SUMO protein
class of proteins
In molecular biology, SUMO (Small Ubiquitin-like MOdifier) proteins are a family of small proteins that are covalently attached to and detached from other proteins in cells to modify their function. This process is called SUMOylation (pronounced soo-muh-lā-shun and sometimes written sumoylation). SUMOylation is a post-translational modification involved in various cellular processes, such as nuclear-cytosolic transport, transcriptional regulation, apoptosis, protein stability, response to stress, and progression through the cell cycle. In human proteins, there are over 53,000 SUMO binding sites, making it a substantial component of fundamental biology.
SUMO proteins are similar to ubiquitin and are considered members of the ubiquitin-like protein family. SUMOylation is directed by an enzymatic cascade analogous to that involved in ubiquitination. In contrast to ubiquitin, SUMO is not used to tag proteins for degradation. Mature SUMO is produced when the last four amino acids of the C-terminus have been cleaved off to allow formation of an isopeptide bond between the C-terminal glycine residue of SUMO and an acceptor lysine on the target protein.
SUMO-interacting motifs (SIMs) are binding regions on proteins that interact with SUMO groups. SIMs are typically composed of short stretches of hydrophobic amino acids flanked by acidic amino acids.
The public source identifies “SUMO protein” as class of proteins. This brief keeps that definition visible, then builds a research path around SUMO, protein and class.
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This entry incorporates text from “SUMO protein” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.