Search Results
Overview
| Uniprot ID | O00148 |
|---|---|
| Protein Name | ATP-dependent RNA helicase DDX39A |
| Gene Name | DDX39A |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 333 | LSRYQQFKDFQRRIL |
| 35 | APPKKDIKGSYVSIH |
Function
Helicase that plays an essential role in mRNA export and is involved in multiple steps in RNA metabolism including alternative splicing (PubMed:33941617, PubMed:38801080). Regulates nuclear mRNA export to the cytoplasm through association with ECD (PubMed:33941617). Also involved in spliceosomal uridine-rich small nuclear RNA (U snRNA) export by stimulating the RNA binding of adapter PHAX (PubMed:39011894). Plays a role in the negative regulation of type I IFN production by increasing the nuclear retention of antiviral transcripts and thus reducing their protein expression (PubMed:32393512). Independently of the interferon pathway, plays an antiviral role against alphaviruses by binding to a 5' conserved sequence element in the viral genomic RNA (PubMed:37949067)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0003729 | mRNA binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0003724 | RNA helicase activity |
| Biological Process | GO:0006406 | mRNA export from nucleus |
| Biological Process | GO:0000398 | mRNA splicing, via spliceosome |
| Biological Process | GO:0045824 | negative regulation of innate immune response |
| Biological Process | GO:0046832 | negative regulation of RNA export from nucleus |
| Biological Process | GO:0006405 | RNA export from nucleus |
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] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[3] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[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.
[6] 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.