P09642 · TBA3_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.

Miscellaneous

This tubulin does not have a C-terminal tyrosine.
There are at least seven alpha tubulin genes (alpha-1 to alpha-6, and alpha-8), and a pseudogene (alpha-7) in chicken.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site15GTP (UniProtKB | ChEBI)
Binding site19GTP (UniProtKB | ChEBI)
Binding site20GTP (UniProtKB | ChEBI)
Binding site54GTP (UniProtKB | ChEBI)
Binding site81GTP (UniProtKB | ChEBI)
Binding site103GTP (UniProtKB | ChEBI)
Active site129

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentmicrotubule
Molecular FunctionGTP binding
Molecular Functionhydrolase activity
Molecular Functionstructural constituent of cytoskeleton
Biological Processmicrotubule cytoskeleton organization
Biological Processmitotic cell cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Tubulin alpha-3 chain
  • EC number

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
    P09642

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000481491-322Tubulin alpha-3 chain

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).

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.

Structure

Family & Domains

Sequence similarities

Belongs to the tubulin family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    322
  • Mass (Da)
    36,088
  • Last updated
    1989-07-01 v1
  • Checksum
    BB39B41C9E916204
ADQCSGLQGFLVFHSFGGGTGSGFTSLLMERLSVEYSKKSKLEFSVYPDRQVSTAVVEPYNSILTTHTTLEHSDCSFMVDNEAIYDICNRNLDIERPTYTNLNRLIGQIVSSVTASLRFNGALNVDLIEFQTNLVPYPRIHFPLTTYARIISAEKAYHEQLSVPEITNACFEFSNQMVKCDPRRGKYMACCLLYRGDVVPKDVNAAIAAIKTRRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGRNSADGGEFEE

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X07442
EMBL· GenBank· DDBJ
CAA30324.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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