title: Tubulin amino acid sequence and consequences.
abstract: The 451 residues of alpha-tubulin from pig brain and the 445 residues of the beta-subunit display 41% sequence identity. Although the primary structure is highly conserved during evolution, several positions in each of the chains are heterogeneous, indicating four alpha-variants and two of the beta-polypeptide. Both C-terminal parts are highly acidic. Small regions can be correlated to sequences of nucleotide binding proteins. Cysteine beta 201 may be involved in the colchicine binding site.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D001665:Binding Sites; D001921:Brain; D002352:Carrier Proteins / Q000378:metabolism; D003078:Colchicine / Q000378:metabolism; D002373:Cyclic AMP Receptor Protein; D014644:Genetic Variation; D009154:Mutation; D013552:Swine; D014404:Tubulin / Q000032:analysis* / Q000235:genetics / Q000378:metabolism
chemical_list: D000596:Amino Acids; D002352:Carrier Proteins; D002373:Cyclic AMP Receptor Protein; D014404:Tubulin; D003078:Colchicine