P55854, P61956

SUMO belong to the ubiquitin-like protein family and are characterized by their conserved beta-grasp fold structure, which is crucial for their ability to conjugate to target proteins through the sumoylation process. This structural integrity allows SUMO to interact effectively with E1, E2, and E3 enzymes, facilitating the attachment of SUMO to lysine residues on substrate proteins. The sumoylation mediated by SUMO plays a vital role in regulating various cellular functions, including nuclear transport, transcriptional regulation, apoptosis, and protein stability, thereby maintaining cellular homeostasis and responding to stress. The ability of SUMO to form poly-SUMO chains through their structural domains enhances their regulatory capacity, influencing processes such as DNA repair, cell cycle progression, and the modulation of transcription factors.