P09652 · TBB4_CHICK

Function

function

Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for binding site.

144950100150200250300350400
TypeIDPosition(s)Description
Binding site11GTP (UniProtKB | ChEBI)
Binding site69GTP (UniProtKB | ChEBI)
Binding site69Mg2+ (UniProtKB | ChEBI)
Binding site138GTP (UniProtKB | ChEBI)
Binding site142GTP (UniProtKB | ChEBI)
Binding site143GTP (UniProtKB | ChEBI)
Binding site144GTP (UniProtKB | ChEBI)
Binding site204GTP (UniProtKB | ChEBI)
Binding site226GTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentmicrotubule
Molecular FunctionGTP binding
Molecular FunctionGTPase activity
Molecular Functionmetal ion binding
Molecular Functionstructural constituent of cytoskeleton
Biological Processaxon guidance
Biological Processmicrotubule cytoskeleton organization
Biological Processmitotic cell cycle

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Tubulin beta-4 chain
  • Alternative names
    • Beta-tubulin class-III

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Galloanserae > Galliformes > Phasianidae > Phasianinae > Gallus

Accessions

  • Primary accession
    P09652

Proteomes

Organism-specific databases

Subcellular Location

Phenotypes & Variants

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000482661-449Tubulin beta-4 chain
Modified residue4385-glutamyl polyglutamate
Modified residue444Phosphoserine

Post-translational modification

Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation 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 polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear.
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (By similarity).
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 (By similarity).

Keywords

PTM databases

Expression

Tissue specificity

Neuron specific.

Interaction

Subunit

Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for motif, region, compositional bias.

TypeIDPosition(s)Description
Motif1-4MREI motif
Region421-449Disordered
Compositional bias431-449Acidic residues

Domain

The MREI motif is common among all beta-tubulin isoforms and may be critical for tubulin autoregulation.

Sequence similarities

Belongs to the tubulin family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    449
  • Mass (Da)
    50,421
  • Last updated
    1989-07-01 v1
  • Checksum
    CECD9B729E0F9A84
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYVPRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTRRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEMYEDDEEESEQGAK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias431-449Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M15052
EMBL· GenBank· DDBJ
AAA49119.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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