Search Results
Overview
| Uniprot ID | Q12904 |
|---|---|
| Protein Name | Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 |
| Gene Name | AIMP1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 114 | SGTKEQIKGGTGDEK |
| 137 | KGEKKEKKQQSIAGS |
| 33 | KQQVSLLKEKAILQA |
| 9 | ANNDAVLKRLEQKGA |
Function
Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase (PubMed:10358004). Binds tRNA. Possesses inflammatory cytokine activity (PubMed:11306575). Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation (By similarity). Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels (By similarity). Promotes dermal fibroblast proliferation and wound repair (PubMed:16472771). Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum (By similarity). Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelial cell apoptosis at high concentrations (PubMed:12237313). Induces maturation of dendritic cells and monocyte cell adhesion (PubMed:11818442). Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7 (PubMed:19362550)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0017101 | aminoacyl-tRNA synthetase multienzyme complex |
| Cellular Component | GO:0009986 | cell surface |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0005794 | Golgi apparatus |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0005125 | cytokine activity |
| Molecular Function | GO:0051020 | GTPase binding |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0000049 | tRNA binding |
| Biological Process | GO:0001525 | angiogenesis |
| Biological Process | GO:0006915 | apoptotic process |
| Biological Process | GO:0007267 | cell-cell signaling |
| Biological Process | GO:0051607 | defense response to virus |
| Biological Process | GO:0006954 | inflammatory response |
| Biological Process | GO:0050900 | leukocyte migration |
| Biological Process | GO:0001937 | negative regulation of endothelial cell proliferation |
| Biological Process | GO:0070094 | positive regulation of glucagon secretion |
| 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] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.
[4] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[5] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.