| ID | Sequence | Length | GC content |
|---|---|---|---|
| GCAGAGUCUGCGGACCCGGCGCCGAGGCGGCCACCCGAGACGCGGCGCG… | 2225 nt | 0.6373 | |
| GCAGAGUCUGCGGACCCGGCGCCGAGGCGGCCACCCGAGACGCGGCGCG… | 2135 nt | 0.6431 | |
| GCAGAGUCUGCGGACCCGGCGCCGAGGCGGCCACCCGAGACGCGGCGCG… | 2228 nt | 0.6373 |
Focal adhesions are actin-rich structures that enable cells to adhere to the extracellular matrix and at which protein complexes involved in signal transduction assemble. Zyxin is a zinc-binding phosphoprotein that concentrates at focal adhesions and along the actin cytoskeleton. Zyxin has an N-terminal proline-rich domain and three LIM domains in its C-terminal half. The proline-rich domain may interact with SH3 domains of proteins involved in signal transduction pathways while the LIM domains are likely involved in protein-protein binding. Zyxin may function as a messenger in the signal transduction pathway that mediates adhesion-stimulated changes in gene expression and may modulate the cytoskeletal organization of actin bundles. Alternative splicing results in multiple transcript variants that encode the same isoform. [provided by RefSeq, Jul 2008]
A study in human burn injury patients identified the ZYX as a significantly upregulated hub gene with promising diagnostic value, showing a p-value < 0.001 and an Area Under the Curve (AUC) > 0.68 in receiver operating characteristic analysis [Zhou et al. DOI:10.3389/fgene.2022.829841].