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]
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]
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.
Publication
Crystal structure of the ectodomain of human transferrin receptor.
The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome. The crystal structure of the dimeric ectodomain of the human TfR, determined here to 3.2 angstroms resolution, reveals a three-domain subunit. One domain closely resembles carboxy- and aminopeptidases, and features ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TFRC TFRC | 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. | High | 1 | BioGRID | 3206389 | |
| TFRC TFRC | Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071). | Low | - | BioGRID | 3829409 | |
| TFRC TFRC | 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 | 1 | BioGRID | 3210771 |
Curated By
- BioGRID