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Literature summary extracted from

  • Ohkawa, N.; Sugisaki, S.; Tokunaga, E.; Fujitani, K.; Hayasaka, T.; Setou, M.; Inokuchi, K.
    N-acetyltransferase ARD1-NAT1 regulates neuronal dendritic development (2008), Genes Cells, 13, 1171-1183.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.255 dendrite
-
 Mus musculus 30425
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.255 30000
-
-
 Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.255 Mus musculus Q9QY36
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.255 brain
-
 Mus musculus
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2.3.1.255 Purkinje cell
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 Mus musculus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.255 additional information ARD1 and NAT1 constitute an N-acetyltransferase complex where ARD1 holds the enzymatic activity of the complex. The ARD1-NAT1 complex mediates N-terminal acetylation of nascent polypeptides that emerge from ribosomes after translation. ARD1 may also acetylate the internal lysine residues of proteins Mus musculus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.255 ? x * 30000, FLAG-tagged enzyme, SDS-PAGE Mus musculus

Synonyms

EC Number Synonyms Comment Organism
2.3.1.255 ARD1
-
 Mus musculus

Expression

EC Number Organism Comment Expression
2.3.1.255 Mus musculus enzyme expression increases during dendritic development up

General Information

EC Number General Information Comment Organism
2.3.1.255 malfunction Aenzyme knockdown significantly reduces dendritic extension in cultured Purkinje cells Mus musculus
2.3.1.255 physiological function the ARD1-NAT1 complex has acetyltransferase activity against microtubules in dendrites and regulates dendritic arborization in neuronal cells Mus musculus