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P40261

- NNMT_HUMAN

UniProt

P40261 - NNMT_HUMAN

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Protein

Nicotinamide N-methyltransferase

Gene
NNMT
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 201S-adenosyl-L-methionine
Binding sitei25 – 251S-adenosyl-L-methionine
Binding sitei69 – 691S-adenosyl-L-methionine
Binding sitei85 – 851S-adenosyl-L-methionine
Binding sitei90 – 901S-adenosyl-L-methionine
Binding sitei163 – 1631S-adenosyl-L-methionine

GO - Molecular functioni

  1. nicotinamide N-methyltransferase activity Source: ProtInc

GO - Biological processi

  1. methylation Source: Reactome
  2. organ regeneration Source: Ensembl
  3. response to drug Source: Ensembl
  4. response to organonitrogen compound Source: Ensembl
  5. small molecule metabolic process Source: Reactome
  6. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiREACT_6946. Methylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinamide N-methyltransferase (EC:2.1.1.1)
Gene namesi
Name:NNMT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:7861. NNMT.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA251.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 264264Nicotinamide N-methyltransferasePRO_0000159706Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP40261.
PaxDbiP40261.
PeptideAtlasiP40261.
PRIDEiP40261.

PTM databases

PhosphoSiteiP40261.

Expressioni

Tissue specificityi

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.

Gene expression databases

ArrayExpressiP40261.
BgeeiP40261.
CleanExiHS_NNMT.
GenevestigatoriP40261.

Organism-specific databases

HPAiHPA059180.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi110900. 5 interactions.
IntActiP40261. 2 interactions.
STRINGi9606.ENSP00000299964.

Structurei

Secondary structure

1
264
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 147
Helixi17 – 259
Helixi33 – 4917
Beta strandi56 – 627
Helixi69 – 713
Helixi74 – 763
Beta strandi78 – 869
Helixi88 – 9811
Helixi108 – 11710
Helixi124 – 1329
Beta strandi135 – 1406
Beta strandi145 – 1473
Turni148 – 1514
Beta strandi157 – 1648
Helixi166 – 1694
Helixi173 – 18412
Beta strandi187 – 20014
Beta strandi203 – 2064
Beta strandi209 – 2124
Helixi218 – 2269
Turni227 – 2293
Beta strandi230 – 2389
Turni244 – 2463
Beta strandi252 – 2598

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IIPX-ray2.05A/B/C/D1-264[»]
3RODX-ray2.72A/B/C/D1-264[»]
ProteinModelPortaliP40261.
SMRiP40261. Positions 3-261.

Miscellaneous databases

EvolutionaryTraceiP40261.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni63 – 642S-adenosyl-L-methionine binding
Regioni142 – 1432S-adenosyl-L-methionine binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG71857.
HOGENOMiHOG000013229.
HOVERGENiHBG000797.
InParanoidiP40261.
KOiK00541.
OMAiLKSSYYM.
OrthoDBiEOG7673B9.
PhylomeDBiP40261.
TreeFamiTF313114.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025818. NNMT.
IPR025820. NNMT/PNMT/TEMT_CS.
IPR000940. NNMT_TEMT_trans.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERiPTHR10867. PTHR10867. 1 hit.
PfamiPF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
PIRSFiPIRSF000384. PNMTase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS01100. NNMT_PNMT_TEMT. 1 hit.
PS51681. SAM_MT_NNMT_PNMT_TEMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40261-1 [UniParc]FASTAAdd to Basket

« Hide

MESGFTSKDT YLSHFNPRDY LEKYYKFGSR HSAESQILKH LLKNLFKIFC    50
LDGVKGDLLI DIGSGPTIYQ LLSACESFKE IVVTDYSDQN LQELEKWLKK 100
EPEAFDWSPV VTYVCDLEGN RVKGPEKEEK LRQAVKQVLK CDVTQSQPLG 150
AVPLPPADCV LSTLCLDAAC PDLPTYCRAL RNLGSLLKPG GFLVIMDALK 200
SSYYMIGEQK FSSLPLGREA VEAAVKEAGY TIEWFEVISQ SYSSTMANNE 250
GLFSLVARKL SRPL 264
Length:264
Mass (Da):29,574
Last modified:February 1, 1995 - v1
Checksum:i280B12748F4488AC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U08021 mRNA. Translation: AAA19904.1.
U20971, U20970 Genomic DNA. Translation: AAA93158.1.
BC000234 mRNA. Translation: AAH00234.1.
CCDSiCCDS8368.1.
PIRiA54060.
RefSeqiNP_006160.1. NM_006169.2.
UniGeneiHs.503911.

Genome annotation databases

EnsembliENST00000299964; ENSP00000299964; ENSG00000166741.
ENST00000535401; ENSP00000441434; ENSG00000166741.
GeneIDi4837.
KEGGihsa:4837.
UCSCiuc001por.1. human.

Polymorphism databases

DMDMi730163.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U08021 mRNA. Translation: AAA19904.1 .
U20971 , U20970 Genomic DNA. Translation: AAA93158.1 .
BC000234 mRNA. Translation: AAH00234.1 .
CCDSi CCDS8368.1.
PIRi A54060.
RefSeqi NP_006160.1. NM_006169.2.
UniGenei Hs.503911.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P40261.
SMRi P40261. Positions 3-261.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110900. 5 interactions.
IntActi P40261. 2 interactions.
STRINGi 9606.ENSP00000299964.

Chemistry

ChEMBLi CHEMBL2346486.
DrugBanki DB00627. Niacin.

PTM databases

PhosphoSitei P40261.

Polymorphism databases

DMDMi 730163.

Proteomic databases

MaxQBi P40261.
PaxDbi P40261.
PeptideAtlasi P40261.
PRIDEi P40261.

Protocols and materials databases

DNASUi 4837.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000299964 ; ENSP00000299964 ; ENSG00000166741 .
ENST00000535401 ; ENSP00000441434 ; ENSG00000166741 .
GeneIDi 4837.
KEGGi hsa:4837.
UCSCi uc001por.1. human.

Organism-specific databases

CTDi 4837.
GeneCardsi GC11P114162.
HGNCi HGNC:7861. NNMT.
HPAi HPA059180.
MIMi 600008. gene.
neXtProti NX_P40261.
PharmGKBi PA251.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG71857.
HOGENOMi HOG000013229.
HOVERGENi HBG000797.
InParanoidi P40261.
KOi K00541.
OMAi LKSSYYM.
OrthoDBi EOG7673B9.
PhylomeDBi P40261.
TreeFami TF313114.

Enzyme and pathway databases

Reactomei REACT_6946. Methylation.

Miscellaneous databases

EvolutionaryTracei P40261.
GeneWikii NNMT.
GenomeRNAii 4837.
NextBioi 18638.
PROi P40261.
SOURCEi Search...

Gene expression databases

ArrayExpressi P40261.
Bgeei P40261.
CleanExi HS_NNMT.
Genevestigatori P40261.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR025818. NNMT.
IPR025820. NNMT/PNMT/TEMT_CS.
IPR000940. NNMT_TEMT_trans.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
PANTHERi PTHR10867. PTHR10867. 1 hit.
Pfami PF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view ]
PIRSFi PIRSF000384. PNMTase. 1 hit.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS01100. NNMT_PNMT_TEMT. 1 hit.
PS51681. SAM_MT_NNMT_PNMT_TEMT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiNNMT_HUMAN
AccessioniPrimary (citable) accession number: P40261
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 3, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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