IFN‐γ‐activated keratinocytes are key contributors to the pathogenetic mechanisms leading to type‐1 immune‐mediated skin disorders. In these epidermal cells, SOCS1 negatively regulates the molecular cascades triggered by IFN‐γ by disabling JAK2 phosphorylation through its kinase inhibitory region (KIR). Aimed at potentiating the SOCS1 inhibitory function on JAK2/STAT1 axis in keratinocytes, we recently developed a set of peptides mimicking the SOCS1 KIR domain, which are capable of efficiently binding JAK2 in vitro. Here, the effects of one such SOCS1 KIR mimetic named PS‐5 on IFN‐γ‐activated human keratinocytes were evaluated. We found that IFN‐γ‐activated keratinocytes treated with PS‐5 exhibited impaired JAK2, IFN‐γRα, and STAT1 phosphorylation. We also observed reduced levels of the IRF‐1 transcription factor, and a strong reduction in ICAM‐1, HLA‐DR, CXCL10, and CCL2 inflammatory gene expression. ICAM‐1 reduced expression resulted in an impaired adhesiveness of T lymphocytes to autologous keratinocytes. Consistently, the migration of T cells toward supernatants from PS‐5‐treated keratinocytes was drastically reduced. Finally, PS‐5 treatment hampered STAT1 activation and the expression of STAT1‐dependent inflammatory genes in IFN‐γ‐treated explants of human skin. These data collectively indicate that PS‐5 has an important therapeutic potential in the treatment of type‐1 immune‐mediated skin diseases.