The SCF (Skp1, Cdc53/Cullin, F box receptor) ubiquitin ligase complex is a conserved protein degradation system in eukaryotes that targets regulatory proteins for destruction by the 26S proteasome. This review summarizes the structure, function, and regulation of SCF, focusing on its role in ubiquitination and substrate degradation. SCF consists of four subunits: Skp1, Cdc53 (cullin), Hrt1, and an F box-containing protein. The F box is a key determinant of substrate specificity, and SCF is known for its role in the degradation of the G1/S cyclin Sic1. The SCF complex is regulated post-translationally, with modifications such as phosphorylation and ubiquitination influencing its activity and substrate specificity. The SCF complex is also involved in the degradation of a wide range of substrates, including cyclins, transcription factors, and signaling molecules. The SCF complex is highly conserved across eukaryotes, and its function is essential for cell cycle regulation and other cellular processes. The SCF complex is composed of multiple subunits, each with distinct roles in substrate recognition, ubiquitin transfer, and complex assembly. The SCF complex is regulated by post-translational modifications, including phosphorylation, ubiquitination, and other modifications that influence its activity and substrate specificity. The SCF complex is also involved in the degradation of a variety of substrates, including cyclins, transcription factors, and signaling molecules. The SCF complex is a key component of the ubiquitin-proteasome system and plays a critical role in the regulation of protein degradation in eukaryotic cells.The SCF (Skp1, Cdc53/Cullin, F box receptor) ubiquitin ligase complex is a conserved protein degradation system in eukaryotes that targets regulatory proteins for destruction by the 26S proteasome. This review summarizes the structure, function, and regulation of SCF, focusing on its role in ubiquitination and substrate degradation. SCF consists of four subunits: Skp1, Cdc53 (cullin), Hrt1, and an F box-containing protein. The F box is a key determinant of substrate specificity, and SCF is known for its role in the degradation of the G1/S cyclin Sic1. The SCF complex is regulated post-translationally, with modifications such as phosphorylation and ubiquitination influencing its activity and substrate specificity. The SCF complex is also involved in the degradation of a wide range of substrates, including cyclins, transcription factors, and signaling molecules. The SCF complex is highly conserved across eukaryotes, and its function is essential for cell cycle regulation and other cellular processes. The SCF complex is composed of multiple subunits, each with distinct roles in substrate recognition, ubiquitin transfer, and complex assembly. The SCF complex is regulated by post-translational modifications, including phosphorylation, ubiquitination, and other modifications that influence its activity and substrate specificity. The SCF complex is also involved in the degradation of a variety of substrates, including cyclins, transcription factors, and signaling molecules. The SCF complex is a key component of the ubiquitin-proteasome system and plays a critical role in the regulation of protein degradation in eukaryotic cells.