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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1990-03

AUTHORS

Samuel E. Lux, Kathryn M. John, Vann Bennett

ABSTRACT

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. More... »

PAGES

36-42

Journal

TITLE

Nature

ISSUE

6261

VOLUME

344

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/344036a0

DOI

http://dx.doi.org/10.1038/344036a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1027049732

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2137557


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