Search Results
Overview
| Uniprot ID | Q9H8H3 |
|---|---|
| Protein Name | Thiol S-methyltransferase TMT1A |
| Gene Name | TMT1A |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 109 | NFEKFLIKSIAENRH |
| 219 | LERASFSKLKLQHIQ |
| 221 | RASFSKLKLQHIQAP |
| 54 | YNEQMASKKRELFSN |
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)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:0005811 | lipid droplet |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:1904724 | tertiary granule lumen |
| Molecular Function | GO:0008168 | methyltransferase activity |
| Molecular Function | GO:0001734 | mRNA m(6)A methyltransferase activity |
| Molecular Function | GO:0008173 | RNA methyltransferase activity |
| Molecular Function | GO:0018708 | thiol S-methyltransferase activity |
| Biological Process | GO:0180035 | lncRNA processing |
| Biological Process | GO:0032259 | methylation |
| Biological Process | GO:0042476 | odontogenesis |
| Biological Process | GO:0001649 | osteoblast differentiation |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.