UNIPROT #

P07437

PROTEIN NAME

beta-tubulin

SYNONYMS

Beta 4 tubulin antibody;Beta 5 tubulin antibody;BetaTubulin antibody;TBB5_HUMAN antibody;TUBB antibody;TUBB2 antibody;TUBB2A antibody;TUBB5 antibody;tubulin beta 2A antibody;Tubulin beta chain antibody;Tubulin beta-5 chain antibody

SEQUENCE SIMILARITIES

Belongs to the tubulin family.

TISSUE SPECIFICITY

Ubiquitously expressed with highest levels in spleen, thymus and immature brain.

POST-TRANSLATIONAL MODIFICATION

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.

SUBCELLULAR LOCATION

Cytoplasm ,cytoskeleton

FUNCTION

Tubulin is one of several members of a small family of globular proteins. The most common members of the tubulin family are α-tubulin and β-tubulin. The beta-tubulin (relative molecular weight about 50 kDa) is counterpart of alpha-tubulin in tubulin heterodimer, it is coded by multiple tubulin genes and it is also posttranslationally modified. Heterogeneity of subunit is concentrated in C-terminal structural domain. Beta-Tubulin may have bound GTP or GDP. Under certain conditions β-tubulin can hydrolyze its bound GTP to GDP plus Pi, release the Pi, and exchange the GDP for GTP.