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]
CSNK2A2
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
The carboxy-terminal domain of Grp94 binds to protein kinase CK2 alpha but not to CK2 holoenzyme.
Surface plasmon resonance analysis shows that the carboxy-terminal domain of Grp94 (Grp94-CT, residues 518-803) physically interacts with the catalytic subunit of protein kinase CK2 (CK2 alpha) under non-stressed conditions. A K(D) of 4 x 10(-7) was determined for this binding. Heparin competed with Grp94-CT for binding to CK2 alpha. CK2 beta also inhibited the binding of Grp94-CT to CK2 alpha, ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID