A tyrosine kinase associated with the red cell membrane phosphorylates band 3.

@article{Dekowski1983ATK,
  title={A tyrosine kinase associated with the red cell membrane phosphorylates band 3.},
  author={Steven A Dekowski and Anne C Rybicki and Kurt Drickamer},
  journal={The Journal of biological chemistry},
  year={1983},
  volume={258 5},
  pages={2750-3}
}
Phosphorylation of Band 3, the anion transport protein of human erythrocyte membranes, has been studied by incubating isolated ghosts with [gamma-32P]ATP. One of the phosphate-acceptor sites is tyrosine 8 in the NH2-terminal cytoplasmic domain of the Band 3 protein. Seven out of 11 residues in the sequence surrounding the phosphorylated tyrosine are Asp or Glu. It is concluded that the erythrocyte, like other cells, contains a membrane-associated tyrosine kinase which phosphorylates highly… CONTINUE READING

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