SUMO2 Human

Small Ubiquitin-Related Modifier 2 (SUMO-2) is a member of the SUMO protein family, which plays a crucial role in post-translational modification of proteins. SUMO proteins are involved in various cellular processes, including nuclear-cytosolic transport, transcriptional regulation, apoptosis, protein stability, response to stress, and progression through the cell cycle .

SUMO-2, like other SUMO proteins, is covalently attached to target proteins through a process called SUMOylation. This modification typically involves the formation of an isopeptide bond between the C-terminal glycine residue of SUMO-2 and an acceptor lysine on the target protein . SUMO-2 shares about 50% sequence identity with SUMO-1 and shows a high degree of similarity to SUMO-3 .

The SUMOylation process is directed by an enzymatic cascade similar to that involved in ubiquitination. However, unlike ubiquitin, SUMO is not used to tag proteins for degradation. Instead, SUMOylation can alter the localization, stability, and interaction partners of the target proteins .

SUMO-2 is involved in a wide range of cellular functions. It plays a critical role in protein stability, nuclear-cytosolic transport, and transcriptional regulation. SUMOylation of target proteins can lead to various outcomes, including altered localization and binding partners. For example, the SUMO modification of RanGAP1 leads to its trafficking from the cytosol to the nuclear pore complex .

In addition to its role in normal cellular processes, SUMO-2 is also involved in the cellular response to stress. Under stress conditions, such as starvation, SUMO-2 can be used for the modification of proteins, which helps the cell to adapt and survive .

Human recombinant SUMO-2 is produced using recombinant DNA technology, which allows for the expression and purification of the protein in a controlled laboratory environment. This recombinant form of SUMO-2 is used in various research applications to study the SUMOylation process and its effects on target proteins.