Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate [goid 4713] [evidence IEA]; Interacting selectively with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator [goid 5524] [evidence IEA]; Interacting selectively with a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose moiety [goid 166] [evidence IEA]; Combining with an extracellular or intracellular messenger to initiate a change in cell activity [goid 4872] [evidence IEA];  [goid 5010] [pmid 7679099] [evidence IDA]; Interacting selectively with the insulin receptor [goid 5158] [pmid 8452530] [evidence IDA]; Interacting selectively with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator [goid 5524] [evidence IEA]; Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2 [goid 16740] [evidence IEA]; Interacting selectively with insulin-like growth factor I [goid 31994] [pmid 8452530] [evidence IPI]; Interacting selectively with an identical protein or proteins [goid 42802] [pmid 11448933] [evidence IPI]; Interacting selectively with a phosphoinositide 3-kinase, any enzyme that catalyzes the addition of a phosphate group to an inositol lipid at the 3' position of the inositol ring [goid 43548] [pmid 7541045] [evidence IPI]; Interacting selectively with insulin, a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms [goid 43559] [pmid 8452530] [evidence IPI]; Interacting selectively with any of the insulin receptor substrate (IRS) proteins, adaptor proteins that bind to the transphosphorylated insulin and insulin-like growth factor receptors, are themselves phosphorylated and in turn recruit SH2 domain-containing signaling molecules to form a productive signaling complex [goid 43560] [pmid 7541045] [evidence IPI]