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

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Lux, SE; John, KM; Bennett, V

Published Date

  • March 1, 1990

Published In

Volume / Issue

  • 344 / 6261

Start / End Page

  • 36 - 42

PubMed ID

  • 2137557

International Standard Serial Number (ISSN)

  • 0028-0836

Digital Object Identifier (DOI)

  • 10.1038/344036a0


  • eng

Conference Location

  • England