Search Results
Overview
| Uniprot ID | Q04726 |
|---|---|
| Protein Name | Transducin-like enhancer protein 3 |
| Gene Name | TLE3 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 225 | ADYSMEAKKRKAEEK |
| 226 | DYSMEAKKRKAEEKD |
| 281 | DKARSLKKDAPTSPA |
| 302 | STPSSKTKDLGHNDK |
| 309 | KDLGHNDKSSTPGLK |
| 316 | KSSTPGLKSNTPTPR |
Function
Transcriptional coregulator that binds to a number of transcription factors. Acts as a regulator of adipogenesis both by acting as a corepressor of Wnt signaling and coactivator for PPARG (PubMed:28689657). Inhibits the transcriptional activation mediated by CTNNB1 and TCF family members in Wnt signaling (PubMed:28689657). Promotes diffentiation of white adipocytes by acting as a coactivator for PPARG and preventing the association between PRDM16 and PPARG, thereby preventing browning of white adipocytes (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:1990907 | beta-catenin-TCF complex |
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005667 | transcription regulator complex |
| Molecular Function | GO:0003713 | transcription coactivator activity |
| Molecular Function | GO:0003714 | transcription corepressor activity |
| Biological Process | GO:0009887 | animal organ morphogenesis |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0045444 | fat cell differentiation |
| Biological Process | GO:0090090 | negative regulation of canonical Wnt signaling pathway |
| Biological Process | GO:0120163 | negative regulation of cold-induced thermogenesis |
| Biological Process | GO:0007165 | signal transduction |
| Biological Process | GO:0050872 | white fat cell differentiation |
| Biological Process | GO:0016055 | Wnt signaling pathway |
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] 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.