In molecular biology, SUMO (S mall U biquitin-like MO difier) proteins are a family of small proteins that are covalently attached to and detached from other proteins in cells to modify their function.
Small ubiquitin-related modifier (SUMO) is a member of the ubiquitin-like protein family and, like ubiquitin, SUMO can be covalently attached to lysine side chains in a variety of target proteins.
SUMO proteins are similar to ubiquitin in their folded structure but possess only about 20% homology to the amino acid sequence of ubiquitin. The number of SUMO genes varies among eukaryotes. SUMO proteins are conjugated to substrate proteins in a manner
Posttranslational modification by small ubiquitin-like modifiers (SUMOs) is critical in regulating diverse cellular processes including gene expression, cell cycle progression, genome integrity, cellular metabolism, and inflammation and immunity.
Besides the characteristics of the traditional fusion tags above, SUMO protein has other advantages, such as small molecules, promoting folding and specific cleaved by SUMO protease 1.
A SUMO protein is a small ubiquitin-related modifier that can attach to target proteins, altering their activity, cellular location, or interactions with other proteins through a series of enzymatic reactions involving E1, E2, and E3 enzymes.
