BLM is a RecQ-family ATP-dependent DNA helicase that moves with 3-prime-to-5-prime polarity and remodels branched DNA structures during genome maintenance. Its helicase, RecQ C-terminal and HRDC regions recognize and process duplex overhangs, replication forks, Holliday junctions, D-loops and G-quadruplex DNA. In the BLM–TOP3A–RMI1–RMI2 complex, BLM drives convergent branch migration and TOP3A removes the resulting DNA entanglement, promoting non-crossover recombination products. BLM also cooperates with DNA2 and EXO1 during DNA-end resection and with shelterin-associated proteins during telomeric DNA processing. It can anneal complementary DNA strands, an activity that cooperates with unwinding during fork remodeling. Nuclear BLM is enriched at repair-associated chromatin and PML nuclear bodies, with localization changing through the cell cycle and after DNA damage. Loss of BLM causes Bloom syndrome and a marked increase in sister-chromatid exchange and chromosome instability.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000079 regulation of cyclin-dependent protein serine/threonine kinase activity | IMP PMID:15604258 A major role for mitotic CDC2 kinase inactivation in the est... | UNDECIDED | Summary: The kinase-regulation assertion requires the original experimental context. Reason: The complete cached abstract uses mitotic BLM phosphorylation as a readout of CDC2 activity. It does not establish that BLM regulates CDC2. The full experimental evidence underlying this IMP assertion was not accessible in the normal cache, and publisher access attempts did not recover it; this remains unresolved rather than being removed on abstract-only evidence. Supporting Evidence: |
| GO:0000166 nucleotide binding | IEA GO_REF:0000002 | MODIFY | Summary: Refine nucleotide binding to ATP binding. Reason: The InterPro domain inference is compatible with the ATP-dependent RecQ motor. ATP binding and hydrolysis are directly supported by the BLM biochemistry; ATP binding is a more informative replacement for this broad nucleotide term. The electronic source and InterPro identifier remain unchanged. Proposed replacements: ATP binding |
| GO:0000228 nuclear chromosome | IDA PMID:23509288 Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndro... | ACCEPT | Summary: BLM associates with nuclear chromosomes at DNA lesions. Reason: The SPIDR study supports BLM localization at damaged-chromosome foci, together with the independent PMID:11309417 evidence. Relevant external Results and Figure 1 were now inspected despite the incomplete normal cache. This updates access scope without changing the accepted location or claiming a whole-paper audit. |
| GO:0000400 four-way junction DNA binding | IDA PMID:11735402 Inhibition of the Bloom's and Werner's syndrome helicases by... | ACCEPT | Summary: Retain recognition of the annotated branched DNA substrate. Reason: The original abstract concerns G-quadruplex recognition and ligand effects; the exact four-way-junction assay is not visible there. Independently read HRDC binding and full-length branch-migration experiments establish engagement of Holliday-junction DNA. Recognition of this substrate contributes to DNA remodeling; it does not create an additional independent core activity. |
| GO:0000400 four-way junction DNA binding | IDA PMID:20639533 Structure and function of the regulatory HRDC domain from hu... | ACCEPT | Summary: The human HRDC domain binds Holliday-junction DNA. Reason: Selected Methods and Results assay purified human BLM residues 1210–1294. Holliday-junction complexes were observed and altered by HRDC substitutions; these assays support the binding term while retaining the isolated-domain/high-concentration context. Supporting Evidence: PMID:20639533 the HJ binding of BLM HRDC is much favorable to ssDNA |
| GO:0000400 four-way junction DNA binding | IDA PMID:25901030 Crystal structure of the Bloom's syndrome helicase indicates... | ACCEPT | Summary: Retain recognition of the annotated branched DNA substrate. Reason: The selected full-length BLM assays test a four-way-junction substrate and its ATP-dependent branch migration, consistent with junction recognition by the helicase. Recognition of this substrate contributes to DNA remodeling; it does not create an additional independent core activity. Supporting Evidence: |
| GO:0000403 Y-form DNA binding | IDA PMID:11735402 Inhibition of the Bloom's and Werner's syndrome helicases by... | ACCEPT | Summary: Retain recognition of the annotated branched DNA substrate. Reason: Y-shaped substrate recognition is consistent with the forked duplex used in the independently read BLM helicase assays. The original ligand-study abstract does not expose its complete substrate panel. Recognition of this substrate contributes to DNA remodeling; it does not create an additional independent core activity. |
| GO:0000405 bubble DNA binding | IDA PMID:11433031 The Bloom's and Werner's syndrome proteins are DNA structure... | ACCEPT | Summary: Retain recognition of the annotated branched DNA substrate. Reason: The complete abstract explicitly compares bubble-containing substrates with other DNA structures and reports efficient BLM unwinding; this is substrate engagement by the motor. Recognition of this substrate contributes to DNA remodeling; it does not create an additional independent core activity. Supporting Evidence: |
| GO:0000405 bubble DNA binding | IDA PMID:11735402 Inhibition of the Bloom's and Werner's syndrome helicases by... | ACCEPT | Summary: Retain recognition of the annotated branched DNA substrate. Reason: The original abstract does not expose its complete bubble-substrate panel. Independent BLM substrate-specificity biochemistry reports efficient unwinding of bubble-containing duplexes, supporting the existing assertion. Recognition of this substrate contributes to DNA remodeling; it does not create an additional independent core activity. |
| GO:0000723 telomere maintenance | IBA GO_REF:0000033 | ACCEPT | Summary: Retain inherited telomere-maintenance function. Reason: The actual PTHR13710 PAINT table places this IBD at PTN002672422 with human BLM and mouse Blm experimental descendants. Human BLM in the source set is legitimate descendant evidence, not circularity. Human telomeric D-loop and shelterin-partner studies independently support the function. No tree/MSA re-curation is claimed. |
| GO:0000723 telomere maintenance | IDA PMID:11735402 Inhibition of the Bloom's and Werner's syndrome helicases by... | ACCEPT | Summary: BLM contributes directly to telomeric DNA maintenance. Reason: The ligand-study abstract proposes telomere relevance rather than demonstrating a complete cellular maintenance pathway. Independent human BLM–TRF1/TRF2 experiments and BLM/POT1 telomeric D-loop unwinding supply functional context for retaining this existing process. BLM itself remodels the DNA substrate. |
| GO:0000723 telomere maintenance | IEA GO_REF:0000117 | ACCEPT | Summary: Retain the electronic telomere-maintenance assertion. Reason: This ARBA inference agrees with BLM engagement and unwinding of telomeric DNA structures and its functional interaction with telomeric proteins. The inference is not relabeled as direct experimental evidence. |
| GO:0000724 double-strand break repair via homologous recombination | IBA GO_REF:0000033 | ACCEPT | Summary: Homologous recombination repair is an inherited BLM function. Reason: The actual PTHR13710 IBD for GO:0000724 is at PTN000344874 and includes human BLM experimental grounding. BLM supplies DNA strand remodeling during end processing and recombination-intermediate dissolution. The phylogenetic assertion is retained without reinterpreting it as pairwise transfer. |
| GO:0000724 double-strand break repair via homologous recombination | IDA PMID:23543748 Role of replication protein A in double holliday junction di... | ACCEPT | Summary: BLM directly participates in homologous recombination repair. Reason: The complete abstract describes BLM–TOP3A–RMI1–RMI2 dissolution of double Holliday junctions, stimulated by RPA. BLM performs the helicase component of this reaction, yielding non-crossover repair products; RPA contacts with RMI1 do not make BLM the RPA-binding subunit in every experiment. Supporting Evidence: |
| GO:0000724 double-strand break repair via homologous recombination | IEA GO_REF:0000117 | ACCEPT | Summary: Retain homologous recombination repair from ARBA. Reason: The electronic inference is consistent with reconstituted BLM-dependent end processing and double-Holliday-junction dissolution. This is direct DNA work within repair, not a process assigned solely from the Bloom syndrome phenotype. |
| GO:0000724 double-strand break repair via homologous recombination | NAS PMID:11309417 Regulation and localization of the Bloom syndrome protein in... | ACCEPT | Summary: Retain the repair role inferred from BLM damage-focus behavior. Reason: Selected human-cell Results place BLM with RAD51 at irradiation-induced foci and presumptive repair-associated single-stranded DNA. Later reconstitution and BLM-mutant complementation independently strengthen the homologous-recombination interpretation; the original NAS evidence code is preserved. |
| GO:0000729 DNA double-strand break processing | IDA PMID:21325134 BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end... | ACCEPT | Summary: BLM unwinding drives DNA-end resection with DNA2. Reason: The complete abstract reports reconstitution using human proteins: BLM helicase activity is required for DNA2-dependent resection, while BLM stimulation of EXO1 uses a distinct noncatalytic mechanism. BLM therefore performs an actual step in double-strand-break end processing. Supporting Evidence: PMID:21325134 requires BLM helicase and DNA2 nuclease functions |
| GO:0000781 chromosome, telomeric region | IDA PMID:10779560 Nuclear structure in normal and Bloom syndrome cells. | ACCEPT | Summary: Retain telomeric association of BLM. Reason: The original abstract reports BLM at a subset of telomeres in the examined human cells. Telomeric DNA processing is independently supported by the shelterin and D-loop studies; the location is not asserted to be constitutive at every chromosome end. |
| GO:0000800 lateral element | IDA PMID:10728666 Association of the Bloom syndrome protein with topoisomerase... | UNDECIDED | Summary: The exact meiotic lateral-element localization remains unverified. Reason: The abstract establishes BLM/TOP3A association in human meiotic and somatic cells but does not describe the lateral-element assay. A publisher full-text link was located but could not be opened. Retain the curator’s source assertion for resolution rather than inferring organism, stage, or misattribution from the abstract. Supporting Evidence: |
| GO:0002039 p53 binding | IPI PMID:11781842 The Bloom syndrome protein interacts and cooperates with p53... | KEEP AS NON CORE | Summary: Retain the mapped p53 interaction as a secondary regulatory contact. Reason: The abstract reports direct BLM–p53 interaction with mapped regions and p53-dependent transcription/growth effects. This specific binding is supported, but the compact core describes BLM’s DNA-processing activities rather than making p53 regulation its principal function. Supporting Evidence: |
| GO:0003676 nucleic acid binding | IEA GO_REF:0000002 | MODIFY | Summary: Refine nucleic-acid binding to DNA binding. Reason: The InterPro inference describes a nucleic-acid-binding helicase region. BLM’s tested substrates are DNA and the structural/biochemical evidence establishes direct DNA binding, so the DNA term is a supported refinement without assigning an RNA function. Proposed replacements: DNA binding |
| GO:0003677 DNA binding | IDA PMID:24816114 Structure of human Bloom's syndrome helicase in complex with... | ACCEPT | Summary: Retain direct DNA binding by the BLM catalytic core. Reason: The abstract describes a human BLM fragment bound to a duplex with a 3-prime overhang; this is direct structural evidence for the DNA substrate interface. Supporting Evidence: |
| GO:0003677 DNA binding | IEA GO_REF:0000002 | ACCEPT | Summary: Retain domain-supported DNA binding. Reason: The InterPro BLM-associated domain inference agrees with structures and binding assays of the BLM DNA-processing core. DNA binding is a mechanistic part of helicase action, not an additional unrelated activity. |
| GO:0003678 DNA helicase activity | IDA PMID:12181313 Telomere-binding protein TRF2 binds to and stimulates the We... | MODIFY | Summary: Use the established 3-prime-to-5-prime DNA helicase activity. Reason: The source reports a direct BLM–TRF2 interaction and stimulation of duplex unwinding by purified BLM. The direction-specific term is a refinement of the existing DNA-helicase assertion, corroborated by the original polarity study; the original experimental source remains intact. Proposed replacements: 3'-5' DNA helicase activity |
| GO:0003678 DNA helicase activity | IDA PMID:12818200 Characterization and mutational analysis of the RecQ core of... | MODIFY | Summary: Use the established 3-prime-to-5-prime DNA helicase activity. Reason: The source examines a monomeric human BLM642–1290 fragment expressed in E. coli, with DNA-dependent ATPase and helicase activities; the expression host is not the gene being annotated. The direction-specific term is a refinement of the existing DNA-helicase assertion, corroborated by the original polarity study; the original experimental source remains intact. Proposed replacements: 3'-5' DNA helicase activity |
| GO:0003678 DNA helicase activity | IDA PMID:17878217 Structural and functional analyses of disease-causing missen... | MODIFY | Summary: Use the established 3-prime-to-5-prime DNA helicase activity. Reason: Selected Methods and Results assay the BLM642–1290 catalytic fragment and disease-associated substitutions; strand unwinding and ATP-dependent motor function are separated from annealing. The direction-specific term is a refinement of the existing DNA-helicase assertion, corroborated by the original polarity study; the original experimental source remains intact. Proposed replacements: 3'-5' DNA helicase activity |
| GO:0003678 DNA helicase activity | IDA PMID:19734539 Telomeric D-loops containing 8-oxo-2'-deoxyguanosine are pre... | MODIFY | Summary: Use the established 3-prime-to-5-prime DNA helicase activity. Reason: The source reports preferential BLM unwinding of oxidatively damaged telomeric D-loops. The direction-specific term is a refinement of the existing DNA-helicase assertion, corroborated by the original polarity study; the original experimental source remains intact. Proposed replacements: 3'-5' DNA helicase activity |
| GO:0003678 DNA helicase activity | IDA PMID:24816114 Structure of human Bloom's syndrome helicase in complex with... | MODIFY | Summary: Use the established 3-prime-to-5-prime DNA helicase activity. Reason: The source structure identifies the DNA-bound human BLM motor with a 3-prime overhang. The direction-specific term is a refinement of the existing DNA-helicase assertion, corroborated by the original polarity study; the original experimental source remains intact. Proposed replacements: 3'-5' DNA helicase activity |
| GO:0003678 DNA helicase activity | IDA PMID:25901030 Crystal structure of the Bloom's syndrome helicase indicates... | MODIFY | Summary: Use the established 3-prime-to-5-prime DNA helicase activity. Reason: Selected Results directly assay full-length wild-type and mutant BLM on forked duplex DNA, Holliday junctions and a reconstituted dissolution substrate. The direction-specific term is a refinement of the existing DNA-helicase assertion, corroborated by the original polarity study; the original experimental source remains intact. Proposed replacements: 3'-5' DNA helicase activity |
| GO:0003678 DNA helicase activity | IDA PMID:9388193 The Bloom's syndrome gene product is a 3'-5' DNA helicase. | MODIFY | Summary: Use the established 3-prime-to-5-prime DNA helicase activity. Reason: The source directly establishes ATP/Mg-dependent human BLM DNA unwinding with 3-prime-to-5-prime polarity. The direction-specific term is a refinement of the existing DNA-helicase assertion, corroborated by the original polarity study; the original experimental source remains intact. Proposed replacements: 3'-5' DNA helicase activity Supporting Evidence: |
| GO:0003678 DNA helicase activity | IMP PMID:21325134 BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end... | MODIFY | Summary: Use the established 3-prime-to-5-prime DNA helicase activity. Reason: The human resection reconstitution requires BLM helicase activity for DNA2-dependent processing. The direction-specific term is a refinement of the existing DNA-helicase assertion, corroborated by the original polarity study; the original experimental source remains intact. Proposed replacements: 3'-5' DNA helicase activity |
| GO:0003697 single-stranded DNA binding | IDA PMID:12818200 Characterization and mutational analysis of the RecQ core of... | ACCEPT | Summary: The BLM motor fragment binds single-stranded DNA. Reason: The complete abstract reports DNA-binding and ATPase/helicase assays of the purified BLM642–1290 monomer. Single-stranded DNA recognition is intrinsic to the motor’s substrate handling. Supporting Evidence: |
| GO:0003697 single-stranded DNA binding | IDA PMID:20639533 Structure and function of the regulatory HRDC domain from hu... | ACCEPT | Summary: The isolated human HRDC domain has measurable ssDNA affinity. Reason: Selected Methods/Results use purified human BLM1210–1294 and NMR/EMSA. Binding is weak, approximately 100 micromolar in these assays, and differs from the HRDC mode of Holliday-junction recognition. The term is retained without converting weak isolated-domain binding into a high-affinity cellular interaction. Supporting Evidence: PMID:20639533 the BLM HRDC domain interacts with ssDNA |
| GO:0004386 helicase activity | IDA PMID:10871376 Potent inhibition of werner and bloom helicases by DNA minor... | MODIFY | Summary: Refine broad helicase activity to the DNA motor with established polarity. Reason: The source assays inhibition of BLM DNA unwinding by minor-groove ligands. Independent human BLM biochemistry establishes the more informative 3-prime-to-5-prime DNA helicase activity. Proposed replacements: 3'-5' DNA helicase activity |
| GO:0004386 helicase activity | IEA GO_REF:0000002 | MODIFY | Summary: Refine broad helicase activity to the DNA motor with established polarity. Reason: The InterPro RecQ-family inference identifies a helicase domain, not an RNA-specific enzyme. Independent human BLM biochemistry establishes the more informative 3-prime-to-5-prime DNA helicase activity. Proposed replacements: 3'-5' DNA helicase activity |
| GO:0005515 protein binding | IPI PMID:10728666 Association of the Bloom syndrome protein with topoisomerase... | MODIFY | Summary: Refine the TOP3A interaction to DNA topoisomerase binding. Reason: GOA identifies TOP3A/Q13472, and the complete abstract reports BLM–TOP3A association in human cells. The binding term’s definition covers DNA topoisomerases and does not assert that BLM itself catalyzes topoisomerization. BTR biochemistry corroborates the functional complex. Proposed replacements: DNA topoisomerase binding |
| GO:0005515 protein binding | IPI PMID:10825162 Replication protein A physically interacts with the Bloom's ... | KEEP AS NON CORE | Summary: Retain the experimentally supported BLM–RPA1 interaction as non-core. Reason: The complete PMID:10825162 abstract reports physical interaction of purified BLM with the 70-kDa RPA subunit and stimulation of long-duplex unwinding. This establishes the source-specific interaction. The regulatory direction is from RPA to BLM; it does not give BLM an RPA-activator or adaptor function. Retain the supported generic association under the explicit ClinGen project instruction because no evidence-backed narrower molecular function was established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:11309417 Regulation and localization of the Bloom syndrome protein in... | MODIFY | Summary: Refine the RAD51 interaction to ATPase binding. Reason: GOA names human RAD51/Q06609. Selected Results show DNase/ethidium-resistant retention of RAD51 from lysate by GST-BLM and anti-RAD51 co-IP, while explicitly noting incomplete proof of the interaction in intact cells. RAD51 is an ATP-hydrolyzing recombinase; the replacement describes its enzyme class without assigning recombinase activity to BLM. Proposed replacements: ATPase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:11919194 Colocalization, physical, and functional interaction between... | MODIFY | Summary: Purified BLM binds WRN and inhibits its DNA exonuclease in vitro. Reason: The abstract and selected publisher Results for Figure 6 support direct binding and inhibition of full-length WRN and its N-terminal exonuclease fragment. Heat-inactivated BLM lost inhibition; unrelated exonuclease controls were unaffected, while Ku stimulation dominated in the combined assay. This meets GO:0060703 binding-and-inhibition semantics within the tested in-vitro conditions. It does not establish inhibition of WRN in human cells, of every WRN activity, or as a core BLM function. The original IPI evidence is preserved; the functional proposal also uses the same paper's biochemical assay. Proposed replacements: deoxyribonuclease inhibitor activity Supporting Evidence: PMID:11919194 BLM inhibited the exonuclease activity of WRN |
| GO:0005515 protein binding | IPI PMID:12181313 Telomere-binding protein TRF2 binds to and stimulates the We... | KEEP AS NON CORE | Summary: Retain the experimentally supported BLM–TRF2 interaction as non-core. Reason: PMID:12181313 reports direct BLM–TRF2 binding and stimulation of BLM duplex unwinding; the matching human-pair IntAct record uses an enzyme-linked immunosorbent assay. TRF2 regulates BLM in this experiment, which does not establish activation of the shelterin partner by BLM. Retain the supported generic interaction under the explicit ClinGen project instruction without inventing a narrower BLM activity. Supporting Evidence: PMID:12181313 TRF2 interaction with either WRN or BLM results in a notable stimulation of their helicase activities. |
| GO:0005515 protein binding | IPI PMID:12975363 Functional interaction between the Bloom's syndrome helicase... | KEEP AS NON CORE | Summary: Retain the mapped BLM–RAD51D interaction as non-core. Reason: The complete PMID:12975363 abstract reports direct RAD51D contact through the BLM N terminus and stimulation of Holliday-junction disruption by RAD51D–XRCC2; a BLM truncation lacking that contact is not stimulated. Retain this supported association under the explicit ClinGen project instruction. The partner name and ATP binding alone do not establish the catalytic partner class required for an ATPase-binding refinement; the bounded partner-class assessment is recorded in the notes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:14688284 Stimulation of flap endonuclease-1 by the Bloom's syndrome p... | MODIFY | Summary: Refine FEN1 binding to endodeoxyribonuclease activation. Reason: The complete abstract reports direct physical interaction with human FEN1 and stimulation of its endonuclease and exonuclease activities, independent of BLM helicase activity. This supports an activity-regulator term rather than merely DNA exposure by unwinding. The endodeoxyribonuclease-activator child captures FEN1 flap cleavage; the broader exonuclease stimulation is described in the reason without adding a new annotation. Proposed replacements: endodeoxyribonuclease activator activity Supporting Evidence: PMID:14688284 BLM protein stimulates both the endonucleolytic and exonucleolytic cleavage activity of FEN-1 |
| GO:0005515 protein binding | IPI PMID:15229185 Association and regulation of the BLM helicase by the telome... | KEEP AS NON CORE | Summary: Retain the experimentally supported BLM–TRF1 interaction as non-core. Reason: PMID:15229185 describes TRF1 binding to BLM and inhibition of telomeric unwinding. Matching human-pair IntAct records include ELISA and coimmunoprecipitation, supporting association rather than merely colocalization. The regulation is exerted on BLM, not an enzyme-activator function of BLM toward TRF1. Retain the interaction under the explicit ClinGen project instruction without an unsupported narrower molecular function. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15229185 Association and regulation of the BLM helicase by the telome... | KEEP AS NON CORE | Summary: Retain the experimentally supported BLM–TRF2 interaction as non-core. Reason: PMID:15229185 describes BLM–TRF2 association and stimulation of telomeric unwinding, including association in ALT cells. Matching human-pair IntAct coimmunoprecipitation records corroborate the source linkage. The regulatory direction does not establish a BLM activator function toward TRF2. Retain the supported generic interaction under the explicit ClinGen project instruction, with cellular association distinguished from the biochemical regulatory assay. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15775963 BLAP75, an essential component of Bloom's syndrome protein c... | KEEP AS NON CORE | Summary: Retain the RPA1-containing BLM complex association demonstrated by this source. Reason: Selected PMID:15775963 Results and Figure 1A–C now resolve this source-specific assertion: immunopurified HeLa BLM complexes contain RPA, and the inspected Figure 1A/B identifies RPA70. Preimmune-serum and bead controls accompany the experiment. This supports a cellular complex association without proving a binary interface in this assay. Retain it as non-core under the explicit ClinGen project instruction; the independent purified interaction in PMID:10825162 remains corroboration. |
| GO:0005515 protein binding | IPI PMID:15775963 BLAP75, an essential component of Bloom's syndrome protein c... | MODIFY | Summary: Refine the established TOP3A partner to topoisomerase binding. Reason: The RMI1/BLAP75 abstract describes a stable BLM multiprotein complex. GOA explicitly records TOP3A/Q13472. Independent BLM–TOP3A physical association and BTR reconstitution corroborate this particular pair, while the original paper-specific interaction experiment is not claimed to have been fully audited. Proposed replacements: DNA topoisomerase binding |
| GO:0005515 protein binding | IPI PMID:15775963 BLAP75, an essential component of Bloom's syndrome protein c... | KEEP AS NON CORE | Summary: Retain the source-supported BLM–RMI1 complex association as non-core. Reason: Selected PMID:15775963 Results and Figure 1 show reciprocal BLM/BLAP75 immunopurification from HeLa extracts, mass-spectrometric identification and immunoblot confirmation, with mock controls. BLAP75 is RMI1. These data support the annotated association; complex membership does not by itself assign BLM an adaptor activity or establish a purified binary interface. Retain the supported generic association under the explicit ClinGen project instruction. |
| GO:0005515 protein binding | IPI PMID:15965237 Physical and functional mapping of the replication protein a... | KEEP AS NON CORE | Summary: Retain the source-supported BLM–RPA1 interaction as non-core. Reason: PMID:15965237 compares full-length human BLM with the 642–1290 fragment lacking its N-terminal RPA-interaction region. The fragment loses efficient RPA-dependent long-duplex unwinding; matching human BLM–RPA1 IntAct records report ELISA. These observations support the interaction while retaining the construct limit. RPA stimulation of BLM does not establish the reverse regulatory function. Retain the association under the explicit ClinGen project instruction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16030011 POT1 stimulates RecQ helicases WRN and BLM to unwind telomer... | KEEP AS NON CORE | Summary: Retain the experimentally supported BLM–POT1 interaction as non-core. Reason: The complete PMID:16030011 abstract reports binding of purified POT1 to BLM in vitro and stimulation of telomeric fork/D-loop unwinding. It also describes full-length POT1 splice variant 1 recovering endogenous BLM from HeLa extract, less efficiently than WRN. Preserve that POT1 construct scope without inventing a BLM isoform assignment. Retain the association under the explicit ClinGen project instruction; stimulation of BLM does not give BLM an activator activity toward POT1. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16864798 MPS1-dependent mitotic BLM phosphorylation is important for ... | UNDECIDED | Summary: The literal RPS27 partner is not resolved by the available abstract. Reason: GOA and the UniProt interaction list identify P42677/RPS27 for this row, separately from the PLK1 row. The paper abstract emphasizes MPS1 and PLK1, but MPS1/TTK is not inferred to be P42677 from the paper’s title. The exact RPS27 experiment requires the unavailable full interaction evidence; no wrong-gene or false-interaction claim is made. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16864798 MPS1-dependent mitotic BLM phosphorylation is important for ... | MODIFY | Summary: Refine the PLK1 contact to protein kinase binding. Reason: GOA identifies PLK1/P53350. The abstract reports association of phosphorylated BLM with the PLK1 polo-box domain. Protein kinase binding describes the partner’s catalytic class; it does not assign kinase activity to BLM or assume that the separate P42677 row is MPS1. Proposed replacements: protein kinase binding Supporting Evidence: PMID:16864798 Phosphorylated BLM interacts with polo-like kinase 1 |
| GO:0005515 protein binding | IPI PMID:17961633 Interaction of human SUV3 RNA/DNA helicase with BLM helicase... | MODIFY | Summary: Refine the SUV3 helicase interaction to ATPase binding. Reason: GOA names SUPV3L1/Q8IYB8. The abstract reports direct interaction of purified human SUV3 with BLM, with an approximately 0.5-nanomolar apparent affinity. SUV3 is an ATP-dependent helicase, so its partner class supports ATPase binding. Mouse knockout phenotypes in the same paper are not presented as the human binding assay. Proposed replacements: ATPase binding Supporting Evidence: PMID:17961633 human SUV3 protein interacts with human WRN and BLM helicases |
| GO:0005515 protein binding | IPI PMID:20360068 Systematic analysis of human protein complexes identifies ch... | UNDECIDED | Summary: The exact survey-derived TOP3A pair awaits dataset-level adjudication. Reason: The available MitoCheck text describes its screening strategy, but the specific BLM–TOP3A pair-level result and controls were not inspected. The pair is biologically plausible from BTR literature, but that does not verify this particular survey assertion. Preserve its original source and partner rather than treating absent detail in the abstract/partial body as negative evidence. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20360068 Systematic analysis of human protein complexes identifies ch... | UNDECIDED | Summary: The exact survey-derived RMI1 pair awaits dataset-level adjudication. Reason: The available MitoCheck text describes its screening strategy, but the specific BLM–RMI1 pair-level result and controls were not inspected. The pair is biologically plausible from BTR literature, but that does not verify this particular survey assertion. Preserve its original source and partner rather than treating absent detail in the abstract/partial body as negative evidence. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20711169 Rif1 provides a new DNA-binding interface for the Bloom synd... | MODIFY | Summary: Refine the established TOP3A partner to topoisomerase binding. Reason: The Rif1 paper abstract establishes a BLM-associated complex but does not individually resolve the TOP3A co-IP. GOA explicitly records TOP3A/Q13472. Independent BLM–TOP3A physical association and BTR reconstitution corroborate this particular pair, while the original paper-specific interaction experiment is not claimed to have been fully audited. Proposed replacements: DNA topoisomerase binding |
| GO:0005515 protein binding | IPI PMID:20711169 Rif1 provides a new DNA-binding interface for the Bloom synd... | KEEP AS NON CORE | Summary: Retain the BLM–RMI1 complex association represented in the Rif1 study. Reason: Selected PMID:20711169 Results and Figure 1 identify BLM and RMI1 in HeLa complexes. Figure 1A expressly reproduces the earlier BLM/RMI1 immunopurification panel from PMID:15775963, while Rif1 immunopurification and immunoblotting also recover BLM-complex components. Retain the supported association as non-core under the explicit ClinGen project instruction. The reused panel is not independent replication, and these complex experiments do not prove a binary interface or a BLM adaptor function. |
| GO:0005515 protein binding | IPI PMID:20826342 Crystal structures of RMI1 and RMI2, two OB-fold regulatory ... | KEEP AS NON CORE | Summary: Retain the source-supported BLM–RMI1 association as non-core. Reason: Selected PMID:20826342 Results show that Flag-tagged wild-type RMI1 coimmunoprecipitates endogenous BLM and TOP3A in HeLa cells; deletion of the RMI1 insertion loop disrupts these associations while retaining RMI2 binding. This supports the source-specific complex association without transferring RMI1 regulatory functions to BLM. Retain the generic interaction under the explicit ClinGen project instruction; no narrower BLM molecular function follows from this co-IP alone. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21240188 Interaction between the helicases genetically linked to Fanc... | MODIFY | Summary: Refine the FANCJ interaction to ATPase binding. Reason: GOA identifies BRIP1/FANCJ/Q9BX63. The complete abstract and available Discussion describe reciprocal human nuclear-extract co-IP and DNA-independent binding of purified BLM and FANCJ, two ATP-dependent helicases. The available cache lacks complete Results; this limitation does not erase the explicit biochemical interaction described by the authors. Proposed replacements: ATPase binding Supporting Evidence: PMID:21240188 BLM and FANCJ helicases directly bind to each other |
| GO:0005515 protein binding | IPI PMID:21325134 BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end... | MODIFY | Summary: Refine DNA2 binding to the more specific ATPase-binding class. Reason: GOA identifies DNA2/P51530, and the complete human-protein reconstitution abstract reports a specific physical BLM–DNA2 interaction. The reviewed human UniProt P51530 record independently establishes DNA2 ATP hydrolysis activity. GO:0051117 describes binding to that enzyme class; it does not require BLM to activate DNA2 ATP hydrolysis or bind its ATPase domain. The source assigns BLM helicase and DNA2 nuclease work in resection. No nuclease-activator mechanism is inferred merely from BLM exposing single-stranded substrate. Proposed replacements: ATPase binding Supporting Evidence: PMID:21325134 BLM and DNA2 physically and specifically interact |
| GO:0005515 protein binding | IPI PMID:23509288 Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndro... | MODIFY | Summary: Refine the established TOP3A partner to topoisomerase binding. Reason: The available SPIDR discussion describes recruitment of the BTR complex; the complete original Results panel was not recovered. GOA explicitly records TOP3A/Q13472. Independent BLM–TOP3A physical association and BTR reconstitution corroborate this particular pair, while the original paper-specific interaction experiment is not claimed to have been fully audited. Proposed replacements: DNA topoisomerase binding |
| GO:0005515 protein binding | IPI PMID:23509288 Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndro... | KEEP AS NON CORE | Summary: Retain the source-supported BLM–SPIDR interaction as non-core. Reason: Selected PMID:23509288 Results and Figure 1 report controlled co-IP and recombinant GST-BLM binding to in vitro-translated SPIDR. SPIDR is the scaffold. That scaffold role belongs to SPIDR and is not transferred to BLM. Retain the supported association under the explicit ClinGen project instruction without an unsupported BLM adaptor assignment. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23509288 Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndro... | KEEP AS NON CORE | Summary: Retain the BLM–RMI1 association tested directly in the SPIDR study. Reason: PMID:23509288 Figure 1A/D shows BLM-associated RMI1. Selected Results also report N-terminal mapping through BLM deletion/pull-down assays (Figure S3E/I). Figure 1 was viewed; the supplementary images were not. This resolves the original source gap without asserting a purified binary interface. Retain the source-supported interaction under the explicit ClinGen project instruction without assigning a new BLM adaptor activity. |
| GO:0005515 protein binding | IPI PMID:23708797 Ubiquitin-dependent recruitment of the Bloom syndrome helica... | KEEP AS NON CORE | Summary: Retain the ubiquitin-dependent BLM–RAP80 association as non-core. Reason: The complete PMID:23708797 abstract describes ubiquitylation of the BLM N-terminal region followed by association with the ubiquitin-interacting motifs of RAP80/UIMC1. The association is supported in its modified-protein context; it need not imply direct recognition of an unmodified BLM peptide. BLM is the modified partner, so this does not assign it ubiquitin-binding or ligase activity. Retain the generic association under the explicit ClinGen project instruction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24126761 hPrimpol1/CCDC111 is a human DNA primase-polymerase required... | UNDECIDED | Summary: The BLM–RPA1 control or interaction record is not exposed by this partial cache. Reason: The PMID:24126761 cache is flagged full_text_available=true but its body contains abstract, introduction and limited Methods without the Results or interaction figures. Those sections establish PRIMPOL–RPA1 rather than resolving the original BLM–RPA1 record. This is missing assay context, not evidence of a wrong-gene annotation; the independently known BLM–RPA1 pair does not by itself verify this citation. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | UNDECIDED | Summary: The exact survey-derived TOP3A pair awaits dataset-level adjudication. Reason: The available text from the quantitative HeLa interaction survey describes its screening strategy, but the specific BLM–TOP3A pair-level result and controls were not inspected. The pair is biologically plausible from BTR literature, but that does not verify this particular survey assertion. Preserve its original source and partner rather than treating absent detail in the abstract/partial body as negative evidence. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | UNDECIDED | Summary: The exact survey-derived RMI1 pair awaits dataset-level adjudication. Reason: The available text from the quantitative HeLa interaction survey describes its screening strategy, but the specific BLM–RMI1 pair-level result and controls were not inspected. The pair is biologically plausible from BTR literature, but that does not verify this particular survey assertion. Preserve its original source and partner rather than treating absent detail in the abstract/partial body as negative evidence. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28506294 hSSB1 associates with and promotes stability of the BLM heli... | KEEP AS NON CORE | Summary: Retain the cellular BLM–NABP2 association with its directness limit. Reason: Selected PMID:28506294 Results demonstrate BLM/hSSB1-NABP2 coimmunoprecipitation in human cells without requiring INTS3. Recombinant hSSB1 and BLM did not show detectable direct interaction in the tested assay; indirect association or missing modifications remain possible. Retain the supported cellular association under the explicit ClinGen project instruction. This decision does not upgrade co-IP to a purified binary interface or assign NABP2 DNA-binding activity to BLM. Supporting Evidence: PMID:28506294 we were unable to detect a direct interaction between the two proteins |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | UNDECIDED | Summary: The exact survey-derived TOP3A pair awaits dataset-level adjudication. Reason: The available OpenCell text describes its screening strategy, but the specific BLM–TOP3A pair-level result and controls were not inspected. The pair is biologically plausible from BTR literature, but that does not verify this particular survey assertion. Preserve its original source and partner rather than treating absent detail in the abstract/partial body as negative evidence. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | UNDECIDED | Summary: The exact survey-derived RMI1 pair awaits dataset-level adjudication. Reason: The available OpenCell text describes its screening strategy, but the specific BLM–RMI1 pair-level result and controls were not inspected. The pair is biologically plausible from BTR literature, but that does not verify this particular survey assertion. Preserve its original source and partner rather than treating absent detail in the abstract/partial body as negative evidence. Supporting Evidence: |
| GO:0005524 ATP binding | IDA PMID:24816114 Structure of human Bloom's syndrome helicase in complex with... | ACCEPT | Summary: ATP binding is integral to the BLM helicase motor. Reason: The source describes an ADP-bound BLM structure; ATP-dependent motor assays independently establish ATP as the catalytic nucleotide. Retaining ATP binding does not make it a separate core function from ATP-coupled DNA remodeling. |
| GO:0005524 ATP binding | IDA PMID:25901030 Crystal structure of the Bloom's syndrome helicase indicates... | ACCEPT | Summary: ATP binding is integral to the BLM helicase motor. Reason: The source describes an ADP-bound BLM structure; ATP-dependent motor assays independently establish ATP as the catalytic nucleotide. Retaining ATP binding does not make it a separate core function from ATP-coupled DNA remodeling. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: ATP binding is integral to the BLM helicase motor. Reason: The InterPro mapping from IPR011545 and IPR012532 is consistent with the experimentally characterized ATP-dependent motor. Retaining ATP binding does not make it a separate core function from ATP-coupled DNA remodeling. |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: Retain inherited nuclear localization. Reason: The actual PAINT IBD at PTN001415789 is an eukaryotic nuclear-localization assertion and includes human BLM among its experimental descendants. Multiple human-cell localization studies corroborate the inference; the target’s presence among descendants is not circular. |
| GO:0005634 nucleus | IDA PMID:11500040 The N-terminal internal region of BLM is required for the fo... | ACCEPT | Summary: Retain nuclear localization in the GFP-BLM study. Reason: The abstract reports SUMO-associated nuclear dots for expressed BLM and cytoplasmic localization after deletion of its nuclear-localization sequence. The deletion construct does not establish that wild-type BLM is exclusively cytoplasmic. Supporting Evidence: |
| GO:0005634 nucleus | IDA PMID:31772289 Functional conservation of RecQ helicase BLM between humans ... | ACCEPT | Summary: Human BLM localizes to nuclei in the heterologous S2 assay. Reason: Selected Methods and Figure 3 text identify a human BLM cDNA expressed from UASp in Drosophila S2 cells. Human-specific immunofluorescence places that transgene product in DAPI-stained nuclei. The assayed protein is human BLM, while the host cells are Drosophila; the source qualifier and evidence are preserved. Supporting Evidence: PMID:31772289 hBLM localized to the DAPI-stained nucleus |
| GO:0005634 nucleus | IDA PMID:9388480 BLM (the causative gene of Bloom syndrome) protein transloca... | ACCEPT | Summary: Retain BLM nuclear localization and its C-terminal targeting sequence. Reason: The complete abstract reports GFP-BLM nuclear localization in HeLa cells and loss of nuclear targeting after deleting the relevant C-terminal region. This directly supports the nuclear location. Supporting Evidence: |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: Retain the UniProt nuclear-location mapping. Reason: The electronic subcellular-location inference agrees with direct localization of human BLM and its nuclear DNA-repair function. |
| GO:0005634 nucleus | NAS PMID:23543748 Role of replication protein A in double holliday junction di... | ACCEPT | Summary: Retain the nuclear context of the BLM dissolvasome. Reason: The original NAS citation focuses on reconstituted BTR/RPA double-Holliday-junction dissolution rather than an independent localization assay. Nuclear localization is directly corroborated by the cited BLM cell studies; the NAS source is not promoted to IDA. |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | ACCEPT | Summary: Retain the curated nucleoplasmic localization. Reason: The GO_REF identifies fusion-protein localization curation. The original image resource was not re-inspected, but human BLM nuclear fractionation and damage-focus studies independently agree with a nucleoplasmic pool. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-174438 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, Formation of the Flap Intermediate on the C-strand, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4568914 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, SUMOylation of BLM with SUMO2,3, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5684875 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, Binding of ATR:ATRIP to RPA at resected DNA DSBs, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5684882 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, CHEK1 is recruited to resected DNA DSBs, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5684887 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, Activation of CHEK1 at resected DNA DSBs, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685011 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, ATR activation at DNA DSBs, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685156 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, ATR phosphorylates RPA2, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685341 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, BCDX2 complex stabilizes RAD51 filament, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685838 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, CX3 complex binds D-loop structures, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685985 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, EXO1 or DNA2 in complex with BLM or WRN binds initially resected DNA DSBs along with BRIP1 recruitment, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685994 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, Long-range resection of DNA DSBs by EXO1 or DNA2, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686398 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, SPIDR binds BLM:TOP3A:RMI1:RMI2, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686410 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, BLM mediates dissolution of double Holliday junction, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686440 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, MUS81:EME1,EME2 cleaves D-loop, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686469 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, Resolution of D-loops cleaved by MUS81:EME1 or MUS81:EME2, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686483 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, Resolution of Holliday junctions cleaved by GEN1 or SLX1A:SLX4:MUS81:EME1,(MUS81:EME2), is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686642 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, RAD52 promotes single strand annealing at resected DNA DSBs, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686657 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, ERCC1:XPF cleaves flaps generated by SSA, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686663 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, Completion of SSA, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693539 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, Ligation of DNA and formation of Holliday structures following repair synthesis, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693542 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, Association of RPA complexes with ssDNA at resected DNA DSBs, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693561 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, RAD51 binds BRCA2 at resected DNA DSBs, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693564 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, Association of RAD51 with RAD52:DNA double-strand break ends, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693580 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, Association of RAD52 with the RPA complex at resected DNA DSBs, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693584 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, Cleavage of Holliday junctions by GEN1 or SLX1A:SLX4:MUS81:EME1,(MUS81:EME2), is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693589 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, D-loop dissociation and strand annealing, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693593 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, D-loop extension by DNA polymerases, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693620 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, D-loop formation mediated by PALB2, BRCA2 and RAD51, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6799332 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, ATR phosphorylates TP53, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9701199 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, Defective D-loop formation mediated by PALB2, BRCA2 and RAD51 due to loss-of-function of BRCA1 in PALB2 binding, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9704330 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, Defective D-loop formation mediated by PALB2, BRCA2 and RAD51 due to loss-of-function of PALB2 in BRCA1 binding, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9704408 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, Defective D-loop formation mediated by PALB2, BRCA2 and RAD51 due to loss-of-function of PALB2 in binding to BRCA2/RAD51/RAD51C, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9709571 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, BRCA2 mutants with BRC defects or a defect in the C-terminal RAD51 binding site do not bind RAD51, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9709601 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, Defective recruitment of BRCA2 and RAD51 due to loss of BRCA2 function in PALB2 binding, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9853389 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, FIGNL1 binds RAD51, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9980006 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, ERCC1:XPF binds DNA DSBs with annealed 3' ssDNA overhangs and displaced flaps generated by SSA, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9980021 | ACCEPT | Summary: Retain nucleoplasmic location in the curated repair context. Reason: The cached Reactome event, LIG1 binds SSA sites, is a pathway-context source for this cellular-component annotation. The assertion is only nucleoplasm: it does not assign the named kinase, nuclease, polymerase or ligase reaction to BLM. Some summaries do not name BLM individually, so they are not treated as independent BLM localization experiments. Direct human BLM nuclear-matrix/repair-focus evidence corroborates the location. |
| GO:0005657 replication fork | ISS GO_REF:0000024 | ACCEPT | Summary: Retain replication-fork association inferred from mouse Blm. Reason: The ISS source identifies mouse Blm/O88700. Purified human BLM catalyzes model fork regression and works with DNA2 in end processing, making fork association mechanistically consistent. These corroborating assays do not replace the original orthology provenance with a newly claimed human imaging experiment. |
| GO:0005694 chromosome | IBA GO_REF:0000033 | ACCEPT | Summary: Retain the phylogenetic chromosome association. Reason: The actual PAINT IBD at PTN000344873 includes human BLM experimental grounding among the descendants. Chromosomal DNA remodeling and human damage-focus localization support this location; the ancestral node and tree are not re-curated here. |
| GO:0005730 nucleolus | IDA PMID:10779560 Nuclear structure in normal and Bloom syndrome cells. | KEEP AS NON CORE | Summary: Retain the S-phase nucleolar pool as a context-dependent location. Reason: The original abstract reports nucleolar redistribution of BLM and WRN during S phase. This is compatible with a multifunctional nuclear helicase and is not contradicted by prominent PML-body localization. The compact core does not infer a specific ribosomal-RNA catalytic function from localization alone. Supporting Evidence: |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain the cytoplasmic IBA as a secondary localization inference. Reason: The actual PTHR13710 table contains the GO:0005737 IBD at PTN000344873 with experimental descendant sources. Nuclear enrichment in the inspected human studies does not demonstrate loss of every cytoplasmic pool. No phylogenetic node error, donor-count weakness or human loss is established, so the assertion is retained as non-core with its inference provenance; its specific human context remains a question. Supporting Evidence: GO_REF:0000033 |
| GO:0006260 DNA replication | IBA GO_REF:0000033 | ACCEPT | Summary: BLM contributes to DNA replication through difficult-substrate processing. Reason: The actual PTN000344874 IBD includes human BLM among the experimental descendants. BLM remodels stalled fork structures and facilitates synthesis through telomeric DNA. This process term does not identify BLM as the general replicative polymerase or the CMG replicative helicase. |
| GO:0006260 DNA replication | IEA GO_REF:0000002 | ACCEPT | Summary: BLM contributes to DNA replication through difficult-substrate processing. Reason: The original evidence is an InterPro inference from IPR012532 and IPR018982. BLM remodels stalled fork structures and facilitates synthesis through telomeric DNA. This process term does not identify BLM as the general replicative polymerase or the CMG replicative helicase. |
| GO:0006260 DNA replication | ISS GO_REF:0000024 | ACCEPT | Summary: BLM contributes to DNA replication through difficult-substrate processing. Reason: The original ISS evidence transfers from mouse Blm/O88700. BLM remodels stalled fork structures and facilitates synthesis through telomeric DNA. This process term does not identify BLM as the general replicative polymerase or the CMG replicative helicase. |
| GO:0006281 DNA repair | IEA GO_REF:0000002 | ACCEPT | Summary: Retain DNA repair as a central BLM process. Reason: The InterPro mapping from IPR018982 agrees with the direct BLM reconstitution evidence. BLM catalyzes DNA processing during resection and recombination-intermediate dissolution. |
| GO:0006281 DNA repair | NAS PMID:7585968 The Bloom's syndrome gene product is homologous to RecQ heli... | ACCEPT | Summary: Retain DNA repair as a central BLM process. Reason: The original cloning paper provides broad NAS context; later human biochemical work independently establishes BLM participation in repair. BLM catalyzes DNA processing during resection and recombination-intermediate dissolution. |
| GO:0006310 DNA recombination | IEA GO_REF:0000002 | ACCEPT | Summary: Retain the DNA recombination role. Reason: The InterPro inference from IPR004589 is compatible with the established motor function. BLM promotes productive non-crossover processing while suppressing excessive crossover outcomes; the broad recombination term does not imply a uniform increase in every recombination pathway. |
| GO:0006310 DNA recombination | NAS PMID:10728666 Association of the Bloom syndrome protein with topoisomerase... | ACCEPT | Summary: Retain the DNA recombination role. Reason: The original BLM–TOP3A association supports recombination-complex context. BLM promotes productive non-crossover processing while suppressing excessive crossover outcomes; the broad recombination term does not imply a uniform increase in every recombination pathway. |
| GO:0006310 DNA recombination | NAS PMID:7585968 The Bloom's syndrome gene product is homologous to RecQ heli... | ACCEPT | Summary: Retain the DNA recombination role. Reason: The original cloning-paper NAS context is strengthened by later direct biochemical evidence. BLM promotes productive non-crossover processing while suppressing excessive crossover outcomes; the broad recombination term does not imply a uniform increase in every recombination pathway. |
| GO:0006974 DNA damage response | IDA PMID:23509288 Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndro... | ACCEPT | Summary: BLM is recruited to DNA-damage processing sites. Reason: The available SPIDR discussion describes BLM recruitment to damaged chromosomes and repair foci. Independently read human BLM irradiation experiments and purified repair reactions support the broader DNA-damage-response process without assigning BLM the upstream checkpoint-kinase role. |
| GO:0006974 DNA damage response | IMP PMID:12818200 Characterization and mutational analysis of the RecQ core of... | ACCEPT | Summary: Retain the established DNA-damage-response function with heterologous context. Reason: The original study expresses the human BLM642–1290 fragment in E. coli and examines its biochemical activity and recombination effects; it is not a full human-cell damage-response assay. Independent human BLM damage-focus and resection experiments support the process, while the original IMP source is retained. |
| GO:0007095 mitotic G2 DNA damage checkpoint signaling | IDA PMID:11309417 Regulation and localization of the Bloom syndrome protein in... | MODIFY | Summary: Use cellular response to DNA damage rather than checkpoint signaling. Reason: Selected Results distinguish BLM accumulation during the G2 delay from induction of the checkpoint itself: abolishing the G2 delay largely prevents sustained BLM accumulation. The GO checkpoint term requires detecting damage and negatively regulating G2/M progression. These assays directly support BLM participation in the damage response and repair-associated foci, not that signaling role. The broader damage-response term preserves the supported biological essence; it does not deny checkpoint functions that other studies may establish. Proposed replacements: DNA damage response Supporting Evidence: PMID:11309417 the rise in BLM after IR most likely reflected the transient G2 arrest |
| GO:0008094 ATP-dependent activity, acting on DNA | IDA PMID:10359700 Oligomeric ring structure of the Bloom's syndrome helicase. | MODIFY | Summary: Refine ATP-dependent DNA activity to the established helicase. Reason: The source characterizes oligomeric BLM complexes with helicase activity. The specific 3-prime-to-5-prime DNA helicase term captures the ATP-driven DNA reaction already established for BLM. Proposed replacements: 3'-5' DNA helicase activity |
| GO:0008094 ATP-dependent activity, acting on DNA | IDA PMID:24816114 Structure of human Bloom's syndrome helicase in complex with... | MODIFY | Summary: Refine ATP-dependent DNA activity to the established helicase. Reason: The source characterizes the DNA-bound BLM catalytic core and its nucleotide-coupled motor. The specific 3-prime-to-5-prime DNA helicase term captures the ATP-driven DNA reaction already established for BLM. Proposed replacements: 3'-5' DNA helicase activity |
| GO:0008094 ATP-dependent activity, acting on DNA | IDA PMID:25901030 Crystal structure of the Bloom's syndrome helicase indicates... | MODIFY | Summary: Refine ATP-dependent DNA activity to the established helicase. Reason: The source characterizes the DNA-bound BLM catalytic core and its nucleotide-coupled motor. The specific 3-prime-to-5-prime DNA helicase term captures the ATP-driven DNA reaction already established for BLM. Proposed replacements: 3'-5' DNA helicase activity |
| GO:0008270 zinc ion binding | IDA PMID:24816114 Structure of human Bloom's syndrome helicase in complex with... | KEEP AS NON CORE | Summary: Retain structural zinc binding. Reason: The BLM catalytic-core structural work identifies the zinc-binding domain. This metal contributes to protein architecture and DNA substrate engagement; it is not a separate primary activity or evidence that BLM is a zinc transporter. Supporting Evidence: |
| GO:0008270 zinc ion binding | IDA PMID:25901030 Crystal structure of the Bloom's syndrome helicase indicates... | KEEP AS NON CORE | Summary: Retain structural zinc binding. Reason: The BLM catalytic-core structural work identifies the zinc-binding domain. This metal contributes to protein architecture and DNA substrate engagement; it is not a separate primary activity or evidence that BLM is a zinc transporter. Supporting Evidence: |
| GO:0009378 four-way junction helicase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Retain Holliday-junction remodeling by the BLM helicase. Reason: The actual IBD at PTN000344873 has human BLM and other RecQ-family experimental descendants; this is a phylogenetic assertion, not a donor-count argument. BLM unwinds/migrates the junction; it is not the endonuclease that cuts a Holliday junction. |
| GO:0009378 four-way junction helicase activity | IDA PMID:11433031 The Bloom's and Werner's syndrome proteins are DNA structure... | ACCEPT | Summary: Retain Holliday-junction remodeling by the BLM helicase. Reason: The complete abstract directly reports efficient unwinding of synthetic X-junction DNA by human BLM. BLM unwinds/migrates the junction; it is not the endonuclease that cuts a Holliday junction. |
| GO:0009378 four-way junction helicase activity | IDA PMID:11735402 Inhibition of the Bloom's and Werner's syndrome helicases by... | ACCEPT | Summary: Retain Holliday-junction remodeling by the BLM helicase. Reason: The original ligand-study abstract does not display every junction assay, but independent human BLM junction biochemistry and selected branch-migration assays establish the function. BLM unwinds/migrates the junction; it is not the endonuclease that cuts a Holliday junction. |
| GO:0009378 four-way junction helicase activity | IDA PMID:12818200 Characterization and mutational analysis of the RecQ core of... | ACCEPT | Summary: Retain Holliday-junction remodeling by the BLM helicase. Reason: The original human BLM642–1290 study reports helicase activity of the isolated motor; the junction-specific function is independently demonstrated in the corroborating full-length assays. BLM unwinds/migrates the junction; it is not the endonuclease that cuts a Holliday junction. |
| GO:0009378 four-way junction helicase activity | IDA PMID:25901030 Crystal structure of the Bloom's syndrome helicase indicates... | ACCEPT | Summary: Retain Holliday-junction remodeling by the BLM helicase. Reason: Selected full-length wild-type/mutant assays explicitly measure four-way-junction branch migration. BLM unwinds/migrates the junction; it is not the endonuclease that cuts a Holliday junction. Supporting Evidence: |
| GO:0010165 response to X-ray | IDA PMID:11309417 Regulation and localization of the Bloom syndrome protein in... | KEEP AS NON CORE | Summary: Retain the measured response to X-irradiation. Reason: Selected human-cell Results show BLM accumulation and redistribution to repair-associated nuclear foci after X-rays. This is an experimentally supported stress context of its repair machinery, retained outside the compact molecular-function core. Supporting Evidence: |
| GO:0016363 nuclear matrix | IDA PMID:11309417 Regulation and localization of the Bloom syndrome protein in... | ACCEPT | Summary: Retain nuclear-matrix association in the tested human cells. Reason: Selected Results recover BLM predominantly with the nuclear matrix using both high-salt extraction and a lower-ionic-strength/amine-modification method, with lamin B as a marker. This is the operational cellular fraction tested, not an assertion that every BLM molecule is permanently matrix bound. Supporting Evidence: |
| GO:0016605 PML body | IDA PMID:10728666 Association of the Bloom syndrome protein with topoisomerase... | ACCEPT | Summary: Retain BLM localization to PML nuclear bodies. Reason: The BLM–TOP3A abstract explicitly reports colocalization in PML nuclear bodies. Independently read BLM/RAD51 Results support PML-associated repair assemblies, while other nuclear pools remain compatible. |
| GO:0016605 PML body | IDA PMID:10779560 Nuclear structure in normal and Bloom syndrome cells. | ACCEPT | Summary: Retain BLM localization to PML nuclear bodies. Reason: The localization abstract reports PML bodies as a prominent BLM pool, with redistribution in S phase. Independently read BLM/RAD51 Results support PML-associated repair assemblies, while other nuclear pools remain compatible. |
| GO:0016818 hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides | IEA GO_REF:0000002 | MODIFY | Summary: Refine the broad phosphoric-anhydride hydrolase mapping to ATP hydrolysis. Reason: The InterPro inference is compatible with the nucleotide-dependent motor. Purified human BLM hydrolyzes ATP during its DNA-processing cycle, so ATP hydrolysis is the supported substrate-specific refinement. This remains distinct from assigning BLM a phosphatase acting on proteins. Proposed replacements: ATP hydrolysis activity |
| GO:0016887 ATP hydrolysis activity | EXP PMID:24816114 Structure of human Bloom's syndrome helicase in complex with... | ACCEPT | Summary: Retain ATP hydrolysis coupled to DNA remodeling. Reason: The structural/keyword assertion is corroborated by direct BLM ATPase assays. ATP hydrolysis powers the motor and is not represented as a second unrelated ATPase core. |
| GO:0016887 ATP hydrolysis activity | EXP PMID:25901030 Crystal structure of the Bloom's syndrome helicase indicates... | ACCEPT | Summary: Retain ATP hydrolysis coupled to DNA remodeling. Reason: Selected full-length BLM assays directly measure DNA-stimulated ATPase activity. ATP hydrolysis powers the motor and is not represented as a second unrelated ATPase core. Supporting Evidence: |
| GO:0016887 ATP hydrolysis activity | EXP PMID:9388193 The Bloom's syndrome gene product is a 3'-5' DNA helicase. | ACCEPT | Summary: Retain ATP hydrolysis coupled to DNA remodeling. Reason: The original human BLM biochemistry directly establishes ATP-dependent DNA helicase activity. ATP hydrolysis powers the motor and is not represented as a second unrelated ATPase core. Supporting Evidence: |
| GO:0016887 ATP hydrolysis activity | IEA GO_REF:0000120 | ACCEPT | Summary: Retain ATP hydrolysis coupled to DNA remodeling. Reason: The combined automated IEA assertion, with ARBA:ARBA00043426 and RHEA:13065 in WITH/FROM, is corroborated by direct BLM ATPase assays. ATP hydrolysis powers the motor and is not represented as a second unrelated ATPase core. |
| GO:0031297 replication fork processing | IDA PMID:17115688 The Werner and Bloom syndrome proteins catalyze regression o... | ACCEPT | Summary: BLM catalyzes remodeling of model stalled replication forks. Reason: The complete abstract reports purified BLM-mediated fork regression coordinated through DNA unwinding and strand annealing. BLM performs the substrate-remodeling step itself; this is direct biochemical support for replication-fork processing. Supporting Evidence: |
| GO:0031297 replication fork processing | IEA GO_REF:0000117 | ACCEPT | Summary: Retain inferred replication-fork processing. Reason: The ARBA inference agrees with purified BLM fork-regression experiments. This is specific DNA work by BLM rather than assignment from replication-stress sensitivity alone. |
| GO:0031422 RecQ family helicase-topoisomerase III complex | IPI PMID:24984776 The dissolution of double Holliday junctions. | ACCEPT | Summary: BLM is the helicase component of the BTR dissolvasome. Reason: PMID:24984776 is a review describing the BLM–TOP3A–RMI1/RMI2 assembly, not a new pairwise experiment despite the original IPI code. Selected primary reconstitution and HeLa complex data independently support membership in the RecQ helicase–topoisomerase III complex. The original evidence/source fields remain unchanged. |
| GO:0032201 telomere maintenance via semi-conservative replication | TAS Reactome:R-HSA-174438 | ACCEPT | Summary: BLM facilitates lagging-strand replication through telomeric repeats. Reason: The complete Reactome summary explicitly states that BLM or WRN helicase is needed for polymerase-delta progression and strand displacement across G-rich telomeric repeats during C-strand synthesis. This supports the existing telomere-replication process without assigning polymerase activity to BLM. Supporting Evidence: Reactome:R-HSA-174438 |
| GO:0032392 DNA geometric change | IDA PMID:11735402 Inhibition of the Bloom's and Werner's syndrome helicases by... | ACCEPT | Summary: Retain DNA geometric remodeling by the BLM motor. Reason: The original ligand-study citation is compatible with altered DNA structure during helicase action, although its complete assay panel is unavailable. Direct fork regression, Holliday-junction branch migration and DNA unwinding demonstrate structural changes to DNA; these are not a new claim of BLM topoisomerase activity. |
| GO:0032392 DNA geometric change | IEA GO_REF:0000117 | ACCEPT | Summary: Retain DNA geometric remodeling by the BLM motor. Reason: The original assertion is electronic or orthology-based and is retained at that evidence level. Direct fork regression, Holliday-junction branch migration and DNA unwinding demonstrate structural changes to DNA; these are not a new claim of BLM topoisomerase activity. |
| GO:0032392 DNA geometric change | ISS GO_REF:0000024 | ACCEPT | Summary: Retain DNA geometric remodeling by the BLM motor. Reason: The original assertion is electronic or orthology-based and is retained at that evidence level. Direct fork regression, Holliday-junction branch migration and DNA unwinding demonstrate structural changes to DNA; these are not a new claim of BLM topoisomerase activity. |
| GO:0032991 protein-containing complex | IDA PMID:10359700 Oligomeric ring structure of the Bloom's syndrome helicase. | KEEP AS NON CORE | Summary: Retain the experimentally observed oligomeric protein assembly. Reason: The abstract describes high-molecular-weight BLM oligomers, including ring-like particles. It does not establish that those particles are the BTR heterocomplex; the generic complex annotation is retained in its homooligomeric context and is not replaced by a different complex based on unrelated evidence. Supporting Evidence: |
| GO:0042802 identical protein binding | IDA PMID:10359700 Oligomeric ring structure of the Bloom's syndrome helicase. | KEEP AS NON CORE | Summary: Retain BLM self-association. Reason: The oligomeric-ring study supports association of identical BLM subunits. Self-association is a structural property of the tested preparation, not an independent core molecular activity or evidence that all active BLM must be hexameric. Supporting Evidence: |
| GO:0042803 protein homodimerization activity | IDA PMID:28228481 A helical bundle in the N-terminal domain of the BLM helicas... | KEEP AS NON CORE | Summary: Retain the reported BLM homodimerization activity. Reason: The complete abstract identifies an N-terminal dimerization domain in vertebrate BLM and oligomeric effects on unwinding. Retain the curator’s human source assertion with the vertebrate construct context; the entire construct panel was not independently inspected. The activity does not replace the DNA motor core. Supporting Evidence: |
| GO:0043138 3'-5' DNA helicase activity | EXP PMID:24816114 Structure of human Bloom's syndrome helicase in complex with... | ACCEPT | Summary: Retain the defining 3-prime-to-5-prime DNA helicase activity. Reason: The human BLM–DNA structural study is consistent with the motor’s established polarity. BLM supplies ATP-driven DNA strand separation; associated TOP3A provides the topoisomerase chemistry. |
| GO:0043138 3'-5' DNA helicase activity | EXP PMID:25901030 Crystal structure of the Bloom's syndrome helicase indicates... | ACCEPT | Summary: Retain the defining 3-prime-to-5-prime DNA helicase activity. Reason: Selected BLM structures and biochemical motor assays support DNA unwinding, with polarity independently grounded in the original helicase study. BLM supplies ATP-driven DNA strand separation; associated TOP3A provides the topoisomerase chemistry. |
| GO:0043138 3'-5' DNA helicase activity | EXP PMID:9765292 The Bloom's syndrome helicase unwinds G4 DNA. | ACCEPT | Summary: Retain the defining 3-prime-to-5-prime DNA helicase activity. Reason: The G4-DNA study directly reports ATP-dependent 3-prime-to-5-prime unwinding and a requirement for an appropriate tail. BLM supplies ATP-driven DNA strand separation; associated TOP3A provides the topoisomerase chemistry. Supporting Evidence: |
| GO:0043138 3'-5' DNA helicase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Retain the defining 3-prime-to-5-prime DNA helicase activity. Reason: The actual PTN000344873 IBD includes human BLM experimental evidence and supports inherited helicase polarity. BLM supplies ATP-driven DNA strand separation; associated TOP3A provides the topoisomerase chemistry. |
| GO:0043138 3'-5' DNA helicase activity | IDA PMID:9388193 The Bloom's syndrome gene product is a 3'-5' DNA helicase. | ACCEPT | Summary: Retain the defining 3-prime-to-5-prime DNA helicase activity. Reason: The source directly establishes the 3-prime-to-5-prime human BLM DNA helicase activity. BLM supplies ATP-driven DNA strand separation; associated TOP3A provides the topoisomerase chemistry. Supporting Evidence: |
| GO:0043138 3'-5' DNA helicase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Retain the defining 3-prime-to-5-prime DNA helicase activity. Reason: The electronic mapping agrees with the experimentally established motor direction. BLM supplies ATP-driven DNA strand separation; associated TOP3A provides the topoisomerase chemistry. |
| GO:0043138 3'-5' DNA helicase activity | TAS Reactome:R-HSA-174438 | ACCEPT | Summary: Retain the defining 3-prime-to-5-prime DNA helicase activity. Reason: The Reactome event explicitly names BLM or WRN helicase support of telomeric strand displacement; the direction-specific assertion is corroborated by the original purified BLM assay. BLM supplies ATP-driven DNA strand separation; associated TOP3A provides the topoisomerase chemistry. |
| GO:0045893 positive regulation of DNA-templated transcription | IDA PMID:11781842 The Bloom syndrome protein interacts and cooperates with p53... | KEEP AS NON CORE | Summary: Retain the p53-associated transcriptional effect as secondary. Reason: The abstract reports that BLM overexpression augments p53-driven transcriptional activation through its p53-contacting region. This supports the existing regulatory process in that experimental context but does not establish BLM as a sequence-specific transcription factor or make transcription activation its main role. Supporting Evidence: |
| GO:0045910 negative regulation of DNA recombination | IEA GO_REF:0000117 | ACCEPT | Summary: Retain suppression of excessive recombination outcomes. Reason: The ARBA inference from rule ARBA00086129 agrees with BLM–TOP3A-mediated non-crossover dissolution and complementation of elevated sister-chromatid exchange in BLM-deficient cells. BLM can also support productive repair, so the negative-regulation term is interpreted for aberrant/crossover outcomes rather than all recombination. |
| GO:0045910 negative regulation of DNA recombination | IMP PMID:9671747 Bloom's and Werner's syndrome genes suppress hyperrecombinat... | ACCEPT | Summary: Retain suppression of hyperrecombination with the heterologous assay context. Reason: The source expresses human BLM in yeast sgs1 cells and reports suppression of hyperrecombination and hydroxyurea sensitivity. This is evidence on the human protein in a yeast host, independently corroborated by human BLM-deficient-cell sister-chromatid-exchange complementation. |
| GO:0051259 protein complex oligomerization | IDA PMID:28228481 A helical bundle in the N-terminal domain of the BLM helicas... | KEEP AS NON CORE | Summary: Retain BLM oligomerization as a structural/regulatory property. Reason: The abstract describes N-terminal-domain-mediated assembly and ATP-associated changes between oligomeric states. These source annotations concern assembly of BLM itself; they do not demonstrate a general role assembling unrelated protein complexes. The redundant broad/specific oligomerization terms remain source records outside the compact core. Supporting Evidence: |
| GO:0051260 protein homooligomerization | IDA PMID:28228481 A helical bundle in the N-terminal domain of the BLM helicas... | KEEP AS NON CORE | Summary: Retain BLM oligomerization as a structural/regulatory property. Reason: The abstract describes N-terminal-domain-mediated assembly and ATP-associated changes between oligomeric states. These source annotations concern assembly of BLM itself; they do not demonstrate a general role assembling unrelated protein complexes. The redundant broad/specific oligomerization terms remain source records outside the compact core. Supporting Evidence: |
| GO:0051782 negative regulation of cell division | IMP PMID:11781842 The Bloom syndrome protein interacts and cooperates with p53... | KEEP AS NON CORE | Summary: Retain the p53-dependent antiproliferative effect as non-core. Reason: The complete abstract reports an enhanced antiproliferative effect of BLM overexpression in a p53-dependent context. This is an experimentally supported regulatory outcome, not evidence that BLM is a universal cell-division inhibitor. Supporting Evidence: |
| GO:0051880 G-quadruplex DNA binding | IDA PMID:11433031 The Bloom's and Werner's syndrome proteins are DNA structure... | ACCEPT | Summary: Retain recognition of G-quadruplex DNA. Reason: The source compares BLM activity on G4 and other DNA structures. This is a relevant substrate-recognition property of the DNA motor, not a separate inference that every G4 sequence is processed equally. Supporting Evidence: |
| GO:0051880 G-quadruplex DNA binding | IDA PMID:11735402 Inhibition of the Bloom's and Werner's syndrome helicases by... | ACCEPT | Summary: Retain recognition of G-quadruplex DNA. Reason: The source directly examines ligand inhibition of BLM binding and unwinding of G4 DNA. This is a relevant substrate-recognition property of the DNA motor, not a separate inference that every G4 sequence is processed equally. Supporting Evidence: |
| GO:0061749 forked DNA-dependent helicase activity | IDA PMID:11735402 Inhibition of the Bloom's and Werner's syndrome helicases by... | ACCEPT | Summary: Retain forked-duplex DNA unwinding. Reason: The original abstract does not expose its full fork-substrate panel; independently read purified BLM forked-duplex assays directly support the activity. The term describes the substrate acted on, without requiring that the in-vitro fork is a complete cellular replisome. |
| GO:0061749 forked DNA-dependent helicase activity | IDA PMID:25901030 Crystal structure of the Bloom's syndrome helicase indicates... | ACCEPT | Summary: Retain forked-duplex DNA unwinding. Reason: Selected full-length wild-type and mutant BLM assays explicitly use a forked duplex substrate. The term describes the substrate acted on, without requiring that the in-vitro fork is a complete cellular replisome. Supporting Evidence: |
| GO:0061820 telomeric D-loop disassembly | IDA PMID:16030011 POT1 stimulates RecQ helicases WRN and BLM to unwind telomer... | ACCEPT | Summary: BLM directly disassembles telomeric D-loop substrates. Reason: The source reports POT1-stimulated BLM unwinding of telomeric D-loop structures. BLM performs strand displacement itself; this is mechanistic telomere-DNA processing rather than a phenotype-only assignment. Supporting Evidence: |
| GO:0061820 telomeric D-loop disassembly | IDA PMID:19734539 Telomeric D-loops containing 8-oxo-2'-deoxyguanosine are pre... | ACCEPT | Summary: BLM directly disassembles telomeric D-loop substrates. Reason: The source directly reports BLM unwinding of telomeric D-loops, enhanced for substrates carrying 8-oxodG. BLM performs strand displacement itself; this is mechanistic telomere-DNA processing rather than a phenotype-only assignment. Supporting Evidence: |
| GO:0061821 telomeric D-loop binding | IDA PMID:19734539 Telomeric D-loops containing 8-oxo-2'-deoxyguanosine are pre... | ACCEPT | Summary: Retain binding associated with BLM telomeric D-loop processing. Reason: The original abstract establishes BLM action on telomeric D-loops and the inspected primary-text search result describes the constructed D-loop substrates and BLM processing. Productive substrate engagement supports the existing binding assertion. Detailed binding constants and the complete original binding panel were not recovered, so no preferential binding claim is added. Supporting Evidence: |
| GO:0061849 telomeric G-quadruplex DNA binding | IDA PMID:19734539 Telomeric D-loops containing 8-oxo-2'-deoxyguanosine are pre... | UNDECIDED | Summary: The telomeric G-quadruplex-specific binding assay remains unresolved. Reason: The cached abstract focuses on damaged telomeric D-loops, and accessible primary-text excerpts discuss possible G-quadruplex formation within these substrates. That does not expose a direct BLM binding assay on a separately defined telomeric G4. General BLM G4 recognition is well supported elsewhere, but the exact sequence/structure claim in this source remains unadjudicated; no misattribution is alleged. Supporting Evidence: |
| GO:0071139 resolution of DNA recombination intermediates | IDA PMID:23543748 Role of replication protein A in double holliday junction di... | ACCEPT | Summary: Retain processing of recombination intermediates by BTR dissolution. Reason: The complete abstract describes reconstituted double-Holliday-junction dissolution by BLM–TOP3A–RMI1/RMI2. The existing resolution term is retained for processing the intermediate into intact products, while the mechanism is explicitly dissolution with non-crossover outcomes. BLM is not assigned junction endonuclease activity; TOP3A performs transient strand cleavage and rejoining. Supporting Evidence: PMID:23543748 non-crossover formation via the dissolution of the double Holliday Junction |
| GO:0071479 cellular response to ionizing radiation | IDA PMID:23509288 Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndro... | KEEP AS NON CORE | Summary: Retain the ionizing radiation response as a repair-related context. Reason: The source connects SPIDR-dependent BLM recruitment with damage-associated nuclear foci and sensitivity to DNA-damaging conditions. Its available cache contains Discussion but lacks the complete Results panel. Independently read human BLM accumulation and repair-focus experiments after X-rays corroborate this context without reconstructing the original SPIDR assay. These contexts are secondary to the core DNA-processing activities. |
| GO:0072711 cellular response to hydroxyurea | IDA PMID:23509288 Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndro... | KEEP AS NON CORE | Summary: Retain the hydroxyurea response as a repair-related context. Reason: External PMID:23509288 Results and Figure 2 now resolve the BLM focus assay under hydroxyurea. PMID:28506294 provides the previously inspected independent support. Retain this secondary repair context while distinguishing recruitment from a BLM-specific survival experiment. The normal cache remains incomplete; that no longer describes the available external evidence. |
| GO:0072757 cellular response to camptothecin | IDA PMID:23509288 Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndro... | KEEP AS NON CORE | Summary: Retain the documented camptothecin-associated BLM recruitment response as non-core. Reason: Selected PMID:23509288 Results and Figures 1G/2 report camptothecin-induced BLM nuclear foci and SPIDR-dependent recruitment. This observed recruitment supports the broad cellular-response annotation, as it does for hydroxyurea; the hydroxyurea context also has independent support from PMID:28506294. An untreated panel in the inspected subset or a BLM-specific survival experiment is not required to retain the documented localization response. The SPIDR depletion/rescue experiments establish SPIDR dependence and are not relabeled as BLM survival evidence. Retain this damage-response context outside the core molecular-function synthesis. Supporting Evidence: |
| GO:0090656 t-circle formation | TAS PMID:27918544 A balance between elongation and trimming regulates telomere... | UNDECIDED | Summary: The BLM-specific t-circle-formation assertion needs further source resolution. Reason: Selected full-cache Results distinguish T-circles, C-circles and C-rich overhangs. BLM depletion did not change C-circle abundance in the examined human embryonic stem cells; the positive T-circle experiment tests NBS1, with separate XRCC3 effects on overhangs. This does not establish that BLM lacks t-circle roles in other contexts or resolve every cited background study. The TAS assertion remains undecided rather than being removed by equating a C-circle null result with universal absence of t-circle formation. Supporting Evidence: PMID:27918544 Cells depleted of TRF1, BLM, WRN or Exo1, exhibited similar amounts of C-circles as control cells |
| GO:1905773 8-hydroxy-2'-deoxyguanosine DNA binding | IDA PMID:19734539 Telomeric D-loops containing 8-oxo-2'-deoxyguanosine are pre... | ACCEPT | Summary: Retain engagement of 8-oxodG-containing DNA during BLM unwinding. Reason: The source reports enhanced BLM unwinding of telomeric D-loops containing 8-oxodG. This supports interaction with the damaged DNA substrate. It does not establish BLM as an 8-oxodG glycosylase, nor does the reported POT1 binding preference alone prove a separate BLM lesion-sensing mechanism. Supporting Evidence: |
| GO:1990814 DNA/DNA annealing activity | IDA PMID:17878217 Structural and functional analyses of disease-causing missen... | ACCEPT | Summary: Retain BLM-mediated annealing of complementary DNA strands. Reason: Selected Methods and Figure 9 text directly test complementary oligonucleotides with human BLM642–1290, including reactions without ATP. The Discussion reports detectable annealing above 80 nM and explicitly contrasts an earlier negative result for that fragment. The activity is retained with concentration/construct limits and is not assumed to equal the ATP-driven unwinding reaction. Supporting Evidence: |
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Download this section (compressed HTML)Q: Which full experimental results support BLM regulation of CDC2 in PMID:15604258, rather than BLM phosphorylation simply reporting CDC2 activity?
Q: What exact RPS27/P42677 interaction experiment underlies the separate PMID:16864798 row, and how should it be distinguished from MPS1/TTK and PLK1?
Q: Which primary BLM experiment supports t-circle formation in PMID:27918544, given the reported BLM C-circle null result and the separate NBS1/XRCC3 experiments?
Q: Which human cellular context supports the inherited cytoplasmic localization, and does it involve a specific physiological or cell-cycle-dependent BLM pool?
Q: Should GO:0071139 explicitly distinguish non-crossover BTR dissolution from endonucleolytic Holliday-junction resolution, while retaining both routes to intact repair products?
Q: In which human cellular contexts does BLM binding inhibit WRN exonuclease, and how do Ku-containing assemblies alter this biochemical effect?
Experiment: Compare full-length human BLM and the characterized catalytic fragment at matched active concentrations, with ATP, RPA and BTR components varied independently; quantify annealing, fork regression and unwinding on defined substrates.
Hypothesis: BLM DNA strand annealing and unwinding make separable contributions to fork remodeling.
Experiment: Reconstitute binding with defined BLM/NABP2 modification states and candidate bridging factors, alongside cellular co-IP and DNA/nuclease controls. Measure direct binding separately from BLM stability and chromatin recruitment.
Hypothesis: The cellular BLM–NABP2 association requires either an additional factor or a modification absent from the recombinant proteins.
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