2.1.1.244: protein N-terminal methyltransferase
This is an abbreviated version!
For detailed information about protein N-terminal methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.244
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2.1.1.244
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methyltransferases
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rna-dependent
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mtase
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trimethylation
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dengue
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flavivirus
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bisubstrate
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methyltransferase-like
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drug development
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pharmacology
- 2.1.1.244
- methyltransferases
-
rna-dependent
- mtase
-
trimethylation
- dengue
- flavivirus
-
bisubstrate
-
methyltransferase-like
- drug development
- pharmacology
Reaction
2 S-adenosyl-L-methionine
+
Synonyms
alpha-N-methyltransferase, alpha-N-terminal methyltransferase 1, alphaN-methyltransferase, CG1675, dNTMT, EEF1A lysine methyltransferase 1, eEF1A-KMT1, EEF1AKMT1, Efm5, Efm7, elongation factor methyltransferase 7, FEAT, METT11B, METTL11A, METTL11a/C9orf32/Ad-003, METTL13, METTL13/FEAT, N-terminal and lysine methyltransferase, N-terminal methyltransferase, N-terminal methyltransferase 1, N-terminal RCC1 methyltransferase, N-terminal RCC1 methyltransferase 1, N-terminal Xaa-Pro-Lys N-methyltransferase 1, N6AMT2, NMT1, NNT1, NRMT, NRMT1, Ntm1, NTMT1, peptide N-terminal methyltransferase, PrmA, protein methyltransferase, protein N-terminal methyltransferase 1, Rkm2, SS alphaN-methyltransferase, SSMT, TAE1, YBR261C, YBR261C/Tae1, YGR001C, YLR285W
ECTree
2.1.1.244 protein N-terminal methyltransferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.1.1.244 - protein N-terminal methyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D178A/D181A
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site-directed mutagenesis, mutating the residues Asp178 and Asp181 at the lip of the active site to Ala decreases enzyme activity, which is further decreased by reverse-charge mutagenesis to Lys
D180N
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
D212N
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
E213A
site-directed mutagenesis, the mutant shows 15% reduced activity compared to wild-type
H140A
the mutant loses the catalytic activity, but retains binding affinity to the peptide substrate
N168A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
N168K
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S183K
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W136L
site-directed mutagenesis, the mutant shows 92% reduced activity compared to wild-type
Y19A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Y19F
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Y215A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
Y215I
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
additional information
additional information
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depleting NRMT in 293LT cells, using lentivirus, significantly decreases methylation of endogenous RCC1, while not affecting overall RCC1 level, depleting NRMT in HeLa cells using short interfering RNAs causing the same effects, RCC1 methylation is rescued by expression of murine NRMT-FLAG, which is not targeted by the human shRNA
additional information
generation of NTMT1 knockout HEK-293FT cells by CRISPR-Cas9
additional information
NRMT1 co-expression with NRMT2 increases the trimethylation rate of NRMT1. Generation of truncation constructs of NRMT1. Full-length FLAG-tagged NRMT1 only weakly interacts with the first 112 aa of NRMT2, though strongly interacts with a GFP-tagged NRMT2 fragment (amino acids 77-223) that is missing the 59 aa tail that is also lacking from the crystal structure and subsequent model. Full-length FLAG-tagged NRMT2 strongly interacts with the first 59 aa of NRMT1, as well as, amino acids 52-172. There is a decreased interaction of FLAG-tagged NRMT2-FLAG with the C-terminal fragment of NRMT1 (amino acids 178-223). Generation of NRMT1 knockout mutant, NRMT2 overexpression cannot rescue NRMT1 knockout phenotypes
additional information
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the intact dimethylated Rpl12ab species isolated from the YBR261C/tae1 deletion strain is fragmented, and a b20 ion is detected with the addition of one methyl group, suggesting partial methylation of lysine 3. Neither of these species is dimethylated at the N-terminal residue. Rps25a/Rps25b isolated from the YBR261C/tae1 deletion strain is 28 Da less than the wild type, and the fragmentation data indicate no methylation is present
