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P40261 (NNMT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nicotinamide N-methyltransferase

EC=2.1.1.1
Gene names
Name:NNMT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is important for biotransformation of many drugs and xenobiotic compounds.

Catalytic activity

S-adenosyl-L-methionine + nicotinamide = S-adenosyl-L-homocysteine + 1-methylnicotinamide.

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Tissue specificity

Predominantly expressed in the liver. A lower expression is seen in the kidney, lung, skeletal muscle, placenta and heart. Not detected in the brain or pancreas.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. NNMT/PNMT/TEMT family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264Nicotinamide N-methyltransferase
PRO_0000159706

Regions

Region63 – 642S-adenosyl-L-methionine binding
Region142 – 1432S-adenosyl-L-methionine binding

Sites

Binding site201S-adenosyl-L-methionine
Binding site251S-adenosyl-L-methionine
Binding site691S-adenosyl-L-methionine
Binding site851S-adenosyl-L-methionine
Binding site901S-adenosyl-L-methionine
Binding site1631S-adenosyl-L-methionine

Amino acid modifications

Modified residue391N6-acetyllysine Ref.5

Secondary structure

.............................................. 264
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40261 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 280B12748F4488AC

FASTA26429,574
        10         20         30         40         50         60 
MESGFTSKDT YLSHFNPRDY LEKYYKFGSR HSAESQILKH LLKNLFKIFC LDGVKGDLLI 

        70         80         90        100        110        120 
DIGSGPTIYQ LLSACESFKE IVVTDYSDQN LQELEKWLKK EPEAFDWSPV VTYVCDLEGN 

       130        140        150        160        170        180 
RVKGPEKEEK LRQAVKQVLK CDVTQSQPLG AVPLPPADCV LSTLCLDAAC PDLPTYCRAL 

       190        200        210        220        230        240 
RNLGSLLKPG GFLVIMDALK SSYYMIGEQK FSSLPLGREA VEAAVKEAGY TIEWFEVISQ 

       250        260 
SYSSTMANNE GLFSLVARKL SRPL 

« Hide

References

« Hide 'large scale' references
[1]"Human liver nicotinamide N-methyltransferase. cDNA cloning, expression, and biochemical characterization."
Aksoy S., Szumlanski C.L., Weinshilboum R.M.
J. Biol. Chem. 269:14835-14840(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-16 AND 151-184.
Tissue: Liver.
[2]"Human nicotinamide N-methyltransferase gene: molecular cloning, structural characterization and chromosomal localization."
Aksoy S., Brandriff B.F., Ward A., Little P.F., Weinshilboum R.M.
Genomics 29:555-561(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
[4]"Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping."
Hubbard M.J., McHugh N.J.
Electrophoresis 21:3785-3796(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Liver.
[5]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"The crystal structure of human nicotinamide N-methyltransferase in complex with SAH."
Structural genomics consortium (SGC)
Submitted (OCT-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U08021 mRNA. Translation: AAA19904.1.
U20971, U20970 Genomic DNA. Translation: AAA93158.1.
BC000234 mRNA. Translation: AAH00234.1.
PIRA54060.
RefSeqNP_006160.1. NM_006169.2.
UniGeneHs.503911.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IIPX-ray2.05A/B/C/D1-264[»]
3RODX-ray2.72A/B/C/D1-264[»]
ProteinModelPortalP40261.
SMRP40261. Positions 3-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110900. 5 interactions.
IntActP40261. 2 interactions.
STRING9606.ENSP00000299964.

Chemistry

ChEMBLCHEMBL2346486.
DrugBankDB00627. Niacin.

PTM databases

PhosphoSiteP40261.

Polymorphism databases

DMDM730163.

Proteomic databases

PaxDbP40261.
PeptideAtlasP40261.
PRIDEP40261.

Protocols and materials databases

DNASU4837.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299964; ENSP00000299964; ENSG00000166741.
ENST00000535401; ENSP00000441434; ENSG00000166741.
GeneID4837.
KEGGhsa:4837.
UCSCuc001por.1. human.

Organism-specific databases

CTD4837.
GeneCardsGC11P114162.
HGNCHGNC:7861. NNMT.
HPAHPA059180.
MIM600008. gene.
neXtProtNX_P40261.
PharmGKBPA251.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG71857.
HOGENOMHOG000013229.
HOVERGENHBG000797.
InParanoidP40261.
KOK00541.
OMALKSSYYM.
OrthoDBEOG7673B9.
PhylomeDBP40261.
TreeFamTF313114.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP40261.
BgeeP40261.
CleanExHS_NNMT.
GenevestigatorP40261.

Family and domain databases

InterProIPR025818. NNMT.
IPR025820. NNMT/PNMT/TEMT_CS.
IPR000940. NNMT_TEMT_trans.
[Graphical view]
PANTHERPTHR10867. PTHR10867. 1 hit.
PfamPF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
PIRSFPIRSF000384. PNMTase. 1 hit.
PROSITEPS01100. NNMT_PNMT_TEMT. 1 hit.
PS51681. SAM_MT_NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP40261.
GeneWikiNNMT.
GenomeRNAi4837.
NextBio18638.
PROP40261.
SOURCESearch...

Entry information

Entry nameNNMT_HUMAN
AccessionPrimary (citable) accession number: P40261
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM