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
TERF2
Gene Ontology Biological Process
- age-dependent telomere shortening [NAS]
- cellular senescence [NAS]
- negative regulation of telomere maintenance [IDA, IMP]
- negative regulation of telomere maintenance via semi-conservative replication [NAS]
- protection from non-homologous end joining at telomere [IMP]
- protein localization to chromosome, telomeric region [IMP]
- telomere capping [IMP, NAS]
- telomere maintenance [IMP, TAS]
- telomere maintenance via telomerase [IC]
- telomeric loop formation [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
Association and regulation of the BLM helicase by the telomere proteins TRF1 and TRF2.
In addition to increased DNA-strand exchange, a cytogenetic feature of cells lacking the RecQ-like BLM helicase is a tendency for telomeres to associate. We also report additional cellular and biochemical evidence for the role of BLM in telomere maintenance. BLM co-localizes and complexes with the telomere repeat protein TRF2 in cells that employ the recombination-mediated mechanism of telomere lengthening known ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TERF2 BLM | Affinity Capture-MS Affinity Capture-MS 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 is identified by mass spectrometric methods. | Low | - | BioGRID | 716901 | |
| BLM TERF2 | 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 | - | |
| BLM TERF2 | 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 | 245087 |
Curated By
- BioGRID