HSPA5
Gene Ontology Biological Process
- ATP catabolic process [ISS]
- ER-associated ubiquitin-dependent protein catabolic process [TAS]
- activation of signaling protein activity involved in unfolded protein response [TAS]
- blood coagulation [TAS]
- cellular protein metabolic process [TAS]
- cellular response to glucose starvation [IDA]
- endoplasmic reticulum unfolded protein response [TAS]
- maintenance of protein localization in endoplasmic reticulum [IMP]
- negative regulation of apoptotic process [IMP, TAS]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive regulation of cell migration [IMP]
- regulation of protein folding in endoplasmic reticulum [TAS]
- substantia nigra development [IEP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- COP9 signalosome [IDA]
- endoplasmic reticulum [IDA, IMP, TAS]
- endoplasmic reticulum chaperone complex [IDA]
- endoplasmic reticulum lumen [TAS]
- endoplasmic reticulum membrane [TAS]
- endoplasmic reticulum-Golgi intermediate compartment [IDA]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- integral component of endoplasmic reticulum membrane [IDA]
- membrane [IDA]
- midbody [IDA]
- nucleus [IDA, IMP]
FLNA
Gene Ontology Biological Process
- actin crosslink formation [IDA]
- actin cytoskeleton reorganization [IDA]
- adenylate cyclase-inhibiting dopamine receptor signaling pathway [IMP]
- blood coagulation [TAS]
- cell junction assembly [TAS]
- cilium assembly [IMP]
- cytoplasmic sequestering of protein [IMP]
- establishment of protein localization [IDA]
- negative regulation of protein catabolic process [IMP]
- negative regulation of sequence-specific DNA binding transcription factor activity [IDA]
- platelet activation [TAS]
- platelet aggregation [IMP]
- platelet degranulation [TAS]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IMP]
- positive regulation of transcription factor import into nucleus [IMP]
- protein localization to cell surface [IDA]
- protein stabilization [IMP]
- receptor clustering [IDA]
- spindle assembly involved in mitosis [IDA]
Gene Ontology Molecular Function- Fc-gamma receptor I complex binding [IDA]
- Rac GTPase binding [IDA]
- Ral GTPase binding [IDA]
- Rho GTPase binding [IDA]
- actin filament binding [IDA]
- glycoprotein binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein homodimerization activity [IDA]
- signal transducer activity [IMP]
- small GTPase binding [IDA]
- transcription factor binding [IPI]
- Fc-gamma receptor I complex binding [IDA]
- Rac GTPase binding [IDA]
- Ral GTPase binding [IDA]
- Rho GTPase binding [IDA]
- actin filament binding [IDA]
- glycoprotein binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein homodimerization activity [IDA]
- signal transducer activity [IMP]
- small GTPase binding [IDA]
- transcription factor binding [IPI]
Gene Ontology Cellular Component
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.
Publication
CDK7/GRP78 signaling axis contributes to tumor growth and metastasis in osteosarcoma.
Osteosarcoma derives from primitive bone-forming mesenchymal cells and is the most common primary bone malignancy. Therapeutic targeting of osteosarcoma has been unsuccessful; therefore, identifying novel osteosarcoma pathogenesis could offer new therapeutic options. CDK7 is a subunit within the general transcription factor TFIIH. We aim to explore the new mechanism by which CDK7 regulates osteosarcoma and our studies may provide new ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| HSPA5 FLNA | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | High | - | BioGRID | 3436943 |
Curated By
- BioGRID