  Thermodynamic scaling theory, previously applied mainly to small proteins,
here analyzes quantitative evolution of the titled functional network giant hub
enzymes. The broad domain structure identified homologically is confirmed
hydropathically using amino acid sequences only. The most surprising results
concern the evolution of the tyrosine kinase globular surface roughness from
avian to mammals, which is first order, compared to the evolution within
mammals from rodents to humans, which is second order. The mystery of the
unique amide terminal region of proto oncogene tyrosine protein kinase is
resolved by the discovery there of a septad targeting cluster, which is
paralleled by an octad catalytic cluster in tyrosine kinase in humans and a few
other species. These results, which go far towards explaining why these
proteins are among the largest giant hubs in protein interaction networks, use
no adjustable parameters.
