Reviewed, UniProtKB/Swiss-Prot P40261 (NNMT_HUMAN)

Names and origin

Protein names

Recommended name:
    Nicotinamide N-methyltransferase
    EC=2.1.1.1

Gene names

Name:

NNMT

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	264 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 NNMT/PNMT/TEMT family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	nicotinamide N-methyltransferase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 264	264	Nicotinamide N-methyltransferase		PRO_0000159706
Regions
	Region	63 – 64	2	S-adenosyl-L-methionine binding
	Region	142 – 143	2	S-adenosyl-L-methionine binding
Sites
	Binding site	20	1	S-adenosyl-L-methionine
	Binding site	25	1	S-adenosyl-L-methionine
	Binding site	69	1	S-adenosyl-L-methionine
	Binding site	85	1	S-adenosyl-L-methionine
	Binding site	90	1	S-adenosyl-L-methionine
	Binding site	163	1	S-adenosyl-L-methionine

Sequences

	Sequence		Length	Mass (Da)
	P40261-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 280B12748F4488AC	FASTA	264	29,574
	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

References

	« Hide 'large scale' referencesShow '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: 8182091] [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: 8575745] [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: 15489334] [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: 11271497] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY. Tissue: Liver.
[5]	"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

EMBLGenBankDDBJ

U08021 mRNA. Translation: AAA19904.1.
U20971, U20970 Genomic DNA. Translation: AAA93158.1.
BC000234 mRNA. Translation: AAH00234.1.

PIR

A54060.

RefSeq

NP_006160.1.

UniGene

Hs.503911

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IIP	X-ray	2.05	A/B/C/D	1-264	[»]

SMR

P40261. Positions 1-260.

ModBase

Search...

PTM databases

PhosphoSite

P40261.

Proteomic databases

PeptideAtlas

P40261.

Genome annotation databases

Ensembl

ENSG00000166741. Homo sapiens. [Contig view]

GeneID

4837.

KEGG

hsa:4837.

Organism-specific databases

H-InvDB

HIX0010142.

HGNC

HGNC:7861. NNMT.

MIM

600008. gene.

PharmGKB

PA251.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P40261.

HOVERGEN

P40261.

Enzyme and pathway databases

Reactome

REACT_2063. Metabolism of xenobiotics.

Gene expression databases

ArrayExpress

P40261.

CleanEx

HS_NNMT.

GermOnline

ENSG00000166741. Homo sapiens.

Family and domain databases

InterPro

IPR000940. NNMT_TEMT_trans.
[Graphical view]

PANTHER

PTHR10867. NNMT_TEMT_trans. 1 hit.

Pfam

PF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]

PIRSF

PIRSF000384. PNMTase. 1 hit.

PROSITE

PS01100. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00627. Niacin.

LinkHub

P40261.

NextBio

18638.

SOURCE

Search...

Entry information

Entry name

NNMT_HUMAN

Accession

Primary (citable) accession number: P40261

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 25, 2008
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)