NNMT
entrez
4837
canonical
uniprot
P40261
canonical
ensembl
ENSG00000166741
resolver
ensp
ENSP00000299964
resolver
ensp
ENSP00000441434
resolver
ensp
ENSP00000518865
resolver
ensp
ENSP00000528536
resolver
ensp
ENSP00000528537
resolver
ensp
ENSP00000528538
resolver
ensp
ENSP00000528539
resolver
ensp
ENSP00000528540
resolver
ensp
ENSP00000528541
resolver
ensp
ENSP00000528542
resolver
ensp
ENSP00000528543
resolver
ensp
ENSP00000528544
resolver
ensp
ENSP00000528545
resolver
ensp
ENSP00000528546
resolver
ensp
ENSP00000528547
resolver
ensp
ENSP00000528548
resolver
ensp
ENSP00000617505
resolver
ensp
ENSP00000617506
resolver
ensp
ENSP00000617507
resolver
ensp
ENSP00000617508
resolver
enst
ENST00000299964
resolver
enst
ENST00000535401
resolver
enst
ENST00000713573
resolver
enst
ENST00000858477
resolver
enst
ENST00000858478
resolver
enst
ENST00000858479
resolver
enst
ENST00000858480
resolver
enst
ENST00000858481
resolver
enst
ENST00000858482
resolver
enst
ENST00000858483
resolver
enst
ENST00000858484
resolver
enst
ENST00000858485
resolver
enst
ENST00000858486
resolver
enst
ENST00000858487
resolver
enst
ENST00000858488
resolver
enst
ENST00000858489
resolver
enst
ENST00000947446
resolver
enst
ENST00000947447
resolver
enst
ENST00000947448
resolver
enst
ENST00000947449
resolver
genesymbol
NNMT
resolver
hgnc
HGNC:7861
resolver
uniprot
A0A024R3J0
resolver
uniprot
B0YJ53
resolver
uniprot
Q6FH49
resolver
uniprot_entry
B0YJ53_HUMAN
resolver
uniprot_entry
NNMT_HUMAN
resolver
uniprot_sec
A0A024R3J0
resolver
uniprot_sec
Q6FH49
resolver
activity_regulation
ACTIVITY REGULATION: Inactivated by deimination on Arg-132. {ECO:0000269|PubMed:30044909}.
uniprot
proteins
amino_acid_sequence
MESGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLIDIGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGNRVKGPEKEEKLRQAVKQVLKCDVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAVEAAVKEAGYTIEWFEVISQSYSSTMANNEGLFSLVARKLSRPL
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:21823666, PubMed:23455543, PubMed:8182091). Plays a central role in regulating cellular methylation potential, by consuming S-adenosyl-L-methionine and limiting its availability for other methyltransferases. Actively mediates genome-wide epigenetic and transcriptional changes through hypomethylation of repressive chromatin marks, such as H3K27me3 (PubMed:23455543, PubMed:26571212, PubMed:31043742). In a developmental context, contributes to low levels of the repressive histone marks that characterize pluripotent embryonic stem cell pre-implantation state (PubMed:26571212). Acts as a metabolic regulator primarily on white adipose tissue energy expenditure as well as hepatic gluconeogenesis and cholesterol biosynthesis. 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 (By similarity). Via its product N1-methylnicotinamide regulates protein acetylation in hepatocytes, by repressing the ubiquitination and increasing the stability of SIRT1 deacetylase (By similarity). Can also N-methylate other pyridines structurally related to nicotinamide and play a role in xenobiotic detoxification (PubMed:30044909). {ECO:0000250|UniProtKB:O55239, ECO:0000269|PubMed:21823666, ECO:0000269|PubMed:23455543, ECO:0000269|PubMed:26571212, ECO:0000269|PubMed:30044909, ECO:0000269|PubMed:31043742, ECO:0000269|PubMed:8182091}.
uniprot
proteins
mass_dalton
29574
uniprot
proteins
mutagenesis
MUTAGEN 18; /note="R->K: Has no effect on N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:30044909"; MUTAGEN 20; /note="Y->A: Loss of N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:21823666, ECO:0000269|PubMed:23455543"; MUTAGEN 20; /note="Y->F: Decreases N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:21823666"; MUTAGEN 132; /note="R->K: Loss of N-methyltransferase activity like its citrullinated counterpart."; /evidence="ECO:0000269|PubMed:30044909"; MUTAGEN 181; /note="R->K: Has no effect on N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:30044909"; MUTAGEN 197; /note="D->A: Loss of N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:21823666"; MUTAGEN 201; /note="S->A: Has no effect on N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:21823666"; MUTAGEN 213; /note="S->A: Has no effect on N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:21823666
uniprot
proteins
pathway_participation
PATHWAY: Cofactor metabolism. {ECO:0000305|PubMed:21823666, ECO:0000305|PubMed:23455543}.; PATHWAY: Amino-acid degradation. {ECO:0000305|PubMed:21823666, ECO:0000305|PubMed:23455543}.
uniprot
proteins
post_translational_modification
PTM: Deiminated by PADI1 and PADI2. {ECO:0000269|PubMed:30044909}.
uniprot
proteins
protein_family
Class I-like SAM-binding methyltransferase superfamily
uniprot
proteins
protein_family
NNMT/PNMT/TEMT family
uniprot
proteins
pubmed
11271497
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21823666
uniprot
proteins
pubmed
23455543
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26571212
uniprot
proteins
pubmed
30044909
uniprot
proteins
pubmed
31043742
uniprot
proteins
pubmed
8182091
uniprot
proteins
pubmed
8575745
uniprot
proteins
sequence_length
264
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm.
uniprot
proteins