SKP1 (S-phase kinase associated protein 1) functions as an essential adapter component of SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complexes, which mediate targeted protein degradation through the ubiquitin-proteasome pathway 1. The protein serves as a crucial link between F-box proteins and CUL1, enabling the formation of diverse SCF complexes with distinct substrate specificities 2. SKP1-containing complexes target numerous proteins for ubiquitination, including cell cycle regulators, transcription factors, and signaling molecules 3. Beyond canonical SCF complexes, SKP1 participates in E3-E3 super-assemblies with RBR-type ligases like ARIH1, expanding the range of substrates that can be effectively ubiquitinated 3. The protein also plays specialized roles in meiosis, where SKP1 localizes to chromosome 5 and orchestrates the prophase I to metaphase I transition by maintaining chromosome 5 and enabling metaphase competence acquisition 4. Additionally, SKP1 mediates non-canonical ubiquitination pathways, including sugar-mediated ubiquitination that regulates transcription factor activation 5. Loss of SKP1 has been implicated in cancer progression, particularly in breast cancer where 5q deletions affect SKP1 expression and contribute to oncogenic signaling 6.