http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID270681
Outgoing Links
| Predicate | Object |
|---|---|
| abstract | Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. |
| title | PTKc_VEGFR2 |
| isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/22067480 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7187047 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30154541 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/15310581 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/25137194 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/32183830 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/324667 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20720965 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30168805 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11939664 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13966393 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/19378746 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/22053450 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20711061 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7917245 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7910545 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/22077651 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11934381 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/31523959 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1664777 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4391825 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20724546 |
| type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
Total number of triples: 35.