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Literature summary for 2.3.1.258 extracted from

  • Lyon, G.
    From molecular understanding to organismal biology of N-terminal acetyltransferases (2019), Structure, 27, 1053-1055 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression ofthe NatA/Naa50 complex, i.e. NatE, in Escherichia coli Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
NatA/Naa50 complex, i.e. NatE, including full-length ScNaa15 (residues 1-854), C-terminally truncated ScNaa10 (1-226 out of 238 total residues), and full-length ScNaa50 (residues 1-176), in the presence of inositol hexaphosphate (IP6) and bi-substrate analogues for both Naa10 and Naa50, X-ray diffraction structure determination and analysis Saccharomyces cerevisiae
NatA/Naa50 complex, i.e. NatE, X-ray diffraction structure determination and analysis Schizosaccharomyces pombe

Protein Variants

Protein Variants Comment Organism
additional information N-terminal analyses comparing wild-type and scNaa50 deletion strains of Saccharomyces cerevisiae Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Schizosaccharomyces pombe 5829
-
cytosol
-
Saccharomyces cerevisiae 5829
-
cytosol
-
Homo sapiens 5829
-
ribosome near to Schizosaccharomyces pombe 5840
-
ribosome near to Saccharomyces cerevisiae 5840
-
ribosome near to Homo sapiens 5840
-

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9GZZ1 AND P41227 AND Q9BXJ9 NatE subunits Naa50,Naa10, and Naa15
-
Saccharomyces cerevisiae Q08689 AND P41227 AND P12945 NatE complex subunits Naa50, Naa10 (ARD1), and Naa15 (Nat1)
-
Saccharomyces cerevisiae ATCC 204508 Q08689 AND P41227 AND P12945 NatE complex subunits Naa50, Naa10 (ARD1), and Naa15 (Nat1)
-
Schizosaccharomyces pombe
-
-
-
Schizosaccharomyces pombe 972
-
-
-
Schizosaccharomyces pombe ATCC 24843
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information N-terminal acetylation (NTA) is an irreversible protein modification Schizosaccharomyces pombe ?
-
-
additional information N-terminal acetylation (NTA) is an irreversible protein modification Saccharomyces cerevisiae ?
-
-
additional information N-terminal acetylation (NTA) is an irreversible protein modification Homo sapiens ?
-
-
additional information N-terminal acetylation (NTA) is an irreversible protein modification Schizosaccharomyces pombe ATCC 24843 ?
-
-
additional information N-terminal acetylation (NTA) is an irreversible protein modification Schizosaccharomyces pombe 972 ?
-
-
additional information N-terminal acetylation (NTA) is an irreversible protein modification Saccharomyces cerevisiae ATCC 204508 ?
-
-

Subunits

Subunits Comment Organism
More the NatE enzyme complex is composed of the subunits Naa50 and Naa15 Schizosaccharomyces pombe
More the NatE enzyme complex is composed of the subunits Naa50 and Naa15 Saccharomyces cerevisiae
More the NatE enzyme complex is composed of the subunits Naa50, Naa10, and Naa15 Homo sapiens

Synonyms

Synonyms Comment Organism
ARD1
-
Schizosaccharomyces pombe
ARD1
-
Saccharomyces cerevisiae
NAA10
-
Schizosaccharomyces pombe
NAA10
-
Saccharomyces cerevisiae
NAA10
-
Homo sapiens
NAA15
-
Schizosaccharomyces pombe
NAA15
-
Saccharomyces cerevisiae
NAA15
-
Homo sapiens
Naa50
-
Schizosaccharomyces pombe
Naa50
-
Saccharomyces cerevisiae
Naa50
-
Homo sapiens
NAT1
-
Schizosaccharomyces pombe
NAT1
-
Saccharomyces cerevisiae
NAT5 UniProt Schizosaccharomyces pombe
NAT5 UniProt Saccharomyces cerevisiae
NAT5 UniProt Homo sapiens
NatE
-
Schizosaccharomyces pombe
NatE
-
Saccharomyces cerevisiae
NatE
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
Schizosaccharomyces pombe
acetyl-CoA
-
Saccharomyces cerevisiae
acetyl-CoA
-
Homo sapiens

General Information

General Information Comment Organism
evolution there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.) Homo sapiens
evolution there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.). SpNaa50 and ScNaa50 do not contain an optimal Q/RxxGxG/A consensus acetyl-CoA binding motif Schizosaccharomyces pombe
evolution there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.). SpNaa50 and ScNaa50 do not contain an optimal Q/RxxGxG/A consensus acetyl-CoA binding motif Saccharomyces cerevisiae
metabolism the enzyme is involved in the co-translational N-terminal protein modification process, overview Schizosaccharomyces pombe
metabolism the enzyme is involved in the co-translational N-terminal protein modification process, overview Saccharomyces cerevisiae
metabolism the enzyme is involved in the co-translational N-terminal protein modification process, overview Homo sapiens
additional information the NatE enzyme complex is composed of the subunits Naa50 and Naa15 Schizosaccharomyces pombe
additional information the NatE enzyme complex is composed of the subunits Naa50 and Naa15 Saccharomyces cerevisiae
additional information the NatE enzyme complex is composed of the subunits Naa50, Naa10, and Naa15 Homo sapiens
physiological function N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is an irreversible protein modification Schizosaccharomyces pombe
physiological function N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is an irreversible protein modification Saccharomyces cerevisiae
physiological function N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is estimated to affect up to 90% of human proteins and influences their folding, localization, complex formation, and degradation, along with a variety of cellular functions ranging from apoptosis to gene regulation. NTA is an irreversible protein modification Homo sapiens