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Information on EC 2.1.1.299 - protein N-terminal monomethyltransferase
for references in articles please use BRENDA:EC2.1.1.299
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.299 protein N-terminal monomethyltransferase
IUBMB Comments
This enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. In contrast to EC 2.1.1.244, protein N-terminal methyltransferase, the protein only adds one methyl group to the N-terminal.
The enzyme appears in viruses and cellular organisms
- 2.1.1.299
- methyltransferases
-
trimethylation
-
monomethylated
-
trimethylase
-
priming
Reaction Schemes
show+
=
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N-terminal-(A,P,S)PK-[protein]
=
+
N-terminal-N-methyl-N-(A,P,S)PK-[protein]
Synonyms
nrmt2, ntmt2, mettl11b, n-terminal monomethylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
METTL11B
N-terminal monomethylase
NRMT2
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:N-terminal-(A,P,S)PK-[protein] monomethyltransferase
This enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. In contrast to EC 2.1.1.244, protein N-terminal methyltransferase, the protein only adds one methyl group to the N-terminal.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + PPKRIA
2 S-adenosyl-L-homocysteine + ?
Substrates: mono- and dimethylation by NTMT2
Products: -
Products: -
?
3 S-adenosyl-L-methionine + GPKRIA
3 S-adenosyl-L-homocysteine + ?
Substrates: mono-, di-, and trimethylation by NTMT2
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + APKRIA
S-adenosyl-L-homocysteine + ?
Substrates: monomethylation by NTMT2
Products: -
Products: -
?
S-adenosyl-L-methionine + CPKRIA
S-adenosyl-L-homocysteine + ?
Substrates: monomethylation by NTMT2
Products: -
Products: -
?
S-adenosyl-L-methionine + FPKRIA
S-adenosyl-L-homocysteine + ?
Substrates: monomethylation by NTMT2
Products: -
Products: -
?
S-adenosyl-L-methionine + HPKRIA
S-adenosyl-L-homocysteine + ?
Substrates: monomethylation by NTMT2
Products: -
Products: -
?
S-adenosyl-L-methionine + KPKRIA
S-adenosyl-L-homocysteine + ?
Substrates: monomethylation by NTMT2, very low activity
Products: -
Products: -
?
S-adenosyl-L-methionine + LPKRIA
S-adenosyl-L-homocysteine + ?
Substrates: monomethylation by NTMT2, very low activity
Products: -
Products: -
?
S-adenosyl-L-methionine + MPKRIA
S-adenosyl-L-homocysteine + ?
Substrates: monomethylation by NTMT2
Products: -
Products: -
?
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]
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-terminal-Ala-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-Ala-Pro-Lys-[protein]
S-adenosyl-L-methionine + N-terminal-Pro-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-Pro-Pro-Lys-[protein]
S-adenosyl-L-methionine + N-terminal-Ser-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-Ser-Pro-Lys-[protein]
S-adenosyl-L-methionine + RCC1
S-adenosyl-L-homocysteine + ?
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + RPKRIA
S-adenosyl-L-homocysteine + ?
Substrates: monomethylation by NTMT2
Products: -
Products: -
?
S-adenosyl-L-methionine + SPKRIA
S-adenosyl-L-homocysteine + ?
Substrates: binding structure of SAM/SAH and of the substrate peptide, overview. SPKRIA peptide is derived from N-terminus of RCC1 protein. NTMT2, unlike NTMT1 (EC 2.1.1.244), fails to di-/tri-methylate SPKRIA
Products: -
Products: -
?
S-adenosyl-L-methionine + SPKRIAKRRSPPADA
?
Substrates: substrate peptide consisting of the first 15 amino acids of RCC1
Products: -
Products: -
?
S-adenosyl-L-methionine + WPKRIA
S-adenosyl-L-homocysteine + ?
Substrates: monomethylation by NTMT2
Products: -
Products: -
?
S-adenosyl-L-methionine + YPKRIA
S-adenosyl-L-homocysteine + ?
Substrates: monomethylation by NTMT2
Products: -
Products: -
?
S-adenosyl-L-methionine + N-terminal-Ala-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-Ala-Pro-Lys-[protein]
Substrates: the enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. In contrast to EC 2.1.1.244, protein N-terminal methyltransferase, the protein only adds one methyl group to the N-terminal
Products: -
Products: -
?
S-adenosyl-L-methionine + N-terminal-Ala-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-Ala-Pro-Lys-[protein]
-
Substrates: the enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. In contrast to EC 2.1.1.244, protein N-terminal methyltransferase, the protein only adds one methyl group to the N-terminal
Products: -
Products: -
?
S-adenosyl-L-methionine + N-terminal-Pro-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-Pro-Pro-Lys-[protein]
Substrates: the enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. In contrast to EC 2.1.1.244, protein N-terminal methyltransferase, the protein only adds one methyl group to the N-terminal
Products: -
Products: -
?
S-adenosyl-L-methionine + N-terminal-Pro-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-Pro-Pro-Lys-[protein]
-
Substrates: the enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. In contrast to EC 2.1.1.244, protein N-terminal methyltransferase, the protein only adds one methyl group to the N-terminal
Products: -
Products: -
?
S-adenosyl-L-methionine + N-terminal-Ser-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-Ser-Pro-Lys-[protein]
Substrates: the enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. In contrast to EC 2.1.1.244, protein N-terminal methyltransferase, the protein only adds one methyl group to the N-terminal
Products: -
Products: -
?
S-adenosyl-L-methionine + N-terminal-Ser-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-Ser-Pro-Lys-[protein]
-
Substrates: the enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. In contrast to EC 2.1.1.244, protein N-terminal methyltransferase, the protein only adds one methyl group to the N-terminal
Products: -
Products: -
?
additional information
?
-
Substrates: NRMT2 exhibits monomethylase activity in vitro. Isozymes NRMT1 and NRMT2 can interact both in vitro and in vivo, modeling of NRMT1 and NRMT2 interactions. No activity with the MYL9 peptide SSKRAKAKTTKKRP
Products: -
Products: -
?
additional information
?
-
Substrates: NTMT2 is a mono-methyltransferase, substrate specificity, overview. But NTMT2 is also able to di-/tri-methylate the GPKRIA peptide and di-methylate the PPKRIA peptide, otherwise it is predominantly a mono-methyltransferase. The residue N89 of NTMT2 serves as a gatekeeper residue that regulates the binding of unmethylated versus mono-methylated substrate peptide.The substrate peptide is deeply inserted into the binding pocket through hydrophilic and hydrophobic interactions, and the alpha-amine of the first residue (S1) points towards the sulfur atom of SAH. In the NTMT2 complex, S1 fits snugly into the channel, where the main-chain O atom is anchored by N223 in NTMT2 (N168 in NTMT1, EC 2.1.1.244) through hydrogen bonding. No activity with peptides TPKRIA, VPKRIA, IPKRIA, DPKRIA, EPKRIA, NPKRIA, and QPKRIA
Products: -
Products: -
?
additional information
?
-
-
Substrates: NTMT2 is a mono-methyltransferase, substrate specificity, overview. But NTMT2 is also able to di-/tri-methylate the GPKRIA peptide and di-methylate the PPKRIA peptide, otherwise it is predominantly a mono-methyltransferase. The residue N89 of NTMT2 serves as a gatekeeper residue that regulates the binding of unmethylated versus mono-methylated substrate peptide.The substrate peptide is deeply inserted into the binding pocket through hydrophilic and hydrophobic interactions, and the alpha-amine of the first residue (S1) points towards the sulfur atom of SAH. In the NTMT2 complex, S1 fits snugly into the channel, where the main-chain O atom is anchored by N223 in NTMT2 (N168 in NTMT1, EC 2.1.1.244) through hydrogen bonding. No activity with peptides TPKRIA, VPKRIA, IPKRIA, DPKRIA, EPKRIA, NPKRIA, and QPKRIA
Products: -
Products: -
?
additional information
?
-
Substrates: the substrate recognition motif is X-P-K/R. Although NTMT2 is proposed to be a monomethylase, it can also fully methylate both GPKRIA and PPKRIA peptides, but to a low level. NTMT2 is able to methylate hexamer peptides
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is responsible for the monomethylation of protein N-termini
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
Substrates: -
Products: -
Products: -
?
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]
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-terminal-Ala-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-Ala-Pro-Lys-[protein]
S-adenosyl-L-methionine + N-terminal-Pro-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-Pro-Pro-Lys-[protein]
S-adenosyl-L-methionine + N-terminal-Ser-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-Ser-Pro-Lys-[protein]
additional information
?
-
-
Substrates: the enzyme is responsible for the monomethylation of protein N-termini
Products: -
Products: -
-
S-adenosyl-L-methionine + N-terminal-Ala-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-Ala-Pro-Lys-[protein]
Substrates: the enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. In contrast to EC 2.1.1.244, protein N-terminal methyltransferase, the protein only adds one methyl group to the N-terminal
Products: -
Products: -
?
S-adenosyl-L-methionine + N-terminal-Ala-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-Ala-Pro-Lys-[protein]
-
Substrates: the enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. In contrast to EC 2.1.1.244, protein N-terminal methyltransferase, the protein only adds one methyl group to the N-terminal
Products: -
Products: -
?
S-adenosyl-L-methionine + N-terminal-Pro-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-Pro-Pro-Lys-[protein]
Substrates: the enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. In contrast to EC 2.1.1.244, protein N-terminal methyltransferase, the protein only adds one methyl group to the N-terminal
Products: -
Products: -
?
S-adenosyl-L-methionine + N-terminal-Pro-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-Pro-Pro-Lys-[protein]
-
Substrates: the enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. In contrast to EC 2.1.1.244, protein N-terminal methyltransferase, the protein only adds one methyl group to the N-terminal
Products: -
Products: -
?
S-adenosyl-L-methionine + N-terminal-Ser-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-Ser-Pro-Lys-[protein]
Substrates: the enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. In contrast to EC 2.1.1.244, protein N-terminal methyltransferase, the protein only adds one methyl group to the N-terminal
Products: -
Products: -
?
S-adenosyl-L-methionine + N-terminal-Ser-Pro-Lys-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-Ser-Pro-Lys-[protein]
-
Substrates: the enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. In contrast to EC 2.1.1.244, protein N-terminal methyltransferase, the protein only adds one methyl group to the N-terminal
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
dependent on, binding structure of SAM/SAH, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
not inhibited by bisubstrates composed of (2S)-2-amino-4-({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl}amino)butanoic acid and the peptide GPKRIA linked by a 4-C, 3-C, 4-C or 5-C atom linker
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0556
SPKRIAKRRSPPADA
recombinant NRMT2, pH and temperature not specified in the publication
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
NRMT2 mRNA is enriched in the liver and in the skeletal muscle. Expressed at fairly low levels in all tissues examined
brenda
additional information
-
NRMT2 mRNA is enriched in the liver and in the skeletal muscle. Expressed at fairly low levels in all tissues examined
brenda
additional information
NRMT2 is a monomethylase expressed at low levels in a tissue-specific manner
brenda
additional information
NTMT2 is predominantly expressed in heart and skeletal muscle tissues
brenda
additional information
-
the enzyme is expressed in all major tissues at moderate levels
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
when expressed in HeLa cells the enzyme is enriched in the nuclear compartment
brenda
-
when expressed in HeLa cells the enzyme is enriched in the nuclear compartment
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
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
physiological function
additional information
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
structural comparison of isozymes NTMT1 and NTMT2, structural alignment of NTMT1 (PDB ID 5E1B) and NTMT2, overview. NTMT1 and NTMT2 employ a similar substrate recognition mode. NTMT2 is a SAM-dependent class I methyltransferase
malfunction
the N209I endometrial and P211S lung cancer mutants decrease the trimethylation level of RCC1, whereas the Q144H lung cancer mutant increases the trimethylation level of RCC1 with minimal levels of mono- and dimethylated RCC1. For NTMT2, the V224L breast cancer mutant shows marginal methylation activity for methylation states. Those data infer that methylation levels may play different roles in different cancers
physiological function
isozyme NRMT2 expression activates isozyme NRMT1 activity, not through priming, but by increasing its stability and substrate affinity. NRMT2 overexpression cannot rescue NRMT1 knockout phenotypes
physiological function
protein methylation participates in regulation of a broad spectrum of cellular processes. Besides the extensively studied 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
physiological function
the METTL11A dimer can bind the enzyme monomer, which increases the half-life and methylation activity of METTL11A against non-canonical substrates. The enzyme plays the role of a non-catalytic stabilizing protein for METTL11A
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 (EC 2.1.1.244) and NTMT2, and proposed catalytic mechanism of NTMT2, overview
additional information
-
substrate and ligand binding structures of NTMT1 (EC 2.1.1.244) and NTMT2, and proposed catalytic mechanism of NTMT2, overview
additional information
substrate recognition and catalytic mechanisms, overview
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NTM1B_DANRE
278
0
32383
Swiss-Prot
other Location (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
monomer
1 * 35700, recombinant isozyme NRMT2, SDS-PAGE and analytical ultracentrifugation
additional information
enzyme NRMT1 primarily exists as a monomer. Isozymes NRMT1 and NRMT2, when co-expressed, form a heterotrimer, interaction analysis, overview
additional information
based on the folding pattern, NTMT2 is a SAM-dependent class I methyltransferase, which consists of a central seven-stranded beta-sheet (beta1-beta5 and beta8-beta9), flanked by three alpha-helices (alpha3-alpha5) and two alpha-helices (alpha6-alpha7) on each side, respectively. In addition, NTMT2 contains two auxiliary regions: an N-terminal alpha-lid (nu1, alpha1-alpha2), and a beta-lid (beta6-beta7) inserted between beta5 and alpha8. These two lids cover the core domain that contributes to the substrate recognition
additional information
-
based on the folding pattern, NTMT2 is a SAM-dependent class I methyltransferase, which consists of a central seven-stranded beta-sheet (beta1-beta5 and beta8-beta9), flanked by three alpha-helices (alpha3-alpha5) and two alpha-helices (alpha6-alpha7) on each side, respectively. In addition, NTMT2 contains two auxiliary regions: an N-terminal alpha-lid (nu1, alpha1-alpha2), and a beta-lid (beta6-beta7) inserted between beta5 and alpha8. These two lids cover the core domain that contributes to the substrate recognition
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of crystal structures of NRMT1 and NRMT2 (PDB IDs 2EX4 and 5UBB, determined to 1.75 and 2.0 A, respectively), homology modeling
purified recombinant NTMT2 in binary complex with S-adenosyl-L-methionine and in ternary complex with S-adenosyl-L-homocysteine and unmethylated substrate peptide SPKRIA, X-ray diffraction structure determination and analysis at 1.20-2.0 A resolution. A methylated alpha-amino group in the N-terminus of the peptide is traced in the crystal structure
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N89G
site-directed mutagenesis, the mutant shows profoundly altered catalytic activities and product specificities
additional information
co-expression of NRMT2 with NRMT1 increases the trimethylation rate of NRMT1. Generation of truncation constructs of NRMT2
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene NTMT2, recombinant expression of His-tagged NRMT2 in Escherichia coli and of wild-type and mutant FLAG-tagged NRMT2s in HEK-293 cells, recombinant expression of GFP-tagged enzyme in HCT-116 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme mRNA is upregulated during myogenic and also osteoblastogenic and osteocytic differentiation
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
high enzyme expression correlates with worse prognosis in colon cancer
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Petkowski, J.J.; Bonsignore, L.A.; Tooley, J.G.; Wilkey, D.W.; Merchant, M.L.; Macara, I.G.; Schaner Tooley, C.E.
NRMT2 is an N-terminal monomethylase that primes for its homologue NRMT1
Biochem. J.
456
453-462
2013
Homo sapiens (Q5VVY1), Homo sapiens, Mus musculus
brenda
Huang, R.
Chemical biology of protein N-terminal methyltransferases
ChemBioChem
20
976-984
2019
Homo sapiens (Q5VVY1)
brenda
Dong, C.; Dong, G.; Li, L.; Zhu, L.; Tempel, W.; Liu, Y.; Huang, R.; Min, J.
An asparagine/glycine switch governs product specificity of human N-terminal methyltransferase NTMT2
Commun. Biol.
1
183
2018
Homo sapiens (Q5VVY1), Homo sapiens
brenda
Faughn, J.D.; Dean, W.L.; Schaner Tooley, C.E.
The N-terminal methyltransferase homologs NRMT1 and NRMT2 exhibit novel regulation of activity through heterotrimer formation
Protein Sci.
27
1585-1599
2018
Homo sapiens (Q5VVY1)
brenda
Conner, M.M.; Schaner Tooley, C.E.
Three's a crowd - why did three N-terminal methyltransferases evolve for one job?
J. Cell Sci.
136
jcs260424
2023
Homo sapiens (Q5VVY1)
brenda
Chen, D.; Dong, C.; Dong, G.; Srinivasan, K.; Min, J.; Noinaj, N.; Huang, R.
Probing the plasticity in the active site of protein N-terminal methyltransferase 1 using bisubstrate analogues
J. Med. Chem.
63
8419-8431
2020
Homo sapiens (Q5VVY1)
brenda
Hoernstein, S.N.W.; Schlosser, A.; Fiedler, K.; van Gessel, N.; Igloi, G.L.; Lang, D.; Reski, R.
A snapshot of the Physcomitrella N-terminome reveals N-terminal methylation of organellar proteins
Plant Cell Rep.
43
250
2024
Physcomitrium patens
brenda
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