Sumoylation is a post-translational modification of proteins by covalently attaching a small ubiquitin-related modifier (SUMO) to the proteins. However, unlike ubiquitination, Sumoylation does not target proteins for proteolytic degradation, it regulates protein functions in various cellular precesses, such as, nuclear-cytosolic transport, transcriptional regulation, apoptosis, protein stability, response to stress, and progression through the cell cycle.
Structure of SUMO
Although SUMO has very little sequence identity with ubiquitin at the amino acid sequence, it has a nearly identical structural fold. There are four SUMO paralogues. Usually, SUMO has around 100 amino acids in length. The exact length and mass of SUMO varies between SUMO family members and in different organisms.
Function of SUMO
Sumoylation is involved in regulating the subcellular localization of a number of substrate proteins. Depending on the target protein, sumoylation can occur in the cytoplasm or nucleus. For example, transport of RanGAP1, a ribonucleoprotein, across the NPC is regulated by addition of SUMO. Sumoylation also regulates the transcription process. The activities of many transcription factors are associated with interaction of PML and NBs, and assembly of PML and NBs requires sumoylation of the PML protein. Moreover, sumoylation has held an important role in chromosome cohesion and kinetochore assembly. Malfunction of SUMO-1 disrupted proper distribution of chromatins into the replicated cells.
Creative Proteomics has established a highly sensitive HPLC-MS/MS platform that can analyze sumoylation in multiple samples and in both eukaryotic and prokaryotic organisms. In addition, we have optimized our protocol to enable more fast and sensitive site mapping service for sumoylation analysis.
Workflow of our sumoylation analysis service:
Creative Proteomics also provide the following bioinformatics services in Protein Post-translational Modification Analysis:
Functional annotation and enrichment analysis
Proteomic analysis of post-translational modifications
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