Nnmt
entrez
18113
canonical
uniprot
O55239
canonical
ensembl
ENSMUSG00000032271
resolver
ensp
ENSMUSP00000034808
resolver
ensp
ENSMUSP00000112381
resolver
ensp
ENSMUSP00000220165
resolver
ensp
ENSMUSP00000357344
resolver
enst
ENSMUST00000034808
resolver
enst
ENSMUST00000119426
resolver
genesymbol
Nnmt
resolver
uniprot
D3YX59
resolver
uniprot
Q9D9X3
resolver
uniprot_entry
D3YX59_MOUSE
resolver
uniprot_entry
NNMT_MOUSE
resolver
uniprot_entry
Q9D9X3_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by 6-methoxynicotinamide (JBSNF-000088). {ECO:0000269|PubMed:29483571}.
uniprot
proteins
amino_acid_sequence
MESGFTSKDTYLSHFNPRDYLEKYYSFGSRHCAENEILRHLLKNLFKIFCLGAVKGELLIDIGSGPTIYQLLSACESFTEIIVSDYTDQNLWELQKWLKKEPGAFDWSPVVTYVCDLEGNRMKGPEKEEKLRRAIKQVLKCDVTQSQPLGGVSLPPADCLLSTLCLDAACPDLPAYRTALRNLGSLLKPGGFLVMVDALKSSYYMIGEQKFSSLPLGWETVRDAVEEAGYTIEQFEVISQNYSSTTSNNEGLFSLVGRKPGRSE
uniprot
proteins
ec_number
2.1.1.1
uniprot
proteins
function
FUNCTION: Catalyzes the N-methylation of nicotinamide using the universal methyl donor S-adenosyl-L-methionine to form N1-methylnicotinamide and S-adenosyl-L-homocysteine, a predominant nicotinamide/vitamin B3 clearance pathway (PubMed:26168293, PubMed:29483571). Plays a central role in regulating cellular methylation potential, by consuming S-adenosyl-L-methionine and limiting its availability for other methyltransferases (By similarity). Actively mediates genome-wide epigenetic and transcriptional changes through hypomethylation of repressive chromatin marks, such as H3K27me3. In a developmental context, contributes to low levels of the repressive histone marks that characterize pluripotent embryonic stem cell pre-implantation state (By similarity). Acts as a metabolic regulator primarily on white adipose tissue energy expenditure as well as hepatic gluconeogenesis and cholesterol biosynthesis (PubMed:24717514, PubMed:26168293). In white adipocytes, regulates polyamine flux by consuming S-adenosyl-L-methionine which provides for propylamine group in polyamine biosynthesis, whereas by consuming nicotinamide controls NAD(+) levels through the salvage pathway (PubMed:24717514). Via its product N1-methylnicotinamide regulates protein acetylation in hepatocytes, by repressing the ubiquitination and increasing the stability of SIRT1 deacetylase (PubMed:26168293). Can also N-methylate other pyridines structurally related to nicotinamide and play a role in xenobiotic detoxification (By similarity). {ECO:0000250|UniProtKB:P40261, ECO:0000269|PubMed:24717514, ECO:0000269|PubMed:26168293, ECO:0000269|PubMed:29483571}.
uniprot
proteins
mass_dalton
29598
uniprot
proteins
mutagenesis
MUTAGEN 20; /note="Y->W: Loss of N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:26168293"; MUTAGEN 198; /note="A->W: Loss of N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:26168293
uniprot
proteins
pathway_participation
PATHWAY: Cofactor metabolism. {ECO:0000250|UniProtKB:P40261}.; PATHWAY: Amino-acid degradation. {ECO:0000250|UniProtKB:P40261}.
uniprot
proteins
post_translational_modification
PTM: Deiminated by PADI1 and PADI2. {ECO:0000250|UniProtKB:P40261}.
uniprot
proteins
protein_family
Class I-like SAM-binding methyltransferase superfamily
uniprot
proteins
protein_family
NNMT/PNMT/TEMT family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
24717514
uniprot
proteins
pubmed
26168293
uniprot
proteins
pubmed
29483571
uniprot
proteins
pubmed
9464457
uniprot
proteins
pubmed
9726248
uniprot
proteins
sequence_length
264
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm.
uniprot
proteins