Q9JJZ2 · TBA8_MOUSE

  • Protein
    Tubulin alpha-8 chain
  • Gene
    Tuba8
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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.

Miscellaneous

This tubulin does not have a C-terminal tyrosine; however, its C-terminal phenylalanine residue can be cleaved.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site11GTP (UniProtKB | ChEBI)
Binding site71GTP (UniProtKB | ChEBI)
Binding site71Mg2+ (UniProtKB | ChEBI)
Binding site140GTP (UniProtKB | ChEBI)
Binding site144GTP (UniProtKB | ChEBI)
Binding site145GTP (UniProtKB | ChEBI)
Binding site179GTP (UniProtKB | ChEBI)
Binding site206GTP (UniProtKB | ChEBI)
Binding site228GTP (UniProtKB | ChEBI)
Active site254

GO annotations

AspectTerm
Cellular Componentacrosomal vesicle
Cellular Componentcytoplasm
Cellular Componentmicrotubule
Molecular FunctionGTP binding
Molecular Functionhydrolase activity
Molecular Functionmetal ion binding
Molecular Functionstructural constituent of cytoskeleton
Biological Processmicrotubule cytoskeleton organization
Biological Processmitotic cell cycle
Biological Processspermatid development
Biological Processspermatogenesis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      Tuba8

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9JJZ2
  • Secondary accessions
    • D4P911
    • Q9CV57

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004564351-448Dephenylalaninated tubulin alpha-8 chain
ChainPRO_00000481251-449Tubulin alpha-8 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. Cilia and flagella glycylation is required for their stability and maintenance. Flagella glycylation controls sperm motility (PubMed:33414192).
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843).
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).
Glutamylation is also involved in cilia motility (PubMed:23897886).
The C-terminal phenylalanine residue is cleaved by MATCAP1/KIAA0895L.

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed at highest levels in the testis, followed by skeletal and heart muscle. Expressed at low levels in the developing brain.

Developmental stage

At embryonic day (E) 13.5, expressed in the cortical preplate and cingulate cortex. By 15.5 dpc, the strongest expression is seen in the cortical plate. By 18.5 dpc, cortical expression is most intense in the upper layers and subplate. There is strong expression in the areas CA1-3 of the hippocampus. At P0, cortical expression is strongest in the dense cortical plate and subplate. Hippocampal expression is more intense in areas CA1-3 than in the dentate gyrus. At P8, lamination is almost complete and cortical expression is strongest in layers II-III and V and the subplate. There is also expression in the mediodorsal nuclei of the thalamus, the mitral cell layer of the olfactory bulb, and the external granular layer, molecular layer, and internal granular cell layer of the cerebellum.

Gene expression databases

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

Miscellaneous

Structure

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif1-4MREC motif

Domain

The MREC motif 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)
    50,052
  • Last updated
    2000-10-01 v1
  • Checksum
    AA979E2DB21FC5DD
MRECISVHVGQAGVQIGNACWELFCLEHGIQADGTFGTQASKINDDDSFTTFFSETGNGKHVPRAVMVDLEPTVVDEVRAGTYRQLFHPEQLITGKEDAANNYARGHYTVGKESIDLVLDRIRKLTDACSGLQGFLIFHSFGGGTGSGFTSLLMERLSLDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLVTYAPIISAEKAYHEQLSVAEITSSCFEPNSQMVKCDPRHGKYMACCMLYRGDVVPKDVNVAIAAIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGTDSFEEENEGEEF

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict447in Ref. 5; BAB26288

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ245923
EMBL· GenBank· DDBJ
CAB88033.1
EMBL· GenBank· DDBJ
mRNA
GU591980
EMBL· GenBank· DDBJ
ADD82895.1
EMBL· GenBank· DDBJ
mRNA
CH466523
EMBL· GenBank· DDBJ
EDK99659.1
EMBL· GenBank· DDBJ
Genomic DNA
BC017631
EMBL· GenBank· DDBJ
AAH17631.1
EMBL· GenBank· DDBJ
mRNA
AK009439
EMBL· GenBank· DDBJ
BAB26288.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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