Update publication information. Ticks are widely distributed ectoparasitic arthropods that suck blood from the body surface of livestock, wild animals, and humans. Ticks not only transmit a variety of pathogens but also cause various degrees of damage to their hosts' skin during blood feeding. To explore the molecular regulatory mechanism employed by the host skin to withstand tick bites, larval, nymphal, and adult Haemaphysalis longicornis, which is distributed in East Asia, were used to bite the skin tissues of healthy rabbits in the present study. The quantitative proteomic technology data-independent acquisition was then employed to investigate in depth the changes in protein expression and phosphorylation in rabbit skin after tick bite. The results showed that among the 4034 proteins and 1795 phosphorylated proteins identified, a total of 202 proteins and 435 phosphorylation sites were changed at all time points after H. longicornis bite. Regulated host proteins such as coronin, mannose receptor C-type 1, dendritic cell-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN), ezrin, and integrin play important roles in immune defence against tick bite. Fibrinogen, fibronectin, integrin-linked kinase (ILK), and tenascin C jointly regulate the coagulation and wound healing processes in the host. Trichohyalin and peptidyl arginine deiminase 3 were downregulated to induce hair loss in the host. In addition, the changes in the phosphorylation of interleukin-4 receptor, microtubule-actin crosslinking factor 1, and Nck adaptor protein 1 would play important roles in host immunity and vascular repair.