TFRC
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- blood microparticle [IDA]
- cell surface [IDA]
- coated pit [IDA]
- cytoplasmic membrane-bounded vesicle [IDA]
- endosome [IDA]
- extracellular region [IDA]
- extracellular space [IDA]
- extracellular vesicular exosome [IDA]
- integral component of plasma membrane [TAS]
- intracellular membrane-bounded organelle [IDA]
- membrane [NAS]
- plasma membrane [TAS]
- recycling endosome [IDA]
- vesicle [IDA]
TINF2
Gene Ontology Biological Process
- negative regulation of epithelial cell proliferation [IMP]
- negative regulation of protein ADP-ribosylation [IGI]
- negative regulation of telomere maintenance via telomerase [IC, IGI]
- positive regulation of telomere maintenance [IMP]
- protein localization to chromosome [IC, IMP]
- protein localization to chromosome, telomeric region [IMP]
- telomere assembly [IMP]
- telomere maintenance [TAS]
- telomere maintenance via telomere lengthening [IMP]
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
A shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins.
Mammalian telomeres are protected by a six-protein complex: shelterin. Shelterin contains two closely related proteins (TRF1 and TRF2), which recruit various proteins to telomeres. We dissect the interactions of TRF1 and TRF2 with their shared binding partner (TIN2) and other shelterin accessory factors. TRF1 recognizes TIN2 using a conserved molecular surface in its TRF homology (TRFH) domain. However, this same ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TFRC TINF2 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | - | |
| TFRC TINF2 | 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