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2 S-adenosyl-L-methionine + CPKRIA
2 S-adenosyl-L-homocysteine + ?
mono- and dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + FPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation and low level trimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + HPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + IPKRIA
2 S-adenosyl-L-homocysteine + ?
mono- and dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + KPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation and low level trimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + LPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation and low level trimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + MPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation and low level trimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + N-terminal-histone 2B
2 S-adenosyl-L-homocysteine + ?
dimethylation of fruit fly histone 2B by NTMT1 over an N-terminal sequence of 1PPKTSGKAA9
-
-
?
2 S-adenosyl-L-methionine + NPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + PPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + QPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + RPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation and low level trimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + TPKRIA
2 S-adenosyl-L-homocysteine + ?
mono- and dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + VPKRIA
2 S-adenosyl-L-homocysteine + ?
mono- and dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + WPKRIA
2 S-adenosyl-L-homocysteine + ?
mono- and dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + YPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation by NTMT1
-
-
?
3 (E)-hex-2-en-5-ynyl-S-adenosyl-L-methionine + N-terminal-OLA1
?
-
-
-
?
3 S-adenosyl-L-methionine + APKRIA
3 S-adenosyl-L-homocysteine + ?
trimethylation by NTMT1
-
-
?
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
3 S-adenosyl-L-methionine + GPKRIA
3 S-adenosyl-L-homocysteine + ?
trimethylation by NTMT1
-
-
?
3 S-adenosyl-L-methionine + N-terminal-CENP-A
3 S-adenosyl-L-homocysteine + ?
human CENP-A histone, molecular details for CENP-A recognition by NRMT1. State-specific trimethylation of CENP-A by NRMT1
-
-
?
3 S-adenosyl-L-methionine + N-terminal-dimethyl-SPKRIAKRRS-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIAKRRS-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-LPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-LPKRIA-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-methyl-SPKRIAKRRS-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIAKRRS-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-OLA1
3 S-adenosyl-L-homocysteine + ?
3 S-adenosyl-L-methionine + N-terminal-peptide-[BAP1 protein]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-peptide-[BAP1 protein]
-
i.e. BRCA1 associated protein 1, a DNA repair protein
-
-
?
3 S-adenosyl-L-methionine + N-terminal-peptide-[DDB2 protein]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-peptide-[DDB2 protein]
-
DDB2 is a DNA repair protein
-
-
?
3 S-adenosyl-L-methionine + N-terminal-peptide-[PARP3 protein]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-peptide-[PARP3 protein]
-
i.e. poly-ADP-ribosylase 3, a DNA repair protein
-
-
?
3 S-adenosyl-L-methionine + N-terminal-PPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-PPKRIA-[RCC1]
3 S-adenosyl-L-methionine + N-terminal-RPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-RPKRIA-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-SPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIA-[RCC1]
3 S-adenosyl-L-methionine + N-terminal-SPKRIAKRR-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIAKRR-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-SPKRIAKRRS-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIAKRRS-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-SPKRIAKRRSPP-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIAKRRSPP-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-WPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-WPKRIA-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-YPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-YPKRIA-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-[eEF1A]
3 S-adenosyl-L-homocysteine + ?
3 S-adenosyl-L-methionine + N-terminal-[RCC1]
3 S-adenosyl-L-homocysteine + ?
3 S-adenosyl-L-methionine + SPKRIA
3 S-adenosyl-L-homocysteine + ?
trimethylation by NTMT1
-
-
?
L-lysyl-[protein] + 3 S-adenosyl-L-methionine
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine
N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + APKQQLSKY
?
S-adenosyl-L-methionine + DPKRIA
S-adenosyl-L-homocysteine + ?
monomethylation by NTMT1
-
-
?
S-adenosyl-L-methionine + EPKRIA
S-adenosyl-L-homocysteine + ?
monomethylation by NTMT1
-
-
?
S-adenosyl-L-methionine + human histone H3
S-adenosyl-L-homocysteine + ?
-
lower activity with histone H3 compared to histone H4
-
-
?
S-adenosyl-L-methionine + human histone H4
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + N-terminal peptide sequence of a protein
S-adenosyl-L-homocysteine + methylated N-terminal peptide sequence of a protein
-
all known substrates of NTMT1 contain the N-terminal consensus sequence XPK (X = S/P/A/G), although NTMT1 can also methylate peptides with X being F, Y, C, M, K, R, N, Q, or H in vitro, substrate specificity of NTMT1, overview. Structural basis for the specific N-terminal methylation of a consensus motif, XPK, by NTMT1, overview. Hexapeptides composed of the first six residues of RCC1, i.e. regulator of chromosome condensation 1, are recognized by the enzyme. The first residue within the consensus sequence of the NTMT1 substrates is anchored through a hydrogen bond with the conserved Asn168 of NTMT1 in a spacious binding pocket, which exposes the substrate's reactive alpha-amino group to S-adenosyl-L-methionine in the complex structures, and this very N-terminal residue can tolerate most residue substitutions except the negatively charged residues D and E. Asp180 and His140 can act as bases to facilitate deprotonation of the target alpha-N-terminal amino group. Catalytic reaction proceeds probably involving a SN1 mechanism, overview
S-adenosyl-L-homocysteine is bound to NTMT1 in an extended conformation. The carboxylate moiety of SAH forms a salt bridge interaction with the highly conserved Arg74, and the ribosyl group stacks with the indole ring of Trp20. In addition, the adenine moiety of SAH is flanked by the hydrophobic side chains of Ile92 and Val137 and interacts with the main chain amide group of Leu119 and the side chain of Gln120 through hydrogen bonding
-
?
S-adenosyl-L-methionine + N-terminal-(A,P,S)PK-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-(A,P,S)PK-[protein]
-
-
-
?
S-adenosyl-L-methionine + N-terminal-CENP-A
S-adenosyl-L-homocysteine + ?
human CENP-A histone
-
-
?
S-adenosyl-L-methionine + N-terminal-histone 2B
S-adenosyl-L-homocysteine + ?
fruit fly histone 2B
-
-
?
S-adenosyl-L-methionine + PPKQQLSKY
?
S-adenosyl-L-methionine + Ran guanine nucleotide-exchange factor RCC1
S-adenosyl-L-homocysteine + ?
S-adenosyl-L-methionine + retinoblastoma protein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + Rpl12ab
?
-
methylation of Rpl12ab at the N-terminal proline residue
-
-
?
S-adenosyl-L-methionine + Rpl12ab
S-adenosyl-L-homocysteine + ?
S-adenosyl-L-methionine + Rps25a
?
S-adenosyl-L-methionine + Rps25b
?
S-adenosyl-L-methionine + SET/TAF-I/PHAPII
S-adenosyl-L-homocysteine + ?
-
only the SETalpha splicing variant is a substrate for NRMT, since it begins with the NRMT consensus in contrast to the beta splicing variant
-
-
?
S-adenosyl-L-methionine + SPKQQLSKY
?
S-adenosyl-L-methionine + SPKRIAKRRSPPADA
?
substrate peptide consisting of the first 15 amino acids of RCC1. NRMT2 V224L is able to significantly decrease the NRMT1 Km with the RCC1 peptide
-
-
?
S-adenosyl-L-methionine + SSKRAKAKTTKKRP
?
substrate peptide consisting of the first 14 amino acids of MYL9
-
-
?
additional information
?
-
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae
-
-
?
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae. Yeast eEF1A is trimethylated at its N-terminus and dimethylated at lysine 3. Human eEF1A is trimethylated at its N-terminus
-
-
?
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae
-
-
?
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae. Yeast eEF1A is trimethylated at its N-terminus and dimethylated at lysine 3. Human eEF1A is trimethylated at its N-terminus
-
-
?
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
enzyme YLR285W trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae. Yeast eEF1A is trimethylated at its N-terminus and dimethylated at lysine 3. Methylation by Efm7 is affected by the conformation of eEF1A. Efm7 is unable to methylate a synthetic peptide corresponding to the N-terminal 10 amino acids of eEF1A (GKEKSHINVV), but methylates full-length eEF1A in vitro. Human eEF1A is trimethylated at its N-terminus
-
-
?
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae
-
-
?
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae. Yeast eEF1A is trimethylated at its N-terminus and dimethylated at lysine 3. Human eEF1A is trimethylated at its N-terminus
-
-
?
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
enzyme YLR285W trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae. Yeast eEF1A is trimethylated at its N-terminus and dimethylated at lysine 3. Methylation by Efm7 is affected by the conformation of eEF1A. Efm7 is unable to methylate a synthetic peptide corresponding to the N-terminal 10 amino acids of eEF1A (GKEKSHINVV), but methylates full-length eEF1A in vitro. Human eEF1A is trimethylated at its N-terminus
-
-
?
3 S-adenosyl-L-methionine + N-terminal-OLA1
3 S-adenosyl-L-homocysteine + ?
i.e. Obg-like ATPase 1 (OLA1) protein, target validation using normal and NTMT1 knockout HEK-293FT cells demonstrates that OLA1, a protein involved in many critical cellular functions, is methylated in vivo by NTMT1
-
-
?
3 S-adenosyl-L-methionine + N-terminal-OLA1
3 S-adenosyl-L-homocysteine + ?
i.e. Obg-like ATPase 1 (OLA1) protein
-
-
?
3 S-adenosyl-L-methionine + N-terminal-PPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-PPKRIA-[RCC1]
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-PPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-PPKRIA-[RCC1]
-
best substrate
-
-
?
3 S-adenosyl-L-methionine + N-terminal-SPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIA-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-SPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIA-[RCC1]
-
high activity
-
-
?
3 S-adenosyl-L-methionine + N-terminal-SPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIA-[RCC1]
-
i.e. regulator of chromosome condensation 1
-
-
?
3 S-adenosyl-L-methionine + N-terminal-[eEF1A]
3 S-adenosyl-L-homocysteine + ?
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-[eEF1A]
3 S-adenosyl-L-homocysteine + ?
specifically, the C-terminal domain is able to methylate peptides derived from the first 15 amino acids of eEF1A, whereas the N-terminal domain is sufficient for methylation of Lys55. High specificity of METTL13 for eEF1A
-
-
?
3 S-adenosyl-L-methionine + N-terminal-[eEF1A]
3 S-adenosyl-L-homocysteine + ?
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-[eEF1A]
3 S-adenosyl-L-homocysteine + ?
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-[RCC1]
3 S-adenosyl-L-homocysteine + ?
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-[RCC1]
3 S-adenosyl-L-homocysteine + ?
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-[RCC1]
3 S-adenosyl-L-homocysteine + ?
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-[RCC1]
3 S-adenosyl-L-homocysteine + ?
RCC1p and methionine-removed RCC1
-
-
?
L-lysyl-[protein] + 3 S-adenosyl-L-methionine
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
-
-
-
?
L-lysyl-[protein] + 3 S-adenosyl-L-methionine
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
-
-
-
?
L-lysyl-[protein] + 3 S-adenosyl-L-methionine
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
-
-
-
?
L-lysyl-[protein] + 3 S-adenosyl-L-methionine
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
-
-
-
?
N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine
N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
-
-
-
?
N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine
N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
-
-
-
?
N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine
N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
-
-
-
?
N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine
N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + APKQQLSKY
?
synthetic peptide, modified yeast protein Rps25a/Rps25b-derived peptide
-
-
?
S-adenosyl-L-methionine + APKQQLSKY
?
-
synthetic peptide, modified yeast protein Rps25a/Rps25b-derived peptide
-
-
?
S-adenosyl-L-methionine + APKQQLSKY
?
-
synthetic peptide, modified Rps25a/Rps25b-derived peptide
-
-
?
S-adenosyl-L-methionine + PPKQQLSKY
?
synthetic peptide, yeast protein Rps25a/Rps25b-derived peptide
-
-
?
S-adenosyl-L-methionine + PPKQQLSKY
?
-
synthetic peptide, yeast protein Rps25a/Rps25b-derived peptide
-
-
?
S-adenosyl-L-methionine + PPKQQLSKY
?
-
synthetic peptide, Rps25a/Rps25b-derived peptide
-
-
?
S-adenosyl-L-methionine + Ran guanine nucleotide-exchange factor RCC1
S-adenosyl-L-homocysteine + ?
-
NRMT is the predominant alpha-N-methyltransferase for RCC1
-
-
?
S-adenosyl-L-methionine + Ran guanine nucleotide-exchange factor RCC1
S-adenosyl-L-homocysteine + ?
-
substrate docking and mutational analysis of RCC1 defining the NRMT recognition sequence, the first 3 residues Ser-Pro-Lys interact with NRMT, overview
-
-
?
S-adenosyl-L-methionine + Rpl12ab
S-adenosyl-L-homocysteine + ?
-
the yeast Rpl12ab protein is dimethylated at the N-terminal proline residue, trimethylated at Lys-3 by Rkm2, and monomethylated at Arg66
-
-
?
S-adenosyl-L-methionine + Rpl12ab
S-adenosyl-L-homocysteine + ?
-
the yeast Rpl12ab protein is dimethylated at the N-terminal proline residue, trimethylated at Lys-3 by Rkm2, and monomethylated at Arg66. Utilization of top down mass spectrometry to determine the sites of methylation of Rpl12ab
-
-
?
S-adenosyl-L-methionine + Rpl12ab
S-adenosyl-L-homocysteine + ?
-
the yeast Rpl12ab protein is dimethylated at the N-terminal proline residue, trimethylated at Lys-3 by Rkm2, and monomethylated at Arg66
-
-
?
S-adenosyl-L-methionine + Rpl12ab
S-adenosyl-L-homocysteine + ?
-
the yeast Rpl12ab protein is dimethylated at the N-terminal proline residue, trimethylated at Lys-3 by Rkm2, and monomethylated at Arg66. Utilization of top down mass spectrometry to determine the sites of methylation of Rpl12ab
-
-
?
S-adenosyl-L-methionine + Rps25a
?
-
-
-
-
?
S-adenosyl-L-methionine + Rps25a
?
-
Rps25a and Rps25b differ only at position 104, a threonine residue is present in the former and an alanine residue in the latter
-
-
?
S-adenosyl-L-methionine + Rps25b
?
-
-
-
-
?
S-adenosyl-L-methionine + Rps25b
?
-
Rps25a and Rps25b differ only at position 104, a threonine residue is present in the former and an alanine residue in the latter
-
-
?
S-adenosyl-L-methionine + SPKQQLSKY
?
synthetic peptide, modified yeast protein Rps25a/Rps25b-derived peptide
-
-
?
S-adenosyl-L-methionine + SPKQQLSKY
?
-
synthetic peptide, modified yeast protein Rps25a/Rps25b-derived peptide
-
-
?
S-adenosyl-L-methionine + SPKQQLSKY
?
-
synthetic peptide, modified Rps25a/Rps25b-derived peptide
-
-
?
additional information
?
-
alpha-N-terminal methylation of histone H2B protein in Drosophila melanogaster
-
-
-
additional information
?
-
the substrate recognition motif is X-P-K
-
-
-
additional information
?
-
PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit
-
-
-
additional information
?
-
the substrate recognition motif is A-K-A/G/K
-
-
-
additional information
?
-
-
enzyme substrates have a unique N-terminal motif, Met-(Ala/Pro/Ser)-Pro-Lys. The initiating Met is cleaved, and the exposed alpha-amino group is mono-, di-, or trimethylated
-
-
?
additional information
?
-
-
the enzyme shows a ternary complex mechanism of catalysis, involving formation of a SAM-enzyme-acceptor complex and direct transfer of the methyl group from SAM to the acceptor protein
-
-
?
additional information
?
-
the methyltransferases specifically recognizes the N-terminal X-Pro-Lys sequence motif. Localization of methylation sites by top down mass spectrometry using collisionally activated dissociation or electron capture dissociation. The enzyme can also recognize species with N-terminal alanine and serine residues in addition to those with proline residues, but the proline residue in position 1 is a preferred substrate
-
-
?
additional information
?
-
-
the methyltransferases specifically recognizes the N-terminal X-Pro-Lys sequence motif. Localization of methylation sites by top down mass spectrometry using collisionally activated dissociation or electron capture dissociation. The enzyme can also recognize species with N-terminal alanine and serine residues in addition to those with proline residues, but the proline residue in position 1 is a preferred substrate
-
-
?
additional information
?
-
-
the protein N-terminal methyltransferase 1 (NTMT1) methylates the alpha-N-terminal amines of proteins
-
-
?
additional information
?
-
-
enzyme NTMT1 catalyzes the transfer of the methyl group from the S-adenosyl-L-methionine to the protein alpha-amine, resulting in formation of S-adenosyl-L-homocysteine and alpha-N-methylated proteins. Inhibition pattern and methylation progress analyses are performed to determine the kinetic mechanism and processivity of NTMT1, the enzyme NTMT1 utilizes a random sequential bi bi mechanism and proceeds in a distributive manner. Residues of RCC1, i.e. regulator of chromosome condensation 1, are recognized by the enzyme. Methylation status of products is analyzed by MALDI-mass spectrometry
-
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additional information
?
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human MTase-like protein 13 (METTL13) is a dual MTase for both N-terminal Gly1 and Lys55 of human eEF1A. To date, eEF1A is the only validated biological substrate for METTL13
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additional information
?
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human MTase-like protein 13 (METTL13) is a dual MTase for both N-terminal Gly1 and Lys55 of human eEF1A. To date, eEF1A is the only validated biological substrate for METTL13
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additional information
?
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protein N-terminal methyltransferase 1 (NTMT1/NRMT1) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (SAM) to protein alpha-N-terminal amines. It recognizes a specific motif X-P-K/R (X represents any amino acid other than D/E)
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additional information
?
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substrate of NTMT1 are regulator of chromosome condensation 1 (RCC1), tumor suppressor retinoblastoma1 (RB1), oncoprotein SET (also known as I2PP2A, TAF1a), damaged DNA-binding protein2 (DDB2), poly(ADP-ribose) polymerase3 (PARP3), and centromere proteins A and B
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additional information
?
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substrate of NTMT1 are regulator of chromosome condensation 1 (RCC1), tumor suppressor retinoblastoma1 (RB1), oncoprotein SET (also known as I2PP2A, TAF1a), damaged DNA-binding protein2 (DDB2), poly(ADP-ribose) polymerase3 (PARP3), and centromere proteins A and B
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additional information
?
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the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1
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additional information
?
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the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1
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additional information
?
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analysis of methylation sites, method, detailed overview
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additional information
?
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analysis of methylation sites, method, detailed overview
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additional information
?
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histone peptide profiling reveals that human NRMT1is highly selective to human CENP-A and fruit fly H2B, which share a common Xaa-Pro-Lys/Arg motif
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additional information
?
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histone peptide profiling reveals that human NRMT1is highly selective to human CENP-A and fruit fly H2B, which share a common Xaa-Pro-Lys/Arg motif
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additional information
?
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motif sequence and signal peptide analyses, and activity-based substrate profiling of NTMT1 utilizing (E)-hex-2-en-5-ynyl-S-adenosyl-L-methionine (Hey-SAM) reveals 72 potential targets, overview
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additional information
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NRMT1 exhibits distributive trimethylase activity in vitro. Isozymes NRMT1 and NRMT2 can interact both in vitro and in vivo, modeling of NRMT1 and NRMT2 interactions. The Ser-Pro-Lys consensus sequence of the RCC1 peptide is a preferred substrate for NRMT1
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additional information
?
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NTMT1 is a tri-methyltransferase
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additional information
?
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NTMT1 is a tri-methyltransferase
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additional information
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the substrate recognition motif is X-P-K/R. NTMT1 is able to methylate hexamer peptides. NTMT1 is known to be a trimethylase that catalyzes mono-, di-, and trimethylation. During the process of multiple methylations, the substrate can be released and rebind to NTMT1, which proceeds through a distributive mechanism for multiple methylations
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additional information
?
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the substrate recognition motif is X-P-K/R. NTMT1 is able to methylate hexamer peptides. NTMT1 is known to be a trimethylase that catalyzes mono-, di-, and trimethylation. During the process of multiple methylations, the substrate can be released and rebind to NTMT1, which proceeds through a distributive mechanism for multiple methylations
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additional information
?
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the substrate recognition sequence is GKEKTH
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additional information
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the substrate recognition sequence is GKEKTH
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additional information
?
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the N-terminal protein methyltransferase catalyzes the modification of two ribosomal protein substrates, Rpl12ab and Rps25a/Rps25b. The yeast RPS25A and RPS25B genes and differ only at a single amino acid residue
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additional information
?
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the methyltransferases specifically recognizes the N-terminal X-Pro-Lys sequence motif. Localization of methylation sites by top down mass spectrometry using collisionally activated dissociation or electron capture dissociation. The yeast enzyme can also recognize species with N-terminal alanine and serine residues in addition to those with proline residues, although to a lesser extent, the proline residue in position 1 is a preferred substrate
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?
additional information
?
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the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1
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additional information
?
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the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1
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additional information
?
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the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1
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additional information
?
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YLR285W, also named elongation factor methyltransferase 7 (Efm7), is a dual MTase that installs methyl groups at both N-terminal Gly1 and Lys2 residues of yeast eEF1A protein. Lys2 is methylated only after trimethylation of Gly1. Yeast eEF1A starts with GKEKSHINV and is the only known substrate of Efm7, although there are 35 other yeast proteins with a G-K sequence at their N termini. But Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A
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additional information
?
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YLR285W, also named elongation factor methyltransferase 7 (Efm7), is a dual MTase that installs methyl groups at both N-terminal Gly1 and Lys2 residues of yeast eEF1A protein. Lys2 is methylated only after trimethylation of Gly1. Yeast eEF1A starts with GKEKSHINV and is the only known substrate of Efm7, although there are 35 other yeast proteins with a G-K sequence at their N termini. But Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A
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additional information
?
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analysis of methylation sites, method, detailed overview
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additional information
?
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analysis of methylation sites, method, detailed overview
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additional information
?
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analysis of methylation sites, method, detailed overview
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additional information
?
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the S-adenosyl-L-methionine-dependent protein methyltransferase EFM7 trimethylates the N-terminal glycine Gly-2 of elongation factor 1-alpha (TEF1 and TEF2), before also catalyzing the mono- and dimethylation of Lys-3. The substrate recognition sequence is GKEKSH. Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A. Efm7 can methylate domain 1 (residues 1-238) of eEF1A, but to a smaller degree of trimethylation. Although yeast Efm7 is not able to methylate the decamer peptide that is derived from yeast N-terminal eEF1A, METTL13 can methylate the 15mer peptide derived from human N-terminal eEF1A
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additional information
?
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the S-adenosyl-L-methionine-dependent protein methyltransferase EFM7 trimethylates the N-terminal glycine Gly-2 of elongation factor 1-alpha (TEF1 and TEF2), before also catalyzing the mono- and dimethylation of Lys-3. The substrate recognition sequence is GKEKSH. Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A. Efm7 can methylate domain 1 (residues 1-238) of eEF1A, but to a smaller degree of trimethylation. Although yeast Efm7 is not able to methylate the decamer peptide that is derived from yeast N-terminal eEF1A, METTL13 can methylate the 15mer peptide derived from human N-terminal eEF1A
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additional information
?
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the substrate recognition motif is X-P-K. YBR261C methylates ribosomal substrates Rp112ab and Rps25a/Rps25b. YBR261C is able to methylate nonamer synthetic peptides, including PPKQQLSKY, which is derived from alpha-N-terminal Rps25a/b and A/S-PKQQLSKY, with Ala or Ser replacing Pro. YBR261C is able to methylate nonamer peptides
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additional information
?
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the substrate recognition motif is X-P-K. YBR261C methylates ribosomal substrates Rp112ab and Rps25a/Rps25b. YBR261C is able to methylate nonamer synthetic peptides, including PPKQQLSKY, which is derived from alpha-N-terminal Rps25a/b and A/S-PKQQLSKY, with Ala or Ser replacing Pro. YBR261C is able to methylate nonamer peptides
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additional information
?
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the substrate recognition motif is X-P-K. YBR261C methylates ribosomal substrates Rp112ab and Rps25a/Rps25b. YBR261C is able to methylate nonamer synthetic peptides, including PPKQQLSKY, which is derived from alpha-N-terminal Rps25a/b and A/S-PKQQLSKY, with Ala or Ser replacing Pro. YBR261C is able to methylate nonamer peptides
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additional information
?
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the substrate recognition motif is X-P-K. YBR261C methylates ribosomal substrates Rp112ab and Rps25a/Rps25b. YBR261C is able to methylate nonamer synthetic peptides, including PPKQQLSKY, which is derived from alpha-N-terminal Rps25a/b and A/S-PKQQLSKY, with Ala or Ser replacing Pro. YBR261C is able to methylate nonamer peptides
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additional information
?
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the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1
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-
-
additional information
?
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the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1
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-
-
additional information
?
-
analysis of methylation sites, method, detailed overview
-
-
-
additional information
?
-
analysis of methylation sites, method, detailed overview
-
-
-
additional information
?
-
YLR285W, also named elongation factor methyltransferase 7 (Efm7), is a dual MTase that installs methyl groups at both N-terminal Gly1 and Lys2 residues of yeast eEF1A protein. Lys2 is methylated only after trimethylation of Gly1. Yeast eEF1A starts with GKEKSHINV and is the only known substrate of Efm7, although there are 35 other yeast proteins with a G-K sequence at their N termini. But Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A
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-
-
additional information
?
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YLR285W, also named elongation factor methyltransferase 7 (Efm7), is a dual MTase that installs methyl groups at both N-terminal Gly1 and Lys2 residues of yeast eEF1A protein. Lys2 is methylated only after trimethylation of Gly1. Yeast eEF1A starts with GKEKSHINV and is the only known substrate of Efm7, although there are 35 other yeast proteins with a G-K sequence at their N termini. But Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A
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additional information
?
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the S-adenosyl-L-methionine-dependent protein methyltransferase EFM7 trimethylates the N-terminal glycine Gly-2 of elongation factor 1-alpha (TEF1 and TEF2), before also catalyzing the mono- and dimethylation of Lys-3. The substrate recognition sequence is GKEKSH. Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A. Efm7 can methylate domain 1 (residues 1-238) of eEF1A, but to a smaller degree of trimethylation. Although yeast Efm7 is not able to methylate the decamer peptide that is derived from yeast N-terminal eEF1A, METTL13 can methylate the 15mer peptide derived from human N-terminal eEF1A
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additional information
?
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the S-adenosyl-L-methionine-dependent protein methyltransferase EFM7 trimethylates the N-terminal glycine Gly-2 of elongation factor 1-alpha (TEF1 and TEF2), before also catalyzing the mono- and dimethylation of Lys-3. The substrate recognition sequence is GKEKSH. Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A. Efm7 can methylate domain 1 (residues 1-238) of eEF1A, but to a smaller degree of trimethylation. Although yeast Efm7 is not able to methylate the decamer peptide that is derived from yeast N-terminal eEF1A, METTL13 can methylate the 15mer peptide derived from human N-terminal eEF1A
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additional information
?
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the enzyme alpha-N-methylates the small subunit of ribulose-1,5-bisphohate carboxylase/oxygenase
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additional information
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the substrate recognition motif is M-L/M/K-G/Q. PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit
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additional information
?
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the substrate recognition motif is M-L/M/K-G/Q. PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit
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additional information
?
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the substrate recognition motif is M-L/M/K-G/Q. PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
3 S-adenosyl-L-methionine + GPKRIA
3 S-adenosyl-L-homocysteine + ?
trimethylation by NTMT1
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?
3 S-adenosyl-L-methionine + N-terminal-OLA1
3 S-adenosyl-L-homocysteine + ?
i.e. Obg-like ATPase 1 (OLA1) protein, target validation using normal and NTMT1 knockout HEK-293FT cells demonstrates that OLA1, a protein involved in many critical cellular functions, is methylated in vivo by NTMT1
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?
3 S-adenosyl-L-methionine + N-terminal-PPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-PPKRIA-[RCC1]
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-
?
3 S-adenosyl-L-methionine + N-terminal-[eEF1A]
3 S-adenosyl-L-homocysteine + ?
3 S-adenosyl-L-methionine + N-terminal-[RCC1]
3 S-adenosyl-L-homocysteine + ?
L-lysyl-[protein] + 3 S-adenosyl-L-methionine
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine
N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + N-terminal-(A,P,S)PK-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-(A,P,S)PK-[protein]
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?
S-adenosyl-L-methionine + N-terminal-CENP-A
S-adenosyl-L-homocysteine + ?
human CENP-A histone
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?
S-adenosyl-L-methionine + N-terminal-histone 2B
S-adenosyl-L-homocysteine + ?
fruit fly histone 2B
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?
S-adenosyl-L-methionine + Ran guanine nucleotide-exchange factor RCC1
S-adenosyl-L-homocysteine + ?
-
NRMT is the predominant alpha-N-methyltransferase for RCC1
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?
S-adenosyl-L-methionine + retinoblastoma protein
S-adenosyl-L-homocysteine + ?
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?
S-adenosyl-L-methionine + Rpl12ab
?
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methylation of Rpl12ab at the N-terminal proline residue
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?
S-adenosyl-L-methionine + Rpl12ab
S-adenosyl-L-homocysteine + ?
S-adenosyl-L-methionine + Rps25a
?
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?
S-adenosyl-L-methionine + Rps25b
?
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?
additional information
?
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3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae
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?
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae
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?
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae
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?
3 S-adenosyl-L-methionine + N-terminal-[eEF1A]
3 S-adenosyl-L-homocysteine + ?
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?
3 S-adenosyl-L-methionine + N-terminal-[eEF1A]
3 S-adenosyl-L-homocysteine + ?
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?
3 S-adenosyl-L-methionine + N-terminal-[eEF1A]
3 S-adenosyl-L-homocysteine + ?
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?
3 S-adenosyl-L-methionine + N-terminal-[RCC1]
3 S-adenosyl-L-homocysteine + ?
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-
-
?
3 S-adenosyl-L-methionine + N-terminal-[RCC1]
3 S-adenosyl-L-homocysteine + ?
-
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-
?
L-lysyl-[protein] + 3 S-adenosyl-L-methionine
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
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-
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?
L-lysyl-[protein] + 3 S-adenosyl-L-methionine
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
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?
L-lysyl-[protein] + 3 S-adenosyl-L-methionine
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
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?
L-lysyl-[protein] + 3 S-adenosyl-L-methionine
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
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-
-
?
N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine
N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
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-
?
N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine
N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
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?
N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine
N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
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-
-
?
N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine
N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
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?
S-adenosyl-L-methionine + Rpl12ab
S-adenosyl-L-homocysteine + ?
-
the yeast Rpl12ab protein is dimethylated at the N-terminal proline residue, trimethylated at Lys-3 by Rkm2, and monomethylated at Arg66
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?
S-adenosyl-L-methionine + Rpl12ab
S-adenosyl-L-homocysteine + ?
-
the yeast Rpl12ab protein is dimethylated at the N-terminal proline residue, trimethylated at Lys-3 by Rkm2, and monomethylated at Arg66
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?
additional information
?
-
alpha-N-terminal methylation of histone H2B protein in Drosophila melanogaster
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additional information
?
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PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit
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-
additional information
?
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the protein N-terminal methyltransferase 1 (NTMT1) methylates the alpha-N-terminal amines of proteins
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?
additional information
?
-
human MTase-like protein 13 (METTL13) is a dual MTase for both N-terminal Gly1 and Lys55 of human eEF1A. To date, eEF1A is the only validated biological substrate for METTL13
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-
-
additional information
?
-
human MTase-like protein 13 (METTL13) is a dual MTase for both N-terminal Gly1 and Lys55 of human eEF1A. To date, eEF1A is the only validated biological substrate for METTL13
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additional information
?
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protein N-terminal methyltransferase 1 (NTMT1/NRMT1) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (SAM) to protein alpha-N-terminal amines. It recognizes a specific motif X-P-K/R (X represents any amino acid other than D/E)
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-
-
additional information
?
-
substrate of NTMT1 are regulator of chromosome condensation 1 (RCC1), tumor suppressor retinoblastoma1 (RB1), oncoprotein SET (also known as I2PP2A, TAF1a), damaged DNA-binding protein2 (DDB2), poly(ADP-ribose) polymerase3 (PARP3), and centromere proteins A and B
-
-
-
additional information
?
-
substrate of NTMT1 are regulator of chromosome condensation 1 (RCC1), tumor suppressor retinoblastoma1 (RB1), oncoprotein SET (also known as I2PP2A, TAF1a), damaged DNA-binding protein2 (DDB2), poly(ADP-ribose) polymerase3 (PARP3), and centromere proteins A and B
-
-
-
additional information
?
-
the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1
-
-
-
additional information
?
-
-
the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1
-
-
-
additional information
?
-
-
the N-terminal protein methyltransferase catalyzes the modification of two ribosomal protein substrates, Rpl12ab and Rps25a/Rps25b. The yeast RPS25A and RPS25B genes and differ only at a single amino acid residue
-
-
?
additional information
?
-
the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1
-
-
-
additional information
?
-
the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1
-
-
-
additional information
?
-
-
the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1
-
-
-
additional information
?
-
YLR285W, also named elongation factor methyltransferase 7 (Efm7), is a dual MTase that installs methyl groups at both N-terminal Gly1 and Lys2 residues of yeast eEF1A protein. Lys2 is methylated only after trimethylation of Gly1. Yeast eEF1A starts with GKEKSHINV and is the only known substrate of Efm7, although there are 35 other yeast proteins with a G-K sequence at their N termini. But Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A
-
-
-
additional information
?
-
YLR285W, also named elongation factor methyltransferase 7 (Efm7), is a dual MTase that installs methyl groups at both N-terminal Gly1 and Lys2 residues of yeast eEF1A protein. Lys2 is methylated only after trimethylation of Gly1. Yeast eEF1A starts with GKEKSHINV and is the only known substrate of Efm7, although there are 35 other yeast proteins with a G-K sequence at their N termini. But Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A
-
-
-
additional information
?
-
the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1
-
-
-
additional information
?
-
the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1
-
-
-
additional information
?
-
YLR285W, also named elongation factor methyltransferase 7 (Efm7), is a dual MTase that installs methyl groups at both N-terminal Gly1 and Lys2 residues of yeast eEF1A protein. Lys2 is methylated only after trimethylation of Gly1. Yeast eEF1A starts with GKEKSHINV and is the only known substrate of Efm7, although there are 35 other yeast proteins with a G-K sequence at their N termini. But Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A
-
-
-
additional information
?
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YLR285W, also named elongation factor methyltransferase 7 (Efm7), is a dual MTase that installs methyl groups at both N-terminal Gly1 and Lys2 residues of yeast eEF1A protein. Lys2 is methylated only after trimethylation of Gly1. Yeast eEF1A starts with GKEKSHINV and is the only known substrate of Efm7, although there are 35 other yeast proteins with a G-K sequence at their N termini. But Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A
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additional information
?
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the substrate recognition motif is M-L/M/K-G/Q. PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit
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-
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additional information
?
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the substrate recognition motif is M-L/M/K-G/Q. PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit
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-
-
additional information
?
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the substrate recognition motif is M-L/M/K-G/Q. PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit
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evolution
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METTL11a, i.e. NRMT, encodes a 25 kDa protein in the methyltransferase 11 family, most members of which methylate metabolites or other small molecules. alpha-N-methyltransferase is a conserved member of a superfamily of non-SET domain enzymes
evolution
-
Rkm2 belongs to the SET domain methyltransferases
evolution
enzymatic functional conservation of NRMT1 across species, evolutionary conservation of histone alpha-N-modification. Coevolution of NRMT1 recognition motifs in RCC1, CENP-A, and CENP-B, in which sequences 1SPKRIA6 of RCC1, 1GPRRRS6 of CENP-A, and 1GPKRRQ6 of CENP-B co-occur in mammals but are all missing in lower organisms. In contrast, the NRMT1 recognition motif of histone H2B is conserved from ciliates to insects but is lost in mammals. Remarkably, yeast and chicken orthologues of the above proteins do not harbor an NRMT1 recognition motif, suggesting that NRMT1 may exert its cellular function in these organisms through other protein substrates
evolution
enzyme Efm5 is a distinct type of eukaryotic N-terminal methyltransferase as, unlike the three other known eukaryotic N-terminal methyltransferases, its substrate does not have an N-terminal [A/P/S]-P-K motif. The N-terminal methylation of eEF1A is also present in human catalyzed by enzyme N6AMT2, this conservation over a large evolutionary distance suggests it to be of functional importance. The trimethylation of Lys79 in eEF1A is conserved from yeast to human. Human enzyme N6AMT2 is the direct orthologue of the yeast Efm5, and Efm5 and N6AMT2 can methylate eEF1A from either species in vitro
evolution
structural comparison of isozymes NTMT1 and NTMT2 (EC 2.1.1.299), overview. NTMT1 and NTMT2 employ a similar substrate recognition mode
evolution
the enzyme belongs to the methyltransferase like (METTL) family of class I methyltransferases containing seven-beta-strand methyltransferase motifs and Rossman folds for binding SAM. The N-terminal methyltransferase homologs NRMT1 (N-terminal RCC1 methyltransferase 1) and NRMT2 (N-terminal RCC1 methyltransferase 2), which following cleavage of the initiating methionine, methylate the alpha-amine of the first N-terminal residue of their substrates. NRMT1 and NRMT2 are 50% identical and 75% similar and share an N-terminal X-P-K consensus sequence. Although structurally similar, they differ in their catalytic activities
evolution
the enzyme is a distinct type of eukaryotic N-terminal methyltransferase as, unlike the three other known eukaryotic N-terminal methyltransferases, its substrate does not have an N-terminal [A/P/S]-P-K motif. The N-terminal methylation of eEF1A is also present in yeast catalyzed by enzymes Efm5 and Efm7, this conservation over a large evolutionary distance suggests it to be of functional importance. The trimethylation of Lys79 in eEF1A is conserved from yeast to human. Human enzyme N6AMT2 is the direct orthologue of the yeast Efm5, and Efm5 and N6AMT2 can methylate eEF1A from either species in vitro. Methyltransferases that act on lysine 79 in eEF1A are conserved from yeast to human
evolution
YLR285W is termed elongation factor methyltransferase 7 (Efm7). This enzyme is a distinct type of eukaryotic N-terminal methyltransferase as, unlike the three other known eukaryotic N-terminal methyltransferases, its substrate does not have an N-terminal [A/P/S]-P-K motif. The N-terminal methylation of eEF1A is also present in human catalyzed by enzyme N6AMT2, this conservation over a large evolutionary distance suggests it to be of functional importance. The trimethylation of Lys79 in eEF1A is conserved from yeast to human
evolution
-
Rkm2 belongs to the SET domain methyltransferases
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evolution
-
enzyme Efm5 is a distinct type of eukaryotic N-terminal methyltransferase as, unlike the three other known eukaryotic N-terminal methyltransferases, its substrate does not have an N-terminal [A/P/S]-P-K motif. The N-terminal methylation of eEF1A is also present in human catalyzed by enzyme N6AMT2, this conservation over a large evolutionary distance suggests it to be of functional importance. The trimethylation of Lys79 in eEF1A is conserved from yeast to human. Human enzyme N6AMT2 is the direct orthologue of the yeast Efm5, and Efm5 and N6AMT2 can methylate eEF1A from either species in vitro
-
evolution
-
YLR285W is termed elongation factor methyltransferase 7 (Efm7). This enzyme is a distinct type of eukaryotic N-terminal methyltransferase as, unlike the three other known eukaryotic N-terminal methyltransferases, its substrate does not have an N-terminal [A/P/S]-P-K motif. The N-terminal methylation of eEF1A is also present in human catalyzed by enzyme N6AMT2, this conservation over a large evolutionary distance suggests it to be of functional importance. The trimethylation of Lys79 in eEF1A is conserved from yeast to human
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malfunction
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loss of the Saccharomyces cerevisiae ORF YBR261c/TAE results in the loss of the N-terminal methylation of both Rpl12ab and Rps25a/Rps25b
malfunction
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methylation-defective mutants of RCC1 have reduced affinity for DNA and cause mitotic defects, and non-methylatable mutants of RCC1 are defective in chromatin association, and their expression in a wild-type background produces supernumerary spindle poles and missegregation of mitotic chromosomes, most likely due to the disruption of the Ran gradient
malfunction
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loss of the N-terminal methyltransferase NRMT1 increases sensitivity to DNA damage and promotes mammary oncogenesis. Enzyme NRMT1 knockdown significantly enhances the sensitivity of breast cancer cell lines to both etoposide treatment and gamma-irradiation, as well as, increases proliferation rate, invasive potential, anchorage-independent growth, xenograft tumor size, and tamoxifen sensitivity, e.g. in MCF-7 cells. NRMT1 knockdown promotes growth of excision repair positive breast cancer cell lines, but has no effect on the normally low NRMT1-expressing SKBR-3 and MDA-MB-231 cells. Phenotype, overview
malfunction
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NTMT1 is upregulated in a variety of cancers and knockdown of NTMT1 results in cell mitotic defects
malfunction
aberrant N-terminal methylation has been implicated in several cancers and developmental diseases
malfunction
deletion of YBR261C in yeast abolishes N-terminal methylation, which consequently alters the ribosomal profile and leads to defects in both translational efficiency and fidelity. Overexpression of YBR261 validates its involvement in protein synthesis
malfunction
deletion of YLR285W results in the loss of N-terminal and lysine methylation in vivo, whereas overexpression of YLR285W results in an increase of methylation at these sites
malfunction
in vivo, complete knockout of NRMT1 via homologous recombination or CRISPR/Cas9 abolishes N-terminal trimethylation
malfunction
knockdown of NTMT1 results in hypersensitivity of breast cancer cell lines to doublestranded DNA breaks (DSBs) and increased proliferation of estrogen receptor positive breast cancer cells MCF-7 and LCC9
malfunction
knockdown of NTMT1 results in mitotic defects and sensitizes etoposide and gamma irradiation in breast cancer cell lines such as MCF-7 and LCC9
malfunction
loss of eEF1A trimethylation at Lys79 upon knockout of YGR001C
malfunction
mutation and deletion of PrmA causes no growth defects or any distinct phenotype in Escherichia coli
malfunction
mutation and deletion of PrmA causes no growth defects or any distinct phenotype in Thermus thermophilus
malfunction
the activity of the D577A mutant decreases the enzymatic activity by about half
malfunction
-
mutation and deletion of PrmA causes no growth defects or any distinct phenotype in Thermus thermophilus
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malfunction
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deletion of YBR261C in yeast abolishes N-terminal methylation, which consequently alters the ribosomal profile and leads to defects in both translational efficiency and fidelity. Overexpression of YBR261 validates its involvement in protein synthesis
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malfunction
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loss of eEF1A trimethylation at Lys79 upon knockout of YGR001C
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malfunction
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deletion of YLR285W results in the loss of N-terminal and lysine methylation in vivo, whereas overexpression of YLR285W results in an increase of methylation at these sites
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malfunction
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mutation and deletion of PrmA causes no growth defects or any distinct phenotype in Thermus thermophilus
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metabolism
protein alpha-N-terminal methylation is catalyzed by prokaryotic and eukaryotic protein N-terminal methyltransferases. The prevalent occurrence of this methylation in ribosomes, myosin, and histones implies its function in protein-protein interactions. Functions of methylated glycine, alanine, and serine, overview
metabolism
protein alpha-N-terminal methylation is catalyzed by prokaryotic and eukaryotic protein N-terminal methyltransferases. The prevalent occurrence of this methylation in ribosomes, myosin, and histones implies its function in protein-protein interactions. Functions of methylated glycine, alanine, and serine, overview
metabolism
protein alpha-N-terminal methylation is catalyzed by prokaryotic and eukaryotic protein N-terminal methyltransferases. The prevalent occurrence of this methylation in ribosomes, myosin, and histones implies its function in protein-protein interactions. Functions of methylated glycine, alanine, and serine, overview
metabolism
protein alpha-N-terminal methylation is catalyzed by prokaryotic and eukaryotic protein N-terminal methyltransferases. The prevalent occurrence of this methylation in ribosomes, myosin, and histones implies its function in protein-protein interactions. The alpha-N-terminal methylation has been reported on various N-terminal sequences in prokaryotic proteins. Functions of methylated glycine, alanine, and serine, overview
metabolism
protein alpha-N-terminal methylation is catalyzed by prokaryotic and eukaryotic protein N-terminal methyltransferases. The prevalent occurrence of this methylation in ribosomes, myosin, and histones implies its function in protein-protein interactions. The alpha-N-terminal methylation has been reported on various N-terminal sequences in prokaryotic proteins. Functions of methylated glycine, alanine, and serine, overview
metabolism
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protein alpha-N-terminal methylation is catalyzed by prokaryotic and eukaryotic protein N-terminal methyltransferases. The prevalent occurrence of this methylation in ribosomes, myosin, and histones implies its function in protein-protein interactions. The alpha-N-terminal methylation has been reported on various N-terminal sequences in prokaryotic proteins. Functions of methylated glycine, alanine, and serine, overview
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metabolism
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protein alpha-N-terminal methylation is catalyzed by prokaryotic and eukaryotic protein N-terminal methyltransferases. The prevalent occurrence of this methylation in ribosomes, myosin, and histones implies its function in protein-protein interactions. Functions of methylated glycine, alanine, and serine, overview
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metabolism
-
protein alpha-N-terminal methylation is catalyzed by prokaryotic and eukaryotic protein N-terminal methyltransferases. The prevalent occurrence of this methylation in ribosomes, myosin, and histones implies its function in protein-protein interactions. The alpha-N-terminal methylation has been reported on various N-terminal sequences in prokaryotic proteins. Functions of methylated glycine, alanine, and serine, overview
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physiological function
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importance of alpha-N-methylation for normal bipolar spindle formation and chromosome segregation. Function of the alpha-N-methylation is not solely to stabilize chromatin associations, but may have a more general role in the regulation of electrostatic interactions
physiological function
protein X-Pro-Lys N-terminal methylation reactions catalyzed by the enzyme may be widespread in nature
physiological function
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the N-terminal protein methyltransferase catalyzes the modification of two ribosomal protein substrates, Rpl12ab and Rps25a/Rps25b, the YBR261C/TAE1 product is necessary for the formation of the dimethylproline residue in each of these ribosomal proteins. Protein X-Pro-Lys N-terminal methylation reactions catalyzed by the enzyme may be widespread in nature
physiological function
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alpha-N-terminal methylation seems to regulate protein stability via N-end rule pathways or mediate proteinprotein interactions. The enzyme also mediates protein-DNA interactions between chromatin and regulator of chromatin condensation
physiological function
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enzyme NRMT1 acts as a tumor suppressor protein involved in multiple DNA repair pathways, role of N-terminal methylation in DNA repair. N-terminal methylation of DDB2 by NRMT1 is necessary for its recruitment to UV-induced DNA damage and proper execution of nucleotide excision repai. Additional NRMT1 targets, BRCA1 associated protein 1 (BAP1) and poly-ADP-ribosylase 3 (PARP3), are involved in DNA double strand break repair. BAP1 is a deubiquitinating enzyme recruited to DNA and required for appropriate assembly of homologous recombination factors during DSB. PARP3 poly-ADP-ribosylates proteins at DSBs and promotes NHEJ
physiological function
biological significances of NTMT1 in cell mitosis, chromatin segregation, and damaged DNA repair, along with its implications in cancer and aging
physiological function
dNTMT is mainly located in the nucleus, where the majority of chromatin-bound H2B is methylated. dNTMT recognizes the N-terminal sequence of Drosophila melanogaster H2B (PPKTSG), which conforms to the canonical X-P-K recognition motif for its mammalian orthologues (X=A, P, or S). dNTMT methylation is not processive since monomethylated Pro is accumulated during the methylation reaction. In addition, dART8, a PRMT for H3R2 methylation, negatively regulated H2B N-terminal methylation, thus suggesting crosstalk between methylation on two histone tails
physiological function
eukaryotic elongation factor 1A (eEF1A) is an essential, highly methylated protein that facilitates translational elongation by delivering aminoacyl-tRNAs to ribosomes. Eukaryotic protein N-terminal methyltransferase from Saccharomyces cerevisiae, YLR285W, methylates eEF1A at a previously undescribed high-stoichiometry N-terminal site and at the adjacent lysine
physiological function
METTL13/FEAT is implicated in tumorigenesis in vivo by suppressing apoptosis. METTL13/FEAT protein is also implied as a tumor suppressor in bladder carcinoma by negatively regulating cell proliferation, migration, and invasion in bladder cancer cells
physiological function
N-terminal methylation is a regulator of protein-DNA and protein-protein interactions for a number of proteins, such as RCC1, CENPA/B, DDB2, PARP3, an MYL9, playing important roles in cell mitotic progression, DNA damage repair, and regulation of protein function. N-terminal methyltransferase 1 (NTMT1) catalyzes the N-terminal methylation of proteins with a specific N-terminal motif after methionine removal. Obg-like ATPase 1 (OLA1) protein, a protein involved in many critical cellular functions, is methylated in vivo by NTMT1, NTMT1 is responsible for OLA1 methylation in vivo
physiological function
NRMT1 is a ubiquitously expressed distributive trimethylase
physiological function
NRMT1 is an N-terminal methyltransferase that methylates histone CENP-A as well as nonhistone substrates
physiological function
PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit
physiological function
PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit
physiological function
protein lysine/arginine methylation, the addition of a methyl group at the free alpha-N-termini of proteins represents a unique mode of post-translational modification. NTMT1 is an S-adenosyl-L-methionine (SAM)-dependent methyltransferase. During the enzymatic reaction, NTMT1 transfers a methyl group from SAM to the alpha-amino group of the protein substrates, resulting in the production of S-adenosyl-L-homocysteine (SAH) and alpha-N-methylated proteins. NTMT1 recognizes proteins bearing an N-terminal X-P-K/R consensus sequence, including RCC1, RB1, DDB2, CENP-A/B, PARP3, etc.
physiological function
protein N-terminal methyltransferase 1 (NTMT1) plays an important role in regulating mitosis and DNA repair
physiological function
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PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit
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physiological function
-
eukaryotic elongation factor 1A (eEF1A) is an essential, highly methylated protein that facilitates translational elongation by delivering aminoacyl-tRNAs to ribosomes. Eukaryotic protein N-terminal methyltransferase from Saccharomyces cerevisiae, YLR285W, methylates eEF1A at a previously undescribed high-stoichiometry N-terminal site and at the adjacent lysine
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physiological function
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PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit
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additional information
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both full-length and truncated forms of the enzyme catalyze methylation of the alpha-amine of the N-terminal methionine of the small subunit of Rubisco
additional information
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the enzyme contains two characteristic structural elements, a beta hairpin and an N-terminal extension, that contribute to its substrate specificity. Identification of key elements involved in locking the consensus substrate motif XPK (X indicates any residue type other than D/E) into the catalytic pocket for alpha-N-terminal methylation, NTMT1 prefers an XPK sequence motif, catalytic mechanism for alpha-N-terminal methylation and overall structure of the NTMT1 ternary complexes, verview
additional information
analysis of crystal structures of NRMT1 and NRMT2 (PDB IDs 2EX4 and 5UBB, determined to 1.75 and 2.0 A, respectively), homology modeling. Modeling of NRMT1 and NRMT2 heterotrimer, interaction analysis, overview
additional information
substrate and ligand binding structures of NTMT1 and NTMT2 (EC 2.1.1.299), overview
additional information
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substrate and ligand binding structures of NTMT1 and NTMT2 (EC 2.1.1.299), overview
additional information
substrate recognition and catalytic mechanisms, overview
additional information
substrate recognition and catalytic mechanisms, overview
additional information
substrate recognition and catalytic mechanisms, overview
additional information
substrate recognition and catalytic mechanisms, overview
additional information
substrate recognition and catalytic mechanisms, overview. Conformational changes are necessary for the recognition of multiple substrate sites
additional information
substrate recognition and catalytic mechanisms, overview. Efm7 substrate recognition may require the three-dimensional structure, which is different from the classic linear X-P-K/R motif recognition by other eukaryotic protein NTMTs
additional information
substrate recognition and catalytic mechanisms, overview. Efm7 substrate recognition may require the three-dimensional structure, which is different from the classic linear X-P-K/R motif recognition by other eukaryotic protein NTMTs
additional information
substrate recognition and catalytic mechanisms, overview. Ligand binding structures are analyzed. NTMT1-catalyzed methylation follows a random sequential Bi Bi mechanism, which involves the formation of a ternary complex with either substrate binding to NTMT1 first. Two highly conserved Asp180 and His140 act as general bases to facilitate deprotonation of the alpha-amino group of the N-terminus to attack SAM to transfer the methyl group
additional information
substrate recognition and catalytic mechanisms, overview. Ligand binding structures are analyzed. NTMT1-catalyzed methylation follows a random sequential Bi Bi mechanism, which involves the formation of a ternary complex with either substrate binding to NTMT1 first. Two highly conserved Asp180 and His140 act as general bases to facilitate deprotonation of the alpha-amino group of the N-terminus to attack SAM to transfer the methyl group
additional information
substrate recognition and catalytic mechanisms, overview. METTL13 has two distinct MTase domains: N- and C-terminal domains that appear to have different recognition preferences. The C-terminal domain of dual MTase METTL13 is responsible for the a-N-terminal methylation of eEF1A. The unique interaction of Asp577 with the alpha-amino group of Gly1 is required for enzymatic activity
additional information
substrate recognition and catalytic mechanisms, overview. METTL13 has two distinct MTase domains: N- and C-terminal domains that appear to have different recognition preferences. The C-terminal domain of dual MTase METTL13 is responsible for the a-N-terminal methylation of eEF1A. The unique interaction of Asp577 with the alpha-amino group of Gly1 is required for enzymatic activity
additional information
ternary structures of human NRMT1 bound to alpha-N-methylated peptides of human histone CENP-A or fruit fly histone H2B in the presence of SAH, NRMT1 adopts a core methyltransferase fold that resembles DOT1L and PRMT but not SET domain family histone methyltransferases, key substrate recognition and catalytic residues, NTMT1 structure-function analysis, overview. NRMT1 harbors a canonical SAM-dependent methyltransferase (SAM-MTase) core fold consisting of a seven-stranded beta-sheet (beta1-beta7) sandwiched by five flanking alpha-helices. Active site structure and catalytic mechanism analysis
additional information
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ternary structures of human NRMT1 bound to alpha-N-methylated peptides of human histone CENP-A or fruit fly histone H2B in the presence of SAH, NRMT1 adopts a core methyltransferase fold that resembles DOT1L and PRMT but not SET domain family histone methyltransferases, key substrate recognition and catalytic residues, NTMT1 structure-function analysis, overview. NRMT1 harbors a canonical SAM-dependent methyltransferase (SAM-MTase) core fold consisting of a seven-stranded beta-sheet (beta1-beta7) sandwiched by five flanking alpha-helices. Active site structure and catalytic mechanism analysis
additional information
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substrate recognition and catalytic mechanisms, overview
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additional information
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substrate recognition and catalytic mechanisms, overview
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additional information
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substrate recognition and catalytic mechanisms, overview. Efm7 substrate recognition may require the three-dimensional structure, which is different from the classic linear X-P-K/R motif recognition by other eukaryotic protein NTMTs
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additional information
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substrate recognition and catalytic mechanisms, overview
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Ying, Z.; Mulligan, R.; Janney, N.; Royer, M.; Houtz, R.
Related alphaN- and epsilonN-methyltransferases methylate the large and small subunits of Rubisco
Acta Biol. Hung.
49
173-184
1998
Spinacia oleracea
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Webb, K.J.; Lipson, R.S.; Al-Hadid, Q.; Whitelegge, J.P.; Clarke, S.G.
Identification of protein N-terminal methyltransferases in yeast and humans
Biochemistry
49
5225-5235
2010
Saccharomyces cerevisiae, Mus musculus, Homo sapiens (Q9BV86), Homo sapiens
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Chemogenetic analysis of human protein methyltransferases
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78
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Webb, K.; Laganowsky, A.; Whitelegge, J.; Clarke, S.
Identification of two SET domain proteins required for methylation of lysine residues in yeast ribosomal protein Rpl42ab
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Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
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NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein
Nature
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2010
Homo sapiens
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Structural basis for substrate recognition by the human N-terminal methyltransferase 1
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Homo sapiens
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Homo sapiens
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Loss of the N-terminal methyltransferase NRMT1 increases sensitivity to DNA damage and promotes mammary oncogenesis
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2015
Homo sapiens
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Design, synthesis, and kinetic analysis of potent protein N-terminal methyltransferase 1 inhibitors
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2015
Homo sapiens
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Jia, K.; Huang, G.; Wu, W.; Shrestha, R.; Wu, B.; Xiong, Y.; Li, P.
In vivo methylation of OLA1 revealed by activity-based target profiling of NTMT1
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2019
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Chemical biology of protein N-terminal methyltransferases
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20
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2019
Escherichia coli (P0A8T1), Saccharomyces cerevisiae (P38340), Saccharomyces cerevisiae (Q05874), Drosophila melanogaster (Q6NN40), Thermus thermophilus (Q84BQ9), Homo sapiens (Q8N6R0), Homo sapiens (Q9BV86), Thermus thermophilus DSM 579 (Q84BQ9), Saccharomyces cerevisiae ATCC 204508 (P38340), Saccharomyces cerevisiae ATCC 204508 (Q05874), Thermus thermophilus ATCC 27634 (Q84BQ9)
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An asparagine/glycine switch governs product specificity of human N-terminal methyltransferase NTMT2
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Molecular basis for histone N-terminal methylation by NRMT1
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2015
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Discovery of bisubstrate inhibitors for protein N-terminal methyltransferase 1
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Hamey, J.J.; Winter, D.L.; Yagoub, D.; Overall, C.M.; Hart-Smith, G.; Wilkins, M.R.
Novel N-terminal and lysine methyltransferases that target translation elongation factor 1A in yeast and human
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2016
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