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Information on EC 2.3.1.256 - N-terminal methionine Nalpha-acetyltransferase NatC
for references in articles please use BRENDA:EC2.3.1.256
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.256 N-terminal methionine Nalpha-acetyltransferase NatC
IUBMB Comments
N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic, and may also play a role in membrane targeting and gene silencing. The NatC complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to bulky hydrophobic residues at the second position, including Leu, Ile, Phe, Trp, and Tyr residues.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 2.3.1.256
- acetyltransferases
- dsrnas
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viruslike
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nonfermentable
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co-translationally
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non-mendelian
Reaction Schemes
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an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[protein]
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Synonyms
mak10, mak3p, naa30, nat12, naa38, naa35, mak31, mak31p, hnaa30, n-terminal acetyltransferase complex c, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 2.3.1.88
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formerly, part transferred
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embryonic growth-associated protein
EGAP, subunit of the yeast NatC complex
MAK10
MAK3
MAK31
N-terminal acetyltransferase
NAA30
NAA35
NAA38
NAT
NatC
NatC complex
SPBC15D4.06
TcNaa30
TcNaa35
TcNatC
MAK3
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MAK31
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NAA30
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NAA35
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NAA38
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + an N-terminal-L-methionyl-L-isoleucyl-[protein] = an N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA
(2)
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acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] = an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
(1)
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acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein] = an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
(3)
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acetyl-CoA + an N-terminal-L-methionyl-L-tryptophyl-[protein] = an N-terminal-Nalpha-acetyl-L-methionyl-L-tryptophyl-[protein] + CoA
(4)
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acetyl-CoA + an N-terminal-L-methionyl-L-tyrosyl-[protein] = an N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA
(5)
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PATHWAY SOURCE
PATHWAYS
MetaCyc
Ac/N-end rule pathway
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:N-terminal-Met-Leu/Ile/Phe/Trp/Tyr-[protein] Met Nalpha-acetyltransferase
N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic, and may also play a role in membrane targeting and gene silencing. The NatC complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to bulky hydrophobic residues at the second position, including Leu, Ile, Phe, Trp, and Tyr residues.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + an N-terminal-L-methionyl-L-histidyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-histidyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-isoleucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[Arl8b protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[Arl8b protein] + CoA
Substrates: high activity, the full sequence is MLALISRRWGRPVGRRRRPVRVYP
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein] + CoA
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[mTOR protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[mTOR protein] + CoA
Substrates: highest activity. The full sequence is MLGTGPARWGRPVGRRRRPVRVYP
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[RNP F protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[RNP F protein] + CoA
Substrates: the full sequence is MLGTEGGRWGRPVGRRRRPVRVYP
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[RNP H protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[RNP H protein] + CoA
Substrates: high activity, the full sequence is MLGTEGGRWGRPVGRRRRPVRVYP
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-lysyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-lysyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-methionyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-methionyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-methionyl-L-tryptophyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tryptophyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-methionyl-L-tyrosinyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosinyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-methionyl-L-valyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-valyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + L-Met-Ile-Arg-Leu-Lys-Ala
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-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + MAHLVGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-AHLVGSRRR + CoA
Substrates: i.e. modification of decapeptide derived from N-terminus of yeast Arl3 protein
Products: -
Products: -
?
acetyl-CoA + MEHLVGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-EHLVGSRRR + CoA
Substrates: i.e. modification of decapeptide derived from N-terminus of yeast Arl3 protein
Products: -
Products: -
?
acetyl-CoA + MFALVGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-FALVGSRRR + CoA
Substrates: i.e. modification of decapeptide derived from N-terminus of yeast Arl3 protein
Products: -
Products: -
?
acetyl-CoA + MFELVGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-FELVGSRRR + CoA
Substrates: i.e. modification of decapeptide derived from N-terminus of yeast Arl3 protein
Products: -
Products: -
?
acetyl-CoA + MFHAVGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-FHAVGSRRR + CoA
Substrates: i.e. modification of decapeptide derived from N-terminus of yeast Arl3 protein
Products: -
Products: -
?
acetyl-CoA + MFHEVGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-FHEVGSRRR + CoA
Substrates: i.e. modification of decapeptide derived from N-terminus of yeast Arl3 protein
Products: -
Products: -
?
acetyl-CoA + MFHFVGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-FHFVGSRRR + CoA
Substrates: i.e. modification of decapeptide derived from N-terminus of yeast Arl3 protein
Products: -
Products: -
?
acetyl-CoA + MFHLEGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-FHLEGSRRR + CoA
Substrates: i.e. modification of decapeptide derived from N-terminus of yeast Arl3 protein
Products: -
Products: -
?
acetyl-CoA + MFHLVGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-FHLVGSRRR + CoA
Substrates: i.e. peptide derived from N-terminus of yeast Arl3 protein
Products: -
Products: -
?
acetyl-CoA + MFRLVGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-FRLVGSRRR + CoA
Substrates: i.e. modification of decapeptide derived from N-terminus of yeast Arl3 protein
Products: -
Products: -
?
acetyl-CoA + MKHLVGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-KHLVGSRRR + CoA
Substrates: i.e. modification of decapeptide derived from N-terminus of yeast Arl3 protein
Products: -
Products: -
?
acetyl-CoA + MLEFVGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-MLEFVGSRRR + CoA
Substrates: i.e. modification of peptide containing the N-terminal five residues of the major capsid protein (Gag) of the Saccharomyces cerevisiae virus L-A
Products: -
Products: -
?
acetyl-CoA + MLHLVGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-LHLVGSRRR + CoA
Substrates: i.e. modification of decapeptide derived from N-terminus of yeast Arl3 protein
Products: -
Products: -
?
acetyl-CoA + MLREVGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-MLREVGSRRR + CoA
Substrates: i.e. peptide containing the N-terminal five residues of the major capsid protein (Gag) of the Saccharomyces cerevisiae virus L-A
Products: -
Products: -
?
acetyl-CoA + MLRFEGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-MLRFEGSRRR + CoA
Substrates: i.e. peptide containing the N-terminal five residues of the major capsid protein (Gag) of the Saccharomyces cerevisiae virus L-A
Products: -
Products: -
?
acetyl-CoA + MLRFVGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-MLRFVGSRRR + CoA
Substrates: i.e. peptide containing the N-terminal five residues of the major capsid protein (Gag) of the Saccharomyces cerevisiae virus L-A
Products: -
Products: -
?
acetyl-CoA + MRHLVGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-RHLVGSRRR + CoA
Substrates: i.e. modification of decapeptide derived from N-terminus of yeast Arl3 protein
Products: -
Products: -
?
acetyl-CoA + MWHLVGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-WHLVGSRRR + CoA
Substrates: i.e. modification of decapeptide derived from N-terminus of yeast Arl3 protein
Products: -
Products: -
?
acetyl-CoA + MYHLVGSRRR
N-terminal-Nalpha-acetyl-L-methionyl-YHLVGSRRR + CoA
Substrates: i.e. modification of decapeptide derived from N-terminus of yeast Arl3 protein
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-alanyl-[PLD]
N-terminal-Nalpha-acetyl-L-methionyl-L-alanyl-[PLD] + CoA
Substrates: a NatF-type substrate
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-isoleucyl-[Lrg1 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[Lrg1 protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-isoleucyl-[Sly41 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[Sly41 protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-isoleucyl-[Ymr31 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[Ymr31 protein] + CoA
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-glycyl-L-proline + CoA
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-[Bem1 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[Bem11 protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-[Glr1 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[Glr1 protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-[GPE]
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[GPE] + CoA
Substrates: a NatE-type substrate
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-[GTG]
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[GTG] + CoA
Substrates: a NatC-type substrate
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-[Pda1 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[Pda1 protein] + CoA
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-[RYFRR]
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[RYFRR] + CoA
Substrates: DP11 peptide (MARYFRR) is a substrate of NatC, a synthetic peptide
Products: -
Products: -
ir
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-[Trm1-II protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[Trm1-II protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-phenylalanyl-[Arl3 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[Arl3 protein] + CoA
acetyl-CoA + N-terminal-L-methionyl-L-phenylalanyl-[Rfc2 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[Rfc2 protein] + CoA
acetyl-CoA + N-terminal-L-methionyl-L-phenylalanyl-[Rrn11 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[Rrn11 protein] + CoA
acetyl-CoA + N-terminal-L-methionyl-L-phenylalanyl-[Sec18 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[Sec18 protein] + CoA
acetyl-CoA + N-terminal-L-methionyl-L-phenylalanyl-[Tma20 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[Tma20 protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-tryptanoyl-[ARFP1 peptide]
N-terminal-Nalpha-acetyl-L-methionyl-L-tryptanoyl-[ARFP1 peptide] + CoA
Substrates: i.e. decapeptide derived from N-terminus of human ARFP1 3 protein
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-tyrosinyl-[Nup157 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosinyl-[Nup157 protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-tyrosinyl-[Pxl1 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosinyl-[Pxl1 protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-tyrosinyl-[Tgl1 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosinyl-[Tgl1 protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-isoleucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-isoleucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-isoleucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-tryptophyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tryptophyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-tryptophyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tryptophyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-tryptophyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tryptophyl-[protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-tyrosinyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosinyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-tyrosinyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosinyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + MLRFVTKRWGRPVGRRRRP
Nalpha-acetyl-L-methionyl-LRFVTKRWGRPVGRRRRP + CoA
O74311; Q9USY3; O43080
Substrates: -
Products: -
Products: -
?
acetyl-CoA + MLRFVTKRWGRPVGRRRRP
Nalpha-acetyl-L-methionyl-LRFVTKRWGRPVGRRRRP + CoA
O74311; Q9USY3; O43080
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-isoleucyl-[Ymr31 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[Ymr31 protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-isoleucyl-[Ymr31 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[Ymr31 protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-glycyl-L-proline + CoA
Q4DGZ6; Q4DJ45; Q4D159, Q4CRN8; Q4DLD9; Q4D159
Substrates: -
Products: -
Products: -
ir
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-glycyl-L-proline + CoA
Q4DGZ6; Q4DJ45; Q4D159, Q4CRN8; Q4DLD9; Q4D159
Substrates: -
Products: -
Products: -
ir
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-[Pda1 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[Pda1 protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-[Pda1 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[Pda1 protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-phenylalanyl-[Arl3 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[Arl3 protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-phenylalanyl-[Arl3 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[Arl3 protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-phenylalanyl-[Rfc2 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[Rfc2 protein] + CoA
-
Substrates: -
Products: -
Products: -
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acetyl-CoA + N-terminal-L-methionyl-L-phenylalanyl-[Rfc2 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[Rfc2 protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-phenylalanyl-[Rrn11 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[Rrn11 protein] + CoA
-
Substrates: -
Products: -
Products: -
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acetyl-CoA + N-terminal-L-methionyl-L-phenylalanyl-[Rrn11 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[Rrn11 protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-phenylalanyl-[Sec18 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[Sec18 protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-phenylalanyl-[Sec18 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[Sec18 protein] + CoA
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: almost no activity with nuclear factor kappaB p65 (MDELFPLRWGRPVGRRRRPVRVYP), kinesin KIF4A (MKEEVKGRWGRPVGRRRRPVRVYP), and high-mobility group protein A1 (SESSSKSRWGRPVGRRRRPVRVYP)
Products: -
Products: -
?
additional information
?
-
Substrates: full-length Naa30 acetylates a classical NatC substrate peptide in vitro, whereas no significant NAT activity is detected for Naa3028. Neither full-length Naa30 nor Naa30288 display any lysine acetyltransferase activity, and neither Naa30 isoforms have KAT activity towards histones. The SESSS, EEEIA and MDELF peptides are negative controls and represent NatA, Naa10 and NatB substrates, respectively. Poor activity with SGRGK peptide, which contains the natural 28-mer N-terminal sequence of histone H4, and represents a NatD-type substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: full-length Naa30 acetylates a classical NatC substrate peptide in vitro, whereas no significant NAT activity is detected for Naa3028. Neither full-length Naa30 nor Naa30288 display any lysine acetyltransferase activity, and neither Naa30 isoforms have KAT activity towards histones. The SESSS, EEEIA and MDELF peptides are negative controls and represent NatA, Naa10 and NatB substrates, respectively. Poor activity with SGRGK peptide, which contains the natural 28-mer N-terminal sequence of histone H4, and represents a NatD-type substrate
Products: -
Products: -
?
additional information
?
-
Substrates: analysis of substrate preference of RimIMtb: substrate peptide DPC (NatA substrate) is custom synthesized with single residue modifications at its N-terminus to represent substrate specificities of NatE (DP9), NatB (DP10), NatC (DP11), and substrate Leu (DP8) and tested, all the peptides are modified by RimIMtb, substrates and sequences, detailed overview. The NatB substrate peptide MERYFRR (DP10) is a poor substrate for RimI. RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed gainst peptide representing N-terminus of GroES. RimIMtb acetylates DP11 (NatC substrate) about 1.7fold better than DPC (NatA substrate). RimIMtb acetylates N-terminus of ribosomal proteins and of neighboring non-ribosomal proteins
Products: -
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additional information
?
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Q03503; P23059; Q02197
Substrates: in addition to N-termini starting with ML, MI, MF, and MW, yeast NatC substrates also include MY, MK, MM, MA, MV, and MS. For some of these substrate types (MY, MK, MV, and MS), redundancy between yeast NatC and NatE/Naa50 may be involved
Products: -
Products: -
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additional information
?
-
Q4DGZ6; Q4DJ45; Q4D159
Substrates: analysis of in vitro acetyltransferase activity of GST-tagged TcNaa30: no activity with peptides STPD, EEEIA, MDEL, and MLGP
Products: -
Products: -
?
additional information
?
-
Q4CRN8; Q4DLD9; Q4D159
Substrates: analysis of in vitro acetyltransferase activity of GST-tagged TcNaa30: no activity with peptides STPD, EEEIA, MDEL, and MLGP
Products: -
Products: -
?
additional information
?
-
Q4DGZ6; Q4DJ45; Q4D159
Substrates: analysis of in vitro acetyltransferase activity of GST-tagged TcNaa30: no activity with peptides STPD, EEEIA, MDEL, and MLGP
Products: -
Products: -
?
additional information
?
-
Q4CRN8; Q4DLD9; Q4D159
Substrates: analysis of in vitro acetyltransferase activity of GST-tagged TcNaa30: no activity with peptides STPD, EEEIA, MDEL, and MLGP
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + an N-terminal-L-methionyl-L-histidyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-histidyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-isoleucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[Arl8b protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[Arl8b protein] + CoA
Substrates: high activity, the full sequence is MLALISRRWGRPVGRRRRPVRVYP
Products: -
Products: -
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acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein] + CoA
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[mTOR protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[mTOR protein] + CoA
Substrates: highest activity. The full sequence is MLGTGPARWGRPVGRRRRPVRVYP
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[RNP F protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[RNP F protein] + CoA
Substrates: the full sequence is MLGTEGGRWGRPVGRRRRPVRVYP
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[RNP H protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[RNP H protein] + CoA
Substrates: high activity, the full sequence is MLGTEGGRWGRPVGRRRRPVRVYP
Products: -
Products: -
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acetyl-CoA + an N-terminal-L-methionyl-L-lysyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-lysyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-methionyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-methionyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-methionyl-L-tryptophyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tryptophyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-methionyl-L-tyrosinyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosinyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-methionyl-L-valyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-valyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal-L-methionyl-L-phenylalanyl-[Arl3 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[Arl3 protein] + CoA
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: almost no activity with nuclear factor kappaB p65 (MDELFPLRWGRPVGRRRRPVRVYP), kinesin KIF4A (MKEEVKGRWGRPVGRRRRPVRVYP), and high-mobility group protein A1 (SESSSKSRWGRPVGRRRRPVRVYP)
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-isoleucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-isoleucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-isoleucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[L-A double-stranded RNA virus major coat protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-tryptophyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tryptophyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-tryptophyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tryptophyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-tryptophyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tryptophyl-[protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-tyrosinyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosinyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal-L-methionyl-L-tyrosinyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosinyl-[protein] + CoA
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Inositol hexaphosphate
O74311; Q9USY3; O43080
Kd value 225 nM, binds tightly to NatC to stabilize the complex. Presence of inositol hexaphosphate increases the thermal stability of the NatC complex by 4.9°C
additional information
Q147X3; Q5VZE5; Q9BRA0
human NatC is not stabilized by an IP6 molecule due to a suboptimal IP6 binding site
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hearing Loss
A de novo interstitial deletion of 7q31.2q31.31 identified in a girl with developmental delay and hearing loss.
Neoplasms
A genome-wide approach to link genotype to clinical outcome by utilizing next generation sequencing and gene chip data of 6,697 breast cancer patients.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.19
N-terminal-L-methionyl-L-tryptanoyl-[ARFP1 peptide]
wild-type, pH 7.5, 25°C
-
0.18
MFHLVGSRRR
mutant K500A/K501A/K503A/K504A, pH 7.5, 25°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.2
N-terminal-L-methionyl-L-tryptanoyl-[ARFP1 peptide]
wild-type, pH 7.5, 25°C
-
4.2
MFHLVGSRRR
mutant K500A/K501A/K503A/K504A, pH 7.5, 25°C
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1000
about, purified recombinant RimI, NatC substrate N-terminal L-methionyl-L-leucyl-[RYFRR], pH 8.0, 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
O17003 i.e. auxiliary subunit NatC-1, O16486 i.e. catalytic subunit NatC-2, Q9BL76 i.e. auliliary subunit NatC-3
O17003; O16486; Q9BL76
SwissProt
brenda
O74311 i.e. catalytic subunit Naa30, Q9USY3 i.e. auxiliary subunit Naa35, O43080 i.e. auxiliary subunit Naa38
O74311; Q9USY3; O43080
SwissProt
brenda
O74311 i.e. catalytic subunit Naa30, Q9USY3 i.e. auxiliary subunit Naa35, O43080 i.e. auxiliary subunit Naa38
O74311; Q9USY3; O43080
SwissProt
brenda
Q147X3 i.e. catalytic subunit NAA30, Q5VZE i.e. auxiliary subunit NAA35, Q9BRA0 i.e. auxiliary subunit NAA38
Q147X3; Q5VZE5; Q9BRA0
SwissProt
brenda
Q03503 i.e. catalytic subunit Naa30/MAK3, P23059 i.e. auxiliary subunit Naa38, Q02197 i.e. auxiliary saubunit Naa35
Q03503; P23059; Q02197
SwissProt
brenda
Esmeraldo-like NatC catalytic Naa30 subunit and auxiliary Naa35 subunit, and non-Esmeraldo-like auxiliary Naa38 subunit
Q4CRN8; Q4DLD9; Q4D159
UniProt
brenda
non-Esmeraldo-like NatC catalytic Naa30 subunit and auxiliary Naa35 and Naa38 subunits
Q4DGZ6; Q4DJ45; Q4D159
UniProt
brenda
Esmeraldo-like NatC catalytic Naa30 subunit and auxiliary Naa35 subunit, and non-Esmeraldo-like auxiliary Naa38 subunit
Q4CRN8; Q4DLD9; Q4D159
UniProt
brenda
non-Esmeraldo-like NatC catalytic Naa30 subunit and auxiliary Naa35 and Naa38 subunits
Q4DGZ6; Q4DJ45; Q4D159
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
high level of alternatively spliced nuclear isoform Naa30288
brenda
additional information
additional information
Q4DGZ6; Q4DJ45; Q4D159
the subunits forming the NatC enzyme complex are expressed in the three main life cycle stages of the parasite, form stable complexes in vivo, and partially cosediment with the ribosome in agreement with a cotranslational function. Expression analysis of TcNaa38/TcNaa30 in the parasite
brenda
additional information
Q4CRN8; Q4DLD9; Q4D159
the subunits forming the NatC enzyme complex are expressed in the three main life cycle stages of the parasite, form stable complexes in vivo, and partially cosediment with the ribosome in agreement with a cotranslational function. Expression analysis of TcNaa38/TcNaa30 in the parasite
brenda
additional information
-
the subunits forming the NatC enzyme complex are expressed in the three main life cycle stages of the parasite, form stable complexes in vivo, and partially cosediment with the ribosome in agreement with a cotranslational function. Expression analysis of TcNaa38/TcNaa30 in the parasite
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
immunohistochemic detection in subcellular fractions
-
brenda
additional information
-
immunohistochemic detection in subcellular fractions
-
brenda
additional information
Q4DGZ6; Q4DJ45; Q4D159
TcNatC and TcNatA proteins physically interact with each other and it is plausible that this interaction takes place in the cytoplasm as suggested by their possible ribosomal cosedimentation. Subcellular localization of subunits, overview
-
brenda
additional information
Q4CRN8; Q4DLD9; Q4D159
TcNatC and TcNatA proteins physically interact with each other and it is plausible that this interaction takes place in the cytoplasm as suggested by their possible ribosomal cosedimentation. Subcellular localization of subunits, overview
-
brenda
additional information
-
TcNatC and TcNatA proteins physically interact with each other and it is plausible that this interaction takes place in the cytoplasm as suggested by their possible ribosomal cosedimentation. Subcellular localization of subunits, overview
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
yeast cells lacking MAK3/NAA30 grow poorly in non-fermentable carbon sources and other stress conditions, human NAA30 can functionally replace yeast MAK3/NAA30 depending on the genetic background of the yeast strain. Human NAA30 rescues yeast mak3DELTA growth defects
physiological function
additional information
evolution
enzyme Naa30 belongs to the GNAT superfamily of acetyltransferases characterized by the highly conserved GNAT fold, which promotes Ac-CoA binding and substrate recognition
evolution
the function of MAK3/NAA30 is evolutionarily conserved from yeast to human. In the case of the NAT enzyme family, sequence similarity does not necessarily correlate with structural and functional similarity
evolution
the function of MAK3/NAA30 is evolutionarily conserved from yeast to human. In the case of the NAT enzyme family, sequence similarity does not necessarily correlate with structural and functional similarity
evolution
-
the function of MAK3/NAA30 is evolutionarily conserved from yeast to human. In the case of the NAT enzyme family, sequence similarity does not necessarily correlate with structural and functional similarity
-
malfunction
knockdown of Nalpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant Arf-like GTPase Arl8b localization
malfunction
enzyme depletion results in severe cell growth defects and embryonic lethality
malfunction
knockdown of Naa30 induces the loss of mitochondrial membrane potential and fragmentation of mitochondria
malfunction
depletion of the human N-terminal acetyltransferase hNaa30 disrupts Golgi integrity and Golgi-associated GTPase ADP ribosylation factor related protein 1 (ARFRP1) localization. Depletion of the hNatC catalytic subunit hNaa30 leads to disassembly of the Golgi apparatus and trans-Golgi network (TGN). ARFRP1 shifts from a predominantly cis-Golgi and TGN localization to localizing both Golgi and non-Golgi vesicular structures in hNaa30-depleted cells (smaller vesicle-like membranous compartments). Loss of membrane association of ARFRP1 is not observed. hNaa30 depletion induces Golgi scattering and induces aberrant ARFRP1 Golgi localization. Knockdown of each of the hNatC subunits in HeLa cells leads to p53-dependent apoptosis. Naa30 depletion severely disrupts mitochondrial organization. Knockdown phenotypes are specific for hNaa30 depletion and not a result of si-hNAA30-independent effects. Phenotypes, detailed overview
malfunction
overexpression of full-length Naa30 increases cell viability via inhibition of apoptosis. In contrast, Naa30288 does not exert an anti-apoptotic effect
malfunction
yeast cells lacking MAK3/NAA30 grow poorly in non-fermentable carbon sources and other stress conditions, human NAA30 can functionally replace yeast MAK3/NAA30, human NAA30 rescues yeast mak3DELTA growth defects. In Saccharomyces cerevisiae, deletion of the individual NatC subunits produces less severe phenotypes compared with NatA or NatB deletion strains. Loss of one of the individual NatC subunits also results in reduced growth on non-fermentable carbon sources, such as glycerol and ethanol
malfunction
Depletion of NAA30 disrupts mitochondrial function in human cancer cells and results in reduced levels of mitochondrial matrix proteins, some of which are NatC substrates. Overexpression of NAA30 increases cancer cell viability
malfunction
Q147X3; Q5VZE5; Q9BRA0
heterozygous NAA30 nonsense variant c.244C>T (p.Q82*) has been identified in a 5-year-old boy presenting with global development delay, autism spectrum disorder, hypotonia, tracheal cleft, and recurrent respiratory infections. NAA30-Q82* completely disrupts the N-terminal acetyltransferase activity
malfunction
-
yeast cells lacking MAK3/NAA30 grow poorly in non-fermentable carbon sources and other stress conditions, human NAA30 can functionally replace yeast MAK3/NAA30, human NAA30 rescues yeast mak3DELTA growth defects. In Saccharomyces cerevisiae, deletion of the individual NatC subunits produces less severe phenotypes compared with NatA or NatB deletion strains. Loss of one of the individual NatC subunits also results in reduced growth on non-fermentable carbon sources, such as glycerol and ethanol
-
physiological function
-
MAK3 N-acetyltransferase modifies the L-A gag NH2 terminus which in turn is necessary for virus particle assembly
physiological function
the enzyme is required for double-stranded RNA virus propagation in Saccharomyces cerevisiae
physiological function
the enzyme is essential for mitochondrial integrity and function
physiological function
-
MAK3 is required for the N-terminal acetylation of the killer viral major coat protein, Gag
physiological function
the human NatC complex (hNatC) is an evolutionarily conserved complex composed of the catalytic subunit hNaa30 (hMak3) and the auxiliary subunits hNaa35 (hMak10) and hNaa38 (hMak31). NatC Nt-acetylates Met-Leu-, Met-Ile-, Met-Phe-, Met-Trp-, Met-Val-, Met-Met-, Met-His-, and Met-Lys-N-termini. The NatC complex is one of several Nt-acetyltransferases (NATs) that perform Nt-acetylation in eukaryotes. Nt-acetylation or protein N-alpha-terminal acetylation, is the addition of an acetyl group on the Nalpha-amino group of proteins. It is one of the most abundant protein modifications in eukaryotes and displays a wide array of biological functions. The Golgi apparatus associated GTPase ADP ribosylation factor related protein 1 (ARFRP1) requires N-terminal acetylation for membrane association and based on its N-terminal sequence, it is likely to be a substrate of hNaa30. ARFRP1 is involved in endosome-to-trans-Golgi network (TGN) traffic
physiological function
the NatC complex consists of the catalytic subunit Naa30 and the auxiliary subunits Naa35 and Naa38, and can potentially Nt-acetylate cytoplasmic proteins when the initiator methionine is followed by a bulky hydrophobic/amphipathic residue at position 2. Full-length enzyme Naa30362 improves cell viability and inhibits apoptosis
physiological function
Nalpha-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by Nalpha-acetyltransferases (NATs). RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed gainst peptide representing N-terminus of GroES
physiological function
Q4DGZ6; Q4DJ45; Q4D159, Q4CRN8; Q4DLD9; Q4D159
TcNatC/TcNatA proteins carry out their function independently of each other as suggested in other organisms and they may have specific functions depending on the parasite life cycle stage. But the proteins may also have other functions independent of the NAT-activity as suggested in other species
physiological function
N-terminal acetylation is an irreversible protein modification that primarily occurs co-translationally, and is catalyzed by a highly conserved family of N-terminal acetyltransferases (NATs). The NatC complex (NAA30-NAA35-NAA38) is a major NAT enzyme. The activity of NatC is crucial for the correct functioning of its substrates, which includes translocation to the Golgi apparatus, the inner nuclear membrane as well as proper mitochondrial function. The entire NatC complex is required for proper mitochondrial function. NatC (Mak3) N-terminally acetylates the major viral coat protein Gag of the helper virus L-A, and this modification is necessary for proper viral particle assembly. MAK3 supports growth in both rich and synthetic glycerol medium
physiological function
yeast cells lacking MAK3/NAA30 grow poorly in non-fermentable carbon sources and other stress conditions. Human NAA30 can functionally replace yeast MAK3/NAA30. Human NAA60 can functionally replace yeast MAK3/NAA30 in glycerol
physiological function
N-terminal acetylation is an irreversible protein modification that primarily occurs co-translationally, and is catalyzed by a highly conserved family of N-terminal acetyltransferases (NATs). The NatC complex (NAA30-NAA35-NAA38) is a major NAT enzyme. The activity of NatC is crucial for the correct functioning of its substrates, which includes translocation to the Golgi apparatus, the inner nuclear membrane as well as proper mitochondrial function
physiological function
yeast cells lacking MAK3/NAA30 grow poorly in non-fermentable carbon sources and other stress conditions. Human NAA30 can functionally replace yeast MAK3/NAA30
physiological function
O17003; O16486; Q9BL76
loss of N-terminal acetyltransferase C complex suppresses nipi-3(0) mediated larval arrest and lethality. The NatC complex acts partially through the PMK-1 p38 MAPK pathway
physiological function
Q03503; P23059; Q02197
ectopic expression of human NAA30 rescues NatC phenotypes in a Naa30 deletion strain
physiological function
-
Nalpha-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by Nalpha-acetyltransferases (NATs). RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed gainst peptide representing N-terminus of GroES
-
physiological function
-
TcNatC/TcNatA proteins carry out their function independently of each other as suggested in other organisms and they may have specific functions depending on the parasite life cycle stage. But the proteins may also have other functions independent of the NAT-activity as suggested in other species
-
physiological function
-
N-terminal acetylation is an irreversible protein modification that primarily occurs co-translationally, and is catalyzed by a highly conserved family of N-terminal acetyltransferases (NATs). The NatC complex (NAA30-NAA35-NAA38) is a major NAT enzyme. The activity of NatC is crucial for the correct functioning of its substrates, which includes translocation to the Golgi apparatus, the inner nuclear membrane as well as proper mitochondrial function. The entire NatC complex is required for proper mitochondrial function. NatC (Mak3) N-terminally acetylates the major viral coat protein Gag of the helper virus L-A, and this modification is necessary for proper viral particle assembly. MAK3 supports growth in both rich and synthetic glycerol medium
-
physiological function
-
yeast cells lacking MAK3/NAA30 grow poorly in non-fermentable carbon sources and other stress conditions. Human NAA30 can functionally replace yeast MAK3/NAA30. Human NAA60 can functionally replace yeast MAK3/NAA30 in glycerol
-
physiological function
-
Nalpha-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by Nalpha-acetyltransferases (NATs). RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed gainst peptide representing N-terminus of GroES
-
physiological function
-
the enzyme is required for double-stranded RNA virus propagation in Saccharomyces cerevisiae
-
additional information
homology structure modeling of Naa30 using the crystal structure of human Naa50 (PDB ID 3TFY) as template
additional information
-
homology structure modeling of Naa30 using the crystal structure of human Naa50 (PDB ID 3TFY) as template
additional information
Q4DGZ6; Q4DJ45; Q4D159
Trypanosoma cruzi NatC protein complex consists of one catalytic subunit TcNaa30 and one predicted auxiliary subunit TcNaa35. TcNatC and TcNatA (EC 2.3.1.255) complex subunits interact in vivo and in vitro
additional information
Q4CRN8; Q4DLD9; Q4D159
Trypanosoma cruzi NatC protein complex consists of one catalytic subunit TcNaa30 and one predicted auxiliary subunit TcNaa35. TcNatC and TcNatA (EC 2.3.1.255) complex subunits interact in vivo and in vitro
additional information
the first four amino acids of cognate substrates are recognized at the subunits Naa30-Naa35 interface. A sequence-specific, ligand-induced conformational change in Naa30 enables efficient acetylation
additional information
Q147X3; Q5VZE5; Q9BRA0
NatC can exist in both binary (NAA30/NAA35) and ternary states. Presence of NAA38 increases the thermostability and broadens the substrate-specificity profile. The binary complex is strongly selective for the NatC-only MLRF substrate over the NatC/E substrates MKLN, MLGP, and MFPA, the ternary complex shows comparable activity toward all NatC and NatC/E peptide substrates
additional information
-
Trypanosoma cruzi NatC protein complex consists of one catalytic subunit TcNaa30 and one predicted auxiliary subunit TcNaa35. TcNatC and TcNatA (EC 2.3.1.255) complex subunits interact in vivo and in vitro
-
Show AA Sequence and Transmembrane Helices (1572 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 84000, recombinant MBP-tagged Naa30362, SDS-PAGE, x * 75000, recombinant MBP-Naa30288, SDS-PAGE
dimer
heterotrimer
-
1 * 20000 + 1 * 84000 + 1 * 10000, subunit Mak3p, Mak10p and Mak31p, calculated from amino acid sequence
additional information
dimer
Q4DGZ6; Q4DJ45; Q4D159, Q4CRN8; Q4DLD9; Q4D159
the Trypanosoma cruzi Nat A protein complex consists of an Esmeraldo-like catalytic NatA complex subunit ARD1/TcNaa10 and a non-Esmeraldo-like auxilliary NatA complex subunit Nat1/TcNaa15
dimer
-
the Trypanosoma cruzi Nat A protein complex consists of an Esmeraldo-like catalytic NatA complex subunit ARD1/TcNaa10 and a non-Esmeraldo-like auxilliary NatA complex subunit Nat1/TcNaa15
-
additional information
NatC is a trimeric protein complex that consists of the catalytic subunit NAA30, the ribosomal anchor NAA35, and the auxiliary subunit NAA38, complex composition and amino acid sequence comparisons, overview
additional information
NatC is a trimeric protein complex that consists of the catalytic subunit Mak3 (NAA30), the ribosomal anchor Mak10 (NAA35), and the auxiliary subunit Mak31 (NAA38), complex composition and amino acid sequence comparisons, overview
additional information
-
NatC is a trimeric protein complex that consists of the catalytic subunit Mak3 (NAA30), the ribosomal anchor Mak10 (NAA35), and the auxiliary subunit Mak31 (NAA38), complex composition and amino acid sequence comparisons, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cryo-EM structures of NatC complexes with and without NAA38. NAA38 increases the thermostability and broadens the substrate-specificity profile
Q147X3; Q5VZE5; Q9BRA0
structures of the selenomethionine-derivatized (NatC, apo) and native, CoA-bound (NatC-CoA) complex, to 2.4 and 2.45 A resolution
cryoelectron microscopy structure of NatC with a NatE/C-type bisubstrate analog and inositol hexaphosphate. The presence of three subunits is a prerequisite for normal NatC acetylation activity in yeast. Inositol hexaphosphate binds tightly to NatC to stabilize the complex. Naa38 plays key structural and, likely, functional roles in NatC. The Naa35 auxiliary subunit makes extensive contacts with the protein N-terminal substrate binding loops of Naa30 to influence substrate recognition
O74311; Q9USY3; O43080
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q82*
Q147X3; Q5VZE5; Q9BRA0
heterozygous NAA30 nonsense variant c.244C>T (p.Q82*) has been identified in a 5-year-old boy presenting with global development delay, autism spectrum disorder, hypotonia, tracheal cleft, and recurrent respiratory infections. NAA30-Q82* completely disrupts the N-terminal acetyltransferase activity
DELTAC17
deletion mutant of subunit Naa38, strong decrease in kcat value
E118A
mutant of Naa30, decrease in kcat value, increase in Km value
E118Q
mutant of Naa30, decrease in kcat value, increase in Km value
E120A
mutant of Naa30, decrease in kcat value, increase in Km value
E120Q
mutant of Naa30, decrease in kcat value, increase in Km value
K500A/K501A/K503A/K504A
mutant of Naa35, catalytic parameters similar to wild-type
L27A
mutant of Naa30, strong decrease in kcat value, decrease in Km value
S28A
mutant of Naa30, decrease in kcat value, increase in Km value
Y130A
Y145F
mutant of Naa30, decrease in kcat value, increase in Km value
Y31F
mutant of Naa30, decrease in kcat value, increase in Km value
Y80A
mutant of Naa30, decrease in kcat value, increase in Km value
Y80F
mutant of Naa30, decrease in kcat value, increase in Km value
E109A
O74311; Q9USY3; O43080
mutation of subunit Naa30, decrease in kcat value, increase in Km value
E109Q
O74311; Q9USY3; O43080
mutation of subunit Naa30, decrease in kcat value, strong increase in Km value
N114A
O74311; Q9USY3; O43080
mutation of subunit Naa30, decrease in kcat value, decrease in Km value
Y121F
O74311; Q9USY3; O43080
mutation of subunit Naa30, strong decrease in kcat value, decrease in Km value
Y136A
O74311; Q9USY3; O43080
mutation of subunit Naa30, strong decrease in kcat value, strong decrease in Km value
E25A
-
mutation of subunit Naa30, increase in kcat value, increase in Km value
-
S24A
-
mutation of subunit Naa30, catalytic parameters similar to wild-type
-
Y27A
-
mutation of subunit Naa30, decrease in kcat value, decrease in Km value
-
Y71A
-
mutation of subunit Naa30, increase in kcat value, increase in Km value
-
additional information
additional information
siRNA-mediated knockdown of hNAA30 gene expression in HeLa and CAL-62 cells, phenotypes, detailed overview
additional information
-
siRNA-mediated knockdown of hNAA30 gene expression in HeLa and CAL-62 cells, phenotypes, detailed overview
additional information
identification of a splice variant of human NAA30, which encodes a truncated protein named Naa30288. DNA sequencing reveals that the 900 bp product derived from alternative splicing results in a 222 bp deletion from the 3' end of exon 1 (c.550_771del). The truncated splice variant (867 bp) is otherwise identical to NAA30. Splicing NAA30_v2 translates into a truncated isoform (p.Val184_Leu257del) consisting of 288 amino acids (Naa30288). The splice variant is abundantly present in thyroid cancer tissues and in several different human cancer cell lines. Naa30288 localizes predominantly to the nucleus, as opposed to annotated Naa30 which has a cytoplasmic localization. Naa30288 is missing elements of the GNAT fold. Full-length Naa30 acetylates the classical NatC substrate peptide MLGTG in vitro, whereas no significant NAT activity is detected for Naa3028. Naa30288 appears to be enzymatically inactive. Overexpression of full-length Naa30362 increases cell viability via inhibition of apoptosis. In contrast, Naa30288 does not exert an anti-apoptotic effect
additional information
-
identification of a splice variant of human NAA30, which encodes a truncated protein named Naa30288. DNA sequencing reveals that the 900 bp product derived from alternative splicing results in a 222 bp deletion from the 3' end of exon 1 (c.550_771del). The truncated splice variant (867 bp) is otherwise identical to NAA30. Splicing NAA30_v2 translates into a truncated isoform (p.Val184_Leu257del) consisting of 288 amino acids (Naa30288). The splice variant is abundantly present in thyroid cancer tissues and in several different human cancer cell lines. Naa30288 localizes predominantly to the nucleus, as opposed to annotated Naa30 which has a cytoplasmic localization. Naa30288 is missing elements of the GNAT fold. Full-length Naa30 acetylates the classical NatC substrate peptide MLGTG in vitro, whereas no significant NAT activity is detected for Naa3028. Naa30288 appears to be enzymatically inactive. Overexpression of full-length Naa30362 increases cell viability via inhibition of apoptosis. In contrast, Naa30288 does not exert an anti-apoptotic effect
additional information
construction of a mak3DELTA deletion strains (YPR051DELTA::kanMX6) by PCR-mediated gene disruption by replacing the MAK3 gene with the kanMX6 cassette using homologous recombination, phenotype, overview. Human NAA30 rescues yeast mak3DELTA growth defects. Deletion of MAK3 impairs growth on glycerol and sodium chloride
additional information
-
construction of a mak3DELTA deletion strains (YPR051DELTA::kanMX6) by PCR-mediated gene disruption by replacing the MAK3 gene with the kanMX6 cassette using homologous recombination, phenotype, overview. Human NAA30 rescues yeast mak3DELTA growth defects. Deletion of MAK3 impairs growth on glycerol and sodium chloride
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
subcellular fractionation of HeLa cells and identification of splicing variants of Naa30
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene NAA30, DNA and amino acid sequence, analysis and comparison, alternative splicing variants NAA30_v1 (Naa30362) and NAA30_v2 (Naa30288), cloning from HeLa cells, overexpression of MBP-tagged Naa30362-V5 and Naa30288-V5 in HeLa cells
gene Rv3420c or rimI, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli
genes encoding TcNaa30, TcNaa35, and TcNaa38, DNA and amino acid sequence determination, comparison, and analysis, recombinant expression of GST-tagged subunits
Q4DGZ6; Q4DJ45; Q4D159, Q4CRN8; Q4DLD9; Q4D159
recombinant expression of HA-tagged human NatC in Saccharoymces cerevisiae strain W303-1A
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
liquid growth assays are the method of choice when analyzing subtle growth defects, keeping loss of information to a minimum
analysis
development of an antibody to specifically recognize N-terminally acetylated methionine-starting proteins. The antibody is specific and has selectivity for some subtypes of methionine-starting N-termini, specifically potential substrates of the NatC, NatE and NatF enzymes. It can be used to identify N-terminal acetyltransferase substrates or to analyse changes in N-terminal acetylation
analysis
-
liquid growth assays are the method of choice when analyzing subtle growth defects, keeping loss of information to a minimum
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Polevoda, B.; Sherman, F.
Composition and function of the eukaryotic N-terminal acetyltransferase subunits
Biochem. Biophys. Res. Commun.
308
1-11
2003
Saccharomyces cerevisiae
brenda
Wenzlau, J.M.; Garl, P.J.; Simpson, P.; Stenmark, K.R.; West, J.; Artinger, K.B.; Nemenoff, R.A.; Weiser-Evans, M.C.
Embryonic growth-associated protein is one subunit of a novel N-terminal acetyltransferase complex essential for embryonic vascular development
Circ. Res.
98
846-855
2006
Danio rerio (Q7T322), Danio rerio
brenda
Aksnes, H.; Osberg, C.; Arnesen, T.
N-Terminal acetylation by NatC is not a general determinant for substrate subcellular localization in Saccharomyces cerevisiae
PLoS ONE
8
e61012
2013
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Tercero, J.C.; Dinman, J.D.; Wickner, R.B.
Yeast MAK3 N-acetyltransferase recognizes the N-terminal four amino acids of the major coat protein (gag) of the L-A double-stranded RNA virus
J. Bacteriol.
175
3192-3194
1993
Saccharomyces cerevisiae
brenda
Tercero, J.C.; Riles, L.E.; Wickner, R.B.
Localized mutagenesis and evidence for post-transcriptional regulation of MAK3. A putative N-acetyltransferase required for double-stranded RNA virus propagation in Saccharomyces cerevisiae
J. Biol. Chem.
267
20270-20276
1992
Saccharomyces cerevisiae (Q03503), Saccharomyces cerevisiae ATCC 20450 (Q03503)
brenda
Tercero, J.C.; Wickner, R.B.
MAK3 encodes an N-acetyltransferase whose modification of the L-A gag NH2 terminus is necessary for virus particle assembly
J. Biol. Chem.
267
20277-20281
1992
Saccharomyces cerevisiae
brenda
Polevoda, B.; Sherman, F.
NatC Nalpha-terminal acetyltransferase of yeast contains three subunits, Mak3p, Mak10p, and Mak31p
J. Biol. Chem.
276
20154-20159
2001
Saccharomyces cerevisiae
brenda
Polevoda, B.; Brown, S.; Cardillo, T.; Rigby, S.; Sherman, F.
Yeast Nalpha-terminal acetyltransferases are associated with ribosomes
J. Cell. Biochem.
103
492-508
2008
Saccharomyces cerevisiae
brenda
Starheim, K.; Gromyko, D.; Evjenth, R.; Ryningen, A.; Varhaug, J.; Lillehaug, J.; Arnesen, T.
Knockdown of human Nalpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization
Mol. Cell. Biol.
29
3569-3581
2009
Homo sapiens (Q147X3)
brenda
Van Damme, P.; Kalvik, T.V.; Starheim, K.K.; Jonckheere, V.; Myklebust, L.M.; Menschaert, G.; Varhaug, J.E.; Gevaert, K.; Arnesen, T.
A role for human N-alpha acetyltransferase 30 (Naa30) in maintaining mitochondrial integrity
Mol. Cell. Proteomics
15
3361-3372
2016
Homo sapiens (Q147X3), Homo sapiens
brenda
Pesaresi, P.; Gardner, N.; Masiero, S.; Dietzmann, A.; Eichacker, L.; Wickner, R.; Salamini, F.; Leister, D.
Cytoplasmic N-terminal protein acetylation is required for efficient photosynthesis in Arabidopsis
Plant Cell
15
1817-1832
2003
Arabidopsis thaliana
-
brenda
Osberg, C.; Aksnes, H.; Ninzima, S.; Marie, M.; Arnesen, T.
Microscopy-based Saccharomyces cerevisiae complementation model reveals functional conservation and redundancy of N-terminal acetyltransferases
Sci. Rep.
6
31627
2016
Homo sapiens (Q147X3), Homo sapiens
brenda
Starheim, K.K.; Kalvik, T.V.; Bjoerkoey, G.; Arnesen, T.
Depletion of the human N-terminal acetyltransferase hNaa30 disrupts Golgi integrity and ARFRP1 localization
Biosci. Rep.
37
BSR20170066
2017
Homo sapiens (Q147X3), Homo sapiens
brenda
Varland, S.; Myklebust, L.M.; Goksoeyr, S.O.; Glomnes, N.; Torsvik, J.; Varhaug, J.E.; Arnesen, T.
Identification of an alternatively spliced nuclear isoform of human N-terminal acetyltransferase Naa30
Gene
644
27-37
2018
Homo sapiens (Q147X3), Homo sapiens
brenda
Ochaya, S.; Franzen, O.; Buhwa, D.A.; Foyn, H.; Butler, C.E.; Stove, S.I.; Tyler, K.M.; Arnesen, T.; Matovu, E.; Aslund, L.; Andersson, B.
Characterization of evolutionarily conserved Trypanosoma cruzi NatC and NatA-N-terminal acetyltransferase complexes
J. Parasitol. Res.
2019
6594212
2019
Trypanosoma cruzi (Q4DGZ6 AND Q4DJ45 AND Q4D159), Trypanosoma cruzi (Q4CRN8 AND Q4DLD9 AND Q4D159), Trypanosoma cruzi CL Brener (Q4DGZ6 AND Q4DJ45 AND Q4D159), Trypanosoma cruzi CL Brener (Q4CRN8 AND Q4DLD9 AND Q4D159)
brenda
Pathak, D.; Bhat, A.; Sapehia, V.; Rai, J.; Rao, A.
Biochemical evidence for relaxed substrate specificity of Nalpha-acetyltransferase (Rv3420c/rimI) of Mycobacterium tuberculosis
Sci. Rep.
6
28892
2016
Mycobacterium tuberculosis (I6YG32), Mycobacterium tuberculosis ATCC 25618 (I6YG32), Mycobacterium tuberculosis H37Rv (I6YG32)
brenda
Varland, S.; Brnstad, K.M.; Skinner, S.J.; Arnesen, T.
A nonsense variant in the N-terminal acetyltransferase NAA30 may be associated with global developmental delay and tracheal cleft
Am. J. Med. Genet. A
191
2402-2410
2023
Homo sapiens (Q147X3 and Q5VZE5 and Q9BRA0)
brenda
Larsen, S.K.; Bekkelund, A.K.; Glomnes, N.; Arnesen, T.; Aksnes, H.
Assessing N-terminal acetylation status of cellular proteins via an antibody specific for acetylated methionine
Biochimie
226
113-120
2024
Homo sapiens (Q147X3)
brenda
Drazic, A.; Varland, S.
Human NAA30 can rescue yeast MAK3DELTA mutant growth phenotypes
Biosci. Rep.
41
BSR20202828
2021
Homo sapiens (Q147X3), Saccharomyces cerevisiae (Q03503), Saccharomyces cerevisiae ATCC 204508 (Q03503)
brenda
Van Damme, P.; Osberg, C.; Jonckheere, V.; Glomnes, N.; Gevaert, K.; Arnesen, T.; Aksnes, H.
Expanded in vivo substrate profile of the yeast N-terminal acetyltransferase NatC
J. Biol. Chem.
299
102824
2023
Saccharomyces cerevisiae (Q03503 and P23059 and Q02197)
brenda
Grunwald, S.; Hopf, L.V.M.; Bock-Bierbaum, T.; Lally, C.C.M.; Spahn, C.M.T.; Daumke, O.
Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates
Nat. Commun.
11
5506
2020
Saccharomyces cerevisiae (Q03503)
brenda
Malinow, R.A.; Zhu, M.; Jin, Y.; Kim, K.W.
Forward genetic screening identifies novel roles for N-terminal acetyltransferase C and histone deacetylase in C. elegans development
Sci. Rep.
12
16438
2022
Caenorhabditis elegans (O17003 and O16486 and Q9BL76)
brenda
Deng, S.; Gottlieb, L.; Pan, B.; Supplee, J.; Wei, X.; Petersson, E.J.; Marmorstein, R.
Molecular mechanism of N-terminal acetylation by the ternary NatC complex
Structure
29
1094-1104
2021
Schizosaccharomyces pombe (O74311 and Q9USY3 and O43080), Schizosaccharomyces pombe 972 (O74311 and Q9USY3 and O43080)
brenda
Deng, S.; Gardner, S.M.; Gottlieb, L.; Pan, B.; Petersson, E.J.; Marmorstein, R.
Molecular role of NAA38 in thermostability and catalytic activity of the human NatC N-terminal acetyltransferase
Structure
31
166-173.e4
2023
Homo sapiens (Q147X3 and Q5VZE5 and Q9BRA0)
brenda
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