http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID173625
Outgoing Links
| Predicate | Object |
|---|---|
| abstract | Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. |
| title | PTKc_InsR_like |
| isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4971170 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9897981 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/27391129 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/32744331 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/29400989 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/14588580 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24618806 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8552161 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/15301588 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3068750 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20726407 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/258001 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/21359904 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20726408 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9816734 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11914444 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20013216 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11930274 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/23954667 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20618191 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13847572 |
| type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
Total number of triples: 38.