SUMO1 Conjugation Kit
SUMO1 Conjugation Kit Summary
Human Small Ubiquitin-like Modifier 1 (SUMO1), also known as Sentrin, UBL1, and SMT3C, is synthesized as a 101 amino acid (aa) propeptide with a predicted molecular weight of 11.5 kDa. Human SUMO1 is the most unique of the four identified SUMO proteins and shares only 44%, 47%, and 41% aa sequence identity with SUMO2, SUMO3, and SUMO4, respectively. In contrast, human SUMO1 shares 100% aa sequence identity with the mouse ortholog. SUMOs are a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed SUMOylation. All SUMO proteins share a conserved Ubiquitin domain and a C-terminal diglycine cleavage/attachment site. Following cleavage of a four aa C-terminal prosegment, the C-terminal glycine residue of SUMO1 is enzymatically attached to a lysine residue on a target protein. In humans, SUMO1 is conjugated to a variety of molecules in the presence of the SAE1/UBA2 SUMO-activating (E1) enzyme and the UBE2I/Ubc9 SUMO-conjugating (E2) enzyme. In yeast, the SUMO-activating (E1) enzyme is Aos1/Uba2p. SUMOylation can occur without the requirement of a specific SUMO ligase (E3), where SUMO1 is transferred directly from UBE2I/Ubc9 to specific substrates. In Alzheimers disease models SUMO1 has been shown to influence the generation of Amyloid-beta peptide by promoting the accumulation of BACE-1. Covalent modification of Phosphatase and Tensin Homolog Deleted on Chromosome (PTEN) by SUMO1 is thought to regulate tumorigenesis by retaining PTEN at the plasma membrane, an effect that suppresses PI 3-Kinase/Akt-dependent tumor growth.
Citations for SUMO1 Conjugation Kit
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Using glycyrrhizic acid to target sumoylation processes during Epstein-Barr virus latency
Authors: GL Bentz, AJ Lowrey, DC Horne, V Nguyen, AR Satterfiel, TD Ross, AE Harrod, ON Uchakina, RJ McKallip
PLoS ONE, 2019;14(5):e0217578. 2019
Role of the CBP catalytic core in intramolecular SUMOylation and control of histone H3 acetylation
Authors: S Park, RL Stanfield, MA Martinez-Y, HJ Dyson, IA Wilson, PE Wright
Proc. Natl. Acad. Sci. U.S.A., 2017;0(0):. 2017
Sequential posttranslational modifications program FEN1 degradation during cell-cycle progression.
Authors: Guo Z, Kanjanapangka J, Liu N, Liu S, Liu C, Wu Z, Wang Y, Loh T, Kowolik C, Jamsen J, Zhou M, Truong K, Chen Y, Zheng L, Shen B
Mol Cell, 2012;47(3):444-56. 2012
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