Q9H8H3 · TMT1A_HUMAN
- ProteinThiol S-methyltransferase TMT1A
- GeneTMT1A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids244 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Thiol S-methyltransferase that catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to alkyl and phenolic thiol-containing acceptor substrates. Together with TMT1B accounts for most of S-thiol methylation activity in the endoplasmic reticulum of hepatocytes (PubMed:37137720).
Able to methylate the N6 position of adenosine residues in long non-coding RNAs (lncRNAs). May facilitate lncRNAs transfer into exosomes at the tumor-stroma interface (PubMed:34980213).
Promotes osteogenic and odontogenic differentiation by regulating the expression of genes involved in stem cell differentiation and survival (PubMed:34226523, PubMed:34790668).
Targeted from the endoplasmic reticulum to lipid droplets, where it recruits cellular proteins to form functional organelles (PubMed:19773358).
Able to methylate the N6 position of adenosine residues in long non-coding RNAs (lncRNAs). May facilitate lncRNAs transfer into exosomes at the tumor-stroma interface (PubMed:34980213).
Promotes osteogenic and odontogenic differentiation by regulating the expression of genes involved in stem cell differentiation and survival (PubMed:34226523, PubMed:34790668).
Targeted from the endoplasmic reticulum to lipid droplets, where it recruits cellular proteins to form functional organelles (PubMed:19773358).
(Microbial infection) May be involved in the assembly and release stages of hepatitis C virus (HCV) life cycle and thus play a crucial role in HCV propagation.
Miscellaneous
Selectively methylates drugs containing thiol-moieties such as 7alpha-thiospironolactone and mertansine.
Catalytic activity
- a thiol + S-adenosyl-L-methionine = a methyl thioether + H+ + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
Activity regulation
Inhibited by 2,3-dichloro-alpha-methylbenzylamine (DCMB).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
53.73 μM | S-adenosyl-L-methionine | |||||
39.41 μM | 7alpha-thiospironolactone |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | extracellular region | |
Cellular Component | lipid droplet | |
Cellular Component | membrane | |
Cellular Component | tertiary granule lumen | |
Molecular Function | methyltransferase activity | |
Molecular Function | mRNA m(6)A methyltransferase activity | |
Molecular Function | RNA methyltransferase activity | |
Molecular Function | thiol S-methyltransferase activity | |
Biological Process | lncRNA processing | |
Biological Process | methylation | |
Biological Process | odontogenesis | |
Biological Process | osteoblast differentiation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Alkyl and phenolic thiol methyltransferase.
Names & Taxonomy
Protein names
- Recommended nameThiol S-methyltransferase TMT1A
- EC number
- Alternative names
Gene names
- Community suggested namesThiol methyltransferase 1A.
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H8H3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Inserted in the ER membrane and migrates from the inserted site to lipid droplet.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_050296 | 134 | in dbSNP:rs28372674 | |||
Sequence: A → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 325 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 signal, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-29 | UniProt | |||||
Sequence: MELTIFILRLAIYILTFPLYLLNFLGLWS | |||||||
Chain | PRO_0000251921 | 30-244 | UniProt | Thiol S-methyltransferase TMT1A | |||
Sequence: WICKKWFPYFLVRFTVIYNEQMASKKRELFSNLQEFAGPSGKLSLLEVGCGTGANFKFYPPGCRVTCIDPNPNFEKFLIKSIAENRHLQFERFVVAAGENMHQVADGSVDVVVCTLVLCSVKNQERILREVCRVLRPGGAFYFMEHVAAECSTWNYFWQQVLDPAWHLLFDGCNLTRESWKALERASFSKLKLQHIQAPLSWELVRPHIYGYAVK | |||||||
Modified residue (large scale data) | 69 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Methylated at lysine residues most likely by EZH2.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the liver.
Induction
Silenced by miR-6807-5p.
Gene expression databases
Organism-specific databases
Interaction
Subunit
(Microbial infection) Interacts with HCV non-structural protein 4B/NS4B (via C-terminal region); this interaction may promote the recruitment of NS4B in the proximity of lipid droplet.
Self-associates (PubMed:18477614).
Interacts with SNRNP200; this interaction may promote the odontogenic differentiation (PubMed:34790668).
Interacts with SNRNP200; this interaction may promote the odontogenic differentiation (PubMed:34790668).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9H8H3 | ATXN3 P54252 | 3 | EBI-1390168, EBI-946046 | |
BINARY | Q9H8H3 | ELAVL4 P26378-2 | 3 | EBI-1390168, EBI-21603100 | |
BINARY | Q9H8H3 | FGFR3 P22607 | 3 | EBI-1390168, EBI-348399 | |
BINARY | Q9H8H3 | GSN P06396 | 3 | EBI-1390168, EBI-351506 | |
BINARY | Q9H8H3 | KAT5 Q92993 | 3 | EBI-1390168, EBI-399080 | |
BINARY | Q9H8H3 | LMO3 Q8TAP4-4 | 3 | EBI-1390168, EBI-11742507 | |
BINARY | Q9H8H3 | NDUFS3 O75489 | 3 | EBI-1390168, EBI-1224896 | |
BINARY | Q9H8H3 | PPIA P62937-2 | 3 | EBI-1390168, EBI-25884072 | |
BINARY | Q9H8H3 | PRKCA P17252 | 3 | EBI-1390168, EBI-1383528 | |
BINARY | Q9H8H3 | SETDB1 Q15047-2 | 3 | EBI-1390168, EBI-9090795 | |
BINARY | Q9H8H3 | YWHAG P61981 | 3 | EBI-1390168, EBI-359832 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-28 | Targeting to lipid droplets | ||||
Sequence: MELTIFILRLAIYILTFPLYLLNFLGLW |
Sequence similarities
Belongs to the methyltransferase superfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length244
- Mass (Da)28,319
- Last updated2001-03-01 v1
- Checksum6967783BAB2348BE
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 39 | in Ref. 3; BAB14913 | ||||
Sequence: F → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ536233 EMBL· GenBank· DDBJ | CAD60207.1 EMBL· GenBank· DDBJ | mRNA | ||
AY358797 EMBL· GenBank· DDBJ | AAQ89157.1 EMBL· GenBank· DDBJ | mRNA | ||
AK023693 EMBL· GenBank· DDBJ | BAB14643.1 EMBL· GenBank· DDBJ | mRNA | ||
AK024409 EMBL· GenBank· DDBJ | BAB14913.1 EMBL· GenBank· DDBJ | mRNA | ||
BC004492 EMBL· GenBank· DDBJ | AAH04492.1 EMBL· GenBank· DDBJ | mRNA | ||
BC008180 EMBL· GenBank· DDBJ | AAH08180.1 EMBL· GenBank· DDBJ | mRNA | ||
AL050159 EMBL· GenBank· DDBJ | CAB43300.1 EMBL· GenBank· DDBJ | mRNA | ||
AF113007 EMBL· GenBank· DDBJ | AAF20268.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |