A0A2Y9EAY8 · A0A2Y9EAY8_TRIMA

Function

function

Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released. Required for normal sperm flagellar function. Promotes directional cell locomotion and chemotaxis, through AP2A2-dependent acetylation of alpha-tubulin at clathrin-coated pits that are concentrated at the leading edge of migrating cells. May facilitate primary cilium assembly.

Catalytic activity

Features

Showing features for site, binding site.

TypeIDPosition(s)Description
Site58Crucial for catalytic activity
Binding site124-137acetyl-CoA (UniProtKB | ChEBI)
Binding site160-169acetyl-CoA (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentaxon
Cellular Componentclathrin-coated pit
Cellular Componentcytoplasm
Cellular Componentfocal adhesion
Cellular Componentmicrotubule
Cellular Componentspindle
Molecular Functiontubulin N-acetyltransferase activity
Biological Processalpha-tubulin acetylation
Biological Processneuron development
Biological Processregulation of microtubule cytoskeleton organization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Alpha-tubulin N-acetyltransferase 1
  • EC number
  • Short names
    Alpha-TAT
    ; Alpha-TAT1
    ; TAT
  • Alternative names
    • Acetyltransferase mec-17 homolog

Gene names

    • Name
      ATAT1
    • Synonyms
      MEC17

Organism names

Accessions

  • Primary accession
    A0A2Y9EAY8

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue56N6-acetyllysine; by autocatalysis
Modified residue146N6-acetyllysine; by autocatalysis

Post-translational modification

Autoacetylation strongly increases tubulin acetylation.

Keywords

Interaction

Subunit

Component of the BBSome complex. Interacts with AP2 alpha-adaptins, including AP2A2, but not with AP1 gamma-adaptin (AP1G1/AP1G2); this interaction is required for efficient alpha-tubulin acetylation, hence clathrin-coated pits are sites of microtubule acetylation.

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain1-190N-acetyltransferase
Region196-333Disordered
Compositional bias224-238Basic and acidic residues
Compositional bias255-270Pro residues

Sequence similarities

Belongs to the acetyltransferase ATAT1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    333
  • Mass (Da)
    37,644
  • Last updated
    2018-09-12 v1
  • Checksum
    CFE7303F01577519
MEFPFDVDALLPERITVLDQHLRPPARRPGTTTPARVDLQQQIMTIVDELGKASAKAQQLPAPITSASRMQSNRHVMYVLKDTSARPAGKGAIIGFLKVGYKKLFVLDDREAHNEVEPLCILDFYIHESFQRHGHGRELFQHMLQKERVEPYQLAIDRPSQKLLKFLNKHYKLETTVPQVNNFVIFEGFFAHQHRPPSSSLRATRHARAAAVDPTPTAPARKLPPKRAEGDIKPYSSSDREFLKVAVEPPWPLNRAPRRTTPPAHPPPRSSSLGNSPERGPLRPFVPEQELLRSLRLCPPHPTARLLLTTDPGGSPAQRRRTSSLPRSDESRY

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A2Y9QP06A0A2Y9QP06_TRIMAATAT1421
A0A2Y9EAN8A0A2Y9EAN8_TRIMAATAT1310
A0A2Y9QCZ3A0A2Y9QCZ3_TRIMAATAT1326

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias224-238Basic and acidic residues
Compositional bias255-270Pro residues

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

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