title: A tyrosine kinase associated with the red cell membrane phosphorylates band 3.
abstract: 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 anionic peptide acceptor sites.
mesh_terms: D001457:Anion Exchange Protein 1, Erythrocyte; D001798:Blood Proteins / Q000302:isolation & purification*; D004910:Erythrocyte Membrane / Q000201:enzymology*; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D007700:Kinetics; D010446:Peptide Fragments / Q000032:analysis; D010766:Phosphorylation; D011494:Protein Kinases / Q000097:blood* / Q000302:isolation & purification; D011505:Protein-Tyrosine Kinases
chemical_list: D001457:Anion Exchange Protein 1, Erythrocyte; D001798:Blood Proteins; D010446:Peptide Fragments; D011494:Protein Kinases; D011505:Protein-Tyrosine Kinases