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acetyl-CoA + an N-terminal-L-methionyl-L-histidyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-histidyl-[protein] + CoA
-
-
-
?
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
high activity, the full sequence is MLALISRRWGRPVGRRRRPVRVYP
-
-
?
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
highest activity. The full sequence is MLGTGPARWGRPVGRRRRPVRVYP
-
-
?
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
the full sequence is MLGTEGGRWGRPVGRRRRPVRVYP
-
-
?
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
high activity, the full sequence is MLGTEGGRWGRPVGRRRRPVRVYP
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-lysyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-lysyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-methionyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-methionyl-[protein] + CoA
-
-
-
?
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
-
-
-
?
acetyl-CoA + L-Met-Ile-Arg-Leu-Lys-Ala
?
-
-
-
-
?
acetyl-CoA + N-terminal-L-methionyl-L-alanyl-[PLD]
N-terminal-Nalpha-acetyl-L-methionyl-L-alanyl-[PLD] + CoA
a NatF-type substrate
-
-
?
acetyl-CoA + N-terminal-L-methionyl-L-isoleucyl-[Lrg1 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[Lrg1 protein] + CoA
acetyl-CoA + N-terminal-L-methionyl-L-isoleucyl-[Sly41 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[Sly41 protein] + CoA
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
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-[Glr1 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[Glr1 protein] + CoA
-
-
-
-
?
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-[GPE]
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[GPE] + CoA
a NatE-type substrate
-
-
?
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-[GTG]
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[GTG] + CoA
a NatC-type substrate
-
-
?
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
DP11 peptide (MARYFRR) is a substrate of NatC, a synthetic peptide
-
-
ir
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-[Trm1-II protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[Trm1-II protein] + CoA
-
-
-
-
?
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
-
-
-
-
?
acetyl-CoA + N-terminal-L-methionyl-L-tyrosinyl-[Nup157 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosinyl-[Nup157 protein] + CoA
-
-
-
-
?
acetyl-CoA + N-terminal-L-methionyl-L-tyrosinyl-[Pxl1 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosinyl-[Pxl1 protein] + CoA
-
-
-
-
?
acetyl-CoA + N-terminal-L-methionyl-L-tyrosinyl-[Tgl1 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosinyl-[Tgl1 protein] + CoA
-
-
-
-
?
additional information
?
-
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-isoleucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA
-
-
-
?
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-[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-[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-[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-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
-
-
-
?
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-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
-
-
-
-
?
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-phenylalanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
-
-
-
?
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-tryptophyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tryptophyl-[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-tyrosinyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosinyl-[protein] + CoA
-
-
-
?
acetyl-CoA + N-terminal-L-methionyl-L-isoleucyl-[Lrg1 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[Lrg1 protein] + CoA
-
-
-
-
?
acetyl-CoA + N-terminal-L-methionyl-L-isoleucyl-[Lrg1 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[Lrg1 protein] + CoA
-
-
-
-
?
acetyl-CoA + N-terminal-L-methionyl-L-isoleucyl-[Sly41 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[Sly41 protein] + CoA
-
-
-
-
?
acetyl-CoA + N-terminal-L-methionyl-L-isoleucyl-[Sly41 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[Sly41 protein] + CoA
-
-
-
-
?
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-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
Q4CRN8; Q4DLD9; Q4D159, Q4DGZ6; Q4DJ45; Q4D159
-
-
-
ir
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-glycyl-L-proline + CoA
Q4CRN8; Q4DLD9; Q4D159, Q4DGZ6; Q4DJ45; Q4D159
-
-
-
ir
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-[Bem1 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[Bem11 protein] + CoA
-
-
-
-
?
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-[Bem1 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[Bem11 protein] + CoA
-
-
-
-
?
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-[Arl3 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[Arl3 protein] + CoA
-
-
-
-
?
acetyl-CoA + N-terminal-L-methionyl-L-phenylalanyl-[Arl3 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[Arl3 protein] + CoA
-
-
-
-
?
additional information
?
-
almost no activity with nuclear factor kappaB p65 (MDELFPLRWGRPVGRRRRPVRVYP), kinesin KIF4A (MKEEVKGRWGRPVGRRRRPVRVYP), and high-mobility group protein A1 (SESSSKSRWGRPVGRRRRPVRVYP)
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
Q4CRN8; Q4DLD9; Q4D159
analysis of in vitro acetyltransferase activity of GST-tagged TcNaa30: no activity with peptides STPD, EEEIA, MDEL, and MLGP
-
-
-
additional information
?
-
Q4DGZ6; Q4DJ45; Q4D159
analysis of in vitro acetyltransferase activity of GST-tagged TcNaa30: no activity with peptides STPD, EEEIA, MDEL, and MLGP
-
-
-
additional information
?
-
Q4CRN8; Q4DLD9; Q4D159
analysis of in vitro acetyltransferase activity of GST-tagged TcNaa30: no activity with peptides STPD, EEEIA, MDEL, and MLGP
-
-
-
additional information
?
-
Q4DGZ6; Q4DJ45; Q4D159
analysis of in vitro acetyltransferase activity of GST-tagged TcNaa30: no activity with peptides STPD, EEEIA, MDEL, and MLGP
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
acetyl-CoA + an N-terminal-L-methionyl-L-histidyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-histidyl-[protein] + CoA
-
-
-
?
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
high activity, the full sequence is MLALISRRWGRPVGRRRRPVRVYP
-
-
?
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
highest activity. The full sequence is MLGTGPARWGRPVGRRRRPVRVYP
-
-
?
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
the full sequence is MLGTEGGRWGRPVGRRRRPVRVYP
-
-
?
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
high activity, the full sequence is MLGTEGGRWGRPVGRRRRPVRVYP
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-lysyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-lysyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-methionyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-methionyl-[protein] + CoA
-
-
-
?
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
-
-
-
?
acetyl-CoA + N-terminal-L-methionyl-L-phenylalanyl-[Arl3 protein]
N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[Arl3 protein] + CoA
-
-
-
?
additional information
?
-
almost no activity with nuclear factor kappaB p65 (MDELFPLRWGRPVGRRRRPVRVYP), kinesin KIF4A (MKEEVKGRWGRPVGRRRRPVRVYP), and high-mobility group protein A1 (SESSSKSRWGRPVGRRRRPVRVYP)
-
-
?
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-isoleucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA
-
-
-
?
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-[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-[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-[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-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
-
-
-
?
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-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
-
-
-
-
?
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-phenylalanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
-
-
-
?
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-tryptophyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tryptophyl-[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-tyrosinyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosinyl-[protein] + CoA
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
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
knockdown of Nalpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant Arf-like GTPase Arl8b localization
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
physiological function
-
MAK3 is required for the N-terminal acetylation of the killer viral major coat protein, Gag
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 essential for embryonic development
physiological function
the enzyme is essential for mitochondrial integrity and function
physiological function
the enzyme is required for double-stranded RNA virus propagation in Saccharomyces cerevisiae
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
Q4CRN8; Q4DLD9; Q4D159, Q4DGZ6; Q4DJ45; 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
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
-
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
-
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
-
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
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
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
-
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
-
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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 (Q4CRN8 AND Q4DLD9 AND Q4D159), Trypanosoma cruzi (Q4DGZ6 AND Q4DJ45 AND Q4D159), Trypanosoma cruzi CL Brener (Q4CRN8 AND Q4DLD9 AND Q4D159), Trypanosoma cruzi CL Brener (Q4DGZ6 AND Q4DJ45 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 H37Rv (I6YG32), Mycobacterium tuberculosis ATCC 25618 (I6YG32)
brenda