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Literature summary 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)

EC Number Cloned (Comment) Organism
2.3.1.255 genes NAA10 and NAA15, recombinant enzyme complex NatA expression in Spodoptera frugiperda SF9 cells via transfection using the baculovirus system Saccharomyces cerevisiae
2.3.1.258 recombinant expression ofthe NatA/Naa50 complex, i.e. NatE, in Escherichia coli Saccharomyces cerevisiae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.255 holo-NatA complex in the absence and presence of a bisubstrate peptide-CoA-conjugate inhibitor, as well as the uncomplexed Naa10p catalytic subunit, X-ray diffraction structure determination and analysis Schizosaccharomyces pombe
2.3.1.258 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
2.3.1.258 NatA/Naa50 complex, i.e. NatE, X-ray diffraction structure determination and analysis Schizosaccharomyces pombe

Protein Variants

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

Localization

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.255 100000
-
holo-NatA complex Schizosaccharomyces pombe

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.255 Homo sapiens P41227 AND Q9BXJ9 NatA subunits Naa10 and Naa15
-
2.3.1.255 Saccharomyces cerevisiae P07347 AND P12945 NatA subunits ARD1 and Nat1
-
2.3.1.255 Saccharomyces cerevisiae ATCC 204508 P07347 AND P12945 NatA subunits ARD1 and Nat1
-
2.3.1.255 Schizosaccharomyces pombe Q9UTI3 AND O74985 NatA subunits ARD1 and Nat1
-
2.3.1.255 Schizosaccharomyces pombe 972 Q9UTI3 AND O74985 NatA subunits ARD1 and Nat1
-
2.3.1.255 Schizosaccharomyces pombe ATCC 24843 Q9UTI3 AND O74985 NatA subunits ARD1 and Nat1
-
2.3.1.258 Homo sapiens Q9GZZ1 AND P41227 AND Q9BXJ9 NatE subunits Naa50,Naa10, and Naa15
-
2.3.1.258 Saccharomyces cerevisiae Q08689 AND P41227 AND P12945 NatE complex subunits Naa50, Naa10 (ARD1), and Naa15 (Nat1)
-
2.3.1.258 Saccharomyces cerevisiae ATCC 204508 Q08689 AND P41227 AND P12945 NatE complex subunits Naa50, Naa10 (ARD1), and Naa15 (Nat1)
-
2.3.1.258 Schizosaccharomyces pombe
-
-
-
2.3.1.258 Schizosaccharomyces pombe 972
-
-
-
2.3.1.258 Schizosaccharomyces pombe ATCC 24843
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.255 additional information typical NatA (Naa10) substrates all start with small amino acids (alanine, serine, threonine, or valine) after excision of methionine. N-terminal acetylation (NTA) is an irreversible protein modification Saccharomyces cerevisiae ?
-
?
2.3.1.255 additional information N-terminal acetylation (NTA) is an irreversible protein modification Homo sapiens ?
-
?
2.3.1.255 additional information N-terminal acetylation (NTA) is an irreversible protein modification Schizosaccharomyces pombe ?
-
?
2.3.1.255 additional information N-terminal acetylation (NTA) is an irreversible protein modification Schizosaccharomyces pombe 972 ?
-
?
2.3.1.255 additional information N-terminal acetylation (NTA) is an irreversible protein modification Schizosaccharomyces pombe ATCC 24843 ?
-
?
2.3.1.255 additional information typical NatA (Naa10) substrates all start with small amino acids (alanine, serine, threonine, or valine) after excision of methionine. N-terminal acetylation (NTA) is an irreversible protein modification Saccharomyces cerevisiae ATCC 204508 ?
-
?
2.3.1.258 additional information N-terminal acetylation (NTA) is an irreversible protein modification Saccharomyces cerevisiae ?
-
?
2.3.1.258 additional information N-terminal acetylation (NTA) is an irreversible protein modification Homo sapiens ?
-
?
2.3.1.258 additional information N-terminal acetylation (NTA) is an irreversible protein modification Schizosaccharomyces pombe ?
-
?
2.3.1.258 additional information N-terminal acetylation (NTA) is an irreversible protein modification Schizosaccharomyces pombe 972 ?
-
?
2.3.1.258 additional information N-terminal acetylation (NTA) is an irreversible protein modification Schizosaccharomyces pombe ATCC 24843 ?
-
?
2.3.1.258 additional information N-terminal acetylation (NTA) is an irreversible protein modification Saccharomyces cerevisiae ATCC 204508 ?
-
?

Subunits

EC Number Subunits Comment Organism
2.3.1.255 additional information the NatA enzyme complex is composed of the subunits Naa10 and Naa15 Saccharomyces cerevisiae
2.3.1.255 additional information the NatA enzyme complex is composed of the subunits Naa10 and Naa15 Homo sapiens
2.3.1.255 additional information the NatA enzyme complex is composed of the subunits Naa10 and Naa15 Schizosaccharomyces pombe
2.3.1.258 additional information the NatE enzyme complex is composed of the subunits Naa50 and Naa15 Saccharomyces cerevisiae
2.3.1.258 additional information the NatE enzyme complex is composed of the subunits Naa50, Naa10, and Naa15 Homo sapiens
2.3.1.258 additional information the NatE enzyme complex is composed of the subunits Naa50 and Naa15 Schizosaccharomyces pombe

Synonyms

EC Number Synonyms Comment Organism
2.3.1.255 ARD1
-
Saccharomyces cerevisiae
2.3.1.255 ARD1
-
Schizosaccharomyces pombe
2.3.1.255 hNaa10
-
Homo sapiens
2.3.1.255 hNaa15
-
Homo sapiens
2.3.1.255 NAA10
-
Saccharomyces cerevisiae
2.3.1.255 NAA10
-
Homo sapiens
2.3.1.255 NAA10
-
Schizosaccharomyces pombe
2.3.1.255 NAA15
-
Saccharomyces cerevisiae
2.3.1.255 NAA15
-
Homo sapiens
2.3.1.255 NAA15
-
Schizosaccharomyces pombe
2.3.1.255 NAT1
-
Saccharomyces cerevisiae
2.3.1.255 NatA
-
Saccharomyces cerevisiae
2.3.1.255 NatA
-
Homo sapiens
2.3.1.255 NatA
-
Schizosaccharomyces pombe
2.3.1.255 SCNaa15
-
Saccharomyces cerevisiae
2.3.1.255 ScNatA
-
Saccharomyces cerevisiae
2.3.1.255 SpNaa10
-
Schizosaccharomyces pombe
2.3.1.255 SpNaa15
-
Schizosaccharomyces pombe
2.3.1.258 ARD1
-
Saccharomyces cerevisiae
2.3.1.258 ARD1
-
Schizosaccharomyces pombe
2.3.1.258 NAA10
-
Saccharomyces cerevisiae
2.3.1.258 NAA10
-
Homo sapiens
2.3.1.258 NAA10
-
Schizosaccharomyces pombe
2.3.1.258 NAA15
-
Saccharomyces cerevisiae
2.3.1.258 NAA15
-
Homo sapiens
2.3.1.258 NAA15
-
Schizosaccharomyces pombe
2.3.1.258 Naa50
-
Saccharomyces cerevisiae
2.3.1.258 Naa50
-
Homo sapiens
2.3.1.258 Naa50
-
Schizosaccharomyces pombe
2.3.1.258 NAT1
-
Saccharomyces cerevisiae
2.3.1.258 NAT1
-
Schizosaccharomyces pombe
2.3.1.258 NAT5 UniProt Saccharomyces cerevisiae
2.3.1.258 NAT5 UniProt Homo sapiens
2.3.1.258 NAT5 UniProt Schizosaccharomyces pombe
2.3.1.258 NatE
-
Saccharomyces cerevisiae
2.3.1.258 NatE
-
Homo sapiens
2.3.1.258 NatE
-
Schizosaccharomyces pombe

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.255 acetyl-CoA
-
Saccharomyces cerevisiae
2.3.1.255 acetyl-CoA
-
Homo sapiens
2.3.1.255 acetyl-CoA
-
Schizosaccharomyces pombe
2.3.1.258 acetyl-CoA
-
Saccharomyces cerevisiae
2.3.1.258 acetyl-CoA
-
Homo sapiens
2.3.1.258 acetyl-CoA
-
Schizosaccharomyces pombe

General Information

EC Number General Information Comment Organism
2.3.1.255 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.) Saccharomyces cerevisiae
2.3.1.255 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
2.3.1.255 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.) Schizosaccharomyces pombe
2.3.1.255 malfunction mutations in the X-linked gene NAA10 cause Ogden Syndrome (also known as NAA10-related syndrome), which affects numerous aspects of development. Wide-ranging developmental defects are observed in humans with mutations in NAA10 and NAA15 Saccharomyces cerevisiae
2.3.1.255 metabolism the enzyme is involved in the co-translational N-terminal protein modification process, overview Saccharomyces cerevisiae
2.3.1.255 metabolism the enzyme is involved in the co-translational N-terminal protein modification process, overview Homo sapiens
2.3.1.255 metabolism the enzyme is involved in the co-translational N-terminal protein modification process, overview Schizosaccharomyces pombe
2.3.1.255 additional information the NatA enzyme complex is composed of the subunits Naa10 and Naa15. ScNaa15 has a high degree of structural conservation with SpNaa15 and hNaa15 structures, and ScNaa10 is similarly and completely locked into a cradle by the surrounding Naa15 helices. ScNaa50 has a robust interaction with ScNatA that is maintained even in high salt concentrations (1 M NaCl) Saccharomyces cerevisiae
2.3.1.255 additional information the NatA enzyme complex is composed of the subunits Naa10 and Naa15. ScNaa15 has a high degree of structural conservation with SpNaa15 and hNaa15 structures Homo sapiens
2.3.1.255 additional information the NatA enzyme complex is composed of the subunits Naa10 and Naa15. ScNaa15 has a high degree of structural conservation with SpNaa15 and hNaa15 structures. SpNaa50 has a robust interaction with SpNatA that is maintained even in high salt concentrations (1 M NaCl) Schizosaccharomyces pombe
2.3.1.255 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
2.3.1.255 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
2.3.1.255 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
2.3.1.258 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
2.3.1.258 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
2.3.1.258 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
2.3.1.258 metabolism the enzyme is involved in the co-translational N-terminal protein modification process, overview Saccharomyces cerevisiae
2.3.1.258 metabolism the enzyme is involved in the co-translational N-terminal protein modification process, overview Homo sapiens
2.3.1.258 metabolism the enzyme is involved in the co-translational N-terminal protein modification process, overview Schizosaccharomyces pombe
2.3.1.258 additional information the NatE enzyme complex is composed of the subunits Naa50 and Naa15 Saccharomyces cerevisiae
2.3.1.258 additional information the NatE enzyme complex is composed of the subunits Naa50, Naa10, and Naa15 Homo sapiens
2.3.1.258 additional information the NatE enzyme complex is composed of the subunits Naa50 and Naa15 Schizosaccharomyces pombe
2.3.1.258 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
2.3.1.258 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
2.3.1.258 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