ANKRD13A encodes a ubiquitin-binding protein that specifically recognizes K63-linked ubiquitin chains and plays crucial roles in receptor endocytosis and cellular quality control mechanisms 1. The protein functions as a molecular scaffold in EGFR endocytosis by binding to ubiquitinated EGFR and facilitating complex formation with E3 ligases RNF11 and ITCH, promoting lysosomal degradation of activated receptors 1. ANKRD13A also mediates mitochondrial quality control by recruiting VCP/p97 ATPase to promote outer membrane rupture during PINK1/Parkin-mediated mitophagy 2. In TNF signaling, ANKRD13A acts as a cell-death checkpoint regulator by binding ubiquitinated RIP1 and limiting FADD/caspase-8 association, thereby controlling the threshold for cytotoxic responses 3. The protein contributes to immune evasion in acute myeloid leukemia by promoting HLA-I internalization 4 and participates in host defense against Toxoplasma gondii through p97/VCP-mediated parasitophorous vacuole targeting 5. Additionally, ANKRD13A regulates cell migration and focal adhesion dynamics, with its expression controlled by miR-204 during neural crest and lens cell development 6. Clinical significance includes associations with cancer prognosis and lithium adverse effects 7.