Search Results
Overview
| Uniprot ID | P62328 |
|---|---|
| Protein Name | Thymosin beta-4 |
| Gene Name | TMSB4X |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 12 | PDMAEIEKFDKSKLK |
| 20 | FDKSKLKKTETQEKN |
| 26 | KKTETQEKNPLPSKE |
| 32 | EKNPLPSKETIEQEK |
Function
Plays an important role in the organization of the cytoskeleton (PubMed:10848969, PubMed:1999398). Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (PubMed:10848969, PubMed:1999398)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0031093 | platelet alpha granule lumen |
| Molecular Function | GO:0003785 | actin monomer binding |
| Molecular Function | GO:0003788 | actin monomer sequestering activity |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0140311 | protein sequestering activity |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0007015 | actin filament organization |
| Biological Process | GO:0030837 | negative regulation of actin filament polymerization |
| Cellular Component | GO:0005856 | cytoskeleton |
| Cellular Component | GO:0005829 | cytosol |
| Biological Process | GO:0043124 | negative regulation of canonical NF-kappaB signal transduction |
| Biological Process | GO:0050728 | negative regulation of inflammatory response |
| Biological Process | GO:2001171 | positive regulation of ATP biosynthetic process |
| Biological Process | GO:0043536 | positive regulation of blood vessel endothelial cell migration |
| Biological Process | GO:2001028 | positive regulation of endothelial cell chemotaxis |
| Biological Process | GO:0030334 | regulation of cell migration |
| Biological Process | GO:0033209 | tumor necrosis factor-mediated 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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.
[3] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.
[4] 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.
[5] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.
[6] 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.
[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.