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Literature summary for 2.3.1.255 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
Search for more literature for 2.3.1.255

Localization

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Mus musculus Q9QY36
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Mus musculus
-
Purkinje cell
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

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

Synonyms

Synonyms Comment Organism
ARD1
-
 Mus musculus

Expression

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

General Information

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