Search Results
Overview
| Uniprot ID | O43776 |
|---|---|
| Protein Name | Asparagine--tRNA ligase, cytoplasmic |
| Gene Name | NARS1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 104 | EAKKITIKNDPSLPE |
| 38 | KALMTVGKEPFPTIY |
| 60 | ERWNVISKSQLKNIK |
| 64 | VISKSQLKNIKKMWH |
| 93 | EDSLRREKNLEEAKK |
Function
Catalyzes the attachment of asparagine to tRNA(Asn) in a two-step reaction: asparagine is first activated by ATP to form Asn-AMP and then transferred to the acceptor end of tRNA(Asn) (PubMed:32738225, PubMed:32788587, PubMed:9421509). In addition to its essential role in protein synthesis, acts as a signaling molecule that induced migration of CCR3-expressing cells (PubMed:12235211, PubMed:30171954). Has an essential role in the development of the cerebral cortex, being required for proper proliferation of radial glial cells (PubMed:32788587)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Molecular Function | GO:0004816 | asparagine-tRNA ligase activity |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0031728 | CCR3 chemokine receptor binding |
| Molecular Function | GO:0003676 | nucleic acid binding |
| Molecular Function | GO:0046983 | protein dimerization activity |
| Biological Process | GO:0006421 | asparaginyl-tRNA aminoacylation |
| Biological Process | GO:0016477 | cell migration |
| Biological Process | GO:0021987 | cerebral cortex development |
| Biological Process | GO:0006418 | tRNA aminoacylation for protein translation |
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.
[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.