http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID133194
Outgoing Links
| Predicate | Object |
|---|---|
| abstract | Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). |
| title | PTKc_EphR_A2 |
| isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/21387816 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/27470658 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/19377329 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/22716051 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/25128147 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11242356 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20045304 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13847572 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/26130274 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8566052 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20618191 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24776564 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/23334483 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9242944 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/25471010 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11888629 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1006095 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/19388534 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9198598 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24101734 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/18657976 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/5013544 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/28799099 |
| type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
| Predicate | Subject |
|---|---|
| has component | http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCNP_004422 http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP29317 |
Total number of triples: 28.