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Background: Ubiquitin first time was known at 1975, as an 8.5 KDa protein, existing in the cell. Ubiquitin protein has been highly preserved and it has 96% homology gene sequencing between human and yeast. This peptide has been identified as an index of cell mark for removing it via “proteasome”. But, other functions such as participating in the apoptosis, differentiation and etc. have been considered for ubiquitination. In the present study, we tried to concentrate on role of ubiquitin-proteasome system in spermatogenesis process. Methods: Literature search in Entrez PubMed database, as well as other data sources related to ISI Web of Knowledge. Findings: Ubiquitin is secreted through epithelial cells of epididymis during sperm maturation, and placed on surface of abnormal sperm that is deleted. It is possible that some of this sperms escape from deletion in epididymis and appear in ejaculate. Conclusion: Some researches indicated that ubiquitination may increase as a physiological phenomenon during the sperm capacitation which is a positive marker to confirm sperm quality. Therefore, addition to role of ubiquitination in removing abnormal sperm, it can be involved in sperm capacitation process.