EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.4.22.B67 | di-SUMO + H2O |
25% degradation within 60 min |
Saccharomyces cerevisiae |
2 SUMO |
- |
? |
| 3.4.22.B67 | hexa-SUMO + H2O |
95% degradation within 60 min |
Saccharomyces cerevisiae |
SUMO + ? |
- |
? |
| 3.4.22.B67 | more |
Ulp2 is required for cell division following termination of the DNA damage checkpoint in Sacharomyces cerevisiae. The DNA damage checkpoint is a crucial defense mechanism used by cells to withstand DNA damage. Activation of the checkpoint halts the cell cycle at metaphase and allows time for DNA repair prior to cell division |
Saccharomyces cerevisiae |
? |
- |
? |
| 3.4.22.B67 | more |
Ulp2 SUMO protease is required for proper spindle dynamics during cell cycle resumption following a DNA damage-induced cell cycle arrest. It is proposed that one or more proteins is sumoylated following DNA damage-induced checkpoint activation, and this substrate(s) must be desumoylated by Ulp2 for proper cell cycle resumption |
Saccharomyces cerevisiae |
? |
- |
? |
| 3.4.22.B67 | more |
isozyme Ulp2 is important for the control of poly-SUMO conjugates in cells and to dismantle SUMO chains in vitro. Isozyme Ulp2 acts sequentially rather than stochastically, processing substrate-linked poly-SUMO chains from their distal ends down to two linked SUMO moieties. Three linked SUMO units are the minimum length of a substrate-linked chain required for efficient binding to and processing by isozyme Ulp2, that disassembles SUMO chains by removing one SUMO moiety at a time from their ends, i.e. exo mechanism. Isozyme Ulp2 recognizes surfaces at or near the N-terminus of the distal SUMO moiety, as attachments to this end significantly reduce cleavage efficiency. Recombinant construction and expression of generate SMT3-led constructs, overview. Isozyme Ulp2 has three Smt3 binding sites that need to be occupied simultaneously to achieve full cooperative binding. Substrates equipped with mono- or di-Smt3, in contrast, are hardly bound if at all, substrate specificity analysis of immobilized recombinant enzyme, overview |
Saccharomyces cerevisiae |
? |
- |
? |
| 3.4.22.B67 | polySUMO-protein conjugate + H2O |
- |
Saccharomyces cerevisiae |
SUMO + SUMO-SUMO + SUMO-SUMO-SUMO + truncated polySUMO-protein conjugate |
- |
? |
| 3.4.22.B67 | polySUMO-protein conjugate + H2O |
Ulp2 is capable of cleaving SUMO chains |
Saccharomyces cerevisiae |
SUMO + SUMO-SUMO + SUMO-SUMO-SUMO + truncated polySUMO-protein conjugate |
- |
? |
| 3.4.22.B67 | polySUMO-protein conjugate + H2O |
Ulp2 can cleave the SUMO-SUMO linkage in poly-SUMO chains |
Saccharomyces cerevisiae |
SUMO + truncated polySUMO-protein conjugate + H2O |
- |
? |
| 3.4.22.B67 | polySUMO-protein conjugate + H2O |
Ulp2 can cleave the SUMO-SUMO linkage in poly-SUMO chains. The C-terminal noncatalytic domain of Ulp2 is required for efficient depolymerization of large poly-SUMO conjugates in vivo |
Saccharomyces cerevisiae |
SUMO + truncated polySUMO-protein conjugate + H2O |
- |
? |
| 3.4.22.B67 | Smt3-modified protein conjugate + H2O |
Ulp2 is able to cleave isopeptide-linked Smt3 molecules from natural substrates. Smt3-protein deconjugation by Ulp2 is important for normal meiotic development |
Saccharomyces cerevisiae |
Smt3 + protein |
- |
? |
