RAD51 is the central eukaryotic recombinase of homologous recombination (HR), the ortholog of bacterial RecA and yeast Rad51. It binds single-stranded DNA in an ATP-dependent manner to assemble a helical nucleoprotein (presynaptic) filament on the 3' single-stranded overhangs generated by end resection, after being loaded onto RPA-coated ssDNA by BRCA2/PALB2 and the RAD51 paralog mediators (the BCDX2 and CX3 complexes; RAD51B, RAD51C, RAD51D, XRCC2, XRCC3). The active ATP-bound filament performs homology search within duplex DNA and catalyzes DNA strand invasion and strand exchange, base-pairing the invading strand with the homologous template to form a displacement loop (D-loop). RAD51 is a self-inactivating, DNA-dependent ATPase: ATP binding and hydrolysis, modulated by cofactors such as Ca2+, control filament assembly, stability and turnover. Through this recombinase activity RAD51 is essential for error-free repair of DNA double-strand breaks by HR, for protection and restart of stalled or damaged replication forks, and for interstrand crosslink repair; it also acts at chromatin and can peel nucleosomal DNA at break sites. Additional context- specific roles include meiotic recombination (as a non-catalytic accessory to the meiosis-specific recombinase DMC1), recombination-based telomere maintenance, and maintenance of mitochondrial DNA copy number under oxidative stress. RAD51 is nuclear and concentrates in damage-induced foci at sites of double-strand breaks. A dominant- negative RAD51 variant causes a Fanconi anemia-like disorder (Fanconi anemia complementation group R, FANCR).
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000150 DNA strand exchange activity | IBA GO_REF:0000033 | ACCEPT | Summary: RAD51 catalyzes ATP-dependent homologous DNA pairing and strand exchange, the defining recombinase activity of homologous recombination. Reason: Core molecular function of RAD51. The human protein forms a helical nucleoprotein filament on ssDNA and promotes homology search and strand transfer in vitro; supported by multiple independent IDA/IMP studies and the IBA phylogenetic inference. |
| GO:0000730 DNA recombinase assembly | IBA GO_REF:0000033 | ACCEPT | Summary: Assembly of the RAD51 recombinase (presynaptic) filament on ssDNA. Reason: Captures nucleation/assembly of the RAD51 nucleoprotein filament, a core step; IBA-supported and consistent with biochemistry. |
| GO:0003697 single-stranded DNA binding | IBA GO_REF:0000033 | ACCEPT | Summary: RAD51 binds single-stranded DNA to nucleate the presynaptic nucleoprotein filament. Reason: Well-established core activity; RAD51 binds ssDNA (the 3' resected overhang) in an ATP-dependent manner as the first step of filament assembly. Supported by biochemistry (IDA/IMP) and IBA/ISS. |
| GO:0008094 ATP-dependent activity, acting on DNA | IBA GO_REF:0000033 | ACCEPT | Summary: RAD51 exhibits ATP-dependent activity acting on DNA (DNA-stimulated ATPase within the nucleoprotein filament). Reason: Accurate parent term capturing the DNA-dependent ATPase activity that drives filament dynamics; consistent with the specific ATP hydrolysis and strand-exchange activities. Retained as a broad but correct grouping (IBA/IEA). |
| GO:0003690 double-stranded DNA binding | IBA GO_REF:0000033 | ACCEPT | Summary: RAD51 binds double-stranded DNA, required for homology search and filament interactions with duplex donor. Reason: RAD51 binds dsDNA (donor duplex during homology search and forms filaments on dsDNA); demonstrated biochemically (IDA/IMP) and inferred by IBA/IEA. |
| GO:0042148 DNA strand invasion | IBA GO_REF:0000033 | ACCEPT | Summary: RAD51 catalyzes DNA strand invasion, base-pairing the presynaptic filament ssDNA into homologous duplex to form the D-loop. Reason: Directly demonstrated (PMID:27694622) and inferred by IBA; a defining step of the recombinase mechanism. |
| GO:0007131 reciprocal meiotic recombination | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Reciprocal meiotic recombination (crossover). Reason: RAD51 supports meiotic HR as a non-catalytic accessory to the meiosis-specific recombinase DMC1; a real but tissue-restricted, non-core role. |
| GO:0006312 mitotic recombination | IBA GO_REF:0000033 | ACCEPT | Summary: RAD51 functions in mitotic (somatic) homologous recombination. Reason: Core somatic role; IBA and TAS supported. |
| GO:0000794 condensed nuclear chromosome | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Condensed nuclear chromosome. Reason: Localization to condensed chromosomes (meiotic/mitotic); non-core (IBA/ISS). |
| GO:0070192 chromosome organization involved in meiotic cell cycle | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Chromosome organization involved in meiotic cell cycle. Reason: Meiotic role, non-core in the human somatic context (IBA). |
| GO:0000150 DNA strand exchange activity | IEA GO_REF:0000002 | ACCEPT | Summary: RAD51 catalyzes ATP-dependent homologous DNA pairing and strand exchange, the defining recombinase activity of homologous recombination. Reason: Core molecular function of RAD51. The human protein forms a helical nucleoprotein filament on ssDNA and promotes homology search and strand transfer in vitro; supported by multiple independent IDA/IMP studies and the IBA phylogenetic inference. |
| GO:0000166 nucleotide binding | IEA GO_REF:0000002 | ACCEPT | Summary: Nucleotide binding (broad parent of ATP binding). Reason: Broad InterPro-derived parent term; accurate given RAD51's ATP binding, retained as a correct generalization. |
| GO:0000724 double-strand break repair via homologous recombination | IEA GO_REF:0000120 | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0003677 DNA binding | IEA GO_REF:0000002 | ACCEPT | Summary: DNA binding (broad parent of ss/dsDNA binding). Reason: Broad InterPro-derived DNA-binding term; correct but general, subsumed by the specific ssDNA and dsDNA binding annotations. |
| GO:0003690 double-stranded DNA binding | IEA GO_REF:0000002 | ACCEPT | Summary: RAD51 binds double-stranded DNA, required for homology search and filament interactions with duplex donor. Reason: RAD51 binds dsDNA (donor duplex during homology search and forms filaments on dsDNA); demonstrated biochemically (IDA/IMP) and inferred by IBA/IEA. |
| GO:0003697 single-stranded DNA binding | IEA GO_REF:0000120 | ACCEPT | Summary: RAD51 binds single-stranded DNA to nucleate the presynaptic nucleoprotein filament. Reason: Well-established core activity; RAD51 binds ssDNA (the 3' resected overhang) in an ATP-dependent manner as the first step of filament assembly. Supported by biochemistry (IDA/IMP) and IBA/ISS. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: RAD51 binds ATP; nucleotide state governs the active vs inactive conformation of the filament. Reason: ATP binding is intrinsic to RAD51 (Walker A/B motifs) and regulates filament activity; supported experimentally (IDA PMID:16428451) and by IEA. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: RAD51 localizes to the nucleus, its principal site of action. Reason: Predominant and functionally relevant localization; supported by many EXP/IDA studies and IEA. |
| GO:0005694 chromosome | IEA GO_REF:0000120 | ACCEPT | Summary: RAD51 localizes to chromosomes (damaged chromatin / repair foci). Reason: Chromosomal localization at repair sites; supported by multiple EXP studies and IEA. |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Cytoplasm localization. Reason: Cytoplasmic reservoir of RAD51 prior to nuclear import/loading; non-core relative to its nuclear function. |
| GO:0005759 mitochondrial matrix | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Mitochondrial matrix localization. Reason: Mitochondrial matrix pool consistent with mtDNA maintenance role (PMID:20413593); non-core. |
| GO:0005813 centrosome | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Centrosome localization. Reason: Documented minor localization (UniProt, PMID:21276791); non-core. |
| GO:0006259 DNA metabolic process | IEA GO_REF:0000002 | ACCEPT | Summary: DNA metabolic process (broad parent). Reason: Very broad InterPro-derived grouping; correct but uninformative, subsumed by specific HR/repair terms. Acceptable as a broad IEA. |
| GO:0006281 DNA repair | IEA GO_REF:0000002 | ACCEPT | Summary: RAD51 functions in DNA repair (homologous recombination arm). Reason: Broad but accurate core process (parent of DSBR via HR); retained. |
| GO:0008094 ATP-dependent activity, acting on DNA | IEA GO_REF:0000002 | ACCEPT | Summary: RAD51 exhibits ATP-dependent activity acting on DNA (DNA-stimulated ATPase within the nucleoprotein filament). Reason: Accurate parent term capturing the DNA-dependent ATPase activity that drives filament dynamics; consistent with the specific ATP hydrolysis and strand-exchange activities. Retained as a broad but correct grouping (IBA/IEA). |
| GO:0048471 perinuclear region of cytoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Perinuclear region of cytoplasm. Reason: Perinuclear cytoplasmic localization (PMID:16215984); non-core. |
| GO:0140664 ATP-dependent DNA damage sensor activity | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: ATP-dependent DNA damage sensor activity (InterPro2GO IEA). Reason: RAD51 is a recombinase, not a checkpoint DNA-damage sensor; this InterPro-derived mapping over-interprets the ATP-dependent DNA-acting activity. The accurate MF is DNA strand exchange / ATP-dependent activity acting on DNA. |
| GO:1990426 mitotic recombination-dependent replication fork processing | IEA GO_REF:0000002 | ACCEPT | Summary: RAD51 acts in mitotic recombination-dependent replication fork processing. Reason: Specific and accurate IEA term for RAD51's role in recombination-mediated fork restart; consistent with the experimental fork-processing annotations. |
| GO:0005515 protein binding | IPI PMID:10551859 Expression of BRC repeats in breast cancer cells disrupts th... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:11842113 Involvement of Rad51C in two distinct protein complexes of R... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:12442171 Insights into DNA recombination from the structure of a RAD5... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:12750383 WRN interacts physically and functionally with the recombina... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:15665856 The cell-cycle checkpoint kinase Chk1 is required for mammal... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:15800615 CDK-dependent phosphorylation of BRCA2 as a regulatory mecha... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:16186822 MDC1 interacts with Rad51 and facilitates homologous recombi... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:16395335 Interplay between human DNA repair proteins at a unique doub... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:17541404 Interactions between human BRCA2 protein and the meiosis-spe... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:18264088 Resistance to therapy caused by intragenic deletion in BRCA2... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:19303847 The BRC repeats of BRCA2 modulate the DNA-binding selectivit... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:19338310 Streamline proteomic approach for characterizing protein-pro... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:19628690 The BRC repeats of human BRCA2 differentially regulate RAD51... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:20729832 Purified human BRCA2 stimulates RAD51-mediated recombination... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:20729859 Human BRCA2 protein promotes RAD51 filament formation on RPA... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:20871616 Enhancement of RAD51 recombinase activity by the tumor suppr... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:20871616 Enhancement of RAD51 recombinase activity by the tumor suppr... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:21307306 Molecular basis for enhancement of the meiotic DMC1 recombin... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:21307306 Molecular basis for enhancement of the meiotic DMC1 recombin... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:21399666 A mitotic function for the high-mobility group protein HMG20... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:21601571 Valine 1532 of human BRC repeat 4 plays an important role in... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:21903585 RAD51-associated protein 1 (RAD51AP1) interacts with the mei... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:21903585 RAD51-associated protein 1 (RAD51AP1) interacts with the mei... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:21965664 hSWS1Β·SWSAP1 is an evolutionarily conserved complex required... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:22116401 Synaptonemal complex protein SYCP3 impairs mitotic recombina... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:22193777 ChAM, a novel motif that mediates PALB2 intrinsic chromatin ... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:22293751 APRIN is a cell cycle specific BRCA2-interacting protein req... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:23509288 Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndro... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:24141787 Breast cancer-associated missense mutants of the PALB2 WD40 ... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:24141787 Breast cancer-associated missense mutants of the PALB2 WD40 ... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:24981860 Human-chromatin-related protein interactions identify a deme... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:25282148 Structure and mechanism of action of the BRCA2 breast cancer... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:25640309 Systematic identification of molecular links between core an... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:25640309 Systematic identification of molecular links between core an... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:25640309 Systematic identification of molecular links between core an... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:25640309 Systematic identification of molecular links between core an... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:25642963 Homologous-recombination-deficient tumours are dependent on ... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:28319063 Compromised BRCA1-PALB2 interaction is associated with breas... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:28864920 Discovery of mutations in homologous recombination genes in ... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:33941620 Autism-Associated Vigilin Depletion Impairs DNA Damage Repai... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:9380510 Interaction of p53 with the human Rad51 protein. | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:9396801 A novel nucleic acid-binding protein that interacts with hum... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:9396801 A novel nucleic acid-binding protein that interacts with hum... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:9560268 The BRC repeats in BRCA2 are critical for RAD51 binding and ... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:9660962 XRCC2 and XRCC3, new human Rad51-family members, promote chr... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0042802 identical protein binding | IPI PMID:12442171 Insights into DNA recombination from the structure of a RAD5... | ACCEPT | Summary: RAD51 self-associates (identical protein binding) into homo-oligomers that constitute the nucleoprotein filament. Reason: RAD51 forms linear homo-oligomers giving rise to the recombinase filament; self-interaction is functionally central and is documented by multiple IPI studies. More informative than generic protein binding. |
| GO:0042802 identical protein binding | IPI PMID:19622740 Structural transitions within human Rad51 nucleoprotein fila... | ACCEPT | Summary: RAD51 self-associates (identical protein binding) into homo-oligomers that constitute the nucleoprotein filament. Reason: RAD51 forms linear homo-oligomers giving rise to the recombinase filament; self-interaction is functionally central and is documented by multiple IPI studies. More informative than generic protein binding. |
| GO:0042802 identical protein binding | IPI PMID:19628690 The BRC repeats of human BRCA2 differentially regulate RAD51... | ACCEPT | Summary: RAD51 self-associates (identical protein binding) into homo-oligomers that constitute the nucleoprotein filament. Reason: RAD51 forms linear homo-oligomers giving rise to the recombinase filament; self-interaction is functionally central and is documented by multiple IPI studies. More informative than generic protein binding. |
| GO:0042802 identical protein binding | IPI PMID:25282148 Structure and mechanism of action of the BRCA2 breast cancer... | ACCEPT | Summary: RAD51 self-associates (identical protein binding) into homo-oligomers that constitute the nucleoprotein filament. Reason: RAD51 forms linear homo-oligomers giving rise to the recombinase filament; self-interaction is functionally central and is documented by multiple IPI studies. More informative than generic protein binding. |
| GO:0042802 identical protein binding | IPI PMID:27941862 Cryo-EM structures of human RAD51 recombinase filaments duri... | ACCEPT | Summary: RAD51 self-associates (identical protein binding) into homo-oligomers that constitute the nucleoprotein filament. Reason: RAD51 forms linear homo-oligomers giving rise to the recombinase filament; self-interaction is functionally central and is documented by multiple IPI studies. More informative than generic protein binding. |
| GO:0042802 identical protein binding | IPI PMID:28864920 Discovery of mutations in homologous recombination genes in ... | ACCEPT | Summary: RAD51 self-associates (identical protein binding) into homo-oligomers that constitute the nucleoprotein filament. Reason: RAD51 forms linear homo-oligomers giving rise to the recombinase filament; self-interaction is functionally central and is documented by multiple IPI studies. More informative than generic protein binding. |
| GO:0042802 identical protein binding | IPI PMID:9396801 A novel nucleic acid-binding protein that interacts with hum... | ACCEPT | Summary: RAD51 self-associates (identical protein binding) into homo-oligomers that constitute the nucleoprotein filament. Reason: RAD51 forms linear homo-oligomers giving rise to the recombinase filament; self-interaction is functionally central and is documented by multiple IPI studies. More informative than generic protein binding. |
| GO:0042802 identical protein binding | IPI PMID:9469824 Isolation and characterization of RAD51C, a new human member... | ACCEPT | Summary: RAD51 self-associates (identical protein binding) into homo-oligomers that constitute the nucleoprotein filament. Reason: RAD51 forms linear homo-oligomers giving rise to the recombinase filament; self-interaction is functionally central and is documented by multiple IPI studies. More informative than generic protein binding. |
| GO:0042802 identical protein binding | IPI PMID:9660962 XRCC2 and XRCC3, new human Rad51-family members, promote chr... | ACCEPT | Summary: RAD51 self-associates (identical protein binding) into homo-oligomers that constitute the nucleoprotein filament. Reason: RAD51 forms linear homo-oligomers giving rise to the recombinase filament; self-interaction is functionally central and is documented by multiple IPI studies. More informative than generic protein binding. |
| GO:0000722 telomere maintenance via recombination | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Telomere maintenance via recombination (ALT context). Reason: Recombination-based telomere maintenance; a context-specific role (ortholog ISS/IEA), non-core. |
| GO:0000781 chromosome, telomeric region | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Chromosome, telomeric region (localization). Reason: Telomeric localization in the ALT/recombination context; non-core (IDA/IEA). |
| GO:0007127 meiosis I | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Meiosis I. Reason: Meiotic process; non-core (ortholog IEA). |
| GO:0009410 response to xenobiotic stimulus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Response to xenobiotic stimulus (ortholog IEA). Reason: Ortholog-based, tangential stimulus-response term; non-core. |
| GO:0009636 response to toxic substance | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Response to toxic substance (ortholog IEA). Reason: Ortholog-based, tangential stimulus-response term; non-core. |
| GO:0010165 response to X-ray | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Response to X-ray (ortholog IEA). Reason: Ortholog-based stimulus response; non-core. |
| GO:0010833 telomere maintenance via telomere lengthening | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Telomere maintenance via telomere lengthening. Reason: Telomere-lengthening role in recombination-based maintenance; non-core (ISS/IEA). |
| GO:0035861 site of double-strand break | IEA GO_REF:0000107 | ACCEPT | Summary: RAD51 is active at sites of double-strand breaks (damage-induced foci / repair centers). Reason: The functional site of the RAD51 recombinase; supported by multiple IDA studies showing localization to DSB sites and by ortholog IEA. |
| GO:0071480 cellular response to gamma radiation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cellular response to gamma radiation (ortholog IEA). Reason: Ortholog-based stimulus response; non-core wrapper around DDR. |
| GO:0072719 cellular response to cisplatin | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cellular response to cisplatin (ortholog IEA). Reason: Ortholog-based stimulus response consistent with ICL/crosslink repair; non-core. |
| GO:1904631 response to glucoside | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Response to glucoside (ortholog IEA). Reason: Highly tangential ortholog-projected term with no clear relation to RAD51's characterized functions; over-annotation. |
| GO:1990918 double-strand break repair involved in meiotic recombination | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Double-strand break repair involved in meiotic recombination. Reason: Meiotic DSB repair role; non-core (ISS/IEA). |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:18417535 Identification of a novel human Rad51 variant that promotes ... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0003697 single-stranded DNA binding | ISS GO_REF:0000024 | ACCEPT | Summary: RAD51 binds single-stranded DNA to nucleate the presynaptic nucleoprotein filament. Reason: Well-established core activity; RAD51 binds ssDNA (the 3' resected overhang) in an ATP-dependent manner as the first step of filament assembly. Supported by biochemistry (IDA/IMP) and IBA/ISS. |
| GO:0007131 reciprocal meiotic recombination | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Reciprocal meiotic recombination (crossover). Reason: RAD51 supports meiotic HR as a non-catalytic accessory to the meiosis-specific recombinase DMC1; a real but tissue-restricted, non-core role. |
| GO:0031297 replication fork processing | IDA PMID:18417535 Identification of a novel human Rad51 variant that promotes ... | ACCEPT | Summary: RAD51 acts in replication fork processing β protection and restart of stalled/damaged forks. Reason: Core replication-stress function; supported experimentally (PMID:18417535, PMID:22778135, PMID:25585578) and by ortholog inference. RAD51 protects nascent DNA and enables fork restart. |
| GO:0035861 site of double-strand break | IDA PMID:27797818 The MMS22L-TONSL heterodimer directly promotes RAD51-depende... | ACCEPT | Summary: RAD51 is active at sites of double-strand breaks (damage-induced foci / repair centers). Reason: The functional site of the RAD51 recombinase; supported by multiple IDA studies showing localization to DSB sites and by ortholog IEA. |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:38509361 Cryo-EM structures of RAD51 assembled on nucleosomes contain... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0031491 nucleosome binding | IDA PMID:38509361 Cryo-EM structures of RAD51 assembled on nucleosomes contain... | ACCEPT | Summary: RAD51 filament binds nucleosomal DNA and peels it from the histone octamer at DSB-containing nucleosomes. Reason: Cryo-EM structures show the RAD51 filament directly binds nucleosomal DNA and peels it from the histone surface (PMID:38509361), a physiologically relevant chromatin substrate interaction. Supporting Evidence: PMID:38509361 directly bind to the nucleosomal DNA |
| GO:0000150 DNA strand exchange activity | IDA PMID:39636933 Molecular basis of FIGNL1 in dissociating RAD51 from DNA and... | ACCEPT | Summary: RAD51 catalyzes ATP-dependent homologous DNA pairing and strand exchange, the defining recombinase activity of homologous recombination. Reason: Core molecular function of RAD51. The human protein forms a helical nucleoprotein filament on ssDNA and promotes homology search and strand transfer in vitro; supported by multiple independent IDA/IMP studies and the IBA phylogenetic inference. |
| GO:0000150 DNA strand exchange activity | IDA PMID:41166468 FIGNL1 inhibits homologous recombination in BRCA2 deficient ... | ACCEPT | Summary: RAD51 catalyzes ATP-dependent homologous DNA pairing and strand exchange, the defining recombinase activity of homologous recombination. Reason: Core molecular function of RAD51. The human protein forms a helical nucleoprotein filament on ssDNA and promotes homology search and strand transfer in vitro; supported by multiple independent IDA/IMP studies and the IBA phylogenetic inference. |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:39636933 Molecular basis of FIGNL1 in dissociating RAD51 from DNA and... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:41166468 FIGNL1 inhibits homologous recombination in BRCA2 deficient ... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:37499663 Visualization of direct and diffusion-assisted RAD51 nucleat... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0003697 single-stranded DNA binding | IDA PMID:37499663 Visualization of direct and diffusion-assisted RAD51 nucleat... | ACCEPT | Summary: RAD51 binds single-stranded DNA to nucleate the presynaptic nucleoprotein filament. Reason: Well-established core activity; RAD51 binds ssDNA (the 3' resected overhang) in an ATP-dependent manner as the first step of filament assembly. Supported by biochemistry (IDA/IMP) and IBA/ISS. |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:27941124 A phosphorylation-deubiquitination cascade regulates the BRC... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0035861 site of double-strand break | IDA PMID:27941124 A phosphorylation-deubiquitination cascade regulates the BRC... | ACCEPT | Summary: RAD51 is active at sites of double-strand breaks (damage-induced foci / repair centers). Reason: The functional site of the RAD51 recombinase; supported by multiple IDA studies showing localization to DSB sites and by ortholog IEA. |
| GO:1990918 double-strand break repair involved in meiotic recombination | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Double-strand break repair involved in meiotic recombination. Reason: Meiotic DSB repair role; non-core (ISS/IEA). |
| GO:0000150 DNA strand exchange activity | IDA PMID:19303847 The BRC repeats of BRCA2 modulate the DNA-binding selectivit... | ACCEPT | Summary: RAD51 catalyzes ATP-dependent homologous DNA pairing and strand exchange, the defining recombinase activity of homologous recombination. Reason: Core molecular function of RAD51. The human protein forms a helical nucleoprotein filament on ssDNA and promotes homology search and strand transfer in vitro; supported by multiple independent IDA/IMP studies and the IBA phylogenetic inference. |
| GO:0000150 DNA strand exchange activity | IMP PMID:26681308 A novel Fanconi anaemia subtype associated with a dominant-n... | ACCEPT | Summary: RAD51 catalyzes ATP-dependent homologous DNA pairing and strand exchange, the defining recombinase activity of homologous recombination. Reason: Core molecular function of RAD51. The human protein forms a helical nucleoprotein filament on ssDNA and promotes homology search and strand transfer in vitro; supported by multiple independent IDA/IMP studies and the IBA phylogenetic inference. |
| GO:0000150 DNA strand exchange activity | IDA PMID:7988572 Purification and characterization of the human Rad51 protein... | ACCEPT | Summary: RAD51 catalyzes ATP-dependent homologous DNA pairing and strand exchange, the defining recombinase activity of homologous recombination. Reason: Core molecular function of RAD51. The human protein forms a helical nucleoprotein filament on ssDNA and promotes homology search and strand transfer in vitro; supported by multiple independent IDA/IMP studies and the IBA phylogenetic inference. Supporting Evidence: PMID:7988572 The human Rad51 protein binds to single- and double-stranded DNA and exhibits DNA-dependent ATPase activity. |
| GO:0000150 DNA strand exchange activity | IDA PMID:8929543 Human Rad51 protein promotes ATP-dependent homologous pairin... | ACCEPT | Summary: RAD51 catalyzes ATP-dependent homologous DNA pairing and strand exchange, the defining recombinase activity of homologous recombination. Reason: Core molecular function of RAD51. The human protein forms a helical nucleoprotein filament on ssDNA and promotes homology search and strand transfer in vitro; supported by multiple independent IDA/IMP studies and the IBA phylogenetic inference. Supporting Evidence: PMID:8929543 hRad51 promotes homologous pairing and strand exchange reactions in vitro. |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:12442171 Insights into DNA recombination from the structure of a RAD5... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:15937124 BRCA2 BRC motifs bind RAD51-DNA filaments. | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:17515903 Interaction with the BRCA2 C terminus protects RAD51-DNA fil... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:17515904 Stabilization of RAD51 nucleoprotein filaments by the C-term... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:19303847 The BRC repeats of BRCA2 modulate the DNA-binding selectivit... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0003697 single-stranded DNA binding | IDA PMID:19303847 The BRC repeats of BRCA2 modulate the DNA-binding selectivit... | ACCEPT | Summary: RAD51 binds single-stranded DNA to nucleate the presynaptic nucleoprotein filament. Reason: Well-established core activity; RAD51 binds ssDNA (the 3' resected overhang) in an ATP-dependent manner as the first step of filament assembly. Supported by biochemistry (IDA/IMP) and IBA/ISS. |
| GO:0006974 DNA damage response | IDA PMID:12442171 Insights into DNA recombination from the structure of a RAD5... | ACCEPT | Summary: RAD51 participates in the cellular DNA damage response, forming damage-induced nuclear foci. Reason: Well supported by IDA; RAD51 is recruited to DNA damage sites and forms IR/CPT-induced foci. |
| GO:0035861 site of double-strand break | IDA PMID:19303847 The BRC repeats of BRCA2 modulate the DNA-binding selectivit... | ACCEPT | Summary: RAD51 is active at sites of double-strand breaks (damage-induced foci / repair centers). Reason: The functional site of the RAD51 recombinase; supported by multiple IDA studies showing localization to DSB sites and by ortholog IEA. |
| GO:0000152 nuclear ubiquitin ligase complex | IDA PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | KEEP AS NON CORE | Summary: Nuclear ubiquitin ligase complex (BRCC holoenzyme) membership. Reason: ComplexPortal IDA places RAD51 in the BRCC (BRCA1/BRCA2-containing) holoenzyme reported to have ubiquitin ligase activity (PMID:14636569). Experimental; retained but non-core, deferring to the ComplexPortal curator. |
| GO:0005634 nucleus | IDA PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | ACCEPT | Summary: RAD51 localizes to the nucleus, its principal site of action. Reason: Predominant and functionally relevant localization; supported by many EXP/IDA studies and IEA. |
| GO:0071479 cellular response to ionizing radiation | IMP PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | KEEP AS NON CORE | Summary: Cellular response to ionizing radiation (RAD51 focus formation after IR). Reason: Experimentally supported stimulus-response wrapper around the core DSB-repair function; kept as non-core. |
| GO:2000001 regulation of DNA damage checkpoint | NAS PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | KEEP AS NON CORE | Summary: Regulation of DNA damage checkpoint. Reason: NAS-supported regulatory role linked to the BRCC complex (PMID:14636569); non-core. |
| GO:0005730 nucleolus | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Nucleolus localization (HPA). Reason: HPA imaging-based nucleolar signal; minor localization, non-core. |
| GO:0005739 mitochondrion | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Mitochondrion localization. Reason: RAD51 has a separable mitochondrial pool involved in mtDNA copy-number maintenance under oxidative stress (PMID:20413593); non-core relative to nuclear HR. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Cytosol localization (HPA). Reason: Cytosolic pool; RAD51 is predominantly nuclear with a diffuse cytoplasmic reservoir. Non-core. |
| GO:0005634 nucleus | EXP PMID:15665856 The cell-cycle checkpoint kinase Chk1 is required for mammal... | ACCEPT | Summary: RAD51 localizes to the nucleus, its principal site of action. Reason: Predominant and functionally relevant localization; supported by many EXP/IDA studies and IEA. |
| GO:0005634 nucleus | EXP PMID:19783859 Cellular redistribution of Rad51 in response to DNA damage: ... | ACCEPT | Summary: RAD51 localizes to the nucleus, its principal site of action. Reason: Predominant and functionally relevant localization; supported by many EXP/IDA studies and IEA. |
| GO:0005634 nucleus | EXP PMID:23401855 The MCM8-MCM9 complex promotes RAD51 recruitment at DNA dama... | ACCEPT | Summary: RAD51 localizes to the nucleus, its principal site of action. Reason: Predominant and functionally relevant localization; supported by many EXP/IDA studies and IEA. |
| GO:0005634 nucleus | EXP PMID:23509288 Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndro... | ACCEPT | Summary: RAD51 localizes to the nucleus, its principal site of action. Reason: Predominant and functionally relevant localization; supported by many EXP/IDA studies and IEA. |
| GO:0005634 nucleus | EXP PMID:9192668 RAB22 and RAB163/mouse BRCA2: proteins that specifically int... | ACCEPT | Summary: RAD51 localizes to the nucleus, its principal site of action. Reason: Predominant and functionally relevant localization; supported by many EXP/IDA studies and IEA. |
| GO:0005694 chromosome | EXP PMID:22325354 Plk1 and CK2 act in concert to regulate Rad51 during DNA dou... | ACCEPT | Summary: RAD51 localizes to chromosomes (damaged chromatin / repair foci). Reason: Chromosomal localization at repair sites; supported by multiple EXP studies and IEA. |
| GO:0005694 chromosome | EXP PMID:23401855 The MCM8-MCM9 complex promotes RAD51 recruitment at DNA dama... | ACCEPT | Summary: RAD51 localizes to chromosomes (damaged chromatin / repair foci). Reason: Chromosomal localization at repair sites; supported by multiple EXP studies and IEA. |
| GO:0005694 chromosome | EXP PMID:26811421 TOPBP1 regulates RAD51 phosphorylation and chromatin loading... | ACCEPT | Summary: RAD51 localizes to chromosomes (damaged chromatin / repair foci). Reason: Chromosomal localization at repair sites; supported by multiple EXP studies and IEA. |
| GO:0005694 chromosome | EXP PMID:27797818 The MMS22L-TONSL heterodimer directly promotes RAD51-depende... | ACCEPT | Summary: RAD51 localizes to chromosomes (damaged chromatin / repair foci). Reason: Chromosomal localization at repair sites; supported by multiple EXP studies and IEA. |
| GO:0005694 chromosome | EXP PMID:31844045 ATAD5 promotes replication restart by regulating RAD51 and P... | ACCEPT | Summary: RAD51 localizes to chromosomes (damaged chromatin / repair foci). Reason: Chromosomal localization at repair sites; supported by multiple EXP studies and IEA. |
| GO:0005759 mitochondrial matrix | EXP PMID:20413593 Discovery of a novel function for human Rad51: maintenance o... | KEEP AS NON CORE | Summary: Mitochondrial matrix localization. Reason: Mitochondrial matrix pool consistent with mtDNA maintenance role (PMID:20413593); non-core. Supporting Evidence: PMID:20413593 identify human mtDNA as a novel Rad51 substrate |
| GO:0016887 ATP hydrolysis activity | EXP PMID:15226506 Ca2+ activates human homologous recombination protein Rad51 ... | ACCEPT | Summary: RAD51 hydrolyzes ATP; the self-inactivating ATPase controls presynaptic filament turnover. Reason: Experimentally demonstrated DNA-dependent ATPase; rapid ATP hydrolysis with slow ADP release converts the filament to an inactive state, and Ca2+/slowed hydrolysis stimulates strand exchange (PMID:15226506). Supporting Evidence: PMID:15226506 due to relatively rapid ATP hydrolysis and slow dissociation of ADP |
| GO:0000150 DNA strand exchange activity | IDA PMID:15226506 Ca2+ activates human homologous recombination protein Rad51 ... | ACCEPT | Summary: RAD51 catalyzes ATP-dependent homologous DNA pairing and strand exchange, the defining recombinase activity of homologous recombination. Reason: Core molecular function of RAD51. The human protein forms a helical nucleoprotein filament on ssDNA and promotes homology search and strand transfer in vitro; supported by multiple independent IDA/IMP studies and the IBA phylogenetic inference. Supporting Evidence: PMID:15226506 stimulates DNA strand exchange activity of hRad51 protein |
| GO:0032993 protein-DNA complex | IDA PMID:15226506 Ca2+ activates human homologous recombination protein Rad51 ... | ACCEPT | Summary: RAD51 is part of a protein-DNA complex (the nucleoprotein filament). Reason: Accurate cellular-component/complex term for the RAD51-ssDNA nucleoprotein filament (PMID:15226506). |
| GO:0000150 DNA strand exchange activity | IDA PMID:27694622 The Ξ²-isoform of BCCIP promotes ADP release from the RAD51 p... | ACCEPT | Summary: RAD51 catalyzes ATP-dependent homologous DNA pairing and strand exchange, the defining recombinase activity of homologous recombination. Reason: Core molecular function of RAD51. The human protein forms a helical nucleoprotein filament on ssDNA and promotes homology search and strand transfer in vitro; supported by multiple independent IDA/IMP studies and the IBA phylogenetic inference. |
| GO:0042148 DNA strand invasion | IDA PMID:27694622 The Ξ²-isoform of BCCIP promotes ADP release from the RAD51 p... | ACCEPT | Summary: RAD51 catalyzes DNA strand invasion, base-pairing the presynaptic filament ssDNA into homologous duplex to form the D-loop. Reason: Directly demonstrated (PMID:27694622) and inferred by IBA; a defining step of the recombinase mechanism. Supporting Evidence: PMID:27694622 displacing the homologous strand to form a displacement loop (D-loop) |
| GO:0006310 DNA recombination | IDA PMID:8929543 Human Rad51 protein promotes ATP-dependent homologous pairin... | ACCEPT | Summary: RAD51 mediates DNA recombination (homologous recombination). Reason: Broad but core process term for RAD51's recombinase role; supported by IDA and TAS. |
| GO:0005739 mitochondrion | HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an... | KEEP AS NON CORE | Summary: Mitochondrion localization. Reason: RAD51 has a separable mitochondrial pool involved in mtDNA copy-number maintenance under oxidative stress (PMID:20413593); non-core relative to nuclear HR. |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:26811421 TOPBP1 regulates RAD51 phosphorylation and chromatin loading... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0035861 site of double-strand break | IDA PMID:26811421 TOPBP1 regulates RAD51 phosphorylation and chromatin loading... | ACCEPT | Summary: RAD51 is active at sites of double-strand breaks (damage-induced foci / repair centers). Reason: The functional site of the RAD51 recombinase; supported by multiple IDA studies showing localization to DSB sites and by ortholog IEA. |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:32640219 The ZGRF1 Helicase Promotes Recombinational Repair of Replic... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0005515 protein binding | IPI PMID:32640219 The ZGRF1 Helicase Promotes Recombinational Repair of Replic... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0000150 DNA strand exchange activity | IDA PMID:18417535 Identification of a novel human Rad51 variant that promotes ... | ACCEPT | Summary: RAD51 catalyzes ATP-dependent homologous DNA pairing and strand exchange, the defining recombinase activity of homologous recombination. Reason: Core molecular function of RAD51. The human protein forms a helical nucleoprotein filament on ssDNA and promotes homology search and strand transfer in vitro; supported by multiple independent IDA/IMP studies and the IBA phylogenetic inference. Supporting Evidence: PMID:18417535 Identification of a novel human Rad51 variant that promotes DNA strand exchange |
| GO:0005515 protein binding | IPI PMID:27797818 The MMS22L-TONSL heterodimer directly promotes RAD51-depende... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0003697 single-stranded DNA binding | IDA PMID:8929543 Human Rad51 protein promotes ATP-dependent homologous pairin... | ACCEPT | Summary: RAD51 binds single-stranded DNA to nucleate the presynaptic nucleoprotein filament. Reason: Well-established core activity; RAD51 binds ssDNA (the 3' resected overhang) in an ATP-dependent manner as the first step of filament assembly. Supported by biochemistry (IDA/IMP) and IBA/ISS. |
| GO:0099182 presynaptic intermediate filament cytoskeleton | IDA PMID:18003859 RECQL5/Recql5 helicase regulates homologous recombination an... | MODIFY | Summary: Annotation places RAD51 in the 'presynaptic intermediate filament cytoskeleton' (a neuronal synapse term). Reason: This is a misnomer-driven mis-mapping: PMID:18003859 concerns disruption of the RAD51 *presynaptic (nucleoprotein) filament* of homologous recombination, not a neuronal presynaptic cytoskeleton. The correct component is the RAD51-ssDNA nucleoprotein filament. Proposed replacements: protein-DNA complex Supporting Evidence: PMID:18003859 disruption of Rad51 presynaptic filaments |
| GO:0005515 protein binding | IPI PMID:26833090 Non-catalytic Roles for XPG with BRCA1 and BRCA2 in Homologo... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005634 nucleus | IDA PMID:26833090 Non-catalytic Roles for XPG with BRCA1 and BRCA2 in Homologo... | ACCEPT | Summary: RAD51 localizes to the nucleus, its principal site of action. Reason: Predominant and functionally relevant localization; supported by many EXP/IDA studies and IEA. |
| GO:0032991 protein-containing complex | IDA PMID:26833090 Non-catalytic Roles for XPG with BRCA1 and BRCA2 in Homologo... | MARK AS OVER ANNOTATED | Summary: Protein-containing complex (generic). Reason: Uninformative generic complex term; the specific relevant assemblies (HR/BRCA2-PALB2 complex, nucleoprotein filament) are captured elsewhere. |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:17996710 RAD51AP1 is a structure-specific DNA binding protein that st... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:17996711 Promotion of homologous recombination and genomic stability ... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:27239033 Promotion of RAD51-Mediated Homologous DNA Pairing by the RA... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0005515 protein binding | IPI PMID:17996710 RAD51AP1 is a structure-specific DNA binding protein that st... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:17996711 Promotion of homologous recombination and genomic stability ... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0006974 DNA damage response | IDA PMID:17996710 RAD51AP1 is a structure-specific DNA binding protein that st... | ACCEPT | Summary: RAD51 participates in the cellular DNA damage response, forming damage-induced nuclear foci. Reason: Well supported by IDA; RAD51 is recruited to DNA damage sites and forms IR/CPT-induced foci. |
| GO:0006974 DNA damage response | IDA PMID:17996711 Promotion of homologous recombination and genomic stability ... | ACCEPT | Summary: RAD51 participates in the cellular DNA damage response, forming damage-induced nuclear foci. Reason: Well supported by IDA; RAD51 is recruited to DNA damage sites and forms IR/CPT-induced foci. |
| GO:0006974 DNA damage response | IDA PMID:27239033 Promotion of RAD51-Mediated Homologous DNA Pairing by the RA... | ACCEPT | Summary: RAD51 participates in the cellular DNA damage response, forming damage-induced nuclear foci. Reason: Well supported by IDA; RAD51 is recruited to DNA damage sites and forms IR/CPT-induced foci. |
| GO:0003682 chromatin binding | IDA PMID:23401855 The MCM8-MCM9 complex promotes RAD51 recruitment at DNA dama... | ACCEPT | Summary: RAD51 binds chromatin, consistent with its recruitment to damaged chromatin. Reason: RAD51 associates with chromatin (e.g. via MCM8-MCM9-dependent recruitment); IDA PMID:23401855. |
| GO:0019899 enzyme binding | IPI PMID:23401855 The MCM8-MCM9 complex promotes RAD51 recruitment at DNA dama... | MARK AS OVER ANNOTATED | Summary: Enzyme binding (interactions with MCM8/MCM9 helicase complex, PMID:23401855). Reason: Generic binding term; the underlying interaction is real but does not by itself convey a molecular function. Non-core. |
| GO:0019899 enzyme binding | IPI PMID:23401855 The MCM8-MCM9 complex promotes RAD51 recruitment at DNA dama... | MARK AS OVER ANNOTATED | Summary: Enzyme binding (interactions with MCM8/MCM9 helicase complex, PMID:23401855). Reason: Generic binding term; the underlying interaction is real but does not by itself convey a molecular function. Non-core. |
| GO:0005515 protein binding | IPI PMID:28575657 RPA-Mediated Recruitment of the E3 Ligase RFWD3 Is Vital for... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:16990250 RAD51AP2, a novel vertebrate- and meiotic-specific protein, ... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:16990250 RAD51AP2, a novel vertebrate- and meiotic-specific protein, ... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:16990250 RAD51AP2, a novel vertebrate- and meiotic-specific protein, ... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0032991 protein-containing complex | IDA PMID:16990250 RAD51AP2, a novel vertebrate- and meiotic-specific protein, ... | MARK AS OVER ANNOTATED | Summary: Protein-containing complex (generic). Reason: Uninformative generic complex term; the specific relevant assemblies (HR/BRCA2-PALB2 complex, nucleoprotein filament) are captured elsewhere. |
| GO:0036297 interstrand cross-link repair | IMP PMID:26253028 A Dominant Mutation in Human RAD51 Reveals Its Function in D... | ACCEPT | Summary: RAD51 participates in interstrand crosslink (ICL) repair. Reason: A dominant RAD51 variant (FANCR) reveals a role in ICL repair separable from HR (PMID:26253028); IMP-supported. Supporting Evidence: PMID:26253028 Function in DNA Interstrand Crosslink Repair Independent of Homologous Recombination |
| GO:0000800 lateral element | IDA PMID:9774970 Stable interaction between the products of the BRCA1 and BRC... | KEEP AS NON CORE | Summary: Lateral element (meiotic synaptonemal complex structure). Reason: Meiosis-specific localization; non-core in somatic context (IDA PMID:9774970). |
| GO:0000724 double-strand break repair via homologous recombination | IMP PMID:26681308 A novel Fanconi anaemia subtype associated with a dominant-n... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. Supporting Evidence: PMID:26681308 dominant-negative mutation |
| GO:0003690 double-stranded DNA binding | IMP PMID:26681308 A novel Fanconi anaemia subtype associated with a dominant-n... | ACCEPT | Summary: RAD51 binds double-stranded DNA, required for homology search and filament interactions with duplex donor. Reason: RAD51 binds dsDNA (donor duplex during homology search and forms filaments on dsDNA); demonstrated biochemically (IDA/IMP) and inferred by IBA/IEA. |
| GO:0003697 single-stranded DNA binding | IMP PMID:26681308 A novel Fanconi anaemia subtype associated with a dominant-n... | ACCEPT | Summary: RAD51 binds single-stranded DNA to nucleate the presynaptic nucleoprotein filament. Reason: Well-established core activity; RAD51 binds ssDNA (the 3' resected overhang) in an ATP-dependent manner as the first step of filament assembly. Supported by biochemistry (IDA/IMP) and IBA/ISS. |
| GO:0005634 nucleus | IDA PMID:26681308 A novel Fanconi anaemia subtype associated with a dominant-n... | ACCEPT | Summary: RAD51 localizes to the nucleus, its principal site of action. Reason: Predominant and functionally relevant localization; supported by many EXP/IDA studies and IEA. |
| GO:0005737 cytoplasm | IDA PMID:26681308 A novel Fanconi anaemia subtype associated with a dominant-n... | KEEP AS NON CORE | Summary: Cytoplasm localization. Reason: Cytoplasmic reservoir of RAD51 prior to nuclear import/loading; non-core relative to its nuclear function. |
| GO:0006974 DNA damage response | IMP PMID:26681308 A novel Fanconi anaemia subtype associated with a dominant-n... | ACCEPT | Summary: RAD51 participates in the cellular DNA damage response, forming damage-induced nuclear foci. Reason: Well supported by IDA; RAD51 is recruited to DNA damage sites and forms IR/CPT-induced foci. |
| GO:0000785 chromatin | IDA PMID:26323318 NUCKS1 is a novel RAD51AP1 paralog important for homologous ... | ACCEPT | Summary: RAD51 localizes to chromatin. Reason: Chromatin localization consistent with recruitment to damaged/replicating chromatin (IDA). |
| GO:0005515 protein binding | IPI PMID:26323318 NUCKS1 is a novel RAD51AP1 paralog important for homologous ... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005634 nucleus | IDA PMID:26323318 NUCKS1 is a novel RAD51AP1 paralog important for homologous ... | ACCEPT | Summary: RAD51 localizes to the nucleus, its principal site of action. Reason: Predominant and functionally relevant localization; supported by many EXP/IDA studies and IEA. |
| GO:0005515 protein binding | IPI PMID:22641345 Nucleostemin prevents telomere damage by promoting PML-IV re... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0000722 telomere maintenance via recombination | ISS PMID:21076401 BRCA2 acts as a RAD51 loader to facilitate telomere replicat... | KEEP AS NON CORE | Summary: Telomere maintenance via recombination (ALT context). Reason: Recombination-based telomere maintenance; a context-specific role (ortholog ISS/IEA), non-core. |
| GO:0010833 telomere maintenance via telomere lengthening | ISS PMID:21076401 BRCA2 acts as a RAD51 loader to facilitate telomere replicat... | KEEP AS NON CORE | Summary: Telomere maintenance via telomere lengthening. Reason: Telomere-lengthening role in recombination-based maintenance; non-core (ISS/IEA). |
| GO:0000724 double-strand break repair via homologous recombination | IMP PMID:22778135 RAD51 mutants cause replication defects and chromosomal inst... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0000781 chromosome, telomeric region | IDA PMID:21076401 BRCA2 acts as a RAD51 loader to facilitate telomere replicat... | KEEP AS NON CORE | Summary: Chromosome, telomeric region (localization). Reason: Telomeric localization in the ALT/recombination context; non-core (IDA/IEA). |
| GO:0031297 replication fork processing | IMP PMID:22778135 RAD51 mutants cause replication defects and chromosomal inst... | ACCEPT | Summary: RAD51 acts in replication fork processing β protection and restart of stalled/damaged forks. Reason: Core replication-stress function; supported experimentally (PMID:18417535, PMID:22778135, PMID:25585578) and by ortholog inference. RAD51 protects nascent DNA and enables fork restart. Supporting Evidence: PMID:22778135 RAD51 mutants cause replication defects and chromosomal instability |
| GO:0000785 chromatin | IDA PMID:25585578 FBH1 influences DNA replication fork stability and homologou... | ACCEPT | Summary: RAD51 localizes to chromatin. Reason: Chromatin localization consistent with recruitment to damaged/replicating chromatin (IDA). |
| GO:0005515 protein binding | IPI PMID:23393192 Single-molecule sorting reveals how ubiquitylation affects s... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:24108124 FBH1 helicase disrupts RAD51 filaments in vitro and modulate... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:25585578 FBH1 influences DNA replication fork stability and homologou... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:25585578 FBH1 influences DNA replication fork stability and homologou... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005634 nucleus | IDA PMID:25585578 FBH1 influences DNA replication fork stability and homologou... | ACCEPT | Summary: RAD51 localizes to the nucleus, its principal site of action. Reason: Predominant and functionally relevant localization; supported by many EXP/IDA studies and IEA. |
| GO:0005737 cytoplasm | IDA PMID:25585578 FBH1 influences DNA replication fork stability and homologou... | KEEP AS NON CORE | Summary: Cytoplasm localization. Reason: Cytoplasmic reservoir of RAD51 prior to nuclear import/loading; non-core relative to its nuclear function. |
| GO:0006974 DNA damage response | IDA PMID:25585578 FBH1 influences DNA replication fork stability and homologou... | ACCEPT | Summary: RAD51 participates in the cellular DNA damage response, forming damage-induced nuclear foci. Reason: Well supported by IDA; RAD51 is recruited to DNA damage sites and forms IR/CPT-induced foci. |
| GO:0031297 replication fork processing | IDA PMID:25585578 FBH1 influences DNA replication fork stability and homologou... | ACCEPT | Summary: RAD51 acts in replication fork processing β protection and restart of stalled/damaged forks. Reason: Core replication-stress function; supported experimentally (PMID:18417535, PMID:22778135, PMID:25585578) and by ortholog inference. RAD51 protects nascent DNA and enables fork restart. |
| GO:0035861 site of double-strand break | IDA PMID:24550317 PARP1-dependent recruitment of KDM4D histone demethylase to ... | ACCEPT | Summary: RAD51 is active at sites of double-strand breaks (damage-induced foci / repair centers). Reason: The functional site of the RAD51 recombinase; supported by multiple IDA studies showing localization to DSB sites and by ortholog IEA. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685230 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685341 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685838 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686410 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686440 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686469 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686483 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693539 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693561 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693584 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693589 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693593 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693620 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9701199 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9704330 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9704408 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9709571 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9709601 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9853389 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005515 protein binding | IPI PMID:25642963 Homologous-recombination-deficient tumours are dependent on ... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0000724 double-strand break repair via homologous recombination | IMP PMID:23509288 Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndro... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0005515 protein binding | IPI PMID:23509288 Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndro... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0006974 DNA damage response | IDA PMID:23509288 Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndro... | ACCEPT | Summary: RAD51 participates in the cellular DNA damage response, forming damage-induced nuclear foci. Reason: Well supported by IDA; RAD51 is recruited to DNA damage sites and forms IR/CPT-induced foci. |
| GO:0071479 cellular response to ionizing radiation | IDA PMID:23509288 Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndro... | KEEP AS NON CORE | Summary: Cellular response to ionizing radiation (RAD51 focus formation after IR). Reason: Experimentally supported stimulus-response wrapper around the core DSB-repair function; kept as non-core. |
| GO:0072757 cellular response to camptothecin | IDA PMID:23509288 Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndro... | KEEP AS NON CORE | Summary: Cellular response to camptothecin. Reason: Stimulus-specific response (CPT induces replication-associated DSBs); non-core context (PMID:23509288). |
| GO:0000228 nuclear chromosome | IDA PMID:23754376 FIGNL1-containing protein complex is required for efficient ... | ACCEPT | Summary: RAD51 localizes to the nuclear chromosome. Reason: Nuclear chromosome localization at damage-induced foci (IDA PMID:23754376). |
| GO:0005515 protein binding | IPI PMID:23754376 FIGNL1-containing protein complex is required for efficient ... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:23754376 FIGNL1-containing protein complex is required for efficient ... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:23754376 FIGNL1-containing protein complex is required for efficient ... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0010569 regulation of double-strand break repair via homologous recombination | IDA PMID:23754376 FIGNL1-containing protein complex is required for efficient ... | KEEP AS NON CORE | Summary: Regulation of DSB repair via homologous recombination. Reason: RAD51 filament dynamics/abundance modulate HR outcome (e.g. via FIGNL1, PMID:23754376); regulatory framing, non-core relative to the effector recombinase role. |
| GO:0071479 cellular response to ionizing radiation | IDA PMID:23754376 FIGNL1-containing protein complex is required for efficient ... | KEEP AS NON CORE | Summary: Cellular response to ionizing radiation (RAD51 focus formation after IR). Reason: Experimentally supported stimulus-response wrapper around the core DSB-repair function; kept as non-core. |
| GO:0070182 DNA polymerase binding | IPI PMID:19995904 DNA polymerase POLN participates in cross-link repair and ho... | KEEP AS NON CORE | Summary: DNA polymerase binding β direct interaction with POLN (DNA polymerase nu). Reason: More specific than 'protein binding'; documents a real interaction (PMID:19995904) relevant to a subset of repair, but not a core RAD51 function. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686642 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686657 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686663 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693564 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9007582 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9853878 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9980006 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9980021 | ACCEPT | Summary: RAD51 functions in the nucleoplasm. Reason: Nucleoplasmic localization consistent with nuclear HR reactions; Reactome TAS pathway annotations. Accepted as a valid core location. |
| GO:0005515 protein binding | IPI PMID:22153967 Inhibition of homologous recombination by the PCNA-interacti... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:15665856 The cell-cycle checkpoint kinase Chk1 is required for mammal... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:9461559 Regulation of Rad51 function by c-Abl in response to DNA dam... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005634 nucleus | IDA PMID:18417535 Identification of a novel human Rad51 variant that promotes ... | ACCEPT | Summary: RAD51 localizes to the nucleus, its principal site of action. Reason: Predominant and functionally relevant localization; supported by many EXP/IDA studies and IEA. |
| GO:0005515 protein binding | IPI PMID:20154705 A PP4 phosphatase complex dephosphorylates RPA2 to facilitat... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:21252223 The role of the human SWI5-MEI5 complex in homologous recomb... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:21252223 The role of the human SWI5-MEI5 complex in homologous recomb... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:20871616 Enhancement of RAD51 recombinase activity by the tumor suppr... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:20729832 Purified human BRCA2 stimulates RAD51-mediated recombination... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005634 nucleus | IDA PMID:16215984 Cellular localization of human Rad51C and regulation of ubiq... | ACCEPT | Summary: RAD51 localizes to the nucleus, its principal site of action. Reason: Predominant and functionally relevant localization; supported by many EXP/IDA studies and IEA. |
| GO:0005737 cytoplasm | IDA PMID:16215984 Cellular localization of human Rad51C and regulation of ubiq... | KEEP AS NON CORE | Summary: Cytoplasm localization. Reason: Cytoplasmic reservoir of RAD51 prior to nuclear import/loading; non-core relative to its nuclear function. |
| GO:0048471 perinuclear region of cytoplasm | IDA PMID:16215984 Cellular localization of human Rad51C and regulation of ubiq... | KEEP AS NON CORE | Summary: Perinuclear region of cytoplasm. Reason: Perinuclear cytoplasmic localization (PMID:16215984); non-core. |
| GO:0005739 mitochondrion | IDA PMID:20413593 Discovery of a novel function for human Rad51: maintenance o... | KEEP AS NON CORE | Summary: Mitochondrion localization. Reason: RAD51 has a separable mitochondrial pool involved in mtDNA copy-number maintenance under oxidative stress (PMID:20413593); non-core relative to nuclear HR. Supporting Evidence: PMID:20413593 identify human mtDNA as a novel Rad51 substrate |
| GO:0005515 protein binding | IPI PMID:11309417 Regulation and localization of the Bloom syndrome protein in... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0016605 PML body | IDA PMID:11309417 Regulation and localization of the Bloom syndrome protein in... | KEEP AS NON CORE | Summary: PML body localization. Reason: RAD51 localizes to PML nuclear bodies (PMID:11309417); minor, non-core. |
| GO:0005515 protein binding | IPI PMID:16756962 XPA versus ERCC1 as chemosensitising agents to cisplatin and... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:17515903 Interaction with the BRCA2 C terminus protects RAD51-DNA fil... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:16428451 Differential contributions of mammalian Rad54 paralogs to re... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0005524 ATP binding | IDA PMID:16428451 Differential contributions of mammalian Rad54 paralogs to re... | ACCEPT | Summary: RAD51 binds ATP; nucleotide state governs the active vs inactive conformation of the filament. Reason: ATP binding is intrinsic to RAD51 (Walker A/B motifs) and regulates filament activity; supported experimentally (IDA PMID:16428451) and by IEA. |
| GO:0005515 protein binding | IPI PMID:12242698 Highlight: BRCA1 and BRCA2 proteins in breast cancer. | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005515 protein binding | IPI PMID:9396801 A novel nucleic acid-binding protein that interacts with hum... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0005634 nucleus | ISS GO_REF:0000024 | ACCEPT | Summary: RAD51 localizes to the nucleus, its principal site of action. Reason: Predominant and functionally relevant localization; supported by many EXP/IDA studies and IEA. |
| GO:0000793 condensed chromosome | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Condensed chromosome. Reason: Chromosome-condensation-associated localization (largely meiotic/mitotic); non-core (ISS). |
| GO:0000794 condensed nuclear chromosome | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Condensed nuclear chromosome. Reason: Localization to condensed chromosomes (meiotic/mitotic); non-core (IBA/ISS). |
| GO:0006310 DNA recombination | TAS PMID:7988572 Purification and characterization of the human Rad51 protein... | ACCEPT | Summary: RAD51 mediates DNA recombination (homologous recombination). Reason: Broad but core process term for RAD51's recombinase role; supported by IDA and TAS. |
| GO:0051321 meiotic cell cycle | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Meiotic cell cycle. Reason: Meiotic role; non-core (ISS). |
| GO:0000724 double-strand break repair via homologous recombination | TAS PMID:12427746 Complex formation by the human Rad51B and Rad51C DNA repair ... | ACCEPT | Summary: RAD51 is the essential effector of double-strand break repair via homologous recombination. Reason: Central biological role of RAD51, supported by extensive experimental evidence (numerous IDA/IMP) and IBA/IEA; RAD51 performs the strand-invasion step of HR-mediated DSB repair. |
| GO:0003690 double-stranded DNA binding | IDA PMID:7988572 Purification and characterization of the human Rad51 protein... | ACCEPT | Summary: RAD51 binds double-stranded DNA, required for homology search and filament interactions with duplex donor. Reason: RAD51 binds dsDNA (donor duplex during homology search and forms filaments on dsDNA); demonstrated biochemically (IDA/IMP) and inferred by IBA/IEA. Supporting Evidence: PMID:7988572 The human Rad51 protein binds to single- and double-stranded DNA and exhibits DNA-dependent ATPase activity. |
| GO:0003697 single-stranded DNA binding | IDA PMID:7988572 Purification and characterization of the human Rad51 protein... | ACCEPT | Summary: RAD51 binds single-stranded DNA to nucleate the presynaptic nucleoprotein filament. Reason: Well-established core activity; RAD51 binds ssDNA (the 3' resected overhang) in an ATP-dependent manner as the first step of filament assembly. Supported by biochemistry (IDA/IMP) and IBA/ISS. Supporting Evidence: PMID:7988572 The human Rad51 protein binds to single- and double-stranded DNA and exhibits DNA-dependent ATPase activity. |
| GO:0005515 protein binding | IPI PMID:8675009 The XPB and XPD DNA helicases are components of the p53-medi... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
| GO:0006281 DNA repair | TAS PMID:8358431 Cloning of human, mouse and fission yeast recombination gene... | ACCEPT | Summary: RAD51 functions in DNA repair (homologous recombination arm). Reason: Broad but accurate core process (parent of DSBR via HR); retained. |
| GO:0006312 mitotic recombination | TAS PMID:8358431 Cloning of human, mouse and fission yeast recombination gene... | ACCEPT | Summary: RAD51 functions in mitotic (somatic) homologous recombination. Reason: Core somatic role; IBA and TAS supported. |
| GO:0007131 reciprocal meiotic recombination | TAS PMID:8358431 Cloning of human, mouse and fission yeast recombination gene... | KEEP AS NON CORE | Summary: Reciprocal meiotic recombination (crossover). Reason: RAD51 supports meiotic HR as a non-catalytic accessory to the meiosis-specific recombinase DMC1; a real but tissue-restricted, non-core role. |
| GO:0005634 nucleus | IDA PMID:12442171 Insights into DNA recombination from the structure of a RAD5... | ACCEPT | Summary: RAD51 localizes to the nucleus, its principal site of action. Reason: Predominant and functionally relevant localization; supported by many EXP/IDA studies and IEA. |
| GO:0005515 protein binding | IPI PMID:12442171 Insights into DNA recombination from the structure of a RAD5... | MARK AS OVER ANNOTATED | Summary: Generic protein binding supported by many pairwise interaction (IPI) experiments with HR partners (BRCA2, PALB2, RAD51AP1, RAD54L, XRCC3, RAD51C, TP53, SPIDR, FIGNL1, TOPBP1, MCM8/9, etc.). Reason: Per curation guidelines, 'protein binding' is uninformative as a molecular function. The individual interactions are real and biologically important but are captured in UniProt SUBUNIT and in the specific process annotations; not a core function. |
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Download this section (compressed HTML)Q: To what extent are RAD51's mitochondrial mtDNA-maintenance and nuclear HR functions mechanistically separable, and does mitochondrial RAD51 act as a recombinase there?
Q: How is the balance between RAD51 filament stabilization (BRCA2, RAD51AP1) and active dismantling (FIGNL1, RECQL5, PARI/PARPBP) controlled to switch between HR and fork protection outcomes?
Experiment: Separation-of-function RAD51 mutants (e.g. FANCR-type dominant variants) assayed in parallel for HR, replication fork protection, and ICL repair to map the domains/activities specific to each process.
Experiment: Single-molecule / cryo-EM analysis of RAD51 filament dynamics on nucleosomal versus naked DNA to quantify the nucleosome-peeling step and its ATP dependence.
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