HSP90B1
Gene Ontology Biological Process
- ER-associated ubiquitin-dependent protein catabolic process [IMP]
- actin rod assembly [IDA]
- activation of signaling protein activity involved in unfolded protein response [TAS]
- cellular protein metabolic process [TAS]
- cellular response to ATP [IDA]
- endoplasmic reticulum unfolded protein response [TAS]
- innate immune response [TAS]
- negative regulation of apoptotic process [IMP, TAS]
- protein transport [NAS]
- regulation of phosphoprotein phosphatase activity [IDA]
- response to hypoxia [IDA]
- sequestering of calcium ion [NAS]
- toll-like receptor signaling pathway [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- cytosol [IDA]
- endocytic vesicle lumen [TAS]
- endoplasmic reticulum [IDA, TAS]
- endoplasmic reticulum lumen [IDA, TAS]
- endoplasmic reticulum membrane [IDA]
- extracellular matrix [IDA]
- extracellular region [TAS]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- membrane [IDA]
- midbody [IDA]
- nucleus [IDA]
- perinuclear region of cytoplasm [IDA]
CNPY2
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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).
Publication
Cross-linking mass spectrometry discovers, evaluates, and corroborates structures and protein-protein interactions in the human cell.
Significant recent advances in structural biology, particularly in the field of cryoelectron microscopy, have dramatically expanded our ability to create structural models of proteins and protein complexes. However, many proteins remain refractory to these approaches because of their low abundance, low stability, or-in the case of complexes-simply not having yet been analyzed. Here, we demonstrate the power of using cross-linking ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| HSP90B1 CNPY2 | 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 | 3719903 | |
| CNPY2 HSP90B1 | 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 | 3678163 | |
| HSP90B1 CNPY2 | 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 | 2787315 |
Curated By
- BioGRID