F2
Gene Ontology Biological Process
- blood coagulation [TAS]
- blood coagulation, intrinsic pathway [TAS]
- cell surface receptor signaling pathway [IDA]
- cellular protein metabolic process [TAS]
- cytosolic calcium ion homeostasis [IDA]
- fibrinolysis [IDA]
- leukocyte migration [TAS]
- multicellular organismal development [TAS]
- negative regulation of astrocyte differentiation [IDA]
- negative regulation of fibrinolysis [TAS]
- negative regulation of platelet activation [TAS]
- negative regulation of proteolysis [IDA]
- peptidyl-glutamic acid carboxylation [TAS]
- platelet activation [IDA, TAS]
- positive regulation of blood coagulation [IDA]
- positive regulation of collagen biosynthetic process [IDA]
- positive regulation of phospholipase C-activating G-protein coupled receptor signaling pathway [IDA]
- positive regulation of protein phosphorylation [IDA]
- positive regulation of reactive oxygen species metabolic process [IDA]
- positive regulation of release of sequestered calcium ion into cytosol [IDA]
- post-translational protein modification [TAS]
- proteolysis [TAS]
- regulation of blood coagulation [TAS]
- response to wounding [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
ST13
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Biochemical Activity (Proteolytic Processing)
An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.
Publication
Domain structure of the HSC70 cochaperone, HIP.
The domain structure of the HSC70-interacting protein (HIP), a 43-kDa cytoplasmic cochaperone involved in the regulation of HSC70 chaperone activity and the maturation of progesterone receptor, has been probed by limited proteolysis and biophysical and biochemical approaches. HIP proteolysis by thrombin and chymotrypsin generates essentially two fragments, an NH2-terminal fragment of 25 kDa (N25) and a COOH-terminal fragment of 18 ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID