ITGA5
Gene Ontology Biological Process
- angiogenesis [TAS]
- axon guidance [TAS]
- blood coagulation [TAS]
- cell adhesion [TAS]
- cell-substrate adhesion [IMP]
- endodermal cell differentiation [IMP]
- extracellular matrix organization [TAS]
- heterotypic cell-cell adhesion [IMP]
- leukocyte migration [TAS]
- negative regulation of anoikis [IMP]
- positive regulation of peptidyl-tyrosine phosphorylation [IMP]
- positive regulation of vascular endothelial growth factor receptor signaling pathway [TAS]
- wound healing, spreading of epidermal cells [IEP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
Affinity Capture-Western
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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.
Publication
Novel vascular endothelial growth factor binding domains of fibronectin enhance vascular endothelial growth factor biological activity.
Interactions between integrins and growth factor receptors play a critical role in the development and healing of the vasculature. This study mapped two binding domains on fibronectin (FN) that modulate the activity of the angiogenic factor, vascular endothelial growth factor (VEGF). Using solid-phase assays and surface plasmon resonance analysis, we identified two novel VEGF binding domains within the N- and ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID