6.2.1.45	A189T	improved stability and activity compared to mutant A189T/W714C, but when incubated at 39°C, cells expressing the mutant show increased apoptotic rate ompared to wild-type. Mutant is able to monoubiquitinate histone H2A and to support growth of TS20 cells at 39°C. Compared to mutant A189T/W714C, mutation A189T significantly improves the ubiquitination-dependent disposal of HIF-1alpha	728028	
6.2.1.45	A189T	the mutant enzyme is less stable than its wild-type counterpart, and restrictive temperature (39°C) accelerates its degradation	715718	
6.2.1.45	A189T/W714C	mutant protein is less stable than its wildtype counterpart, and restrictive temperature of 39°C accelerates its degradation	728028	
6.2.1.45	C632A	generation of an active site cysteine mutant of HA-UBE1	735013	
6.2.1.45	D290K/C250A	in this heterodimer, the UBA5 subunit that can form the thioester bond with UFM1 is missing the UFC1 binding site. In the UBA5 (D290K)-UBA5 (K271D/C250A DELTADUIS) heterodimer, binding to the UIS and charging can only take place on the same monomer, thereby supporting a cis-binding mechanism	744655	
6.2.1.45	D576A	Km-value for ATP is 37.8fold higher than wild-type value, KM-value for ubiquitin is 36fold higher than wild-type value. kcat for ubiquitin adenylate formation is 250fold lower than wild-type value. kcat for ubiquitin carrier protein E2 transthiolation is 28.3fold lower than wild-type value	674561	
6.2.1.45	D576A	mutation within the MgATP2- binding site, results in dramatically impaired binding affinities for MgATP2-, a shift from ordered to random addition in co-substrate binding, and a significantly reduced rate of ternary complex formation that shifts the rate-limiting step to ubiquitin adenylate formation. Mutations does not affect the affinity of Ubc2b binding, however, differences in kcat values determined from ternary complex formation versus HsUbc2b transthiolation suggest that binding of the E2 enhances the rate of bound ubiquitin adenylate formation	674561	
6.2.1.45	D576E	Km-value for ATP is 4fold higher than wild-type value, KM-value for ubiquitin is 1.4fold higher than wild-type value. kcat for ubiquitin adenylate formation is 1200fold lower than wild-type value. kcat for ubiquitin carrier protein E2 transthiolation is 34fold lower than wild-type value	674561	
6.2.1.45	D576E	mutation within the MgATP2- binding site, results in dramatically impaired binding affinities for MgATP2-, a shift from ordered to random addition in co-substrate binding, and a significantly reduced rate of ternary complex formation that shifts the rate-limiting step to ubiquitin adenylate formation. Mutations does not affect the affinity of Ubc2b binding, however, differences in kcat values determined from ternary complex formation versus HsUbc2b transthiolation suggest that binding of the E2 enhances the rate of bound ubiquitin adenylate formation	674561	
6.2.1.45	D576N	Km-value for ATP is 5.2fold higher than wild-type value, KM-value for ubiquitin is 5fold higher than wild-type value. kcat for ubiquitin adenylate formation is 545fold lower than wild-type value. kcat for ubiquitin carrier protein E2 transthiolation is 155fold lower than wild-type value	674561