Q8WVM0 · TFB1M_HUMAN
- ProteinDimethyladenosine transferase 1, mitochondrial
- GeneTFB1M
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids346 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Mitochondrial methyltransferase which uses S-adenosyl methionine to dimethylate two highly conserved adjacent adenosine residues (A1583 and A1584) within the loop of helix 45 at the 3-prime end of 12S rRNA, thereby regulating the assembly or stability of the small subunit of the mitochondrial ribosome (PubMed:12496758, PubMed:25305075, PubMed:31251801).
Also required for basal transcription of mitochondrial DNA, probably via its interaction with POLRMT and TFAM. Stimulates transcription independently of the methyltransferase activity (PubMed:11809803, PubMed:12068295, PubMed:12897151).
Also required for basal transcription of mitochondrial DNA, probably via its interaction with POLRMT and TFAM. Stimulates transcription independently of the methyltransferase activity (PubMed:11809803, PubMed:12068295, PubMed:12897151).
Miscellaneous
It has been proposed that variations in TFB1M may influence the clinical expression of aminoglycoside-induced deafness caused by the A1555G mutation in the mitochondrial 12S rRNA (PubMed:15110318).
However, this was later questioned as patients with the A1555G mutation had similar 12S rRNA methylation levels to controls (PubMed:25305075).
However, this was later questioned as patients with the A1555G mutation had similar 12S rRNA methylation levels to controls (PubMed:25305075).
Catalytic activity
- adenosine(N)/adenosine(N+1) in rRNA + 4 S-adenosyl-L-methionine = 4 H+ + N6-dimethyladenosine(N)/N6-dimethyladenosine(N+1) in rRNA + 4 S-adenosyl-L-homocysteine
RHEA-COMP:19105 CHEBI:74411 Position: NCHEBI:74411 Position: N+1+ 4 CHEBI:59789 = 4 CHEBI:15378 + RHEA-COMP:19106 CHEBI:74493 Position: NCHEBI:74493 Position: N+1+ 4 CHEBI:57856
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 38 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 63 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 85 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 86 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 111 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 112 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 141 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrial nucleoid | |
Molecular Function | DNA binding | |
Molecular Function | mitochondrial transcription factor activity | |
Molecular Function | RNA binding | |
Molecular Function | rRNA (adenine-N6,N6-)-dimethyltransferase activity | |
Molecular Function | S-adenosyl-L-methionine binding | |
Biological Process | rRNA methylation | |
Biological Process | rRNA modification | |
Biological Process | transcription initiation at mitochondrial promoter |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDimethyladenosine transferase 1, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8WVM0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 65 | Abolishes methyltransferase activity, DNA-binding and SAM-binding. Does not abolish transcription activator function. | ||||
Sequence: G → A | ||||||
Mutagenesis | 85 | Inhibits rRNA (adenine-N6,N6-)-dimethyltransferase activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 86 | Inhibits rRNA (adenine-N6,N6-)-dimethyltransferase activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 111 | Inhibits rRNA (adenine-N6,N6-)-dimethyltransferase activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 112 | Inhibits rRNA (adenine-N6,N6-)-dimethyltransferase activity. | ||||
Sequence: V → A | ||||||
Natural variant | VAR_071246 | 120 | in dbSNP:rs144355958 | |||
Sequence: A → P | ||||||
Mutagenesis | 141 | Does not affect SAM-binding, DNA-binding nor transcription activator function. | ||||
Sequence: N → A | ||||||
Mutagenesis | 183 | Abolishes the interaction between 12S helix 45 and TFB1M; when associated with E-256 and E-257. | ||||
Sequence: R → E | ||||||
Natural variant | VAR_071247 | 211 | in dbSNP:rs769497533 | |||
Sequence: T → A | ||||||
Mutagenesis | 220 | Abolishes methyltransferase activity. Does not affect SAM-binding, DNA-binding nor transcription activator function. | ||||
Sequence: K → A | ||||||
Natural variant | VAR_071248 | 256 | in dbSNP:rs73579353 | |||
Sequence: R → Q | ||||||
Mutagenesis | 256 | Abolishes the interaction between 12S helix 45 and TFB1M; when associated with E-183 and E-257. | ||||
Sequence: R → E | ||||||
Mutagenesis | 257 | Abolishes the interaction between 12S helix 45 and TFB1M; when associated with E-183 and E-256. | ||||
Sequence: R → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 416 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 transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-27 | Mitochondrion | ||||
Sequence: MAASGKLSTCRLPPLPTIREIIKLLRL | ||||||
Chain | PRO_0000273171 | 28-346 | Dimethyladenosine transferase 1, mitochondrial | |||
Sequence: QAAKQLSQNFLLDLRLTDKIVRKAGNLTNAYVYEVGPGPGGITRSILNADVAELLVVEKDTRFIPGLQMLSDAAPGKLRIVHGDVLTFKVEKAFSESLKRPWEDDPPNVHIIGNLPFSVSTPLIIKWLENISCRDGPFVYGRTQMTLTFQKEVAERLAANTGSKQRSRLSVMAQYLCNVRHIFTIPGQAFVPKPEVDVGVVHFTPLIQPKIEQPFKLVEKVVQNVFQFRRKYCHRGLRMLFPEAQRLESTGRLLELADIDPTLRPRQLSISHFKSLCDVYRKMCDEDPQLFAYNFREELKRRKSKNEEKEEDDAENYRL |
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitously expressed.
Induction
By the nuclear respiratory factors NRF1 and NRF2/GABPB2 and PGC-1 coactivators.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with mitochondrial RNA polymerase POLRMT. Interacts with TFAM (PubMed:12068295, PubMed:12897151).
Bound to the maturing mtSSU until the late stages of assembly (By similarity).
Bound to the maturing mtSSU until the late stages of assembly (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8WVM0 | TFAM Q00059 | 2 | EBI-2615570, EBI-1049924 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Sequence similarities
Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. KsgA subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length346
- Mass (Da)39,543
- Last updated2002-03-01 v1
- Checksum4C34F4FD72B01286
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 31-32 | in Ref. 1; AAD34070 | ||||
Sequence: KQ → NE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF151833 EMBL· GenBank· DDBJ | AAD34070.1 EMBL· GenBank· DDBJ | mRNA | ||
AL139101 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC005183 EMBL· GenBank· DDBJ | AAH05183.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC017788 EMBL· GenBank· DDBJ | AAH17788.1 EMBL· GenBank· DDBJ | mRNA |