CANX
Gene Ontology Biological Process
- antigen processing and presentation of exogenous peptide antigen via MHC class II [TAS]
- antigen processing and presentation of peptide antigen via MHC class I [TAS]
- cellular protein metabolic process [TAS]
- clathrin-mediated endocytosis [ISS]
- post-translational protein modification [TAS]
- protein N-linked glycosylation via asparagine [TAS]
- protein folding [TAS]
- protein secretion [TAS]
- synaptic vesicle endocytosis [ISS]
Gene Ontology Molecular Function
PDIA3
Gene Ontology Biological Process
- antigen processing and presentation of exogenous peptide antigen via MHC class I [TAS]
- antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [TAS]
- antigen processing and presentation of peptide antigen via MHC class I [TAS]
- cellular protein metabolic process [TAS]
- post-translational protein modification [TAS]
- protein N-linked glycosylation via asparagine [TAS]
- protein folding [IBA, TAS]
- protein import into nucleus [TAS]
- protein retention in ER lumen [TAS]
- proteolysis [TAS]
- response to endoplasmic reticulum stress [IBA]
- signal transduction [TAS]
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
Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin.
Calnexin and calreticulin are membrane-bound and soluble chaperones, respectively, of the endoplasmic reticulum (ER) which interact transiently with a broad spectrum of newly synthesized glycoproteins. In addition to sharing substantial sequence identity, both calnexin and calreticulin bind to monoglucosylated oligosaccharides of the form Glc(1)Man(5-9)GlcNAc(2), interact with the thiol oxidoreductase, ERp57, and are capable of acting as chaperones in vitro to ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| CANX PDIA3 | 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 | - | BioGRID | 3349552 | |
| CANX PDIA3 | 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). | High | - | BioGRID | - |
Curated By
- BioGRID