P09652 · TBB4_CHICK
- ProteinTubulin beta-4 chain
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids449 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 11 | GTP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 69 | GTP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 69 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 138 | GTP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 142 | GTP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 143 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 144 | GTP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 204 | GTP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 226 | GTP (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | microtubule | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Molecular Function | metal ion binding | |
Molecular Function | structural constituent of cytoskeleton | |
Biological Process | axon guidance | |
Biological Process | microtubule cytoskeleton organization | |
Biological Process | mitotic cell cycle |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended nameTubulin beta-4 chain
- Alternative names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Galloanserae > Galliformes > Phasianidae > Phasianinae > Gallus
Accessions
- Primary accessionP09652
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000048266 | 1-449 | Tubulin beta-4 chain | |||
Sequence: MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYVPRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTRRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEMYEDDEEESEQGAK | ||||||
Modified residue | 438 | 5-glutamyl polyglutamate | ||||
Sequence: E | ||||||
Modified residue | 444 | Phosphoserine | ||||
Sequence: S |
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).
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
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 1-4 | MREI motif | ||||
Sequence: MREI | ||||||
Region | 421-449 | Disordered | ||||
Sequence: EYQQYQDATAEEEGEMYEDDEEESEQGAK | ||||||
Compositional bias | 431-449 | Acidic residues | ||||
Sequence: EEEGEMYEDDEEESEQGAK |
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 statusComplete
- Length449
- Mass (Da)50,421
- Last updated1989-07-01 v1
- ChecksumCECD9B729E0F9A84
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 431-449 | Acidic residues | ||||
Sequence: EEEGEMYEDDEEESEQGAK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M15052 EMBL· GenBank· DDBJ | AAA49119.1 EMBL· GenBank· DDBJ | Genomic DNA |