2.1.1.244	D168X	site-directed mutagenesis, the mutation has no effect on methylation	718160	
2.1.1.244	D178A/D181A	site-directed mutagenesis, mutating the residues Asp178 and Asp181 at the lip of the active site to Ala decreases enzyme activity, which is further decreased by reverse-charge mutagenesis to Lys	718160	
2.1.1.244	D180K	site-directed mutagenesis, inactive mutant	736186	
2.1.1.244	D180N	site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type	756877	
2.1.1.244	D180Y	site-directed mutagenesis, inactive mutant	736186	
2.1.1.244	D212N	site-directed mutagenesis, the mutant shows reduced activity compared to wild-type	756877	
2.1.1.244	E213A	site-directed mutagenesis, the mutant shows 15% reduced activity compared to wild-type	756877	
2.1.1.244	H140A	the mutant loses the catalytic activity, but retains binding affinity to the peptide substrate	756463	
2.1.1.244	H140K	site-directed mutagenesis, inactive mutant	736186	
2.1.1.244	additional information	depleting NRMT in 293LT cells, using lentivirus, significantly decreases methylation of endogenous RCC1, while not affecting overall RCC1 level, depleting NRMT in HeLa cells using short interfering RNAs causing the same effects, RCC1 methylation is rescued by expression of murine NRMT-FLAG, which is not targeted by the human shRNA	718160	
2.1.1.244	additional information	generation of NTMT1 knockout HEK-293FT cells by CRISPR-Cas9	756441	
2.1.1.244	additional information	NRMT1 co-expression with NRMT2 increases the trimethylation rate of NRMT1. Generation of truncation constructs of NRMT1. Full-length FLAG-tagged NRMT1 only weakly interacts with the first 112 aa of NRMT2, though strongly interacts with a GFP-tagged NRMT2 fragment (amino acids 77-223) that is missing the 59 aa tail that is also lacking from the crystal structure and subsequent model. Full-length FLAG-tagged NRMT2 strongly interacts with the first 59 aa of NRMT1, as well as, amino acids 52-172. There is a decreased interaction of FLAG-tagged NRMT2-FLAG with the C-terminal fragment of NRMT1 (amino acids 178-223). Generation of NRMT1 knockout mutant, NRMT2 overexpression cannot rescue NRMT1 knockout phenotypes	758296	
2.1.1.244	additional information	the intact dimethylated Rpl12ab species isolated from the YBR261C/tae1 deletion strain is fragmented, and a b20 ion is detected with the addition of one methyl group, suggesting partial methylation of lysine 3. Neither of these species is dimethylated at the N-terminal residue. Rps25a/Rps25b isolated from the YBR261C/tae1 deletion strain is 28 Da less than the wild type, and the fragmentation data indicate no methylation is present	717248	
2.1.1.244	N168A	site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type	756877	
2.1.1.244	N168K	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	736186	
2.1.1.244	Q169K	site-directed mutagenesis, inactive mutant	718160	
2.1.1.244	S183K	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	718160	
2.1.1.244	W136F	site-directed mutagenesis, almost inactive mutant	736186	
2.1.1.244	W136I	site-directed mutagenesis, inactive mutant	736186	
2.1.1.244	W136L	site-directed mutagenesis, the mutant shows 92% reduced activity compared to wild-type	756877	
2.1.1.244	Y19A	site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type	756877	
2.1.1.244	Y19F	site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type	756877	
2.1.1.244	Y215A	site-directed mutagenesis, the mutant shows reduced activity compared to wild-type	756877	
2.1.1.244	Y215I	site-directed mutagenesis, the mutant shows reduced activity compared to wild-type	756877