Brca1 encodes the mouse homolog of BRCA1, a nuclear genome-maintenance protein. Its primary roles are as a BARD1-associated RING E3 ubiquitin ligase and as a DNA-damage response scaffold that promotes homologous recombination, DNA end resection, repair-checkpoint control, and replication-associated genome stability. Transcriptional, metabolic, centrosomal, and developmental annotations are interpreted as secondary contexts unless directly tied to DNA repair or BRCA1-BARD1 ubiquitin ligase activity.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000724 double-strand break repair via homologous recombination | IBA GO_REF:0000033 | ACCEPT | Summary: BRCA1-BARD1 channels DSB repair toward homologous recombination by promoting end resection and PALB2-BRCA2-RAD51 loading at resected breaks. Reason: Central, defining biological role of BRCA1; broadly supported (IBA/ISO and mechanistic literature). Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0007095 mitotic G2 DNA damage checkpoint signaling | IBA GO_REF:0000033 | ACCEPT | Summary: BRCA1 signals the G2 DNA-damage checkpoint, with BRCA1-mediated RBBP8 ubiquitination regulating CHEK1 activation after damage. Reason: Core checkpoint role tied to BRCA1's repair function; IBA/ISO support. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0004842 ubiquitin-protein transferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Core catalytic activity: BRCA1, as the BRCA1-BARD1 RING heterodimer, accelerates ubiquitin transfer from charged E2~Ub onto substrate lysines (e.g. nucleosomal H2A, CtIP, PCNA) at sites of DNA damage. Reason: Defining molecular function of BRCA1 (EC 2.3.2.27); supported across IBA/ISO/ISS and the BRCA1-BARD1 mechanistic literature. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0031436 BRCA1-BARD1 complex | IBA GO_REF:0000033 | ACCEPT | Summary: Obligate RING-RING heterodimer with BARD1 that constitutes the active E3 ligase; this assembly underlies essentially all BRCA1 catalytic and DNA-repair functions. Reason: Defining functional complex of BRCA1; documented in SUBUNIT and the core mechanistic literature. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0043009 chordate embryonic development | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Brca1 is required for embryonic development, with knockouts being embryonic lethal owing to defective proliferation and genome instability. Reason: Developmental phenotype downstream of BRCA1's essential genome-maintenance role. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Acts as a transcriptional activator at specific target genes, a regulatory output separable from its repair function. Reason: Activator role pleiotropic relative to core repair function. |
| GO:0070531 BRCA1-A complex | IBA GO_REF:0000033 | ACCEPT | Summary: Component of the BRCA1-A complex (with RAP80/UIMC1, ABRAXAS1, BRCC36, BABAM1/2) that recognizes K63-ubiquitin chains and recruits BRCA1 to DNA double-strand-break sites. Reason: Bona fide repair-targeting complex central to BRCA1 recruitment; supported by SUBUNIT and IBA/ISO. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0003677 DNA binding | IEA GO_REF:0000120 | MARK AS OVER ANNOTATED | Summary: Generic DNA-binding term; BRCA1 acts on damaged chromatin via complexes rather than as a sequence-specific DNA binder, so the bare term over-states a direct activity. Reason: Broad IEA MF; BRCA1's chromatin/damage engagement is captured by more specific terms. |
| GO:0004842 ubiquitin-protein transferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Core catalytic activity: BRCA1, as the BRCA1-BARD1 RING heterodimer, accelerates ubiquitin transfer from charged E2~Ub onto substrate lysines (e.g. nucleosomal H2A, CtIP, PCNA) at sites of DNA damage. Reason: Defining molecular function of BRCA1 (EC 2.3.2.27); supported across IBA/ISO/ISS and the BRCA1-BARD1 mechanistic literature. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: BRCA1 acts predominantly in the nucleus, forming DNA-damage-induced foci on chromatin where it carries out repair and checkpoint functions. Reason: Primary site of BRCA1 action; UniProt SUBCELLULAR LOCATION and IDA support. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0005694 chromosome | IEA GO_REF:0000044 | ACCEPT | Summary: BRCA1 localizes to chromosomes/chromatin, where the BRCA1-BARD1 ligase modifies nucleosomal H2A at break sites. Reason: Direct chromatin association is core to BRCA1 function; IDA supported. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Cytoplasmic pool seen e.g. on translocation during UV-induced apoptosis and ACACA binding; not the principal site of repair function. Reason: Secondary localization; BRCA1 acts mainly in the nucleus. |
| GO:0006281 DNA repair | IEA GO_REF:0000120 | ACCEPT | Summary: BRCA1 facilitates cellular responses to DNA damage and is required for FANCD2 targeting and homology-directed repair, maintaining genome integrity. Reason: Core function captured directly in UniProt FUNCTION. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0006310 DNA recombination | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: Broad recombination term encompassing BRCA1's HR role; the specific homologous-recombination/DSB terms capture the core activity more precisely. Reason: General parent process; specific HR terms are the core annotations. |
| GO:0006351 DNA-templated transcription | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: Participation in DNA-templated transcription, reflecting BRCA1's accessory transcriptional roles rather than its repair core. Reason: Broad transcription process not tied to the core repair function. |
| GO:0006629 lipid metabolic process | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: General lipid-metabolism involvement stemming from BRCA1's inhibition of ACACA-driven lipogenesis. Reason: Very broad metabolic term secondary to the ACACA moonlighting role. |
| GO:0006631 fatty acid metabolic process | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: Broadly impinges on fatty-acid metabolism via ACACA regulation, a moonlighting metabolic role. Reason: Broad metabolic term downstream of the ACACA-binding role. |
| GO:0006633 fatty acid biosynthetic process | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: Influences fatty-acid biosynthesis through its inhibitory ACACA interaction, a metabolic role peripheral to genome maintenance. Reason: Metabolic-pathway association secondary to core function. |
| GO:0006974 DNA damage response | IEA GO_REF:0000120 | ACCEPT | Summary: BRCA1 coordinates the DNA-damage response, being phosphorylated by ATM/ATR and assembling repair/checkpoint complexes at break sites. Reason: Core DDR role; IMP-supported and central to BRCA1 biology. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0008270 zinc ion binding | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Zinc coordination by the N-terminal RING-type finger that structurally enables BARD1 heterodimerization and E3 activity. Reason: Structural cofactor binding underpinning, but not equivalent to, the core ligase MF. |
| GO:0016740 transferase activity | IEA GO_REF:0000043 | MODIFY | Summary: Generic transferase parent; BRCA1's actual activity is the specific RING-type ubiquitin-protein transferase function of the BRCA1-BARD1 heterodimer. Reason: IEA parent term too broad; replace with the specific ubiquitin-protein transferase activity child. Proposed replacements: ubiquitin-protein transferase activity |
| GO:0046872 metal ion binding | IEA GO_REF:0000120 | MARK AS OVER ANNOTATED | Summary: Generic metal-binding rollup of the RING zinc-coordination; the functionally meaningful aspect is the RING E3 activity, not metal binding per se. Reason: Keyword-derived broad MF superseded by the specific ligase and zinc-finger terms. |
| GO:0061630 ubiquitin protein ligase activity | IEA GO_REF:0000003 | ACCEPT | Summary: BRCA1-BARD1 RING E3 ligase activity that promotes site-specific (mono)ubiquitination and K6-linked autoubiquitination, coupling enzymatic output to DNA-damage repair pathway choice. Reason: Synonymous core E3-ligase MF; mechanistically established for the BRCA1-BARD1 heterodimer. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0070013 intracellular organelle lumen | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: Very broad luminal compartment term that adds nothing beyond the specific nuclear/nucleoplasm localizations. Reason: Over-broad CC superseded by nucleus/nucleoplasm. |
| GO:0000724 double-strand break repair via homologous recombination | IEA GO_REF:0000107 | ACCEPT | Summary: BRCA1-BARD1 channels DSB repair toward homologous recombination by promoting end resection and PALB2-BRCA2-RAD51 loading at resected breaks. Reason: Central, defining biological role of BRCA1; broadly supported (IBA/ISO and mechanistic literature). Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0000800 lateral element | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Meiotic synaptonemal-complex lateral-element localization tied to BRCA1's role in meiotic chromosome surveillance. Reason: Meiosis-specific localization, a specialized context of genome maintenance. |
| GO:0000976 transcription cis-regulatory region binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Binds cis-regulatory regions consistent with BRCA1's transcriptional-regulation activities at target promoters. Reason: Transcription-associated DNA binding, secondary to repair role. |
| GO:0002039 p53 binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Specific binding assertion that, alone, captures a partnership rather than a BRCA1 molecular function and is electronic-only here. Reason: Uninformative bare-binding MF; any p53-linked role is downstream and not the core function. |
| GO:0003713 transcription coactivator activity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BRCA1 can act as a transcriptional coactivator, a regulatory role secondary to and intertwined with its genome-maintenance function. Reason: Transcription role not the core repair/ligase function; keep as non-core. |
| GO:0003723 RNA binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Reported RNA-binding activity linked to transcription-coupled and RNA-associated functions rather than the core E3/repair role. Reason: Ancillary nucleic-acid binding; not the defining function. |
| GO:0005654 nucleoplasm | IEA GO_REF:0000107 | ACCEPT | Summary: Nucleoplasmic localization consistent with BRCA1's soluble nuclear and chromatin-associated repair/checkpoint activities. Reason: Standard nuclear sublocation for BRCA1; TAS/Reactome supported, do not remove an experimentally consistent site. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0005886 plasma membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Minor plasma-membrane-associated pool reported electronically; peripheral to BRCA1's nuclear repair activity. Reason: Non-core secondary localization with electronic support only. |
| GO:0006301 DNA damage tolerance | IEA GO_REF:0000107 | ACCEPT | Summary: Via BRCA1-BARD1 ubiquitination of PCNA in unperturbed conditions, BRCA1 supports continuous DNA synthesis and suppresses ssDNA-gap accumulation, aiding tolerance of replication stress. Reason: Supported by recent PCNA-ubiquitination/fork-protection findings tied to BRCA1's E3 activity. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0006302 double-strand break repair | IEA GO_REF:0000107 | ACCEPT | Summary: BRCA1 is a key effector of double-strand-break repair, biasing pathway choice away from NHEJ via H2A ubiquitination and 53BP1 repositioning. Reason: Core DSB-repair role; IMP plus electronic support. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0006357 regulation of transcription by RNA polymerase II | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Regulates Pol II transcription through coactivator and partner (LMO4/CCAR2) interactions, a pleiotropic role beyond DNA repair. Reason: Transcriptional regulation secondary to BRCA1's core repair/ligase role. |
| GO:0007059 chromosome segregation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Supports faithful chromosome segregation, a downstream consequence of BRCA1-maintained genome integrity and checkpoint control. Reason: Mitotic-fidelity outcome downstream of the core repair/checkpoint role. |
| GO:0007095 mitotic G2 DNA damage checkpoint signaling | IEA GO_REF:0000107 | ACCEPT | Summary: BRCA1 signals the G2 DNA-damage checkpoint, with BRCA1-mediated RBBP8 ubiquitination regulating CHEK1 activation after damage. Reason: Core checkpoint role tied to BRCA1's repair function; IBA/ISO support. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0010212 response to ionizing radiation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Responds to ionizing radiation as part of damage signaling, an upstream stimulus context of the repair function. Reason: Response-to-stimulus term contextual to the core DDR role. |
| GO:0010575 positive regulation of vascular endothelial growth factor production | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Linked to upregulating VEGF production, a downstream gene-expression output rather than a core activity. Reason: Growth-factor-production role pleiotropic to core function. |
| GO:0010628 positive regulation of gene expression | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Broadly upregulates expression of target genes via its transcriptional-activator activity. Reason: Generic expression-regulation role downstream of transcription activity. |
| GO:0016567 protein ubiquitination | IEA GO_REF:0000120 | ACCEPT | Summary: BRCA1-BARD1 mediates protein ubiquitination of chromatin and repair substrates as its central biochemical activity. Reason: Core ubiquitination function; the specific K6/autoubiquitination children are also annotated. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0016604 nuclear body | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Localization to nuclear bodies, a sub-nuclear focus consistent with damage-induced assembly but not itself a defining site. Reason: Sub-nuclear localization secondary to the core nuclear/chromatin sites. |
| GO:0019899 enzyme binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Non-specific enzyme-binding term that conveys nothing about which enzyme or what BRCA1 does with it. Reason: Uninformative binding MF; specific partner roles are captured elsewhere. |
| GO:0030308 negative regulation of cell growth | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Tumor-suppressor-associated growth restraint, a downstream physiological consequence of intact BRCA1 genome maintenance. Reason: Growth-suppression phenotype downstream of the core repair role. |
| GO:0031436 BRCA1-BARD1 complex | IEA GO_REF:0000107 | ACCEPT | Summary: Obligate RING-RING heterodimer with BARD1 that constitutes the active E3 ligase; this assembly underlies essentially all BRCA1 catalytic and DNA-repair functions. Reason: Defining functional complex of BRCA1; documented in SUBUNIT and the core mechanistic literature. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0031625 ubiquitin protein ligase binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Generic 'binds an E3 ligase' term that is uninformative for a protein that is itself the E3 ligase. Reason: Bare-binding MF adding no functional specificity beyond BRCA1's own catalytic terms. |
| GO:0032991 protein-containing complex | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Root-level complex term superseded by the specific BRCA1-BARD1 and BRCA1-A/B/C complex annotations. Reason: Uninformative generic CC; specific complexes are annotated. |
| GO:0033147 negative regulation of intracellular estrogen receptor signaling pathway | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Represses estrogen-receptor signaling, a hormone-pathway regulatory role pertinent to mammary biology but secondary to repair. Reason: Hormone-signaling regulation pleiotropic to core function. |
| GO:0042802 identical protein binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Generic self-association term that does not capture BRCA1's heterodimeric-with-BARD1 mode of action or any specific function. Reason: Uninformative bare-binding MF; BRCA1's functional partnerships are captured by specific complex terms. |
| GO:0045717 negative regulation of fatty acid biosynthetic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Inhibits fatty-acid synthesis by binding inactive phosphorylated ACACA and preventing its dephosphorylation, a distinct metabolic moonlighting role. Reason: Specific lipid-regulatory function via ACACA, separate from the core repair role. |
| GO:0045739 positive regulation of DNA repair | IEA GO_REF:0000107 | ACCEPT | Summary: BRCA1 positively promotes homology-directed DNA repair by enabling resection and RAD51 loading at damage sites. Reason: Core pro-repair activity; consistent with FUNCTION. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0045766 positive regulation of angiogenesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Reported promotion of angiogenesis, a tissue-level role far downstream of BRCA1's molecular repair function. Reason: Angiogenic role pleiotropic and electronic-only. |
| GO:0045892 negative regulation of DNA-templated transcription | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Can repress transcription at certain targets (e.g. via LMO4/CCAR2-modulated activity), a context-specific regulatory role. Reason: Transcriptional repression not part of the core repair function. |
| GO:0045893 positive regulation of DNA-templated transcription | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Promotes transcription of subsets of target genes as a transcriptional activator, secondary to genome-maintenance roles. Reason: Activator output pleiotropic relative to core function. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Acts as a transcriptional activator at specific target genes, a regulatory output separable from its repair function. Reason: Activator role pleiotropic relative to core repair function. |
| GO:0051865 protein autoubiquitination | IEA GO_REF:0000107 | ACCEPT | Summary: BRCA1 undergoes K6-linked autoubiquitination that does not promote degradation, reflecting its intrinsic E3 ligase activity. Reason: Documented BRCA1 PTM/activity; core to its enzymatic characterization. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0070063 RNA polymerase binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Associates with the RNA polymerase II holoenzyme (via DHX9), underpinning BRCA1's transcriptional-regulation activity. Reason: Transcription-machinery interaction secondary to repair/ligase function. |
| GO:0070531 BRCA1-A complex | IEA GO_REF:0000107 | ACCEPT | Summary: Component of the BRCA1-A complex (with RAP80/UIMC1, ABRAXAS1, BRCC36, BABAM1/2) that recognizes K63-ubiquitin chains and recruits BRCA1 to DNA double-strand-break sites. Reason: Bona fide repair-targeting complex central to BRCA1 recruitment; supported by SUBUNIT and IBA/ISO. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0071356 cellular response to tumor necrosis factor | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Participates in the cellular response to TNF, a signaling-context role distinct from BRCA1's repair catalysis. Reason: Cytokine-response context, not the core function. |
| GO:0071479 cellular response to ionizing radiation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mediates the cellular response to ionizing radiation, with BRCA1 phosphorylated and required for IR-induced S/G2 arrest. Reason: Stress-response context of BRCA1's core DDR/checkpoint role. |
| GO:0071681 cellular response to indole-3-methanol | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Reported response to indole-3-methanol, a chemical-stimulus context secondary to BRCA1's core activities. Reason: Specific chemical-response context, non-core. |
| GO:0085020 protein K6-linked ubiquitination | IEA GO_REF:0000107 | ACCEPT | Summary: BRCA1-BARD1 specifically catalyzes 'Lys-6'-linked polyubiquitin chains, a hallmark non-degradative linkage of this E3 ligase. Reason: Signature catalytic output of BRCA1 stated explicitly in UniProt FUNCTION/PTM. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:1902042 negative regulation of extrinsic apoptotic signaling pathway via death domain receptors | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Modulates death-receptor extrinsic apoptotic signaling, a cell-fate role separable from direct repair catalysis. Reason: Apoptosis-modulation role pleiotropic to core function. |
| GO:1990904 ribonucleoprotein complex | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Association with RNP/RNA-containing complexes linked to BRCA1's reported RNA binding and transcription-coupled roles. Reason: Peripheral complex membership downstream of transcription-associated activity. |
| GO:2000378 negative regulation of reactive oxygen species metabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Limits ROS accumulation, an antioxidant/redox-protective role downstream of BRCA1-maintained genome and metabolic homeostasis. Reason: Redox-regulation role pleiotropic to the core repair function. |
| GO:0005634 nucleus | ISO GO_REF:0000119 | ACCEPT | Summary: BRCA1 acts predominantly in the nucleus, forming DNA-damage-induced foci on chromatin where it carries out repair and checkpoint functions. Reason: Primary site of BRCA1 action; UniProt SUBCELLULAR LOCATION and IDA support. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0000152 nuclear ubiquitin ligase complex | ISO GO_REF:0000119 | ACCEPT | Summary: BRCA1-BARD1 constitutes a nuclear ubiquitin ligase complex that ubiquitinates chromatin and repair-factor substrates at damage sites. Reason: Accurately captures the nuclear E3-ligase nature of the BRCA1-BARD1 heterodimer. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0000724 double-strand break repair via homologous recombination | ISO GO_REF:0000119 | ACCEPT | Summary: BRCA1-BARD1 channels DSB repair toward homologous recombination by promoting end resection and PALB2-BRCA2-RAD51 loading at resected breaks. Reason: Central, defining biological role of BRCA1; broadly supported (IBA/ISO and mechanistic literature). Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0000976 transcription cis-regulatory region binding | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Binds cis-regulatory regions consistent with BRCA1's transcriptional-regulation activities at target promoters. Reason: Transcription-associated DNA binding, secondary to repair role. |
| GO:0002039 p53 binding | ISO GO_REF:0000119 | MARK AS OVER ANNOTATED | Summary: Specific binding assertion that, alone, captures a partnership rather than a BRCA1 molecular function and is electronic-only here. Reason: Uninformative bare-binding MF; any p53-linked role is downstream and not the core function. |
| GO:0003682 chromatin binding | ISO GO_REF:0000096 | ACCEPT | Summary: BRCA1-BARD1 engages chromatin (via BARD1 reading of H4K20me0 / H2AK15ub) to target its E3 activity to damaged nucleosomes. Reason: Chromatin engagement is mechanistically central to BRCA1's repair role. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0003713 transcription coactivator activity | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: BRCA1 can act as a transcriptional coactivator, a regulatory role secondary to and intertwined with its genome-maintenance function. Reason: Transcription role not the core repair/ligase function; keep as non-core. |
| GO:0004842 ubiquitin-protein transferase activity | ISO GO_REF:0000119 | ACCEPT | Summary: Core catalytic activity: BRCA1, as the BRCA1-BARD1 RING heterodimer, accelerates ubiquitin transfer from charged E2~Ub onto substrate lysines (e.g. nucleosomal H2A, CtIP, PCNA) at sites of DNA damage. Reason: Defining molecular function of BRCA1 (EC 2.3.2.27); supported across IBA/ISO/ISS and the BRCA1-BARD1 mechanistic literature. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0005654 nucleoplasm | ISO GO_REF:0000119 | ACCEPT | Summary: Nucleoplasmic localization consistent with BRCA1's soluble nuclear and chromatin-associated repair/checkpoint activities. Reason: Standard nuclear sublocation for BRCA1; TAS/Reactome supported, do not remove an experimentally consistent site. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0005737 cytoplasm | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Cytoplasmic pool seen e.g. on translocation during UV-induced apoptosis and ACACA binding; not the principal site of repair function. Reason: Secondary localization; BRCA1 acts mainly in the nucleus. |
| GO:0005759 mitochondrial matrix | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Reported mitochondrial-matrix pool implicated in mitochondrial genome maintenance, distinct from the dominant nuclear role. Reason: Secondary localization downstream of BRCA1's genome-maintenance function. |
| GO:0005886 plasma membrane | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Minor plasma-membrane-associated pool reported electronically; peripheral to BRCA1's nuclear repair activity. Reason: Non-core secondary localization with electronic support only. |
| GO:0006301 DNA damage tolerance | ISO GO_REF:0000119 | ACCEPT | Summary: Via BRCA1-BARD1 ubiquitination of PCNA in unperturbed conditions, BRCA1 supports continuous DNA synthesis and suppresses ssDNA-gap accumulation, aiding tolerance of replication stress. Reason: Supported by recent PCNA-ubiquitination/fork-protection findings tied to BRCA1's E3 activity. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0006302 double-strand break repair | ISO GO_REF:0000119 | ACCEPT | Summary: BRCA1 is a key effector of double-strand-break repair, biasing pathway choice away from NHEJ via H2A ubiquitination and 53BP1 repositioning. Reason: Core DSB-repair role; IMP plus electronic support. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0006357 regulation of transcription by RNA polymerase II | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Regulates Pol II transcription through coactivator and partner (LMO4/CCAR2) interactions, a pleiotropic role beyond DNA repair. Reason: Transcriptional regulation secondary to BRCA1's core repair/ligase role. |
| GO:0007059 chromosome segregation | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Supports faithful chromosome segregation, a downstream consequence of BRCA1-maintained genome integrity and checkpoint control. Reason: Mitotic-fidelity outcome downstream of the core repair/checkpoint role. |
| GO:0007095 mitotic G2 DNA damage checkpoint signaling | ISO GO_REF:0000119 | ACCEPT | Summary: BRCA1 signals the G2 DNA-damage checkpoint, with BRCA1-mediated RBBP8 ubiquitination regulating CHEK1 activation after damage. Reason: Core checkpoint role tied to BRCA1's repair function; IBA/ISO support. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0010212 response to ionizing radiation | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Responds to ionizing radiation as part of damage signaling, an upstream stimulus context of the repair function. Reason: Response-to-stimulus term contextual to the core DDR role. |
| GO:0010575 positive regulation of vascular endothelial growth factor production | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Linked to upregulating VEGF production, a downstream gene-expression output rather than a core activity. Reason: Growth-factor-production role pleiotropic to core function. |
| GO:0010628 positive regulation of gene expression | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Broadly upregulates expression of target genes via its transcriptional-activator activity. Reason: Generic expression-regulation role downstream of transcription activity. |
| GO:0016567 protein ubiquitination | ISO GO_REF:0000119 | ACCEPT | Summary: BRCA1-BARD1 mediates protein ubiquitination of chromatin and repair substrates as its central biochemical activity. Reason: Core ubiquitination function; the specific K6/autoubiquitination children are also annotated. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0016604 nuclear body | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Localization to nuclear bodies, a sub-nuclear focus consistent with damage-induced assembly but not itself a defining site. Reason: Sub-nuclear localization secondary to the core nuclear/chromatin sites. |
| GO:0019899 enzyme binding | ISO GO_REF:0000119 | MARK AS OVER ANNOTATED | Summary: Non-specific enzyme-binding term that conveys nothing about which enzyme or what BRCA1 does with it. Reason: Uninformative binding MF; specific partner roles are captured elsewhere. |
| GO:0030308 negative regulation of cell growth | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Tumor-suppressor-associated growth restraint, a downstream physiological consequence of intact BRCA1 genome maintenance. Reason: Growth-suppression phenotype downstream of the core repair role. |
| GO:0031436 BRCA1-BARD1 complex | ISO GO_REF:0000119 | ACCEPT | Summary: Obligate RING-RING heterodimer with BARD1 that constitutes the active E3 ligase; this assembly underlies essentially all BRCA1 catalytic and DNA-repair functions. Reason: Defining functional complex of BRCA1; documented in SUBUNIT and the core mechanistic literature. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0031625 ubiquitin protein ligase binding | ISO GO_REF:0000119 | MARK AS OVER ANNOTATED | Summary: Generic 'binds an E3 ligase' term that is uninformative for a protein that is itself the E3 ligase. Reason: Bare-binding MF adding no functional specificity beyond BRCA1's own catalytic terms. |
| GO:0032991 protein-containing complex | ISO GO_REF:0000119 | MARK AS OVER ANNOTATED | Summary: Root-level complex term superseded by the specific BRCA1-BARD1 and BRCA1-A/B/C complex annotations. Reason: Uninformative generic CC; specific complexes are annotated. |
| GO:0033147 negative regulation of intracellular estrogen receptor signaling pathway | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Represses estrogen-receptor signaling, a hormone-pathway regulatory role pertinent to mammary biology but secondary to repair. Reason: Hormone-signaling regulation pleiotropic to core function. |
| GO:0042307 positive regulation of protein import into nucleus | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Promotes nuclear import of partner proteins, an ancillary trafficking role peripheral to repair catalysis. Reason: Partner-trafficking role not part of the core function. |
| GO:0042802 identical protein binding | ISO GO_REF:0000119 | MARK AS OVER ANNOTATED | Summary: Generic self-association term that does not capture BRCA1's heterodimeric-with-BARD1 mode of action or any specific function. Reason: Uninformative bare-binding MF; BRCA1's functional partnerships are captured by specific complex terms. |
| GO:0044027 negative regulation of gene expression via chromosomal CpG island methylation | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Linked to silencing of genes via CpG-island methylation, an epigenetic regulatory role distinct from direct repair. Reason: Epigenetic gene-silencing role pleiotropic to core function. |
| GO:0045717 negative regulation of fatty acid biosynthetic process | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Inhibits fatty-acid synthesis by binding inactive phosphorylated ACACA and preventing its dephosphorylation, a distinct metabolic moonlighting role. Reason: Specific lipid-regulatory function via ACACA, separate from the core repair role. |
| GO:0045739 positive regulation of DNA repair | ISO GO_REF:0000119 | ACCEPT | Summary: BRCA1 positively promotes homology-directed DNA repair by enabling resection and RAD51 loading at damage sites. Reason: Core pro-repair activity; consistent with FUNCTION. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0045766 positive regulation of angiogenesis | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Reported promotion of angiogenesis, a tissue-level role far downstream of BRCA1's molecular repair function. Reason: Angiogenic role pleiotropic and electronic-only. |
| GO:0045892 negative regulation of DNA-templated transcription | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Can repress transcription at certain targets (e.g. via LMO4/CCAR2-modulated activity), a context-specific regulatory role. Reason: Transcriptional repression not part of the core repair function. |
| GO:0045893 positive regulation of DNA-templated transcription | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Promotes transcription of subsets of target genes as a transcriptional activator, secondary to genome-maintenance roles. Reason: Activator output pleiotropic relative to core function. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Acts as a transcriptional activator at specific target genes, a regulatory output separable from its repair function. Reason: Activator role pleiotropic relative to core repair function. |
| GO:0051726 regulation of cell cycle | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Broad cell-cycle regulation reflecting BRCA1's checkpoint-control activities after DNA damage. Reason: General cell-cycle regulation downstream of checkpoint signaling. |
| GO:0051865 protein autoubiquitination | ISO GO_REF:0000119 | ACCEPT | Summary: BRCA1 undergoes K6-linked autoubiquitination that does not promote degradation, reflecting its intrinsic E3 ligase activity. Reason: Documented BRCA1 PTM/activity; core to its enzymatic characterization. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0070063 RNA polymerase binding | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Associates with the RNA polymerase II holoenzyme (via DHX9), underpinning BRCA1's transcriptional-regulation activity. Reason: Transcription-machinery interaction secondary to repair/ligase function. |
| GO:0070531 BRCA1-A complex | ISO GO_REF:0000119 | ACCEPT | Summary: Component of the BRCA1-A complex (with RAP80/UIMC1, ABRAXAS1, BRCC36, BABAM1/2) that recognizes K63-ubiquitin chains and recruits BRCA1 to DNA double-strand-break sites. Reason: Bona fide repair-targeting complex central to BRCA1 recruitment; supported by SUBUNIT and IBA/ISO. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0070532 BRCA1-B complex | ISO GO_REF:0000119 | ACCEPT | Summary: Component of the BRCA1-B complex (BRCA1-BARD1 with BACH1/BRIP1 and TOPBP1) linking BRCA1 to replication-associated DNA repair. Reason: Recognized BRCA1-defined repair complex; consistent with BRCT-BRIP1 interaction in SUBUNIT. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0070533 BRCA1-C complex | ISO GO_REF:0000119 | ACCEPT | Summary: Component of the BRCA1-C complex (BRCA1-BARD1 with CtIP/RBBP8 and the MRN complex) that promotes DNA end resection committing breaks to homologous recombination. Reason: Established BRCA1 resection complex; consistent with BRCA1-RBBP8 interaction in SUBUNIT. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0071356 cellular response to tumor necrosis factor | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Participates in the cellular response to TNF, a signaling-context role distinct from BRCA1's repair catalysis. Reason: Cytokine-response context, not the core function. |
| GO:0071479 cellular response to ionizing radiation | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Mediates the cellular response to ionizing radiation, with BRCA1 phosphorylated and required for IR-induced S/G2 arrest. Reason: Stress-response context of BRCA1's core DDR/checkpoint role. |
| GO:0071681 cellular response to indole-3-methanol | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Reported response to indole-3-methanol, a chemical-stimulus context secondary to BRCA1's core activities. Reason: Specific chemical-response context, non-core. |
| GO:0085020 protein K6-linked ubiquitination | ISO GO_REF:0000119 | ACCEPT | Summary: BRCA1-BARD1 specifically catalyzes 'Lys-6'-linked polyubiquitin chains, a hallmark non-degradative linkage of this E3 ligase. Reason: Signature catalytic output of BRCA1 stated explicitly in UniProt FUNCTION/PTM. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:1902042 negative regulation of extrinsic apoptotic signaling pathway via death domain receptors | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Modulates death-receptor extrinsic apoptotic signaling, a cell-fate role separable from direct repair catalysis. Reason: Apoptosis-modulation role pleiotropic to core function. |
| GO:1990391 DNA repair complex | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Generic membership in a DNA-repair complex; the specific BRCA1-defined complexes (BRCA1-BARD1/A/B/C) capture this more precisely. Reason: Broad complex term subordinate to the specific BRCA1 complexes already annotated. |
| GO:2000378 negative regulation of reactive oxygen species metabolic process | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Limits ROS accumulation, an antioxidant/redox-protective role downstream of BRCA1-maintained genome and metabolic homeostasis. Reason: Redox-regulation role pleiotropic to the core repair function. |
| GO:0005634 nucleus | NAS PMID:18171670 Cell cycle-dependent complex formation of BRCA1.CtIP.MRN is ... | ACCEPT | Summary: BRCA1 acts predominantly in the nucleus, forming DNA-damage-induced foci on chromatin where it carries out repair and checkpoint functions. Reason: Primary site of BRCA1 action; UniProt SUBCELLULAR LOCATION and IDA support. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0005634 nucleus | NAS PMID:20656689 Differential regulation of JAMM domain deubiquitinating enzy... | ACCEPT | Summary: BRCA1 acts predominantly in the nucleus, forming DNA-damage-induced foci on chromatin where it carries out repair and checkpoint functions. Reason: Primary site of BRCA1 action; UniProt SUBCELLULAR LOCATION and IDA support. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0005634 nucleus | NAS PMID:22369660 BRCA1 tumor suppressor network: focusing on its tail. | ACCEPT | Summary: BRCA1 acts predominantly in the nucleus, forming DNA-damage-induced foci on chromatin where it carries out repair and checkpoint functions. Reason: Primary site of BRCA1 action; UniProt SUBCELLULAR LOCATION and IDA support. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0006281 DNA repair | NAS PMID:22369660 BRCA1 tumor suppressor network: focusing on its tail. | ACCEPT | Summary: BRCA1 facilitates cellular responses to DNA damage and is required for FANCD2 targeting and homology-directed repair, maintaining genome integrity. Reason: Core function captured directly in UniProt FUNCTION. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0006282 regulation of DNA repair | NAS PMID:20656689 Differential regulation of JAMM domain deubiquitinating enzy... | ACCEPT | Summary: BRCA1 regulates DNA repair by controlling pathway choice and the loading of downstream HR machinery at breaks. Reason: Core regulatory role over the repair process it executes. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0035825 homologous recombination | NAS PMID:22369660 BRCA1 tumor suppressor network: focusing on its tail. | ACCEPT | Summary: BRCA1 contributes to homologous recombination through its PALB2 interaction and modulation of RAD51 loading during recombinational repair. Reason: Core repair pathway; NAS support consistent with FUNCTION. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0035825 homologous recombination | NAS PMID:30657944 CtIP-BRCA1 complex and MRE11 maintain replication forks in t... | ACCEPT | Summary: BRCA1 contributes to homologous recombination through its PALB2 interaction and modulation of RAD51 loading during recombinational repair. Reason: Core repair pathway; NAS support consistent with FUNCTION. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0044818 mitotic G2/M transition checkpoint | NAS PMID:22369660 BRCA1 tumor suppressor network: focusing on its tail. | ACCEPT | Summary: Required for the DNA-damage-induced G2/M checkpoint arrest that prevents division of cells carrying unrepaired breaks. Reason: Core checkpoint function; IMP-supported and consistent with FUNCTION. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0110025 DNA strand resection involved in replication fork processing | NAS PMID:29709199 The MRE11-RAD50-NBS1 Complex Conducts the Orchestration of D... | ACCEPT | Summary: BRCA1-BARD1 promotes nucleolytic end resection at breaks and protects/processes stalled replication forks, a step committing repair to homology-directed pathways. Reason: Resection is a core BRCA1-driven step (BRCA1-C/CtIP); NAS supported. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0003713 transcription coactivator activity | IDA PMID:20820192 BRCA1 affects global DNA methylation through regulation of D... | KEEP AS NON CORE | Summary: BRCA1 can act as a transcriptional coactivator, a regulatory role secondary to and intertwined with its genome-maintenance function. Reason: Transcription role not the core repair/ligase function; keep as non-core. |
| GO:0006974 DNA damage response | NAS PMID:16651405 DNA damage-induced BARD1 phosphorylation is critical for the... | ACCEPT | Summary: BRCA1 coordinates the DNA-damage response, being phosphorylated by ATM/ATR and assembling repair/checkpoint complexes at break sites. Reason: Core DDR role; IMP-supported and central to BRCA1 biology. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0045787 positive regulation of cell cycle | NAS PMID:15159397 BRCA1-BARD1 complexes are required for p53Ser-15 phosphoryla... | KEEP AS NON CORE | Summary: Reported positive cell-cycle regulation, a context-dependent role secondary to BRCA1's checkpoint function. Reason: Pleiotropic cell-cycle effect downstream of core checkpoint role. |
| GO:2000001 regulation of DNA damage checkpoint | NAS PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | ACCEPT | Summary: BRCA1 regulates DNA-damage checkpoint activation, controlling cell-cycle arrest in coordination with its repair complexes. Reason: Directly tied to BRCA1's checkpoint-control role; NAS supported. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0060816 random inactivation of X chromosome | IGI PMID:12419249 BRCA1 supports XIST RNA concentration on the inactive X chro... | KEEP AS NON CORE | Summary: Implicated in X-chromosome inactivation, a chromatin-level role related to BRCA1's chromosome-surveillance activity. Reason: Specialized chromatin role secondary to core repair function. |
| GO:0044027 negative regulation of gene expression via chromosomal CpG island methylation | IDA PMID:20820192 BRCA1 affects global DNA methylation through regulation of D... | KEEP AS NON CORE | Summary: Linked to silencing of genes via CpG-island methylation, an epigenetic regulatory role distinct from direct repair. Reason: Epigenetic gene-silencing role pleiotropic to core function. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IMP PMID:20820192 BRCA1 affects global DNA methylation through regulation of D... | KEEP AS NON CORE | Summary: Acts as a transcriptional activator at specific target genes, a regulatory output separable from its repair function. Reason: Activator role pleiotropic relative to core repair function. |
| GO:0001741 XY body | IDA PMID:31839538 GCNA Interacts with Spartan and Topoisomerase II to Regulate... | KEEP AS NON CORE | Summary: Localizes to the XY body (sex-body) during male meiosis, reflecting BRCA1's role in meiotic sex-chromosome inactivation/silencing. Reason: Meiosis-specific localization downstream of BRCA1's chromatin/genome-surveillance role. |
| GO:0005634 nucleus | IDA PMID:31839538 GCNA Interacts with Spartan and Topoisomerase II to Regulate... | ACCEPT | Summary: BRCA1 acts predominantly in the nucleus, forming DNA-damage-induced foci on chromatin where it carries out repair and checkpoint functions. Reason: Primary site of BRCA1 action; UniProt SUBCELLULAR LOCATION and IDA support. |
| GO:1990904 ribonucleoprotein complex | ISO PMID:18809582 Nucleophosmin serves as a rate-limiting nuclear export chape... | KEEP AS NON CORE | Summary: Association with RNP/RNA-containing complexes linked to BRCA1's reported RNA binding and transcription-coupled roles. Reason: Peripheral complex membership downstream of transcription-associated activity. |
| GO:0032991 protein-containing complex | ISO PMID:16951165 p27Kip1 repression of ErbB2-induced mammary tumor growth in ... | MARK AS OVER ANNOTATED | Summary: Root-level complex term superseded by the specific BRCA1-BARD1 and BRCA1-A/B/C complex annotations. Reason: Uninformative generic CC; specific complexes are annotated. |
| GO:0003713 transcription coactivator activity | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: BRCA1 can act as a transcriptional coactivator, a regulatory role secondary to and intertwined with its genome-maintenance function. Reason: Transcription role not the core repair/ligase function; keep as non-core. |
| GO:0006357 regulation of transcription by RNA polymerase II | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Regulates Pol II transcription through coactivator and partner (LMO4/CCAR2) interactions, a pleiotropic role beyond DNA repair. Reason: Transcriptional regulation secondary to BRCA1's core repair/ligase role. |
| GO:0070063 RNA polymerase binding | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Associates with the RNA polymerase II holoenzyme (via DHX9), underpinning BRCA1's transcriptional-regulation activity. Reason: Transcription-machinery interaction secondary to repair/ligase function. |
| GO:0044818 mitotic G2/M transition checkpoint | IMP PMID:15254237 BRCA1 is required for common-fragile-site stability via its ... | ACCEPT | Summary: Required for the DNA-damage-induced G2/M checkpoint arrest that prevents division of cells carrying unrepaired breaks. Reason: Core checkpoint function; IMP-supported and consistent with FUNCTION. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0000800 lateral element | ISO PMID:9774970 Stable interaction between the products of the BRCA1 and BRC... | KEEP AS NON CORE | Summary: Meiotic synaptonemal-complex lateral-element localization tied to BRCA1's role in meiotic chromosome surveillance. Reason: Meiosis-specific localization, a specialized context of genome maintenance. |
| GO:0000794 condensed nuclear chromosome | IDA PMID:26490168 FancJ (Brip1) loss-of-function allele results in spermatogon... | ACCEPT | Summary: Localizes to condensed nuclear chromosomes, reflecting chromatin association during mitotic/meiotic chromosome states. Reason: IDA-supported; keep experimental localization rather than removing. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0045893 positive regulation of DNA-templated transcription | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Promotes transcription of subsets of target genes as a transcriptional activator, secondary to genome-maintenance roles. Reason: Activator output pleiotropic relative to core function. |
| GO:0006974 DNA damage response | IMP PMID:23271346 BRCA1 deficiency in skin epidermis leads to selective loss o... | ACCEPT | Summary: BRCA1 coordinates the DNA-damage response, being phosphorylated by ATM/ATR and assembling repair/checkpoint complexes at break sites. Reason: Core DDR role; IMP-supported and central to BRCA1 biology. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0005694 chromosome | IDA PMID:22549958 Meiotic DNA double-strand breaks and chromosome asynapsis in... | ACCEPT | Summary: BRCA1 localizes to chromosomes/chromatin, where the BRCA1-BARD1 ligase modifies nucleosomal H2A at break sites. Reason: Direct chromatin association is core to BRCA1 function; IDA supported. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0005694 chromosome | IDA PMID:23039116 HORMAD2 is essential for synapsis surveillance during meioti... | ACCEPT | Summary: BRCA1 localizes to chromosomes/chromatin, where the BRCA1-BARD1 ligase modifies nucleosomal H2A at break sites. Reason: Direct chromatin association is core to BRCA1 function; IDA supported. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0005654 nucleoplasm | TAS Reactome:R-MMU-912421 | ACCEPT | Summary: Nucleoplasmic localization consistent with BRCA1's soluble nuclear and chromatin-associated repair/checkpoint activities. Reason: Standard nuclear sublocation for BRCA1; TAS/Reactome supported, do not remove an experimentally consistent site. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0005654 nucleoplasm | TAS Reactome:R-MMU-912423 | ACCEPT | Summary: Nucleoplasmic localization consistent with BRCA1's soluble nuclear and chromatin-associated repair/checkpoint activities. Reason: Standard nuclear sublocation for BRCA1; TAS/Reactome supported, do not remove an experimentally consistent site. |
| GO:0005654 nucleoplasm | TAS Reactome:R-MMU-912431 | ACCEPT | Summary: Nucleoplasmic localization consistent with BRCA1's soluble nuclear and chromatin-associated repair/checkpoint activities. Reason: Standard nuclear sublocation for BRCA1; TAS/Reactome supported, do not remove an experimentally consistent site. |
| GO:0005654 nucleoplasm | TAS Reactome:R-MMU-912449 | ACCEPT | Summary: Nucleoplasmic localization consistent with BRCA1's soluble nuclear and chromatin-associated repair/checkpoint activities. Reason: Standard nuclear sublocation for BRCA1; TAS/Reactome supported, do not remove an experimentally consistent site. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0005654 nucleoplasm | TAS Reactome:R-MMU-912468 | ACCEPT | Summary: Nucleoplasmic localization consistent with BRCA1's soluble nuclear and chromatin-associated repair/checkpoint activities. Reason: Standard nuclear sublocation for BRCA1; TAS/Reactome supported, do not remove an experimentally consistent site. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0006302 double-strand break repair | IMP PMID:22186889 BRCA1 is an essential regulator of heart function and surviv... | ACCEPT | Summary: BRCA1 is a key effector of double-strand-break repair, biasing pathway choice away from NHEJ via H2A ubiquitination and 53BP1 repositioning. Reason: Core DSB-repair role; IMP plus electronic support. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0005737 cytoplasm | IDA PMID:11172592 Brca1 and Brca2 protein expression patterns in different tis... | KEEP AS NON CORE | Summary: Cytoplasmic pool seen e.g. on translocation during UV-induced apoptosis and ACACA binding; not the principal site of repair function. Reason: Secondary localization; BRCA1 acts mainly in the nucleus. |
| GO:0000976 transcription cis-regulatory region binding | IDA PMID:20820192 BRCA1 affects global DNA methylation through regulation of D... | KEEP AS NON CORE | Summary: Binds cis-regulatory regions consistent with BRCA1's transcriptional-regulation activities at target promoters. Reason: Transcription-associated DNA binding, secondary to repair role. |
| GO:0000794 condensed nuclear chromosome | IDA PMID:20551173 Functional conservation of Mei4 for meiotic DNA double-stran... | ACCEPT | Summary: Localizes to condensed nuclear chromosomes, reflecting chromatin association during mitotic/meiotic chromosome states. Reason: IDA-supported; keep experimental localization rather than removing. |
| GO:0085020 protein K6-linked ubiquitination | ISS GO_REF:0000024 | ACCEPT | Summary: BRCA1-BARD1 specifically catalyzes 'Lys-6'-linked polyubiquitin chains, a hallmark non-degradative linkage of this E3 ligase. Reason: Signature catalytic output of BRCA1 stated explicitly in UniProt FUNCTION/PTM. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0051865 protein autoubiquitination | ISS GO_REF:0000024 | ACCEPT | Summary: BRCA1 undergoes K6-linked autoubiquitination that does not promote degradation, reflecting its intrinsic E3 ligase activity. Reason: Documented BRCA1 PTM/activity; core to its enzymatic characterization. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0004842 ubiquitin-protein transferase activity | ISS GO_REF:0000024 | ACCEPT | Summary: Core catalytic activity: BRCA1, as the BRCA1-BARD1 RING heterodimer, accelerates ubiquitin transfer from charged E2~Ub onto substrate lysines (e.g. nucleosomal H2A, CtIP, PCNA) at sites of DNA damage. Reason: Defining molecular function of BRCA1 (EC 2.3.2.27); supported across IBA/ISO/ISS and the BRCA1-BARD1 mechanistic literature. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0031436 BRCA1-BARD1 complex | ISS GO_REF:0000024 | ACCEPT | Summary: Obligate RING-RING heterodimer with BARD1 that constitutes the active E3 ligase; this assembly underlies essentially all BRCA1 catalytic and DNA-repair functions. Reason: Defining functional complex of BRCA1; documented in SUBUNIT and the core mechanistic literature. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0003723 RNA binding | ISO PMID:12419249 BRCA1 supports XIST RNA concentration on the inactive X chro... | KEEP AS NON CORE | Summary: Reported RNA-binding activity linked to transcription-coupled and RNA-associated functions rather than the core E3/repair role. Reason: Ancillary nucleic-acid binding; not the defining function. |
| GO:0043009 chordate embryonic development | IMP PMID:9171368 Targeted mutations of breast cancer susceptibility gene homo... | KEEP AS NON CORE | Summary: Brca1 is required for embryonic development, with knockouts being embryonic lethal owing to defective proliferation and genome instability. Reason: Developmental phenotype downstream of BRCA1's essential genome-maintenance role. |
| GO:0045717 negative regulation of fatty acid biosynthetic process | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Inhibits fatty-acid synthesis by binding inactive phosphorylated ACACA and preventing its dephosphorylation, a distinct metabolic moonlighting role. Reason: Specific lipid-regulatory function via ACACA, separate from the core repair role. |
| GO:0005813 centrosome | TAS PMID:10855792 VCP, a weak ATPase involved in multiple cellular events, int... | KEEP AS NON CORE | Summary: Centrosomal pool linked to BRCA1's regulation of centrosomal microtubule nucleation, a function secondary to its nuclear repair role. Reason: Secondary localization downstream of BRCA1's broader genome-stability role. |
| GO:0051298 centrosome duplication | TAS PMID:10855792 VCP, a weak ATPase involved in multiple cellular events, int... | KEEP AS NON CORE | Summary: Regulates centrosome duplication, helping prevent centrosome amplification and aneuploidy. Reason: Centrosome control secondary to BRCA1's genome-stability function. |
| GO:0000793 condensed chromosome | IDA PMID:12913077 Targeted disruption of exons 1 to 6 of the Fanconi Anemia gr... | ACCEPT | Summary: Localizes to condensed chromosomes, consistent with BRCA1's role in genome maintenance through the cell cycle. Reason: IDA-supported localization; retain as observed nuclear/chromosomal site. Supporting Evidence: UniProt:P48754 E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. file:mouse/Brca1/Brca1-deep-research-falcon.md BRCA1 forms an obligate heterodimer with BARD1 through the N-terminal RING domains; the complex acts as an E3 ubiquitin ligase that promotes DNA end resection, antagonizes 53BP1 at breaks, and supports PALB2-BRCA2-RAD51 loading for homology-directed repair. |
| GO:0007098 centrosome cycle | IGI PMID:15123655 Genetic interactions between Brca1 and Gadd45a in centrosome... | KEEP AS NON CORE | Summary: Participates in the centrosome cycle, consistent with AURKA-phosphorylation-regulated control of centrosomal microtubule nucleation. Reason: Centrosome-cycle role secondary to core repair/checkpoint function. |
| GO:0008630 intrinsic apoptotic signaling pathway in response to DNA damage | ISO PMID:14654789 A member of the Pyrin family, IFI16, is a novel BRCA1-associ... | KEEP AS NON CORE | Summary: Engages DNA-damage-triggered intrinsic apoptosis when damage is irreparable, an outcome downstream of BRCA1 damage sensing. Reason: Apoptotic outcome downstream of the core DNA-damage-response role. |
| GO:0003684 damaged DNA binding | IDA PMID:11934988 Genomic instability in mice lacking histone H2AX. | MARK AS OVER ANNOTATED | Summary: BRCA1 is recruited to damaged DNA chiefly via ubiquitin/chromatin readers and partner complexes rather than as a direct damaged-DNA binder; the bare MF over-attributes a direct activity. Reason: Recruitment to damage is complex-mediated; specific complex/chromatin terms capture this better. |
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