2.1.1.202	C260A	the mutant enzyme forms stable RNA-protein complexes in vitro. The complexes are formed due to faulty product release by the modified Trm4p enzyme and contain only natural ribonucleotides within the RNA	672512	
2.1.1.202	C260S	the mutant enzyme forms stable RNA-protein complexes in vitro. The complexes are formed due to faulty product release by the modified Trm4p enzyme and contain only natural ribonucleotides within the RNA	672512	
2.1.1.202	C271A	site-directed mutagenesis, the mutant enzyme forms an irreversible covalent crosslink between itself and the methylated cytosine in its target RNA	735907	
2.1.1.202	C310A	the mutant shows only a slightly lower affinity for RNA compared to wild-type Trm4p. The C310A mutant of Trm4p is unable to bind RNA covalently as well as to transfer the methyl group from SAM to the RNA substrate since no activity was detectable	710546	
2.1.1.202	C326A	site-directed mutagenesis, tRNA binding structure compared to wild-type enzyme, the C326A mutation hampers the breakdown of the covalent intermediates	757846	
2.1.1.202	C424A	organism containing the C424A mutation is not viable	639472	
2.1.1.202	C478A	organism containing the C478A mutation is viable	639472	
2.1.1.202	D266A	site-directed mutagenesis, the mutant shows highly increased binding affinity for SAM and highly reduced methylation activity	757846	
2.1.1.202	D293A	site-directed mutagenesis, the mutation leads to a loss of SAM binding capability and a loss of methylation activity to tRNACys	757846	
2.1.1.202	D323A	site-directed mutagenesis, the mutant shows highly increased binding affinity for SAM and highly reduced methylation activity	757846	
2.1.1.202	F141A	site-directed mutagenesis, the mutant shows activity similar to wild-type enzyme	757846	
2.1.1.202	G679R	naturally occuring mutation	756866	
2.1.1.202	G679R	naturally occurring mutation	756866	
2.1.1.202	K159A	site-directed mutagenesis, the mutant shows moderately decreased activity compared to wild-type enzyme	757846	
2.1.1.202	K159A/R181A	site-directed mutagenesis, the mutant shows highly decreased activity compared to wild-type enzyme	757846	
2.1.1.202	K160A	site-directed mutagenesis, the mutant shows moderately decreased activity compared to wild-type enzyme	757846	
2.1.1.202	K160A/R181A	site-directed mutagenesis, the mutant shows highly decreased activity compared to wild-type enzyme	757846	
2.1.1.202	K248A	site-directed mutagenesis, the mutant shows 5fold increased binding affinity for SAM	757846	
2.1.1.202	K271A	site-directed mutagenesis, the mutant shows highly increased binding affinity for SAM and highly reduced methylation activity	757846	
2.1.1.202	additional information	generation of Arabidopsis thaliana T-DNA insertion mutants of potential mRNA m5C methyltransferases (RCMTs), and of single mutants of TRM4B, trm4b-3 and trm4b-4, the latter exhibit defects in root development. The fulllength transcript of TRM4B and its 3' fragment downstream of the T-DNA insertion sites are greatly decreased in trm4b-3 and undetectable in trm4b-4, implying that trm4b-3 and trm4b-4 could be reduction-of function and loss-of-function mutants, respectively	757702	
2.1.1.202	additional information	generation of NSUN2 knockout mice (homozygous Nsun2Gt[D014D11]Wrs)	758103	
2.1.1.202	additional information	generation of trm4a and trm4a/trm4b deletion mutants, tRNA methylome of wild-type, trm4aDELTA, trm4bDELTA, and trm4aDELTA/trm4bDELTA as determined by genome-wide high-throughput bisulfite sequencing, overview	-, 757846	
2.1.1.202	additional information	generation of trm4b and trm4a/trm4b deletion mutants, tRNA methylome of wild-type, trm4aDELTA, trm4bDELTA, and trm4aDELTA/trm4bDELTA as determined by genome-wide high-throughput bisulfite sequencing, overview	-, 757846	
2.1.1.202	additional information	siRNA-mediated enzyme knockout in HeLa cells	736856	
2.1.1.202	additional information	the only mRNA identified by miCLIP that is differentially expressed when NSun2 is inhibited by RNAi in HEK293 cells is NSun2 itself	735907	
2.1.1.202	R181A	site-directed mutagenesis, the mutant shows highly decreased activity compared to wild-type enzyme	757846