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
ATRX
Gene Ontology Biological Process
- ATP catabolic process [IDA]
- DNA damage response, signal transduction by p53 class mediator [ISS]
- DNA duplex unwinding [TAS]
- DNA methylation [TAS]
- DNA recombination [TAS]
- DNA replication-independent nucleosome assembly [IMP]
- cellular response to hydroxyurea [ISS]
- chromatin remodeling [IDA]
- negative regulation of telomeric RNA transcription from RNA pol II promoter [ISS]
- nucleosome assembly [IDA]
- positive regulation of nuclear cell cycle DNA replication [ISS]
- positive regulation of telomere maintenance [ISS]
- positive regulation of transcription from RNA polymerase II promoter [IMP]
- regulation of transcription, DNA-templated [TAS]
- replication fork processing [ISS]
Gene Ontology Molecular Function
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
BLM helicase stimulates the ATPase and chromatin-remodeling activities of RAD54.
Mutation of BLM helicase results in the autosomal recessive disorder Bloom syndrome (BS). Patients with BS exhibit hyper-recombination and are prone to almost all forms of cancer. BLM can exhibit its anti-recombinogenic function either by dissolution of double Holliday junctions or by disruption of RAD51 nucleofilaments. We have now found that BLM can interact with the pro-recombinogenic protein RAD54 through ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| BLM ATRX | 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 | - | |
| ATRX BLM | 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 | - | |
| ATRX BLM | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | - | BioGRID | - | |
| ATRX 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