Tissue Specificity | Ubiquitously expressed with highest levels in spleen, thymus and immature brain. |
Post Translational Modifications | Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group. Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Some glutamate residues at the C-terminus are 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). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of monoglycylation is still unclear (Probable). Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules. |
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. |
Database Links | Reactome: R-HSA-2565942 |
Cellular Localisation | CytoplasmCytoskeleton |
Protein Name | Tubulin Beta ChainTubulin Beta-5 Chain |
Alternative Names | Anti-Tubulin Beta Chain antibodyAnti-Tubulin Beta-5 Chain antibodyAnti-TUBB antibodyAnti-TUBB5 antibodyAnti-OK antibodyAnti-SW-cl.56 antibody |
Information sourced from uniprot.org