Myopia development has been extensively studied from different perspectives. Myopia recovery is also considered important for understanding the development of myopia. However, despite several previous studies, retinal proteomics during recovery from myopia is still relatively unknown. Therefore, the aim of the present study was to investigate the changes in protein profiles of chicken retinas during early recovery from lens‑induced myopia to evaluate the signals involved in the adjustment of this refractive disorder. Three‑day old chickens wore glasses for 7 days (‑10D lens over the right eye and a plano lens as control over the left eye), followed by 24 h without lenses. Protein expression in the retina was measured by two‑dimensional fluorescence difference gel electrophoresis (2D‑DIGE). Pro‑Q Diamond phosphoprotein staining 2D gel electrophoresis was used to analyze phosphoprotein profiles. Protein spots with significant differences (P<0.05) were analyzed by mass spectrometry. The minus lens‑treated eye became myopic, however following 24 h recovery, less myopia was observed. 2D‑DIGE proteomic analysis demonstrated that three identified protein spots were upregulated at least 1.2‑fold in myopic recovery retinas compared with those of the controls, Ras related protein Rab‑11B, S‑antigen retina and pineal gland and 26S proteasome non‑ATPase regulatory subunit 14. Pro‑Q Diamond images further revealed three protein spots with significant changes (at least 1.8‑fold): β‑tubulin was downregulated, while peroxiredoxin 4 and ubiquitin carboxyl‑terminal hydrolase‑L1 were upregulated in the recovery retinas compared with the control eye retinas. The present study detected previously unreported protein changes in recovering eyes, therefore revealing their potential involvement in retinal remodeling during eye ball reforge.