KDR
Gene Ontology Biological Process
- angiogenesis [TAS]
- calcium-mediated signaling using intracellular calcium source [IMP]
- cell migration involved in sprouting angiogenesis [ISS]
- cellular response to vascular endothelial growth factor stimulus [IDA, IMP]
- embryonic hemopoiesis [ISS]
- endothelium development [ISS]
- extracellular matrix organization [TAS]
- negative regulation of apoptotic process [IMP]
- negative regulation of endothelial cell apoptotic process [IDA]
- peptidyl-tyrosine autophosphorylation [ISS]
- peptidyl-tyrosine phosphorylation [IDA]
- positive regulation of ERK1 and ERK2 cascade [IMP]
- positive regulation of MAPK cascade [IDA]
- positive regulation of angiogenesis [IMP]
- positive regulation of cell migration [IDA, IMP]
- positive regulation of cell proliferation [IDA, IMP]
- positive regulation of endothelial cell migration [IMP]
- positive regulation of endothelial cell proliferation [IMP]
- positive regulation of focal adhesion assembly [IDA]
- positive regulation of nitric-oxide synthase biosynthetic process [IDA, IMP]
- positive regulation of phosphatidylinositol 3-kinase signaling [IDA]
- positive regulation of positive chemotaxis [IDA]
- positive regulation of protein phosphorylation [IDA]
- positive regulation of vasculogenesis [ISS]
- protein autophosphorylation [IDA]
- regulation of cell shape [IDA]
- signal transduction by phosphorylation [TAS]
- transmembrane receptor protein tyrosine kinase signaling pathway [TAS]
- vascular endothelial growth factor receptor signaling pathway [IDA, IMP, TAS]
- vascular endothelial growth factor signaling pathway [IDA]
- vasculogenesis [ISS]
Gene Ontology Molecular Function- Hsp90 protein binding [TAS]
- growth factor binding [IPI]
- integrin binding [IPI]
- protein binding [IPI]
- protein tyrosine kinase activity [IDA]
- receptor signaling protein tyrosine kinase activity [TAS]
- transmembrane receptor protein tyrosine kinase activity [TAS]
- vascular endothelial growth factor binding [IPI]
- vascular endothelial growth factor-activated receptor activity [IDA]
- Hsp90 protein binding [TAS]
- growth factor binding [IPI]
- integrin binding [IPI]
- protein binding [IPI]
- protein tyrosine kinase activity [IDA]
- receptor signaling protein tyrosine kinase activity [TAS]
- transmembrane receptor protein tyrosine kinase activity [TAS]
- vascular endothelial growth factor binding [IPI]
- vascular endothelial growth factor-activated receptor activity [IDA]
Gene Ontology Cellular Component
VEGFA
Gene Ontology Biological Process
- VEGF-activated neuropilin signaling pathway [ISS]
- activation of protein kinase activity [IDA]
- angiogenesis [IDA]
- artery morphogenesis [ISS]
- basophil chemotaxis [IDA]
- blood coagulation [TAS]
- branching morphogenesis of an epithelial tube [ISS]
- camera-type eye morphogenesis [ISS]
- cardiac muscle fiber development [ISS]
- cardiac vascular smooth muscle cell development [ISS]
- cell maturation [ISS]
- cell migration involved in sprouting angiogenesis [IDA]
- cellular response to hypoxia [IDA, TAS]
- cellular response to vascular endothelial growth factor stimulus [IDA]
- commissural neuron axon guidance [ISS]
- coronary artery morphogenesis [ISS]
- coronary vein morphogenesis [ISS]
- dopaminergic neuron differentiation [ISS]
- endothelial cell chemotaxis [IDA]
- epithelial cell differentiation [ISS]
- eye photoreceptor cell development [ISS]
- growth [ISS]
- heart morphogenesis [ISS]
- in utero embryonic development [ISS]
- induction of positive chemotaxis [IDA, NAS]
- kidney development [ISS]
- lactation [ISS]
- lung development [ISS]
- lymph vessel morphogenesis [ISS]
- macrophage differentiation [IDA]
- mammary gland alveolus development [ISS]
- mesoderm development [ISS]
- monocyte differentiation [IDA]
- negative regulation of apoptotic process [IMP]
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [IDA]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- nervous system development [TAS]
- outflow tract morphogenesis [ISS]
- ovarian follicle development [ISS]
- patterning of blood vessels [ISS]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive chemotaxis [IDA]
- positive regulation of CREB transcription factor activity [IDA]
- positive regulation of ERK1 and ERK2 cascade [IDA]
- positive regulation of MAP kinase activity [IDA]
- positive regulation of angiogenesis [IDA, IMP]
- positive regulation of axon extension involved in axon guidance [ISS]
- positive regulation of blood vessel endothelial cell migration [IDA]
- positive regulation of branching involved in ureteric bud morphogenesis [ISS]
- positive regulation of cell adhesion [IDA]
- positive regulation of cell migration [IDA]
- positive regulation of cell migration involved in sprouting angiogenesis [IDA]
- positive regulation of cell proliferation [IDA]
- positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway [IDA]
- positive regulation of cellular component movement [IDA]
- positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway [IDA]
- positive regulation of endothelial cell migration [IDA]
- positive regulation of endothelial cell proliferation [IDA, ISS]
- positive regulation of epithelial cell proliferation [ISS]
- positive regulation of focal adhesion assembly [IDA]
- positive regulation of gene expression [IDA]
- positive regulation of histone deacetylase activity [IDA]
- positive regulation of leukocyte migration [TAS]
- positive regulation of mast cell chemotaxis [IDA]
- positive regulation of mesenchymal cell proliferation [ISS]
- positive regulation of neuroblast proliferation [ISS]
- positive regulation of p38MAPK cascade [IDA]
- positive regulation of peptidyl-serine phosphorylation [IDA]
- positive regulation of peptidyl-tyrosine autophosphorylation [IDA]
- positive regulation of peptidyl-tyrosine phosphorylation [IDA]
- positive regulation of positive chemotaxis [IDA]
- positive regulation of protein autophosphorylation [IDA]
- positive regulation of protein complex assembly [IDA]
- positive regulation of protein kinase C signaling [IDA]
- positive regulation of protein kinase D signaling [IDA]
- positive regulation of protein localization to early endosome [IDA]
- positive regulation of protein phosphorylation [IDA]
- positive regulation of receptor internalization [IDA]
- positive regulation of retinal ganglion cell axon guidance [ISS]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IMP]
- positive regulation of transcription from RNA polymerase II promoter in response to hypoxia [IMP]
- positive regulation of vascular endothelial growth factor receptor signaling pathway [IDA]
- positive regulation of vascular permeability [IDA]
- post-embryonic camera-type eye development [ISS]
- primitive erythrocyte differentiation [ISS]
- regulation of cGMP metabolic process [IDA]
- regulation of cell shape [IDA]
- regulation of retinal ganglion cell axon guidance [ISS]
- regulation of transcription from RNA polymerase II promoter [IMP]
- regulation of transcription from RNA polymerase II promoter in response to hypoxia [TAS]
- response to hypoxia [IDA]
- surfactant homeostasis [ISS]
- tube formation [IDA]
- vascular endothelial growth factor receptor signaling pathway [IDA, TAS]
- vascular endothelial growth factor signaling pathway [IDA]
- vasculogenesis [TAS]
Gene Ontology Molecular Function- chemoattractant activity [IDA]
- cytokine activity [IDA, ISS]
- extracellular matrix binding [IC]
- fibronectin binding [IDA]
- growth factor activity [IDA, ISS]
- heparin binding [IDA, IMP]
- identical protein binding [IPI]
- neuropilin binding [IPI]
- platelet-derived growth factor receptor binding [IPI]
- protein binding [IPI]
- protein heterodimerization activity [IDA]
- protein homodimerization activity [ISS]
- receptor agonist activity [IPI]
- vascular endothelial growth factor receptor 1 binding [IPI]
- vascular endothelial growth factor receptor 2 binding [IPI]
- vascular endothelial growth factor receptor binding [IPI]
- chemoattractant activity [IDA]
- cytokine activity [IDA, ISS]
- extracellular matrix binding [IC]
- fibronectin binding [IDA]
- growth factor activity [IDA, ISS]
- heparin binding [IDA, IMP]
- identical protein binding [IPI]
- neuropilin binding [IPI]
- platelet-derived growth factor receptor binding [IPI]
- protein binding [IPI]
- protein heterodimerization activity [IDA]
- protein homodimerization activity [ISS]
- receptor agonist activity [IPI]
- vascular endothelial growth factor receptor 1 binding [IPI]
- vascular endothelial growth factor receptor 2 binding [IPI]
- vascular endothelial growth factor receptor binding [IPI]
Gene Ontology Cellular Component
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
Immunoglobulin-like domain 4-mediated ligand-independent dimerization triggers VEGFR-2 activation in HUVECs and VEGFR2-positive breast cancer cells.
The extracellular region (EC) of the vascular endothelial growth factor (VEGF) receptor-2 (VEGFR-2) contains seven immunoglobulin-like (Ig-like) domains that are required for specific ligand binding and receptor dimerization. Studies of domain 4-7 deletions and substitutions provided insights into the interaction between receptors in the absence of VEGF. In this study, we investigated the effect of domain 4 in ligand-independent VEGFR-2 ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| VEGFA KDR | Biochemical Activity Biochemical Activity 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. | Low | - | BioGRID | 259129 | |
| VEGFA KDR | Co-localization Co-localization Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments. | Low | - | BioGRID | 2200927 | |
| KDR VEGFA | FRET FRET An interaction is inferred when close proximity of interaction partners is detected by fluorescence resonance energy transfer between pairs of fluorophore-labeled molecules, such as occurs between CFP (donor) and YFP (acceptor) fusion proteins. | Low | - | BioGRID | 2660138 | |
| VEGFA KDR | 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 | - | |
| KDR VEGFA | 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 | - | |
| VEGFA KDR | 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 | 885801 | |
| KDR VEGFA | 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