SUMO, ubiquitin's mysterious cousin.
Covalent modification of cellular proteins by the ubiquitin-like modifier SUMO regulates various cellular processes, such as nuclear transport, signal transduction, stress response and cell-cycle progression. But, in contrast to ubiquitylation, sumoylation does not tag proteins for degradation, but seems to enhance their stability or modulate their subcellular compartmentalization.
Max Planck Institute of Biochemistry, Department of Molecular Cell Biology, Am Klopferspitz 18a, 82152, Martinsried, Germany. stmuelle@biochem.mpg.de
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D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008025:Ligases / Q000378:metabolism; D008969:Molecular Sequence Data; D011506:Proteins / Q000378:metabolism; D025842:SUMO-1 Protein; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D044763:Ubiquitin-Conjugating Enzymes; D014452:Ubiquitins / Q000235:genetics / Q000378:metabolism*; D000098843:Ubiquitin-Conjugating Enzyme UBC9
D011506:Proteins; D025842:SUMO-1 Protein; D014452:Ubiquitins; D044763:Ubiquitin-Conjugating Enzymes; D008025:Ligases; D000098843:Ubiquitin-Conjugating Enzyme UBC9