B2M
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 exogenous peptide antigen via MHC class I, TAP-independent [TAS]
- antigen processing and presentation of peptide antigen via MHC class I [TAS]
- cytokine-mediated signaling pathway [TAS]
- innate immune response [TAS]
- interferon-gamma-mediated signaling pathway [TAS]
- regulation of defense response to virus by virus [TAS]
- regulation of immune response [TAS]
- retina homeostasis [IEP]
- viral process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- ER to Golgi transport vesicle membrane [TAS]
- Golgi apparatus [IDA]
- Golgi membrane [TAS]
- cytoplasm [IDA]
- early endosome lumen [TAS]
- early endosome membrane [TAS]
- endoplasmic reticulum lumen [TAS]
- extracellular region [TAS]
- extracellular space [IDA]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- membrane [IDA]
- phagocytic vesicle membrane [TAS]
- plasma membrane [IDA, TAS]
CRYAB
Gene Ontology Biological Process
Gene Ontology Molecular Function
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
Monitoring the interaction between β2-microglobulin and the molecular chaperone αB-crystallin by NMR and mass spectrometry: αB-crystallin dissociates β2-microglobulin oligomers.
The interaction at neutral pH between wild-type and a variant form (R3A) of the amyloid fibril-forming protein β2-microglobulin (β2m) and the molecular chaperone αB-crystallin was investigated by thioflavin T fluorescence, NMR spectroscopy, and mass spectrometry. Fibril formation of R3Aβ2m was potently prevented by αB-crystallin. αB-crystallin also prevented the unfolding and nonfibrillar aggregation of R3Aβ2m. From analysis of the NMR spectra ... [more]
Throughput
- Low Throughput
Additional Notes
- CRYAB dissociates B2M oligomers, preventing aggregation
Curated By
- BioGRID