BLM
Gene Ontology Biological Process
- ATP catabolic process [IDA]
- DNA double-strand break processing [IDA]
- DNA duplex unwinding [IDA, IMP]
- DNA recombination [NAS]
- DNA repair [NAS]
- DNA strand renaturation [IDA]
- cellular response to DNA damage stimulus [IDA, IMP]
- cellular response to camptothecin [IDA]
- cellular response to hydroxyurea [IDA]
- cellular response to ionizing radiation [IDA]
- double-strand break repair via homologous recombination [NAS]
- mitotic G2 DNA damage checkpoint [IDA]
- negative regulation of DNA recombination [IMP]
- negative regulation of cell division [IMP]
- positive regulation of transcription, DNA-templated [IDA]
- protein oligomerization [IDA]
- regulation of cyclin-dependent protein serine/threonine kinase activity [IMP]
- replication fork processing [IDA]
- replication fork protection [NAS]
- response to X-ray [IDA]
Gene Ontology Molecular Function- ATP binding [IDA]
- ATP-dependent DNA helicase activity [IDA, IMP]
- ATP-dependent helicase activity [IDA]
- ATPase activity [IDA]
- G-quadruplex DNA binding [IDA]
- annealing helicase activity [IDA]
- bubble DNA binding [IDA]
- four-way junction helicase activity [IDA]
- helicase activity [IDA]
- p53 binding [IPI]
- protein binding [IPI]
- single-stranded DNA binding [IDA]
- ATP binding [IDA]
- ATP-dependent DNA helicase activity [IDA, IMP]
- ATP-dependent helicase activity [IDA]
- ATPase activity [IDA]
- G-quadruplex DNA binding [IDA]
- annealing helicase activity [IDA]
- bubble DNA binding [IDA]
- four-way junction helicase activity [IDA]
- helicase activity [IDA]
- p53 binding [IPI]
- protein binding [IPI]
- single-stranded DNA binding [IDA]
Gene Ontology Cellular Component
FEN1
Gene Ontology Biological Process
- DNA catabolic process, endonucleolytic [IDA, IMP]
- DNA catabolic process, exonucleolytic [TAS]
- DNA repair [TAS]
- DNA replication [TAS]
- DNA replication, removal of RNA primer [IDA]
- DNA strand elongation involved in DNA replication [TAS]
- RNA phosphodiester bond hydrolysis, endonucleolytic [IDA]
- UV protection [TAS]
- base-excision repair [TAS]
- double-strand break repair [TAS]
- mitotic cell cycle [TAS]
- telomere maintenance [TAS]
- telomere maintenance via recombination [TAS]
- telomere maintenance via semi-conservative replication [TAS]
Gene Ontology Molecular Function- 5'-3' exonuclease activity [IDA]
- 5'-flap endonuclease activity [IDA, IMP]
- DNA binding [IMP]
- RNA-DNA hybrid ribonuclease activity [IDA]
- damaged DNA binding [TAS]
- double-stranded DNA binding [TAS]
- double-stranded DNA exodeoxyribonuclease activity [TAS]
- endonuclease activity [TAS]
- exonuclease activity [TAS]
- protein binding [IPI]
- 5'-3' exonuclease activity [IDA]
- 5'-flap endonuclease activity [IDA, IMP]
- DNA binding [IMP]
- RNA-DNA hybrid ribonuclease activity [IDA]
- damaged DNA binding [TAS]
- double-stranded DNA binding [TAS]
- double-stranded DNA exodeoxyribonuclease activity [TAS]
- endonuclease activity [TAS]
- exonuclease activity [TAS]
- protein binding [IPI]
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
Publication
Stimulation of flap endonuclease-1 by the Bloom's syndrome protein.
Bloom's syndrome (BS) is a rare autosomal recessive genetic disorder associated with genomic instability and an elevated risk of cancer. Cellular features of BS include an accumulation of abnormal replication intermediates and increased sister chromatid exchange. Although it has been suggested that the underlying defect responsible for hyper-recombination in BS cells is a temporal delay in the maturation of DNA ... [more]
Throughput
- Low Throughput
Additional Notes
- BLM-FEN-1 physical interaction is mediated through a region of the BLM C-terminal domain that shares homology with the FEN-1 interaction domain of the Werner syndrome protein
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| BLM FEN1 | Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | 243897 | |
| FEN1 BLM | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - |
Curated By
- BioGRID