Search Results
Overview
| Uniprot ID | Q13148 |
|---|---|
| Protein Name | TAR DNA-binding protein 43 |
| Gene Name | TARDBP |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 140 | VQVKKDLKTGHSKGF |
| 181 | DCKLPNSKQSQDEPL |
| 263 | HISNAEPKHNSNRQL |
| 84 | YPKDNKRKMDETDAS |
| 95 | TDASSAVKVKRAVQK |
| 97 | ASSAVKVKRAVQKTS |
Function
RNA-binding protein that is involved in various steps of RNA biogenesis and processing (PubMed:23519609). Preferentially binds, via its two RNA recognition motifs RRM1 and RRM2, to GU-repeats on RNA molecules predominantly localized within long introns and in the 3'UTR of mRNAs (PubMed:23519609, PubMed:24240615, PubMed:24464995). In turn, regulates the splicing of many non-coding and protein-coding RNAs including proteins involved in neuronal survival, as well as mRNAs that encode proteins relevant for neurodegenerative diseases (PubMed:21358640, PubMed:29438978). Plays a role in maintaining mitochondrial homeostasis by regulating the processing of mitochondrial transcripts (PubMed:28794432). Also regulates mRNA stability by recruiting CNOT7/CAF1 deadenylase on mRNA 3'UTR leading to poly(A) tail deadenylation and thus shortening (PubMed:30520513). In response to oxidative insult, associates with stalled ribosomes localized to stress granules (SGs) and contributes to cell survival (PubMed:19765185, PubMed:23398327). Also participates in the normal skeletal muscle formation and regeneration, forming cytoplasmic myo-granules and binding mRNAs that encode sarcomeric proteins (PubMed:30464263). Plays a role in the maintenance of the circadian clock periodicity via stabilization of the CRY1 and CRY2 proteins in a FBXL3-dependent manner (PubMed:27123980). Negatively regulates the expression of CDK6 (PubMed:19760257). Regulates the expression of HDAC6, ATG7 and VCP in a PPIA/CYPA-dependent manner (PubMed:25678563)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0010494 | cytoplasmic stress granule |
| Cellular Component | GO:0035061 | interchromatin granule |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005726 | perichromatin fibrils |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0003690 | double-stranded DNA binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0008289 | lipid binding |
| Molecular Function | GO:0140693 | molecular condensate scaffold activity |
| Molecular Function | GO:0003730 | mRNA 3'-UTR binding |
| Molecular Function | GO:0097157 | pre-mRNA intronic binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0000978 | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
| Biological Process | GO:0061158 | 3'-UTR-mediated mRNA destabilization |
| Biological Process | GO:0070935 | 3'-UTR-mediated mRNA stabilization |
| Biological Process | GO:1990000 | amyloid fibril formation |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0043922 | host-mediated suppression of viral transcription |
| Biological Process | GO:0006397 | mRNA processing |
| Biological Process | GO:0010629 | negative regulation of gene expression |
| Biological Process | GO:0001933 | negative regulation of protein phosphorylation |
| Biological Process | GO:0071765 | nuclear inner membrane organization |
| Biological Process | GO:0032024 | positive regulation of insulin secretion |
| Biological Process | GO:0042307 | positive regulation of protein import into nucleus |
| Biological Process | GO:0042981 | regulation of apoptotic process |
| Biological Process | GO:0051726 | regulation of cell cycle |
| Biological Process | GO:0042752 | regulation of circadian rhythm |
| Biological Process | GO:0010468 | regulation of gene expression |
| Biological Process | GO:0031647 | regulation of protein stability |
| Biological Process | GO:0034976 | response to endoplasmic reticulum stress |
| Biological Process | GO:0048511 | rhythmic process |
| Biological Process | GO:0008380 | RNA splicing |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] 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.
[3] 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.
[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] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.
[7] 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.