous E1/E2 or isolated-BARD1 enzyme claim. Existing source fields, including contributes_to where present, are retained. Source assertion: PMID:20351172. Proposed replacements: ubiquitin protein ligase activity |
| GO:0004842 ubiquitin-protein transferase activity | NAS PMID:15905410 BRCA1/BARD1 inhibition of mRNA 3' processing involves target... | MODIFY | Summary: BARD1 contributes to the E3 ubiquitin ligase activity of BRCA1–BARD1. Reason: The relevant chemistry is E3-mediated substrate ubiquitination, which is more specific than generic ubiquitin transferase activity. BARD1 stabilizes and positions the heterodimer; the observed E2 interface is on BRCA1. This is a contribution to complex activity, not an autonomous E1/E2 or isolated-BARD1 enzyme claim. Existing source fields, including contributes_to where present, are retained. Source assertion: PMID:15905410. Proposed replacements: ubiquitin protein ligase activity |
| GO:0005515 protein binding | IPI PMID:10026184 Mapping the functional domains of BRCA1. Interaction of the ... | MODIFY | Summary: BARD1 binds BRCA1 to form its functional heterodimer. Reason: The source directly characterizes the stable heterodimeric RING-region constructs. Together with PMID:11573085, this supports protein heterodimerization activity as a more informative molecular function than protein binding. The refinement does not manufacture another source row. Source assertion: PMID:10026184. Proposed replacements: protein heterodimerization activity Supporting Evidence: PMID:10026184 preferentially form a stable heterodimer |
| GO:0005515 protein binding | IPI PMID:10477523 Functional interaction of BRCA1-associated BARD1 with polyad... | KEEP AS NON CORE | Summary: The reported BARD1–CSTF2 interaction is supporting evidence rather than a core molecular function. Reason: The CSTF2 association is consistent with the BARD1/CstF RNA-processing context reported in PMID:10477523 and PMID:20379136. Retain generic binding as non-core. The accessible abstracts do not independently resolve every binary interface in the multiprotein assembly; do not infer that BARD1 is a nuclease or polyadenylation catalyst. Source assertion: PMID:10477523. |
| GO:0005515 protein binding | IPI PMID:10477523 Functional interaction of BRCA1-associated BARD1 with polyad... | MODIFY | Summary: BARD1 binds BRCA1 to form its functional heterodimer. Reason: The RNA-processing study is interpreted alongside independent structural evidence for the same BRCA1 interaction. Together with PMID:11573085, this supports protein heterodimerization activity as a more informative molecular function than protein binding. The refinement does not manufacture another source row. Source assertion: PMID:10477523. Proposed replacements: protein heterodimerization activity |
| GO:0005515 protein binding | IPI PMID:10477523 Functional interaction of BRCA1-associated BARD1 with polyad... | KEEP AS NON CORE | Summary: The reported BARD1–CSTF1/CstF-50 interaction is supporting evidence rather than a core molecular function. Reason: The CSTF1/CstF-50 association is consistent with the BARD1/CstF RNA-processing context reported in PMID:10477523 and PMID:20379136. Retain generic binding as non-core. The accessible abstracts do not independently resolve every binary interface in the multiprotein assembly; do not infer that BARD1 is a nuclease or polyadenylation catalyst. Source assertion: PMID:10477523. Supporting Evidence: PMID:10477523 BARD1-CstF-50 interaction inhibits polyadenylation in vitro. |
| GO:0005515 protein binding | IPI PMID:15184379 Nucleophosmin/B23 is a candidate substrate for the BRCA1-BAR... | KEEP AS NON CORE | Summary: The reported BARD1–NPM1/nucleophosmin interaction is supporting evidence rather than a core molecular function. Reason: The source reports interaction with NPM1 and ubiquitination by the BRCA1–BARD1 complex in vitro and in cells, with NPM1 stabilization. Retain the binding observation as non-core; it does not make BARD1 a nucleophosmin-like enzyme or establish degradation of this substrate. Source assertion: PMID:15184379. |
| GO:0005515 protein binding | IPI PMID:15265711 BARD1 regulates BRCA1 apoptotic function by a mechanism invo... | MODIFY | Summary: BARD1 binds BRCA1 to form its functional heterodimer. Reason: The source explicitly tests BRCA1–BARD1 association and its effect on nuclear retention. Together with PMID:11573085, this supports protein heterodimerization activity as a more informative molecular function than protein binding. The refinement does not manufacture another source row. Source assertion: PMID:15265711. Proposed replacements: protein heterodimerization activity |
| GO:0005515 protein binding | IPI PMID:15383276 A protein interaction network links GIT1, an enhancer of hun... | KEEP AS NON CORE | Summary: The reported BARD1–TCERG1 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with TCERG1 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:15383276. |
| GO:0005515 protein binding | IPI PMID:15383276 A protein interaction network links GIT1, an enhancer of hun... | KEEP AS NON CORE | Summary: The reported BARD1–KAT7 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with KAT7 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:15383276. |
| GO:0005515 protein binding | IPI PMID:15383276 A protein interaction network links GIT1, an enhancer of hun... | KEEP AS NON CORE | Summary: The reported BARD1–CHD3 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with CHD3 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:15383276. |
| GO:0005515 protein binding | IPI PMID:15383276 A protein interaction network links GIT1, an enhancer of hun... | KEEP AS NON CORE | Summary: The reported BARD1–CEP126 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with CEP126 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:15383276. |
| GO:0005515 protein binding | IPI PMID:15383276 A protein interaction network links GIT1, an enhancer of hun... | KEEP AS NON CORE | Summary: The reported BARD1–GIT1 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with GIT1 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:15383276. |
| GO:0005515 protein binding | IPI PMID:17873885 E2-BRCA1 RING interactions dictate synthesis of mono- or spe... | MODIFY | Summary: BARD1 binds BRCA1 to form its functional heterodimer. Reason: The source studies the heterodimeric ligase and its E2 interactions; E2 catalysis is not assigned to BARD1. Together with PMID:11573085, this supports protein heterodimerization activity as a more informative molecular function than protein binding. The refinement does not manufacture another source row. Source assertion: PMID:17873885. Proposed replacements: protein heterodimerization activity |
| GO:0005515 protein binding | IPI PMID:19117993 BRCA1-associated protein 1 interferes with BRCA1/BARD1 RING ... | KEEP AS NON CORE | Summary: The reported BARD1–BAP1 interaction is supporting evidence rather than a core molecular function. Reason: The source directly maps BAP1–BARD1 association and reports inhibition of heterodimer ligase activity. Retain this regulatory interaction as non-core. BAP1 performs the deubiquitination, and complex disruption can also inhibit ligase activity independently of BAP1 catalysis. Source assertion: PMID:19117993. Supporting Evidence: PMID:19117993 BAP1 interacts with BARD1 to inhibit the E3 ligase activity |
| GO:0005515 protein binding | IPI PMID:19369211 PALB2 is an integral component of the BRCA complex required ... | MODIFY | Summary: BARD1 binds BRCA1 to form its functional heterodimer. Reason: The original assertion names BRCA1; the PALB2-focused abstract is not evidence that this pair was absent from the full study. Together with PMID:11573085, this supports protein heterodimerization activity as a more informative molecular function than protein binding. The refinement does not manufacture another source row. Source assertion: PMID:19369211. Proposed replacements: protein heterodimerization activity |
| GO:0005515 protein binding | IPI PMID:20351172 The UBXN1 protein associates with autoubiquitinated forms of... | KEEP AS NON CORE | Summary: The reported BARD1–UBXN1 interaction is supporting evidence rather than a core molecular function. Reason: The source reports UBXN1 association with autoubiquitinated BRCA1–BARD1 and inhibition of the complex. Retain the physical interaction as non-core without transferring UBXN1's ubiquitin-binding or inhibitory functions to BARD1. Source assertion: PMID:20351172. |
| GO:0005515 protein binding | IPI PMID:20379136 Nuclear deadenylation/polyadenylation factors regulate 3' pr... | KEEP AS NON CORE | Summary: The reported BARD1–PARN interaction is supporting evidence rather than a core molecular function. Reason: The PARN association is consistent with the BARD1/CstF RNA-processing context reported in PMID:10477523 and PMID:20379136. Retain generic binding as non-core. The accessible abstracts do not independently resolve every binary interface in the multiprotein assembly; do not infer that BARD1 is a nuclease or polyadenylation catalyst. Source assertion: PMID:20379136. |
| GO:0005515 protein binding | IPI PMID:20379136 Nuclear deadenylation/polyadenylation factors regulate 3' pr... | KEEP AS NON CORE | Summary: The reported BARD1–CSTF2 interaction is supporting evidence rather than a core molecular function. Reason: The CSTF2 association is consistent with the BARD1/CstF RNA-processing context reported in PMID:10477523 and PMID:20379136. Retain generic binding as non-core. The accessible abstracts do not independently resolve every binary interface in the multiprotein assembly; do not infer that BARD1 is a nuclease or polyadenylation catalyst. Source assertion: PMID:20379136. |
| GO:0005515 protein binding | IPI PMID:22110403 Interplay between BRCA1 and RHAMM regulates epithelial apico... | MODIFY | Summary: BARD1 binds BRCA1 to form its functional heterodimer. Reason: The original assertion names BRCA1 in a polarity study; the abstract does not provide a complete pair-level assay description. Together with PMID:11573085, this supports protein heterodimerization activity as a more informative molecular function than protein binding. The refinement does not manufacture another source row. Source assertion: PMID:22110403. Proposed replacements: protein heterodimerization activity |
| GO:0005515 protein binding | IPI PMID:23680151 Function of BRCA1 in the DNA damage response is mediated by ... | MODIFY | Summary: BARD1 binds BRCA1 to form its functional heterodimer. Reason: The source explicitly describes BRCA1–BARD1 as a RING-domain heterodimer. Together with PMID:11573085, this supports protein heterodimerization activity as a more informative molecular function than protein binding. The refinement does not manufacture another source row. Source assertion: PMID:23680151. Proposed replacements: protein heterodimerization activity |
| GO:0005515 protein binding | IPI PMID:24981860 Human-chromatin-related protein interactions identify a deme... | MODIFY | Summary: BARD1 forms a functional heterodimer with BRCA1. Reason: The original affinity-purification mass-spectrometry survey of chromatin-related proteins supplies the curated BRCA1 interaction assertion. Its complete pair-level construct and supplementary records have not been independently adjudicated, so that survey is not treated as a direct demonstration of heterodimeric stoichiometry. Independent primary evidence in PMID:10026184 shows preferential stable heterodimer formation by BRCA1 and BARD1 RING-region constructs, and PMID:11573085 resolves their heterodimeric solution structure. Those experiments support GO:0046982 for the same canonical BRCA1 partner. This functional refinement uses the additional primary studies; it does not claim that the original survey measured that mechanism or that every alternative product was tested. Proposed replacements: protein heterodimerization activity Supporting Evidence: PMID:11573085 structure of the heterodimer formed between the RING domains of BRCA1 and BARD1. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The reported BARD1–EXOC5 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with EXOC5 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:25416956. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The reported BARD1–LDOC1 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with LDOC1 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:25416956. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The reported BARD1–GOLGA2 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with GOLGA2 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:25416956. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The reported BARD1–KRT40 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with KRT40 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:25416956. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The reported BARD1–FAM9B interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with FAM9B as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:25416956. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The reported BARD1–CEP70 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with CEP70 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:25416956. |
| GO:0005515 protein binding | IPI PMID:29656893 DNA Repair Network Analysis Reveals Shieldin as a Key Regula... | MODIFY | Summary: BARD1 forms a functional heterodimer with BRCA1. Reason: The original proximity-labeling study of DNA-repair interaction neighborhoods supplies the curated BRCA1 interaction assertion. Its complete pair-level construct and supplementary records have not been independently adjudicated, so that survey is not treated as a direct demonstration of heterodimeric stoichiometry. Independent primary evidence in PMID:10026184 shows preferential stable heterodimer formation by BRCA1 and BARD1 RING-region constructs, and PMID:11573085 resolves their heterodimeric solution structure. Those experiments support GO:0046982 for the same canonical BRCA1 partner. This functional refinement uses the additional primary studies; it does not claim that the original survey measured that mechanism or that every alternative product was tested. Proposed replacements: protein heterodimerization activity |
| GO:0005515 protein binding | IPI PMID:31270457 Isomerization of BRCA1-BARD1 promotes replication fork prote... | MODIFY | Summary: BARD1 binds BRCA1 to form its functional heterodimer. Reason: The source studies the BRCA1–BARD1 complex in fork protection. The supporting BRCA1 isoform identifier is preserved; it is not a BARD1 isoform restriction. Together with PMID:11573085, this supports protein heterodimerization activity as a more informative molecular function than protein binding. The refinement does not manufacture another source row. Source assertion: PMID:31270457. Proposed replacements: protein heterodimerization activity |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | KEEP AS NON CORE | Summary: The reported BARD1–LDOC1 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with LDOC1 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:31515488. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The reported BARD1–HSF2BP interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with HSF2BP as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:32296183. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The reported BARD1–LDOC1 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with LDOC1 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:32296183. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The reported BARD1–GOLGA2 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with GOLGA2 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:32296183. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The reported BARD1–TRAF1 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with TRAF1 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:32296183. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The reported BARD1–IKZF1 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with IKZF1 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:32296183. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The reported BARD1–RABEP1 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with RABEP1 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:32296183. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The reported BARD1–MTUS2 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with MTUS2 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:32296183. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The reported BARD1–ZNF655 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with ZNF655 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:32296183. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The reported BARD1–KIFC3 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with KIFC3 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:32296183. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The reported BARD1–AXIN2 interaction is supporting evidence rather than a core molecular function. Reason: Retain the positive curated IPI interaction with AXIN2 as supporting interaction context, without promoting the generic binding assertion to a core molecular function. The source is an interaction survey; its abstract and the curated UniProt interaction record support preserving the pair, but no complete supplementary pair/construct table has been independently adjudicated. A map edge alone does not establish a specific catalytic, adaptor, or biological-process function. The supporting accession and any partner isoform suffix are preserved. Source assertion: PMID:32296183. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: BARD1 forms a functional heterodimer with BRCA1. Reason: The original affinity-purification mass-spectrometry interactome survey supplies the curated BRCA1 interaction assertion. Its complete pair-level construct and supplementary records have not been independently adjudicated, so that survey is not treated as a direct demonstration of heterodimeric stoichiometry. Independent primary evidence in PMID:10026184 shows preferential stable heterodimer formation by BRCA1 and BARD1 RING-region constructs, and PMID:11573085 resolves their heterodimeric solution structure. Those experiments support GO:0046982 for the same canonical BRCA1 partner. This functional refinement uses the additional primary studies; it does not claim that the original survey measured that mechanism or that every alternative product was tested. Proposed replacements: protein heterodimerization activity |
| GO:0005515 protein binding | IPI PMID:34591612 A protein interaction landscape of breast cancer. | MODIFY | Summary: BARD1 forms a functional heterodimer with BRCA1. Reason: The original affinity-purification mass-spectrometry survey of breast-cancer proteins supplies the curated BRCA1 interaction assertion. Its complete pair-level construct and supplementary records have not been independently adjudicated, so that survey is not treated as a direct demonstration of heterodimeric stoichiometry. Independent primary evidence in PMID:10026184 shows preferential stable heterodimer formation by BRCA1 and BARD1 RING-region constructs, and PMID:11573085 resolves their heterodimeric solution structure. Those experiments support GO:0046982 for the same canonical BRCA1 partner. This functional refinement uses the additional primary studies; it does not claim that the original survey measured that mechanism or that every alternative product was tested. Proposed replacements: protein heterodimerization activity |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | UNDECIDED | Summary: The AKT1 interaction requires resolution of the tested wild-type or variant constructs. Reason: PMID:35512704 compares wild-type and mutant-dependent interaction gains. GOA and UniProt record the BARD1–AKT1 pair, but the inspected cache does not expose the exact construct-level pair needed to decide its scope. Neither absence of a BARD1 mention in the main text nor the mutation-focused title refutes the observation. Retain the original assertion unresolved pending the relevant pair/construct data; do not remove it or generalize a variant-only result to wild type. Source assertion: PMID:35512704. |
| GO:0005515 protein binding | IPI PMID:8944023 Identification of a RING protein that can interact in vivo w... | MODIFY | Summary: BARD1 binds BRCA1 to form its functional heterodimer. Reason: The discovery study establishes the BARD1 interaction with BRCA1; later RING structures resolve its heterodimeric organization. Together with PMID:11573085, this supports protein heterodimerization activity as a more informative molecular function than protein binding. The refinement does not manufacture another source row. Source assertion: PMID:8944023. Proposed replacements: protein heterodimerization activity |
| GO:0005634 nucleus | IDA PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | ACCEPT | Summary: BARD1 acts in the nucleus. Reason: Retain experimental nuclear localization in the BRCC study. Nuclear localization is directly supported for human BARD1 by PMID:9342365 and PMID:15632137 and is central to its chromatin-repair function. This annotation need not imply exclusive residence in the nucleus. Source assertion: PMID:14636569. |
| GO:0005634 nucleus | IDA PMID:15265711 BARD1 regulates BRCA1 apoptotic function by a mechanism invo... | ACCEPT | Summary: BARD1 acts in the nucleus. Reason: Retain BRCA1–BARD1 nuclear retention in the transfection study. Nuclear localization is directly supported for human BARD1 by PMID:9342365 and PMID:15632137 and is central to its chromatin-repair function. This annotation need not imply exclusive residence in the nucleus. Source assertion: PMID:15265711. |
| GO:0005634 nucleus | IDA PMID:9342365 Cell cycle-dependent colocalization of BARD1 and BRCA1 prote... | ACCEPT | Summary: BARD1 acts in the nucleus. Reason: Retain cell-cycle-dependent BARD1/BRCA1 nuclear colocalization. Nuclear localization is directly supported for human BARD1 by PMID:9342365 and PMID:15632137 and is central to its chromatin-repair function. This annotation need not imply exclusive residence in the nucleus. Source assertion: PMID:9342365. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: BARD1 acts in the nucleus. Reason: Retain the composite automated localization inference. Nuclear localization is directly supported for human BARD1 by PMID:9342365 and PMID:15632137 and is central to its chromatin-repair function. This annotation need not imply exclusive residence in the nucleus. The source includes mouse and automated localization inputs; target-specific human localization experiments support the location without assuming identical human and rodent NLS sequences. Source assertion: GO_REF:0000120. |
| GO:0005634 nucleus | IMP PMID:15632137 Nuclear targeting and cell cycle regulatory function of huma... | ACCEPT | Summary: BARD1 acts in the nucleus. Reason: Retain mutational analysis of human BARD1 nuclear localization sequences. Nuclear localization is directly supported for human BARD1 by PMID:9342365 and PMID:15632137 and is central to its chromatin-repair function. This annotation need not imply exclusive residence in the nucleus. Source assertion: PMID:15632137. Supporting Evidence: PMID:15632137 two active nuclear localization signals |
| GO:0005634 nucleus | NAS PMID:18171670 Cell cycle-dependent complex formation of BRCA1.CtIP.MRN is ... | ACCEPT | Summary: BARD1 acts in the nucleus. Reason: Retain the source-assigned BRCA1/CtIP/MRN nuclear context. Nuclear localization is directly supported for human BARD1 by PMID:9342365 and PMID:15632137 and is central to its chromatin-repair function. This annotation need not imply exclusive residence in the nucleus. The source abstract alone does not establish a new BARD1 imaging experiment; this is a holistic retention of the location, not an upgrade of the NAS evidence code. Source assertion: PMID:18171670. |
| GO:0005634 nucleus | NAS PMID:20656689 Differential regulation of JAMM domain deubiquitinating enzy... | ACCEPT | Summary: BARD1 acts in the nucleus. Reason: Retain the source-assigned RAP80 complex nuclear context. Nuclear localization is directly supported for human BARD1 by PMID:9342365 and PMID:15632137 and is central to its chromatin-repair function. This annotation need not imply exclusive residence in the nucleus. The source abstract alone does not establish a new BARD1 imaging experiment; this is a holistic retention of the location, not an upgrade of the NAS evidence code. Source assertion: PMID:20656689. |
| GO:0005634 nucleus | NAS PMID:22369660 BRCA1 tumor suppressor network: focusing on its tail. | ACCEPT | Summary: BARD1 acts in the nucleus. Reason: Retain the source-assigned BRCA1 complex nuclear context. Nuclear localization is directly supported for human BARD1 by PMID:9342365 and PMID:15632137 and is central to its chromatin-repair function. This annotation need not imply exclusive residence in the nucleus. The source abstract alone does not establish a new BARD1 imaging experiment; this is a holistic retention of the location, not an upgrade of the NAS evidence code. Source assertion: PMID:22369660. |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | ACCEPT | Summary: BARD1 localizes to the nucleoplasm. Reason: Retain the curated immunofluorescence location. It accords with nuclear BARD1 localization and its chromatin-associated BRCA1 complex; it is not an inference that every nuclear compartment is equivalent. Source assertion: GO_REF:0000052. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5659781 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event BRCA1 forms a heterodimer with BARD1 supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5659781. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5683385 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Formation of BRCA1-A complex at DNA DSBs supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5683385. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5683735 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event CHEK2 is recruited to DNA DSBs supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5683735. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5683801 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event CHEK2 phosphorylates BRCA1 supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5683801. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5684052 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event PIAS4 SUMOylates MDC1 supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5684052. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5684071 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event RNF4 ubiquitinates MDC1 supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5684071. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5684108 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event BRCA1 binds phosphorylated RBBP8 supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5684108. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5684875 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Binding of ATR:ATRIP to RPA at resected DNA DSBs supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5684875. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5684882 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event CHEK1 is recruited to resected DNA DSBs supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5684882. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5684887 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Activation of CHEK1 at resected DNA DSBs supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5684887. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685011 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event ATR activation at DNA DSBs supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5685011. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685156 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event ATR phosphorylates RPA2 supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5685156. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685341 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event BCDX2 complex stabilizes RAD51 filament supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5685341. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685838 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event CX3 complex binds D-loop structures supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5685838. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685985 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event EXO1 or DNA2 in complex with BLM or WRN binds initially resected DNA DSBs along with BRIP1 recruitment supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5685985. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685994 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Long-range resection of DNA DSBs by EXO1 or DNA2 supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5685994. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686410 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event BLM mediates dissolution of double Holliday junction supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5686410. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686440 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event MUS81:EME1,EME2 cleaves D-loop supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5686440. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686469 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Resolution of D-loops cleaved by MUS81:EME1 or MUS81:EME2 supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5686469. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686483 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Resolution of Holliday junctions cleaved by GEN1 or SLX1A:SLX4:MUS81:EME1,(MUS81:EME2) supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5686483. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686642 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event RAD52 promotes single strand annealing at resected DNA DSBs supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5686642. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686657 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event ERCC1:XPF cleaves flaps generated by SSA supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5686657. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686663 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Completion of SSA supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5686663. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686685 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event RIF1 and PAX1IP bind TP53BP1 at DNA DSBs supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5686685. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5689649 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event BAP1 binds BRCA1:BARD1 supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5689649. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5691411 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event BRCA1-A complex deubiquitinates K63polyUb-histone H2A supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5691411. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693539 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Ligation of DNA and formation of Holliday structures following repair synthesis supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5693539. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693542 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Association of RPA complexes with ssDNA at resected DNA DSBs supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5693542. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693551 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Phosphorylation of BRCA1-A complex at multiple sites by ATM supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5693551. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693561 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event RAD51 binds BRCA2 at resected DNA DSBs supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5693561. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693564 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Association of RAD51 with RAD52:DNA double-strand break ends supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5693564. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693580 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Association of RAD52 with the RPA complex at resected DNA DSBs supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5693580. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693584 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Cleavage of Holliday junctions by GEN1 or SLX1A:SLX4:MUS81:EME1,(MUS81:EME2) supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5693584. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693589 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event D-loop dissociation and strand annealing supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5693589. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693593 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event D-loop extension by DNA polymerases supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5693593. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693608 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Initial resection of double-strand break ends supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5693608. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693620 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event D-loop formation mediated by PALB2, BRCA2 and RAD51 supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-5693620. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6799332 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event ATR phosphorylates TP53 supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-6799332. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-69891 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Phosphorylation and activation of CHEK2 by ATM supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-69891. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9663194 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Some pathogenic BRCA1 mutants do not bind BARD1 supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. The disease-event title does not negate the positive wild-type localization assertion; no NOT qualifier is inferred from it. Source assertion: Reactome:R-HSA-9663194. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9699163 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Defective BARD1 does not bind BRCA1 supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. The disease-event title does not negate the positive wild-type localization assertion; no NOT qualifier is inferred from it. Source assertion: Reactome:R-HSA-9699163. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9700998 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event BAP1 disrupts the BRCA1:BARD1 heterodimer supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-9700998. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9701000 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event BRCA1:BARD1 heterodimer autoubiquitinates supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-9701000. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9701003 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event BAP1 binds BRCA1:BARD1 heterodimer supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-9701003. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9701199 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Defective D-loop formation mediated by PALB2, BRCA2 and RAD51 due to loss-of-function of BRCA1 in PALB2 binding supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. The disease-event title does not negate the positive wild-type localization assertion; no NOT qualifier is inferred from it. Source assertion: Reactome:R-HSA-9701199. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9704330 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Defective D-loop formation mediated by PALB2, BRCA2 and RAD51 due to loss-of-function of PALB2 in BRCA1 binding supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. The disease-event title does not negate the positive wild-type localization assertion; no NOT qualifier is inferred from it. Source assertion: Reactome:R-HSA-9704330. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9704408 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: 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 supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. The disease-event title does not negate the positive wild-type localization assertion; no NOT qualifier is inferred from it. Source assertion: Reactome:R-HSA-9704408. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9707051 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event UBXN1 binds BRCA1:BARD1 heterodimer supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-9707051. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9709571 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event BRCA2 mutants with BRC defects or a defect in the C-terminal RAD51 binding site do not bind RAD51 supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. The disease-event title does not negate the positive wild-type localization assertion; no NOT qualifier is inferred from it. Source assertion: Reactome:R-HSA-9709571. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9709601 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event Defective recruitment of BRCA2 and RAD51 due to loss of BRCA2 function in PALB2 binding supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. The disease-event title does not negate the positive wild-type localization assertion; no NOT qualifier is inferred from it. Source assertion: Reactome:R-HSA-9709601. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9853389 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event FIGNL1 binds RAD51 supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-9853389. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9980006 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event ERCC1:XPF binds DNA DSBs with annealed 3' ssDNA overhangs and displaced flaps generated by SSA supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-9980006. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9980021 | ACCEPT | Summary: BARD1 is localized to the nucleoplasm in the curated repair context. Reason: The Reactome event LIG1 binds SSA sites supplies a nuclear DNA-damage/repair context for the source localization assertion. Retain nucleoplasm as a core location, corroborated by the human nuclear-localization studies. This row asserts location, not that BARD1 performs the event's kinase, nuclease, polymerase, deubiquitinase, or DNA-ligase reaction. Source assertion: Reactome:R-HSA-9980021. |
| GO:0005737 cytoplasm | IDA PMID:15265711 BARD1 regulates BRCA1 apoptotic function by a mechanism invo... | KEEP AS NON CORE | Summary: BARD1 can shuttle through the cytoplasm. Reason: The source and human NLS study support nuclear–cytoplasmic trafficking. Cytoplasmic localization is retained as a non-core context relative to the principal nuclear chromatin-repair function. Source assertion: PMID:15265711. |
| GO:0006281 DNA repair | IBA GO_REF:0000033 | ACCEPT | Summary: BARD1 participates in DNA repair as a conserved BRCA1-complex subunit. Reason: Retain the PAINT ancestral-node inference at PANTHER:PTN008607670. Human heterodimer and chromatin studies support repair participation. A short extant donor list is not a weakness; no complete PAINT alignment or node-placement export was available, so no new clade-placement claim is made. Source assertion: GO_REF:0000033. |
| GO:0006281 DNA repair | NAS PMID:22369660 BRCA1 tumor suppressor network: focusing on its tail. | ACCEPT | Summary: DNA repair is a central function of the BARD1-containing BRCA1 complexes. Reason: The source reviews repair complexes. Independent BARD1 chromatin-recognition and heterodimer evidence support the broad repair function; preserve the NAS provenance and do not infer every enzymatic activity of the associated repair proteins. Source assertion: PMID:22369660. |
| GO:0006282 regulation of DNA repair | NAS PMID:20656689 Differential regulation of JAMM domain deubiquitinating enzy... | ACCEPT | Summary: BARD1-containing complexes regulate DNA repair organization. Reason: Retain the source-assigned regulatory process in the RAP80/BRCA1 assembly context. BARD1's chromatin recognition and complex organization provide functional participation, while the JAMM deubiquitinase reaction studied in the source belongs to BRCC36 rather than BARD1. Source assertion: PMID:20656689. |
| GO:0006338 chromatin remodeling | TAS PMID:35351360 BRCA1/BARD1 is a nucleosome reader and writer. | ACCEPT | Summary: BARD1 contributes directly to repair-associated chromatin modification through the BRCA1–BARD1 histone ubiquitin ligase. Reason: GO:0006338 covers changes to chromatin organization and is not restricted to ATP-dependent nucleosome movement; GO:0140993 histone modifying activity has a part_of relation to GO:0006338. PMID:34321665 directly reconstitutes BRCA1–BARD1-dependent H2A modification and shows how BARD1 positions the complex on the nucleosome. That is a direct chromatin-modifying contribution, rather than a conclusion drawn solely from a downstream requirement for SMARCAD1. The primary paper discusses recruitment of SMARCAD1 by C-terminal H2A ubiquitination using earlier work; it does not make BARD1 an ATP-dependent remodeler. Retain the broad TAS process from PMID:35351360 with this independent primary grounding. Supporting Evidence: PMID:34321665 specific monoubiquitylation of H2A |
| GO:0006357 regulation of transcription by RNA polymerase II | TAS PMID:35351360 BRCA1/BARD1 is a nucleosome reader and writer. | KEEP AS NON CORE | Summary: Transcriptional regulation is a supported context of BRCA1–BARD1 chromatin and RNA-processing activities. Reason: The source review covers transcriptional regulation; PMID:15905410 provides a concrete damage-dependent RNAP II ubiquitination/degradation mechanism. Retain this process as non-core without calling BARD1 a DNA-binding transcription factor or treating every transcriptional effect as direct. Source assertion: PMID:35351360. |
| GO:0006974 DNA damage response | NAS PMID:15905410 BRCA1/BARD1 inhibition of mRNA 3' processing involves target... | ACCEPT | Summary: BRCA1–BARD1 participates in the cellular response to DNA damage. Reason: The source demonstrates a damage-responsive RNAP II ubiquitination/processing pathway involving the heterodimer. Its enzymatic contribution and broader chromatin-repair functions support the damage-response process rather than a necessity-only argument. Source assertion: PMID:15905410. |
| GO:0006974 DNA damage response | NAS PMID:16651405 DNA damage-induced BARD1 phosphorylation is critical for the... | ACCEPT | Summary: BARD1 connects DNA-damage signaling to RNA-processing regulation. Reason: The source reports damage-induced BARD1 phosphorylation and loss of the RNA-processing response with BARD1 phosphosite mutants. Retain the broad DNA-damage response. BARD1 is a regulated substrate and complex subunit in these assays, not the kinase. Source assertion: PMID:16651405. |
| GO:0016567 protein ubiquitination | IEA GO_REF:0000041 | ACCEPT | Summary: BARD1 contributes to protein ubiquitination by the BRCA1 heterodimer. Reason: The UniPathway mapping agrees with direct complex ubiquitination assays. The process spans histone modification, autoubiquitination and other experimentally studied substrates, so no single linkage-specific child replaces the entire assertion. Source assertion: GO_REF:0000041. |
| GO:0016567 protein ubiquitination | NAS PMID:15905410 BRCA1/BARD1 inhibition of mRNA 3' processing involves target... | ACCEPT | Summary: BRCA1–BARD1 ubiquitinates RNAP II in the reported damage-response system. Reason: The source tests RNAP IIO as an in vitro substrate and shows BRCA1/BARD1-dependent RNAP II destabilization after damage. This is an enzymatic contribution to ubiquitination, not merely association with a protein that happens to be ubiquitinated. Source assertion: PMID:15905410. |
| GO:0016607 nuclear speck | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: BARD1 has a curated nuclear-speck localization. Reason: Retain the source immunofluorescence annotation as a non-core subnuclear distribution. It does not establish a constitutive spliceosomal role or make speckles the exclusive location of BARD1. Source assertion: GO_REF:0000052. |
| GO:0019900 kinase binding | NAS PMID:15782130 BARD1 induces apoptosis by catalysing phosphorylation of p53... | KEEP AS NON CORE | Summary: BARD1 associates with a kinase-containing p53 regulatory system. Reason: The source reports BARD1 association with Ku70, a regulatory component of DNA-PK, and p53 phosphorylation. Retain the kinase-binding annotation as a contextual association; the read abstract does not resolve all direct interfaces. BARD1 is not assigned kinase catalysis. Source assertion: PMID:15782130. Supporting Evidence: PMID:15782130 BARD1 binds to Ku-70 |
| GO:0031436 BRCA1-BARD1 complex | IBA GO_REF:0000033 | ACCEPT | Summary: BARD1 is the defining partner in the BRCA1–BARD1 heterodimer. Reason: Retain the PAINT assertion at PANTHER:PTN009083508, consistent with direct human structural evidence. BARD1 itself in the extant WITH/FROM list is legitimate target experimental grounding, not circular evidence. No uninspected ancestral node placement is asserted. Source assertion: GO_REF:0000033. |
| GO:0031436 BRCA1-BARD1 complex | IDA PMID:12890688 The BRCA1/BARD1 heterodimer assembles polyubiquitin chains t... | ACCEPT | Summary: BARD1 is a component of the BRCA1–BARD1 complex. Reason: The source assay concerns the heterodimer, and the independent RING-complex structure establishes direct assembly. Retain complex membership as core; neither a regulator binding the complex nor a particular in vitro substrate changes that identity. Source assertion: PMID:12890688. |
| GO:0031436 BRCA1-BARD1 complex | IDA PMID:15265711 BARD1 regulates BRCA1 apoptotic function by a mechanism invo... | ACCEPT | Summary: BARD1 is a component of the BRCA1–BARD1 complex. Reason: The source assay concerns the heterodimer, and the independent RING-complex structure establishes direct assembly. Retain complex membership as core; neither a regulator binding the complex nor a particular in vitro substrate changes that identity. Source assertion: PMID:15265711. |
| GO:0031436 BRCA1-BARD1 complex | IDA PMID:19117993 BRCA1-associated protein 1 interferes with BRCA1/BARD1 RING ... | ACCEPT | Summary: BARD1 is a component of the BRCA1–BARD1 complex. Reason: The source assay concerns the heterodimer, and the independent RING-complex structure establishes direct assembly. Retain complex membership as core; neither a regulator binding the complex nor a particular in vitro substrate changes that identity. Source assertion: PMID:19117993. |
| GO:0031436 BRCA1-BARD1 complex | IDA PMID:20351172 The UBXN1 protein associates with autoubiquitinated forms of... | ACCEPT | Summary: BARD1 is a component of the BRCA1–BARD1 complex. Reason: The source assay concerns the heterodimer, and the independent RING-complex structure establishes direct assembly. Retain complex membership as core; neither a regulator binding the complex nor a particular in vitro substrate changes that identity. Source assertion: PMID:20351172. |
| GO:0031436 BRCA1-BARD1 complex | IPI PMID:11573085 Structure of a BRCA1-BARD1 heterodimeric RING-RING complex. | ACCEPT | Summary: BARD1 is a component of the BRCA1–BARD1 complex. Reason: The source assay concerns the heterodimer, and the independent RING-complex structure establishes direct assembly. Retain complex membership as core; neither a regulator binding the complex nor a particular in vitro substrate changes that identity. Source assertion: PMID:11573085. |
| GO:0031441 negative regulation of mRNA 3'-end processing | NAS PMID:15905410 BRCA1/BARD1 inhibition of mRNA 3' processing involves target... | KEEP AS NON CORE | Summary: BARD1 inhibits pre-mRNA 3′ processing in the damage-response setting. Reason: The source couples BRCA1–BARD1-dependent RNAP II degradation to reduced 3′ cleavage. The earlier CstF-50 study also reports direct inhibition of polyadenylation. Retain a supported regulatory contribution as non-core; BARD1 is not the cleavage or polyadenylation enzyme. Source assertion: PMID:15905410. Supporting Evidence: PMID:15905410 inhibition of 3′ cleavage induced by DNA damage |
| GO:0035825 homologous recombination | NAS PMID:22369660 BRCA1 tumor suppressor network: focusing on its tail. | ACCEPT | Summary: BARD1 participates in homology-directed DNA double-strand-break repair. Reason: BRCA1–BARD1 complex formation and BARD1 nucleosome recognition are central to homologous repair. Retain the source NAS assertion with independent human chromatin evidence. The source paper's focus on other repair components does not by itself establish a misattribution; no BARD1-specific assay is invented from its abstract. Source assertion: PMID:22369660. |
| GO:0035825 homologous recombination | NAS PMID:30657944 CtIP-BRCA1 complex and MRE11 maintain replication forks in t... | ACCEPT | Summary: BARD1 participates in homology-directed DNA double-strand-break repair. Reason: BRCA1–BARD1 complex formation and BARD1 nucleosome recognition are central to homologous repair. Retain the source NAS assertion with independent human chromatin evidence. The source paper's focus on other repair components does not by itself establish a misattribution; no BARD1-specific assay is invented from its abstract. Source assertion: PMID:30657944. |
| GO:0042325 regulation of phosphorylation | IMP PMID:15782130 BARD1 induces apoptosis by catalysing phosphorylation of p53... | KEEP AS NON CORE | Summary: BARD1 modulates p53 phosphorylation in the reported apoptosis pathway. Reason: The source describes BARD1 association with p53 and Ku70 and increased p53 phosphorylation. This supports regulatory participation in that cellular context, not an intrinsic BARD1 protein-kinase reaction or a general phosphorylation core. Source assertion: PMID:15782130. |
| GO:0042803 protein homodimerization activity | IPI PMID:15265711 BARD1 regulates BRCA1 apoptotic function by a mechanism invo... | KEEP AS NON CORE | Summary: BARD1 can homodimerize under tested conditions. Reason: Retain the source self-interaction and the earlier RING-region homodimer observations. The principal chromatin-repair species is the BRCA1–BARD1 heterodimer; homodimer formation in constructs does not establish that a BARD1 homodimer carries the heterodimer's repair functions. Source assertion: PMID:15265711. |
| GO:0043065 positive regulation of apoptotic process | IMP PMID:15782130 BARD1 induces apoptosis by catalysing phosphorylation of p53... | KEEP AS NON CORE | Summary: BARD1 can promote p53-associated apoptosis in the tested cellular systems. Reason: The source supports a proapoptotic pathway involving p53 stabilization/phosphorylation. Keep this context-dependent survival outcome as non-core. It does not contradict an antiapoptotic effect in a distinct BRCA1-retention assay. Source assertion: PMID:15782130. |
| GO:0043066 negative regulation of apoptotic process | IMP PMID:15265711 BARD1 regulates BRCA1 apoptotic function by a mechanism invo... | KEEP AS NON CORE | Summary: BARD1 can suppress BRCA1-dependent apoptosis by nuclear retention. Reason: The source explicitly reports reduced BRCA1-driven apoptosis in transfected MCF-7 cells and increased apoptosis after disrupting the interaction. Retain the condition-specific antiapoptotic role as non-core; do not merge it with the distinct p53/Ku70 mechanism in PMID:15782130. Source assertion: PMID:15265711. Supporting Evidence: PMID:15265711 BARD1 reduced BRCA1-dependent apoptosis |
| GO:0044818 mitotic G2/M transition checkpoint | NAS PMID:22369660 BRCA1 tumor suppressor network: focusing on its tail. | KEEP AS NON CORE | Summary: BARD1-containing repair assemblies contribute to the G2/M damage checkpoint. Reason: Retain the checkpoint role summarized by the source, supported by the direct BRCA1/BARD1 complex study. The checkpoint is a cellular response mediated by multiple proteins rather than an autonomous BARD1 catalytic function. Source assertion: PMID:22369660. |
| GO:0045732 positive regulation of protein catabolic process | NAS PMID:15905410 BRCA1/BARD1 inhibition of mRNA 3' processing involves target... | KEEP AS NON CORE | Summary: BRCA1–BARD1 promotes RNAP II degradation following DNA damage. Reason: The source links ubiquitination and proteasomal loss of RNAP II to the heterodimer. Retain this specific non-core substrate-degradation context. It is not a universal consequence of BRCA1–BARD1 ubiquitination: for example, NPM1 was stabilized in PMID:15184379. Source assertion: PMID:15905410. |
| GO:0045786 negative regulation of cell cycle | NAS PMID:15159397 BRCA1-BARD1 complexes are required for p53Ser-15 phosphoryla... | KEEP AS NON CORE | Summary: BARD1 supports damage-dependent G1/S arrest. Reason: The source reports BRCA1/BARD1-dependent p53 Ser15 phosphorylation and p21 induction after ionizing radiation, with different responses to UV. Retain the condition-specific checkpoint consequence as non-core rather than equating BARD1 with the cell-cycle kinases. Source assertion: PMID:15159397. |
| GO:0046826 negative regulation of protein export from nucleus | IDA PMID:15265711 BARD1 regulates BRCA1 apoptotic function by a mechanism invo... | KEEP AS NON CORE | Summary: BARD1 can retain BRCA1 in the nucleus. Reason: The source directly links BRCA1–BARD1 interaction to BRCA1 nuclear retention. Preserve this substrate-specific trafficking regulation as non-core, without interpreting it as general inhibition of all protein export. Source assertion: PMID:15265711. |
| GO:0046982 protein heterodimerization activity | IPI PMID:15265711 BARD1 regulates BRCA1 apoptotic function by a mechanism invo... | ACCEPT | Summary: BARD1 heterodimerizes with BRCA1. Reason: The source interaction and independent structure support the specific functional heterodimer, which is central to BARD1 complex activity. Source assertion: PMID:15265711. |
| GO:0051726 regulation of cell cycle | NAS PMID:15632137 Nuclear targeting and cell cycle regulatory function of huma... | KEEP AS NON CORE | Summary: Nuclear BARD1 can alter cell-cycle progression. Reason: The source reports G1 arrest after transient expression of human BARD1 and dependence on its NLS. Retain this experimental cell-cycle phenotype as non-core; the assay does not establish that every endogenous BARD1 role is a cell-cycle arrest program. Source assertion: PMID:15632137. |
| GO:0061630 ubiquitin protein ligase activity | IBA GO_REF:0000033 | ACCEPT | Summary: BARD1 contributes to conserved E3 ubiquitin ligase activity. Reason: The PAINT inference at PANTHER:PTN008607670 is supported by human heterodimer biochemistry. Retain the ancestral function without using donor count as a confidence surrogate or inventing the unread family-tree placement. The catalytic claim is interpreted for the BRCA1–BARD1 complex. Source assertion: GO_REF:0000033. |
| GO:0061630 ubiquitin protein ligase activity | IEA GO_REF:0000003 | ACCEPT | Summary: The EC mapping captures the ubiquitin ligase contribution of BARD1. Reason: Direct assays support E3 activity of the BRCA1–BARD1 heterodimer. The EC-based assertion is retained as a complex contribution, with BRCA1 providing the demonstrated E2-binding interface; it is not evidence for an isolated BARD1 enzyme. Source assertion: GO_REF:0000003. |
| GO:0061649 ubiquitin-modified histone reader activity | TAS PMID:35351360 BRCA1/BARD1 is a nucleosome reader and writer. | ACCEPT | Summary: BARD1 recognizes ubiquitin-modified histones at damaged chromatin. Reason: The source reviews BARD1 nucleosome reading; primary structural and binding evidence resolves recognition of N-terminal H2A ubiquitin together with H4K20 state. This is distinct from the C-terminal H2A ubiquitination produced by the BRCA1–BARD1 ligase. Source assertion: PMID:35351360. |
| GO:0070531 BRCA1-A complex | IDA PMID:17525342 Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA... | ACCEPT | Summary: BARD1 is present in the BRCA1-A repair assembly. Reason: Retain the curated complex-membership assertion, independently corroborated by the source description of BRCA1/BARD1, Abraxas, RAP80, BRCC36, BRE and NBA1. This does not assign RAP80's ubiquitin binding or BRCC36's deubiquitinase chemistry to BARD1. Source assertion: PMID:17525342. |
| GO:0070531 BRCA1-A complex | IDA PMID:19261748 MERIT40 facilitates BRCA1 localization and DNA damage repair... | ACCEPT | Summary: BARD1 is present in the BRCA1-A repair assembly. Reason: Retain the curated complex-membership assertion, independently corroborated by the source description of BRCA1/BARD1, Abraxas, RAP80, BRCC36, BRE and NBA1. This does not assign RAP80's ubiquitin binding or BRCC36's deubiquitinase chemistry to BARD1. Source assertion: PMID:19261748. |
| GO:0070531 BRCA1-A complex | IDA PMID:19261749 NBA1, a new player in the Brca1 A complex, is required for D... | ACCEPT | Summary: BARD1 is present in the BRCA1-A repair assembly. Reason: Retain the curated complex-membership assertion, independently corroborated by the source description of BRCA1/BARD1, Abraxas, RAP80, BRCC36, BRE and NBA1. This does not assign RAP80's ubiquitin binding or BRCC36's deubiquitinase chemistry to BARD1. Source assertion: PMID:19261749. |
| GO:0070531 BRCA1-A complex | NAS PMID:20656689 Differential regulation of JAMM domain deubiquitinating enzy... | ACCEPT | Summary: BARD1 is present in the BRCA1-A repair assembly. Reason: Retain the curated complex-membership assertion, independently corroborated by the source description of BRCA1/BARD1, Abraxas, RAP80, BRCC36, BRE and NBA1. This does not assign RAP80's ubiquitin binding or BRCC36's deubiquitinase chemistry to BARD1. Source assertion: PMID:20656689. |
| GO:0070532 BRCA1-B complex | IBA GO_REF:0000033 | ACCEPT | Summary: BARD1 is a constituent of the BRCA1-B repair assembly. Reason: The direct BRCA1/BARD1 complex study supports distinct damage-responsive assemblies involving TopBP1 or MRN-associated machinery. Retain the BRCA1-B membership without transferring the catalytic activities of its partners to BARD1. Preserve the PAINT PANTHER:PTN009083508 inference; target BARD1 in the donor list is not circular, and the complete ancestral-tree placement was not re-evaluated. Source assertion: GO_REF:0000033. |
| GO:0070532 BRCA1-B complex | IPI PMID:16391231 Multifactorial contributions to an acute DNA damage response... | ACCEPT | Summary: BARD1 is a constituent of the BRCA1-B repair assembly. Reason: The direct BRCA1/BARD1 complex study supports distinct damage-responsive assemblies involving TopBP1 or MRN-associated machinery. Retain the BRCA1-B membership without transferring the catalytic activities of its partners to BARD1. Source assertion: PMID:16391231. Supporting Evidence: PMID:16391231 Two distinct DNA damage-dependent super complexes emerged |
| GO:0070533 BRCA1-C complex | IBA GO_REF:0000033 | ACCEPT | Summary: BARD1 is a constituent of the BRCA1-C repair assembly. Reason: The direct BRCA1/BARD1 complex study supports distinct damage-responsive assemblies involving TopBP1 or MRN-associated machinery. Retain the BRCA1-C membership without transferring the catalytic activities of its partners to BARD1. Preserve the PAINT PANTHER:PTN009083508 inference; target BARD1 in the donor list is not circular, and the complete ancestral-tree placement was not re-evaluated. Source assertion: GO_REF:0000033. |
| GO:0070533 BRCA1-C complex | IPI PMID:16391231 Multifactorial contributions to an acute DNA damage response... | ACCEPT | Summary: BARD1 is a constituent of the BRCA1-C repair assembly. Reason: The direct BRCA1/BARD1 complex study supports distinct damage-responsive assemblies involving TopBP1 or MRN-associated machinery. Retain the BRCA1-C membership without transferring the catalytic activities of its partners to BARD1. Source assertion: PMID:16391231. |
| GO:0071479 cellular response to ionizing radiation | IMP PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | ACCEPT | Summary: BARD1 participates in the response to ionizing-radiation damage. Reason: Retain the curated experimental response in the BRCC context. The source abstract emphasizes depletion of BRCC36/BRCC45, so it is not presented as a complete BARD1 perturbation read. Independent BRCA1/BARD1 damage-response and checkpoint work corroborates BARD1 participation. Source assertion: PMID:14636569. |
| GO:0085020 protein K6-linked ubiquitination | IDA PMID:12890688 The BRCA1/BARD1 heterodimer assembles polyubiquitin chains t... | ACCEPT | Summary: BRCA1–BARD1 can assemble K6-linked ubiquitin chains. Reason: Retain the linkage-specific activity demonstrated for the heterodimer in the cited system. K6 is not an exclusive linkage under every E2/substrate condition: PMID:17873885 shows that alternative E2s can support other linkages. This annotation does not equate all K6 modification with proteasomal degradation. Source assertion: PMID:12890688. Supporting Evidence: PMID:12890688 unconventional linkage involving lysine residue K6 |
| GO:0085020 protein K6-linked ubiquitination | IDA PMID:20351172 The UBXN1 protein associates with autoubiquitinated forms of... | ACCEPT | Summary: BRCA1–BARD1 can assemble K6-linked ubiquitin chains. Reason: Retain the linkage-specific activity demonstrated for the heterodimer in the cited system. K6 is not an exclusive linkage under every E2/substrate condition: PMID:17873885 shows that alternative E2s can support other linkages. This annotation does not equate all K6 modification with proteasomal degradation. Source assertion: PMID:20351172. |
| GO:0110025 DNA strand resection involved in replication fork processing | NAS PMID:29709199 The MRE11-RAD50-NBS1 Complex Conducts the Orchestration of D... | UNDECIDED | Summary: BARD1-specific DNA resection during replication-fork processing remains unresolved for this source. Reason: GO:0110025 specifically concerns resection at a stalled replication fork. The canonical PMID:29709199 record contains its abstract and Introduction despite its full-text flag. Separately inspected passages in the longer recovered normal record include every BARD1 mention and the complete MRN fork-dynamics section: the BARD1 passage concerns RAD51 stimulation during homologous repair, whereas fork resection and its restraint are discussed for MRN, BRCA2/RAD51 and other factors. This bounded reading does not identify the direct BARD1 support underlying the narrow NAS assertion. Fork protection in PMID:31270457 and DSB-end resection in PMID:39261729 do not by themselves resolve it. Retain UNDECIDED because the specific evidence remains unadjudicated; absence from the inspected passages is not proof of a false annotation. |
| GO:0140863 histone H2AK127 ubiquitin ligase activity | TAS PMID:35351360 BRCA1/BARD1 is a nucleosome reader and writer. | ACCEPT | Summary: BARD1 contributes to histone H2A K127 ubiquitination by BRCA1–BARD1. Reason: The review and primary nucleosome study support BRCA1–BARD1 modification of the H2A C-terminal lysines. Retain this complex contribution. BARD1 positions the nucleosome while BRCA1 engages the E2; recognition of RNF168-generated N-terminal H2A ubiquitin is a different molecular role. Source assertion: PMID:35351360. |
| GO:0140864 histone H2AK129 ubiquitin ligase activity | TAS PMID:35351360 BRCA1/BARD1 is a nucleosome reader and writer. | ACCEPT | Summary: BARD1 contributes to histone H2A K129 ubiquitination by BRCA1–BARD1. Reason: The review and primary nucleosome study support BRCA1–BARD1 modification of the H2A C-terminal lysines. Retain this complex contribution. BARD1 positions the nucleosome while BRCA1 engages the E2; recognition of RNF168-generated N-terminal H2A ubiquitin is a different molecular role. Source assertion: PMID:35351360. |
| GO:2000001 regulation of DNA damage checkpoint | NAS PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | KEEP AS NON CORE | Summary: BARD1-containing assemblies regulate the DNA-damage checkpoint. Reason: The source links the larger BRCC complex to damage survival and G2/M control. Retain checkpoint regulation as a non-core cellular consequence of repair-complex function; the read abstract's BRCC36/BRCC45 perturbations do not alone establish a new BARD1-specific experiment. Source assertion: PMID:14636569. |
| GO:0120230 recombinase activator activity | IDA PMID:28976962 BRCA1-BARD1 promotes RAD51-mediated homologous DNA pairing. | NEW | Summary: BARD1 contributes to BRCA1–BARD1-mediated activation of RAD51. Reason: Purified BRCA1–BARD1 stimulates RAD51-dependent synaptic complex formation and DNA strand invasion. BARD1 RAD51-contact mutants retain DNA binding but lose efficient RAD51 interaction and stimulation; complementary BRCA1 mutants also impair the activity. This establishes a complex-contributed recombinase activator function, rather than autonomous strand-exchange catalysis by BARD1. The existing DNA-binding and homologous-recombination annotations do not capture this molecular activity. Supporting Evidence: PMID:28976962 BRCA1-BARD1 enhances the recombinase activity of RAD51. |
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Q: What primary BARD1-specific evidence supports replication-fork resection beyond its established homologous-recombination and double-strand-break end-resection functions?
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