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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Ankyrins
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Base Sequence
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Blood Proteins / genetics*
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Cell Cycle / genetics
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Cell Differentiation / genetics
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Cloning, Molecular
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DNA
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Erythrocytes
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Fungal Proteins
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Humans
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Invertebrates
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Membrane Proteins / genetics*
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Molecular Sequence Data
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Molecular Weight
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Proto-Oncogenes
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Repetitive Sequences, Nucleic Acid
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Sequence Homology, Nucleic Acid
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Viral Proteins
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Yeasts
Substances
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Ankyrins
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Blood Proteins
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Fungal Proteins
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Membrane Proteins
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Viral Proteins
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DNA