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Comments and Description Text from UniProtKB
ID:TBA4A_HUMAN DESCRIPTION: RecName: Full=Tubulin alpha-4A chain; AltName: Full=Alpha-tubulin 1; AltName: Full=Testis-specific alpha-tubulin; AltName: Full=Tubulin H2-alpha; AltName: Full=Tubulin alpha-1 chain; FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain. SUBUNIT: Dimer of alpha and beta chains. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. PTM: Some glutamate residues at the C-terminus are polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules (Probable). PTM: Acetylation of alpha-tubulins at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling (By similarity). MISCELLANEOUS: This tubulin does not have a C-terminal tyrosine. SIMILARITY: Belongs to the tubulin family. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/tuba1/"; WEB RESOURCE: Name=Wikipedia; Note=Tubulin entry; URL="http://en.wikipedia.org/wiki/Tubulin";
ModBase Predicted Comparative 3D Structure on P68366
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