Names & Taxonomy

Uniprot ID:
P43490
Entry Name:
NAMPT_HUMAN
Status:
reviewed
Protein Names:
Nicotinamide phosphoribosyltransferase (NAmPRTase) (Nampt) (EC 2.4.2.12) (Pre-B-cell colony-enhancing factor 1) (Pre-B cell-enhancing factor) (Visfatin)
Gene Names:
NAMPT PBEF PBEF1
Gene Names Primary:
NAMPT
Organism:
Homo sapiens (Human)

Structure

Length:
491
Sequence:
MNPAAEAEFNILLATDSYKVTHYKQYPPNTSKVYSYFECREKKTENSKLRKVKYEETVFYGLQYILNKYLKGKVVTKEKIQEAKDVYKEHFQDDVFNEKGWNYILEKYDGHLPIEIKAVPEGFVIPRGNVLFTVENTDPECYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETSGNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGLALIKKYYGTKDPVPGYSVPAAEHSTITAWGKDHEKDAFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIVSRSTQAPLIIRPDSGNPLDTVLKVLEILGKKFPVTENSKGYKLLPPYLRVIQGDGVDINTLQEIVEGMKQKMWSIENIAFGSGGGLLQKLTRDLLNCSFKCSYVVTNGLGINVFKDPVADPNKRSKKGRLSLHRTPAGNFVTLEEGKGDLEEYGQDLLHTVFKNGKVTKSYSFDEIRKNAQLNIELEAAHH
Proteomes:
UP000005640

Subcellular location

Subcellular Location:
Nucleus

Function

Function:
Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway. The secreted form behaves both as a cytokine with immunomodulating properties and an adipokine with anti-diabetic properties, it has no enzymatic activity, partly because of lack of activation by ATP, which has a low level in extracellular space and plasma. Plays a role in the modulation of circadian clock function. NAMPT-dependent oscillatory production of NAD regulates oscillation of clock target gene expression by releasing the core clock component: CLOCK-ARNTL/BMAL1 heterodimer from NAD-dependent SIRT1-mediated suppression (By similarity).
Pathway:
Cofactor biosynthesis; NAD(+) biosynthesis; nicotinamide D-ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and nicotinamide: step 1/1.
Catalytic Activity:
Nicotinamide D-ribonucleotide + diphosphate = nicotinamide + 5-phospho-alpha-D-ribose 1-diphosphate.
Enzyme Regulation:
ENZYME REGULATION: Inhibited by FK866. FK866 competes for the same binding site as nicotinamide, but due to its very low dissociation rate, it is essentially an irreversible inhibitor.
Gene Ontology Go:
cell junction
cytosol
extracellular exosome
extracellular space
nucleoplasm
cytokine activity
drug binding
nicotinamide phosphoribosyltransferase activity
nicotinate-nucleotide diphosphorylase (carboxylating) activity
cell-cell signaling
circadian regulation of gene expression
circadian rhythm
female pregnancy
NAD biosynthetic process
NAD metabolic process
nicotinamide metabolic process
positive regulation of cell proliferation
positive regulation of nitric-oxide synthase biosynthetic process
positive regulation of smooth muscle cell proliferation
positive regulation of transcription from RNA polymerase II promoter
response to organic cyclic compound
signal transduction
small molecule metabolic process
vitamin metabolic process
water-soluble vitamin metabolic process
Gene Ontology Biological Process:
cell-cell signaling
circadian regulation of gene expression
circadian rhythm
female pregnancy
NAD biosynthetic process
NAD metabolic process
nicotinamide metabolic process
positive regulation of cell proliferation
positive regulation of nitric-oxide synthase biosynthetic process
positive regulation of smooth muscle cell proliferation
positive regulation of transcription from RNA polymerase II promoter
response to organic cyclic compound
signal transduction
small molecule metabolic process
vitamin metabolic process
water-soluble vitamin metabolic process
Gene Ontology Molecular Function:
cytokine activity
drug binding
nicotinamide phosphoribosyltransferase activity
nicotinate-nucleotide diphosphorylase (carboxylating) activity
Gene Ontology Cellular Component:
cell junction
cytosol
extracellular exosome
extracellular space
nucleoplasm
Keywords:
3D-structure
Acetylation
Biological rhythms
Complete proteome
Cytokine
Cytoplasm
Glycosyltransferase
Nucleus
Phosphoprotein
Polymorphism
Pyridine nucleotide biosynthesis
Reference proteome
Secreted
Transferase
Interacts With:
P02792; Q01628; P03886

Publication

PubMed ID:
8289818 14702039 12853948 12690205 15489334 15592455 21269460 22462624 21741723 22223895 24130902 24275569 16783377 16959974