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Ubiquitin-like molecules, such as SUMO1, are structurally related to ubiquitin. and can be ligated to target proteins in a similar manner as ubiquitin. However, covalent attachment of UBLs does not result in degradation of the modified proteins. SUMO1 modification is implicated in the targeting of RANGAP1. to the nuclear pore complex, as well as in stabilization of I-kappa-B-alpha from degradation by the 26S proteasome. Like ubiquitin, UBLs are synthesized as precursor proteins, with 1 or more amino acids following the C-terminal glycine-glycine residues of the mature UBL protein. Thus, the tail sequences of the UBL precursors need to be removed by UBL-specific proteases, such as SENP6, prior to their conjugation to target proteins. SENPs also display isopeptidase activity for deconjugation of SUMO-conjugated substrates.
2810017C20Rik; E130319N12Rik; FKSG6; FLJ11355; FLJ11887; KIAA0389; KIAA0797; mKIAA0797; RP1-134M13.1; SENP6; sentrin/SUMO-specific protease SENP6; Sentrin-specific protease 6; Sentrin-specific protease 6-like protein; SSP1; SUMO specific peptidase 6; SUMO/sentrin specific peptidase 6; SUMO/sentrin specific protease 6; SUMO1/sentrin specific peptidase 6; SUMO1/sentrin specific protease 6; Sumo1/sentrin/SMT3 specific peptidase 6; SUMO-1-specific protease 1; Susp1
100 µL
100 µL
100 µg
100 µL
100 µg
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