Q9Y5N5 · N6MT1_HUMAN
- ProteinMethyltransferase N6AMT1
- GeneN6AMT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids214 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Methyltransferase that can methylate proteins and, to a lower extent, arsenic (PubMed:18539146, PubMed:21193388, PubMed:30017583, PubMed:31061526, PubMed:31636962).
Catalytic subunit of a heterodimer with TRMT112, which monomethylates 'Lys-12' of histone H4 (H4K12me1), a modification present at the promoters of numerous genes encoding cell cycle regulators (PubMed:31061526).
Catalytic subunit of a heterodimer with TRMT112, which catalyzes N5-methylation of Glu residue of proteins with a Gly-Gln-Xaa-Xaa-Xaa-Arg motif (PubMed:18539146, PubMed:31632689, PubMed:31636962).
Methylates ETF1 on 'Gln-185'; ETF1 needs to be complexed to ERF3 in its GTP-bound form to be efficiently methylated (PubMed:18539146, PubMed:20606008, PubMed:31061526, PubMed:31636962).
May also play a role in the modulation of arsenic-induced toxicity by mediating the conversion of monomethylarsonous acid 3+ into the less toxic dimethylarsonic acid (PubMed:21193388, PubMed:25997655).
It however only plays a limited role in arsenic metabolism compared with AS3MT (PubMed:25997655).
Catalytic subunit of a heterodimer with TRMT112, which monomethylates 'Lys-12' of histone H4 (H4K12me1), a modification present at the promoters of numerous genes encoding cell cycle regulators (PubMed:31061526).
Catalytic subunit of a heterodimer with TRMT112, which catalyzes N5-methylation of Glu residue of proteins with a Gly-Gln-Xaa-Xaa-Xaa-Arg motif (PubMed:18539146, PubMed:31632689, PubMed:31636962).
Methylates ETF1 on 'Gln-185'; ETF1 needs to be complexed to ERF3 in its GTP-bound form to be efficiently methylated (PubMed:18539146, PubMed:20606008, PubMed:31061526, PubMed:31636962).
May also play a role in the modulation of arsenic-induced toxicity by mediating the conversion of monomethylarsonous acid 3+ into the less toxic dimethylarsonic acid (PubMed:21193388, PubMed:25997655).
It however only plays a limited role in arsenic metabolism compared with AS3MT (PubMed:25997655).
Catalytic activity
- L-lysyl-[histone] + S-adenosyl-L-methionine = H+ + N6-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
- L-glutaminyl-[protein] + S-adenosyl-L-methionine = H+ + N5-methyl-L-glutaminyl-[protein] + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
- methylarsonous acid + S-adenosyl-L-methionine = dimethylarsinate + 2 H+ + S-adenosyl-L-homocysteine
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 29 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 29 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 51 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 51 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 53 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 53 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 77 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 77 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 103 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 103 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 104 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 104 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 122 | N6-methyl-L-lysine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 122 | S-adenosyl-L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 122 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | eRF1 methyltransferase complex | |
Cellular Component | nucleus | |
Cellular Component | protein-containing complex | |
Molecular Function | arsenite methyltransferase activity | |
Molecular Function | histone H4K12 methyltransferase activity | |
Molecular Function | nucleic acid binding | |
Molecular Function | protein methyltransferase activity | |
Molecular Function | protein-glutamine N-methyltransferase activity | |
Molecular Function | S-adenosyl-L-methionine binding | |
Molecular Function | S-adenosylmethionine-dependent methyltransferase activity | |
Molecular Function | site-specific DNA-methyltransferase (adenine-specific) activity | |
Biological Process | arsonoacetate metabolic process | |
Biological Process | methylation | |
Biological Process | negative regulation of gene expression, epigenetic | |
Biological Process | peptidyl-glutamine methylation | |
Biological Process | positive regulation of cell growth | |
Biological Process | toxin metabolic process | |
Biological Process | transcription initiation-coupled chromatin remodeling |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMethyltransferase N6AMT1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y5N5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 24 | Reduced protein N5-glutamine methyltransferase activity. | ||||
Sequence: E → K | ||||||
Mutagenesis | 27 | Abolished protein N5-glutamine methyltransferase activity. | ||||
Sequence: E → K | ||||||
Mutagenesis | 28 | Abolished protein N5-glutamine methyltransferase activity. | ||||
Sequence: D → N | ||||||
Natural variant | VAR_060445 | 34 | in dbSNP:rs1997607 | |||
Sequence: D → N | ||||||
Mutagenesis | 51 | Abolished protein N5-glutamine methyltransferase activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 72 | Strongly reduced protein N5-glutamine methyltransferase activity. | ||||
Sequence: L → D | ||||||
Mutagenesis | 77 | Abolished protein N5-glutamine methyltransferase activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 78 | Abolished protein N5-glutamine methyltransferase activity. | ||||
Sequence: I → A | ||||||
Mutagenesis | 83 | Strongly reduced protein N5-glutamine methyltransferase activity. | ||||
Sequence: A → D | ||||||
Mutagenesis | 103 | Abolished protein N5-glutamine methyltransferase activity. Abolished histone-lysine methyltransferase activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 108 | Strongly reduced protein N5-glutamine methyltransferase activity. | ||||
Sequence: L → D | ||||||
Mutagenesis | 122 | Abolished protein N5-glutamine methyltransferase activity. Abolished histone-lysine methyltransferase activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 122-125 | Abolished DNA methyltransferase activity. | ||||
Sequence: NPPY → AAAA | ||||||
Mutagenesis | 125 | Abolished protein N5-glutamine methyltransferase activity without affecting histone-lysine methyltransferase activity. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 132 | Abolished protein N5-glutamine methyltransferase activity. | ||||
Sequence: E → K | ||||||
Mutagenesis | 139 | Reduced protein N5-glutamine methyltransferase activity. | ||||
Sequence: E → K | ||||||
Natural variant | VAR_060446 | 146 | in dbSNP:rs2205447 | |||
Sequence: R → K | ||||||
Mutagenesis | 154 | Slightly reduced protein N5-glutamine methyltransferase activity. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_060447 | 166 | in dbSNP:rs2205446 | |||
Sequence: R → K | ||||||
Mutagenesis | 176 | Abolished protein N5-glutamine methyltransferase activity. | ||||
Sequence: E → K | ||||||
Mutagenesis | 204 | Abolished protein N5-glutamine methyltransferase activity. | ||||
Sequence: E → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 333 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000088049 | 1-214 | Methyltransferase N6AMT1 | |||
Sequence: MAGENFATPFHGHVGRGAFSDVYEPAEDTFLLLDALEAAAAELAGVEICLEVGSGSGVVSAFLASMIGPQALYMCTDINPEAAACTLETARCNKVHIQPVITDLVKGLLPRLTEKVDLLVFNPPYVVTPPQEVGSHGIEAAWAGGRNGREVMDRFFPLVPDLLSPRGLFYLVTIKENNPEEILKIMKTKGLQGTTALSRQAGQETLSVLKFTKS |
Post-translational modification
Isoform 1
Ubiquitinated, leading to its degradation by the proteasome.
Isoform 2
Ubiquitinated, leading to its degradation by the proteasome.
Keywords
- PTM
Proteomic databases
Interaction
Subunit
Heterodimer; heterodimerization with TRMT112 is required for S-adenosyl-L-methionine-binding.
Isoform 2
Does not interact with TRMT112.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y5N5 | TRMT112 Q9UI30 | 7 | EBI-7966667, EBI-373326 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9Y5N5-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsAlpha, N6AMT1iso1
- Length214
- Mass (Da)22,957
- Last updated2017-09-27 v4
- Checksum65512C91DC85ADDB
Q9Y5N5-2
- Name2
- SynonymsBeta, N6AMT1iso2
- Differences from canonical
- 105-132: Missing
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_040294 | 105-132 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF139682 EMBL· GenBank· DDBJ | AAD38520.1 EMBL· GenBank· DDBJ | mRNA | ||
AK314100 EMBL· GenBank· DDBJ | BAG36794.1 EMBL· GenBank· DDBJ | mRNA | ||
AF227510 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL163248 EMBL· GenBank· DDBJ | CAB90428.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AMYH02037685 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF570251 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF457188 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KC877845 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471079 EMBL· GenBank· DDBJ | EAX09939.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09940.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09941.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC011554 EMBL· GenBank· DDBJ | AAH11554.1 EMBL· GenBank· DDBJ | mRNA |