Nicotinamide N-methyltransferase - Homo sapiens (Human)

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P40261 (NNMT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 114. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Nicotinamide N-methyltransferase
EC=2.1.1.1

Gene names

Name:

NNMT

Organism

Homo sapiens (Human) [Reference proteome]

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	organ regeneration Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to organic nitrogen Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome 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 Ref.1. 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

S-adenosyl-L-methionine binding

Region

142 – 143

S-adenosyl-L-methionine binding

Sites

Binding site

S-adenosyl-L-methionine

Binding site

S-adenosyl-L-methionine

Binding site

S-adenosyl-L-methionine

Binding site

S-adenosyl-L-methionine

Binding site

S-adenosyl-L-methionine

Binding site

163

S-adenosyl-L-methionine

Amino acid modifications

Modified residue

N6-acetyllysine Ref.5

Secondary structure

264

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P40261 [UniParc].

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

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

« Hide

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] [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, 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, MASS SPECTROMETRY.
[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.

IPI

IPI00027681.

PIR

A54060.

RefSeq

NP_006160.1. NM_006169.2.

UniGene

Hs.503911.

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.

ModBase

Search...

Protein-protein interaction databases

IntAct

P40261. 2 interactions.

STRING

9606.ENSP00000299964.

PTM databases

PhosphoSite

P40261.

Polymorphism databases

DMDM

730163.

Proteomic databases

PaxDb

P40261.

PeptideAtlas

P40261.

PRIDE

P40261.

Protocols and materials databases

DNASU

4837.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000299964; ENSP00000299964; ENSG00000166741.
ENST00000535401; ENSP00000441434; ENSG00000166741.

GeneID

4837.

KEGG

hsa:4837.

UCSC

uc001por.1. human.

Organism-specific databases

CTD

4837.

GeneCards

GC11P114162.

HGNC

HGNC:7861. NNMT.

MIM

600008. gene.

neXtProt

NX_P40261.

PharmGKB

PA251.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG71857.

HOGENOM

HOG000013229.

HOVERGEN

HBG000797.

InParanoid

P40261.

K00541.

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

IPR025818. NNMT.
IPR025820. NNMT/PNMT/TEMT_CS.
IPR000940. NNMT_TEMT_trans.
[Graphical view]

PANTHER

PTHR10867. PTHR10867. 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.

EvolutionaryTrace

P40261.

GenomeRNAi

4837.

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:	May 1, 2013
This is version 114 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.

Relevant documents

Human chromosome 11

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents