BAIT
CALCR
CRT, CT-R, CTR, CTR1
calcitonin receptor
GO Process (11)
GO Function (5)
GO Component (2)
Gene Ontology Biological Process
- G-protein coupled receptor signaling pathway [IDA]
- activation of adenylate cyclase activity [IDA]
- activation of phospholipase C activity [IDA]
- adenylate cyclase-activating G-protein coupled receptor signaling pathway [IDA, NAS]
- positive regulation of adenylate cyclase activity [IDA]
- positive regulation of cAMP biosynthetic process [IDA]
- positive regulation of cytosolic calcium ion concentration [IDA]
- protein localization to plasma membrane [IDA]
- protein transport [IDA]
- receptor internalization [IDA]
- response to glucocorticoid [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
THBS1
THBS, THBS-1, TSP, TSP-1, TSP1
thrombospondin 1
GO Process (60)
GO Function (15)
GO Component (12)
Gene Ontology Biological Process
- activation of MAPK activity [IMP]
- behavioral response to pain [ISS]
- blood coagulation [TAS]
- cell adhesion [NAS]
- cell cycle arrest [IDA]
- cell migration [IDA]
- cellular response to heat [NAS]
- chronic inflammatory response [IEP]
- engulfment of apoptotic cell [IDA]
- extracellular matrix organization [TAS]
- immune response [IEP]
- negative regulation of angiogenesis [IDA]
- negative regulation of antigen processing and presentation of peptide or polysaccharide antigen via MHC class II [IDA]
- negative regulation of apoptotic process [IDA]
- negative regulation of blood vessel endothelial cell migration [IDA]
- negative regulation of cGMP-mediated signaling [IDA]
- negative regulation of cell-matrix adhesion [IDA]
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [IDA]
- negative regulation of dendritic cell antigen processing and presentation [IDA]
- negative regulation of endothelial cell chemotaxis [IDA]
- negative regulation of endothelial cell migration [IDA]
- negative regulation of endothelial cell proliferation [IDA, IMP]
- negative regulation of extrinsic apoptotic signaling pathway [TAS]
- negative regulation of fibrinolysis [IDA]
- negative regulation of fibroblast growth factor receptor signaling pathway [IDA]
- negative regulation of focal adhesion assembly [TAS]
- negative regulation of interleukin-12 production [IDA]
- negative regulation of nitric oxide mediated signal transduction [IDA]
- negative regulation of plasma membrane long-chain fatty acid transport [IDA]
- negative regulation of plasminogen activation [IDA]
- peptide cross-linking [IDA]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive regulation of angiogenesis [IMP]
- positive regulation of blood coagulation [IDA]
- positive regulation of blood vessel endothelial cell migration [IDA]
- positive regulation of cell migration [IDA, IMP]
- positive regulation of chemotaxis [IDA]
- positive regulation of endothelial cell apoptotic process [IDA]
- positive regulation of endothelial cell migration [IDA]
- positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [IDA]
- positive regulation of fibroblast migration [IDA]
- positive regulation of macrophage activation [IDA]
- positive regulation of macrophage chemotaxis [ISS]
- positive regulation of phosphorylation [IMP]
- positive regulation of protein kinase B signaling [IDA]
- positive regulation of reactive oxygen species metabolic process [IDA]
- positive regulation of transforming growth factor beta receptor signaling pathway [IDA]
- positive regulation of transforming growth factor beta1 production [ISS]
- positive regulation of translation [IDA]
- positive regulation of tumor necrosis factor biosynthetic process [IDA]
- regulation of cGMP metabolic process [IDA]
- response to calcium ion [IDA]
- response to drug [IEP]
- response to endoplasmic reticulum stress [ISS]
- response to glucose [IDA]
- response to hypoxia [NAS]
- response to magnesium ion [IDA]
- response to progesterone [TAS]
- sprouting angiogenesis [IMP]
Gene Ontology Molecular Function- calcium ion binding [NAS]
- collagen V binding [IDA]
- fibrinogen binding [IDA]
- fibroblast growth factor binding [IDA]
- fibronectin binding [IDA]
- glycoprotein binding [NAS]
- heparin binding [IDA]
- identical protein binding [NAS]
- integrin binding [IMP]
- laminin binding [IDA]
- low-density lipoprotein particle binding [IDA]
- phosphatidylserine binding [IDA]
- protein binding [IPI]
- proteoglycan binding [TAS]
- transforming growth factor beta binding [ISS, TAS]
- calcium ion binding [NAS]
- collagen V binding [IDA]
- fibrinogen binding [IDA]
- fibroblast growth factor binding [IDA]
- fibronectin binding [IDA]
- glycoprotein binding [NAS]
- heparin binding [IDA]
- identical protein binding [NAS]
- integrin binding [IMP]
- laminin binding [IDA]
- low-density lipoprotein particle binding [IDA]
- phosphatidylserine binding [IDA]
- protein binding [IPI]
- proteoglycan binding [TAS]
- transforming growth factor beta binding [ISS, TAS]
Gene Ontology Cellular Component
- cell surface [IDA]
- endoplasmic reticulum [ISS]
- external side of plasma membrane [IDA]
- extracellular matrix [IDA, ISS, TAS]
- extracellular region [TAS]
- extracellular space [IDA]
- extracellular vesicular exosome [IDA]
- fibrinogen complex [IDA]
- platelet alpha granule [IDA]
- platelet alpha granule lumen [TAS]
- sarcoplasmic reticulum [ISS]
- secretory granule [IDA]
Homo sapiens
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 anti-adhesive activity of thrombospondin is mediated by the N-terminal domain of cell surface calreticulin.
Thrombospondin (TSP) induces reorganization of the actin cytoskeleton and restructuring of focal adhesions through binding of amino acids (aa) 17-35 (hep I peptide) of thrombospondin to a cell surface form of calreticulin (CRT). In this report we provide further evidence for the involvement of calreticulin in thrombospondin signaling and characterize thrombospondin-calreticulin interactions. Wild type but not crt(-/-) cells respond to ... [more]
J. Biol. Chem. Oct. 04, 2002; 277(40);37219-28 [Pubmed: 12147682]
Throughput
- Low Throughput
Curated By
- BioGRID