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Literature summary for 2.3.1.108 extracted from

  • Leroux, M.
    Tubulin acetyltransferase discovered: ciliary role in the ancestral eukaryote expanded to neurons in metazoans (2010), Proc. Natl. Acad. Sci. USA, 107, 21238-21239.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
genes alphaTAT/MEC-17, phylogenetic analysis Homo sapiens
genes alphaTAT/MEC-17, phylogenetic analysis Caenorhabditis elegans
genes alphaTAT/MEC-17, phylogenetic analysis Tetrahymena sp.

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + [alpha-tubulin]-L-lysine Homo sapiens
-
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine Caenorhabditis elegans
-
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine Tetrahymena sp.
-
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
additional information Homo sapiens alphaTAT/MEC-17 is a lysine acetyltransferase for tubulin and not histones ?
-
?
additional information Caenorhabditis elegans alphaTAT/MEC-17 is a lysine acetyltransferase for tubulin and not histones ?
-
?
additional information Tetrahymena sp. alphaTAT/MEC-17 is a lysine acetyltransferase for tubulin and not histones ?
-
?

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans
-
-
-
Homo sapiens
-
-
-
Tetrahymena sp.
-
gene MEC17
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information most Caenorhabditis elegans-ciliated sensory neurons lack detectable acetylated tubulin Caenorhabditis elegans
-
neuron MEC-12 is present in touch receptor neurons and other (ciliated) neurons. mec-17 expression is limited to touch receptor neurons, its paralogue atat-2 is also expressed in some ciliated neurons Caenorhabditis elegans
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + [alpha-tubulin]-L-lysine
-
Homo sapiens CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
-
Caenorhabditis elegans CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
-
Tetrahymena sp. CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
additional information alphaTAT/MEC-17 is a lysine acetyltransferase for tubulin and not histones Homo sapiens ?
-
?
additional information alphaTAT/MEC-17 is a lysine acetyltransferase for tubulin and not histones Caenorhabditis elegans ?
-
?
additional information alphaTAT/MEC-17 is a lysine acetyltransferase for tubulin and not histones Tetrahymena sp. ?
-
?

Synonyms

Synonyms Comment Organism
alphaTAT
-
Homo sapiens
alphaTAT
-
Caenorhabditis elegans
alphaTAT
-
Tetrahymena sp.
Mec-17
-
Homo sapiens
Mec-17
-
Caenorhabditis elegans
Mec-17
-
Tetrahymena sp.

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
Homo sapiens
acetyl-CoA
-
Caenorhabditis elegans
acetyl-CoA
-
Tetrahymena sp.

General Information

General Information Comment Organism
evolution distribution of alphaTAT/MEC-17 across all eukaryotic clades reveals that it was present in the last eukaryotic common ancestor, which was ciliated Homo sapiens
evolution distribution of alphaTAT/MEC-17 across all eukaryotic clades reveals that it was present in the last eukaryotic common ancestor, which was ciliated Caenorhabditis elegans
evolution distribution of alphaTAT/MEC-17 across all eukaryotic clades reveals that it was present in the last eukaryotic common ancestor, which was ciliated Tetrahymena sp.
malfunction a delay in cilium formation for cultured human cells depleted of alphaTAT/MEC-17 Homo sapiens
malfunction disrupting MEC17 in Tetrahymena abolishes tubulin acetylation, but no overt defect in cilium formation or motility occurs Tetrahymena sp.
malfunction loss of Caenorhabditis elegans alphaTAT activity in the mec-17, atat-2 double mutant affects touch receptor neuron mechanosensation to a greater extent than having a nonacetylatable MEC-12 (K40R) form of tubulin in the organism Caenorhabditis elegans
physiological function MEC-17 and ATAT-2 are required for body touch sensation, which depends on the nonciliated, acetylated tubulin-containing touch receptor neurons. ATAT-2 is needed for acetylating tubulin in dendritic processes and cilia in those neurons. Additional role(s) for the acetyltransferase independent of tubulin acetylation Caenorhabditis elegans