TLN1
Gene Ontology Biological Process
- activation of signaling protein activity involved in unfolded protein response [TAS]
- axon guidance [TAS]
- blood coagulation [TAS]
- cell-cell junction assembly [TAS]
- cellular component movement [NAS]
- cellular protein metabolic process [TAS]
- cytoskeletal anchoring at plasma membrane [NAS]
- endoplasmic reticulum unfolded protein response [TAS]
- muscle contraction [TAS]
- platelet activation [TAS]
- platelet aggregation [IMP]
- platelet degranulation [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
ITGB3
Gene Ontology Biological Process
- activation of protein kinase activity [IMP]
- angiogenesis involved in wound healing [TAS]
- apolipoprotein A-I-mediated signaling pathway [IMP]
- axon guidance [TAS]
- blood coagulation [TAS]
- cell adhesion [TAS]
- cell growth [IMP]
- cell migration [IMP]
- cell-matrix adhesion [IDA, IMP]
- cell-substrate adhesion [IMP]
- extracellular matrix organization [TAS]
- heterotypic cell-cell adhesion [IMP]
- integrin-mediated signaling pathway [IDA, TAS]
- leukocyte migration [TAS]
- mesodermal cell differentiation [IEP]
- negative chemotaxis [IMP]
- negative regulation of lipid storage [IMP]
- negative regulation of lipid transport [IMP]
- negative regulation of lipoprotein metabolic process [IMP]
- negative regulation of low-density lipoprotein particle receptor biosynthetic process [IMP]
- negative regulation of macrophage derived foam cell differentiation [IMP]
- platelet activation [IMP, TAS]
- platelet aggregation [IMP]
- platelet degranulation [TAS]
- positive regulation of endothelial cell migration [IMP]
- positive regulation of endothelial cell proliferation [IMP]
- positive regulation of peptidyl-tyrosine phosphorylation [IMP]
- positive regulation of protein phosphorylation [TAS]
- positive regulation of vascular endothelial growth factor receptor signaling pathway [TAS]
- protein folding [IDA]
- regulation of bone resorption [TAS]
- smooth muscle cell migration [IMP]
- substrate adhesion-dependent cell spreading [IDA]
- tube development [TAS]
- viral entry into host cell [IMP]
- wound healing [IC]
Gene Ontology Molecular Function- cell adhesion molecule binding [IPI]
- extracellular matrix binding [IDA]
- fibronectin binding [IMP]
- identical protein binding [IPI]
- platelet-derived growth factor receptor binding [TAS]
- protease binding [IDA]
- protein binding [IPI]
- protein disulfide isomerase activity [IDA]
- vascular endothelial growth factor receptor 2 binding [IPI, TAS]
- cell adhesion molecule binding [IPI]
- extracellular matrix binding [IDA]
- fibronectin binding [IMP]
- identical protein binding [IPI]
- platelet-derived growth factor receptor binding [TAS]
- protease binding [IDA]
- protein binding [IPI]
- protein disulfide isomerase activity [IDA]
- vascular endothelial growth factor receptor 2 binding [IPI, TAS]
Gene Ontology Cellular Component
- alphav-beta3 integrin-vitronectin complex [TAS]
- cell surface [IDA]
- extracellular vesicular exosome [IDA]
- filopodium membrane [IDA]
- focal adhesion [IDA]
- integral component of plasma membrane [TAS]
- integrin alphav-beta3 complex [IDA]
- integrin complex [IDA]
- lamellipodium membrane [IDA]
- melanosome [IDA]
- microvillus membrane [IDA]
- nucleus [IDA]
- plasma membrane [IDA, TAS]
- platelet alpha granule membrane [TAS]
- receptor complex [IDA]
- ruffle membrane [IDA]
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
NMR analysis of structure and dynamics of the cytosolic tails of integrin alpha IIb beta 3 in aqueous solution.
The structural and dynamic properties of the cytosolic tails of the adhesion receptor integrin alphaIIbbeta3, fused to a coiled-coil construct via (Gly)(3) linkers, were studied in aqueous solution by nuclear magnetic resonance (NMR) spectroscopy. Both tails were largely flexible and unstructured, although, in the beta3 tail, residues Arg(724)-Ala(735) have a propensity to form a helical structure and residues Asn(744)-Tyr(747) (NPLY) ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TLN1 ITGB3 | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | Low | - | BioGRID | - | |
| ITGB3 TLN1 | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | Low | - | BioGRID | - | |
| TLN1 ITGB3 | Reconstituted Complex 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. | Low | - | BioGRID | - | |
| TLN1 ITGB3 | Reconstituted Complex 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. | Low | - | BioGRID | - | |
| ITGB3 TLN1 | Reconstituted Complex 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. | Low | - | BioGRID | - | |
| TLN1 ITGB3 | Reconstituted Complex 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. | Low | - | BioGRID | - |
Curated By
- BioGRID