P40261 (NNMT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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.
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
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	nicotinamide N-methyltransferase activity 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

Amino acid modifications

Modified residue

39

1

N6-acetyllysine Ref.5

Secondary structure

1

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264

Helix Strand Turn

Details...

Helix

10 – 13

4

Helix

17 – 24

8

Helix

33 – 50

18

Beta strand

58 – 61

4

Helix

69 – 71

3

Helix

74 – 77

4

Beta strand

79 – 86

8

Helix

88 – 98

11

Helix

108 – 117

10

Helix

126 – 134

9

Beta strand

135 – 140

6

Beta strand

145 – 147

3

Beta strand

157 – 164

8

Helix

166 – 169

4

Helix

173 – 182

10

Beta strand

193 – 197

5

Beta strand

203 – 205

3

Beta strand

210 – 212

3

Helix

219 – 227

9

Beta strand

231 – 237

7

Turn

244 – 246

3

Beta strand

253 – 258

6

Sequences

	Sequence		Length	Mass (Da)
	P40261 [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]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-39, MASS SPECTROMETRY.
[6]	"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.

IPI

IPI00027681.

PIR

A54060.

RefSeq

NP_006160.1. NM_006169.2.

UniGene

Hs.503911.
Hs.623245.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IIP	X-ray	2.05	A/B/C/D	1-264	[»]
3ROD	X-ray	2.72	A/B/C/D	1-264	[»]

ProteinModelPortal

P40261.

SMR

P40261. Positions 3-261.

ModBase

Search...

Protein-protein interaction databases

IntAct

P40261. 2 interactions.

STRING

P40261.

PTM databases

PhosphoSite

P40261.

Polymorphism databases

DMDM

730163.

Proteomic databases

PeptideAtlas

P40261.

PRIDE

P40261.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000299964; ENSP00000299964; ENSG00000166741.

GeneID

4837.

KEGG

hsa:4837.

UCSC

uc001por.1. human.

Organism-specific databases

CTD

4837.

GeneCards

GC11P114162.

H-InvDB

HIX0010142.

HGNC

HGNC:7861. NNMT.

MIM

600008. gene.

neXtProt

NX_P40261.

PharmGKB

PA251.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18410.

HOGENOM

HBG270140.

HOVERGEN

HBG000797.

InParanoid

P40261.

OMA

LKSSYYM.

OrthoDB

EOG49079M.

PhylomeDB

P40261.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P40261.

Bgee

P40261.

CleanEx

HS_NNMT.

Genevestigator

P40261.

GermOnline

ENSG00000166741. Homo sapiens.

Family and domain databases

InterPro

IPR000940. NNMT_TEMT_trans.
[Graphical view]

KO

K00541.

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

DrugBank

DB00627. Niacin.

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:	January 25, 2012
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.