Ankyrin repeat domain-containing protein 13A (ANKRD13A)

Ankyrin repeat domain-containing protein 13A (ANKRD13A) is a cytoplasmic protein characterized by three ankyrin repeats in its N-terminal region and four ubiquitin-interacting motifs (UIMs) in its C-terminal region. It functions as a ubiquitin-binding adaptor, regulating the trafficking and internalization of ubiquitinated cell surface receptors such as the epidermal growth factor receptor (EGFR). ANKRD13A also acts as an early cell-death checkpoint regulator in TNF signaling, binding directly to ubiquitinated RIP1 and limiting the recruitment of FADD and caspase-8, thus suppressing apoptosis and necroptosis. Its high expression has been linked to poor prognosis and apoptotic resistance in certain cancers, suggesting a role in tumor progression and survival. No targeted therapies or drugs for ANKRD13A are currently described, but its functional domains make it a candidate for future drug development.

Other names

ANKRD13AANKRD13NY-REN-25Protein KE03NY-REN-25 antigen

Potential modulation of ubiquitin-binding, impacting cell death pathways (such as TNF signaling cascade). Regulation of receptor trafficking (EGFR internalization).