Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins

Nature. 1990 Mar 1;344(6261):36-42. doi: 10.1038/344036a0.


Analysis of complementary DNA for human erythroid ankyrin indicates that the mature protein contains 1,880 amino acids comprising an N-terminal domain binding integral membrane proteins and tubulin, a central domain binding spectrin and vimentin, and an acidic C-terminal 'regulatory' domain containing an alternatively spliced sequence missing from ankyrin variant 2.2. The N-terminal domain is almost entirely composed of 22 tandem 33-amino-acid repeats. Similar repeats are found in yeast and invertebrate proteins involved in cell-cycle control and tissue differentiation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Ankyrins
  • Base Sequence
  • Blood Proteins / genetics*
  • Cell Cycle / genetics
  • Cell Differentiation / genetics
  • Cloning, Molecular
  • DNA
  • Erythrocytes
  • Fungal Proteins
  • Humans
  • Invertebrates
  • Membrane Proteins / genetics*
  • Molecular Sequence Data
  • Molecular Weight
  • Proto-Oncogenes
  • Repetitive Sequences, Nucleic Acid
  • Sequence Homology, Nucleic Acid
  • Viral Proteins
  • Yeasts


  • Ankyrins
  • Blood Proteins
  • Fungal Proteins
  • Membrane Proteins
  • Viral Proteins
  • DNA

Associated data

  • GENBANK/X16609