Q3UX10 · TBAL3_MOUSE

  • Protein
    Tubulin alpha chain-like 3
  • Gene
    Tubal3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    4/5

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.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for binding site, active site.

144650100150200250300350400
Type
IDPosition(s)Description
Binding site11GTP (UniProtKB | ChEBI)
Binding site78GTP (UniProtKB | ChEBI)
Binding site78Mg2+ (UniProtKB | ChEBI)
Binding site147GTP (UniProtKB | ChEBI)
Binding site151GTP (UniProtKB | ChEBI)
Binding site152GTP (UniProtKB | ChEBI)
Binding site186GTP (UniProtKB | ChEBI)
Binding site213GTP (UniProtKB | ChEBI)
Binding site235GTP (UniProtKB | ChEBI)
Active site261

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentmicrotubule
Molecular FunctionGTP binding
Molecular Functionhydrolase activity
Molecular Functionmetal ion binding
Molecular Functionstructural constituent of cytoskeleton
Biological Processmicrotubule-based process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Tubulin alpha chain-like 3
  • EC number

Gene names

    • Name
      Tubal3

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
    Q3UX10
  • Secondary accessions
    • B9EJS3

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003137101-446Tubulin alpha chain-like 3

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.
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).
Glutamylation is also involved in cilia motility (By similarity).

Proteomic databases

PTM databases

Expression

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
    446
  • Mass (Da)
    49,988
  • Last updated
    2011-07-27 v2
  • Checksum
    8A8835DF891E8E80
MRECLSIHIGQAGVQIGDACWELYCLEHGIQPDGFILDHQHDNLENPKVEHMNASLDTFFHETRAGKHVPRTLFMDLEPTVIDGIRVGRYHSLFHPEQLVNGKEDAANTYARGRYSVGSEVIELVLERIRKLAEQCSGLQGFLIYRSFGGGTGSGFTSLLMERLSVEYCKKIKLEFSVYPSPRISTAVVEPYNAILTTHSTIEYSDCAFMVDNEALYDICQHKLGIERPSYASINRLIAQVSSSITASLRFEGPLNVDLIEFQTNLVPYPRIHFPITALAPIISAEKAYQEQLSVSDVTASCFEVSNQLVKCDPRLGKYMACCLLYRGDVVPKDVNEAIAAMKSRTSVQFVDWCPTGFKVGINYQPPAVVPGGDLARVQRAVCMLSNTTAIVEAWARLDHKFDLMYAKKAFLHWYITEGMELGEFVEAREDLAALEKDYEEVGLSF

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict227in Ref. 1; BAE22753

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK135971
EMBL· GenBank· DDBJ
BAE22753.1
EMBL· GenBank· DDBJ
mRNA
BC147507
EMBL· GenBank· DDBJ
AAI47508.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp